Preclinical safety evaluation of a recombinant plasmid vector encoding mature human neutrophil peptide-1 by repeated local administrations in nonhuman primates

Preclinical safety evaluation of a recombinant plasmid vector encoding mature human neutrophil peptide-1 by repeated local administrations in nonhuman primates

In our earlier research, a novel gene remedy method was developed based mostly on a plasmid vector pSecTag2B through which recombinant HNP1 gene was regulated below a cytomegalovirus promoter to encode a mature HNP1 type. We confirmed for the primary time in numerous tumor fashions together with human most cancers xenografts that overexpression of HNP1 within the tumor milieu by intratumoral pSecTag-HNP1 (pHNP1) administration effectively attenuated in vivo tumor development, mediated host immune responses to tumors, and produced a synergistic impact when mixed with chemotherapeutics.

In present research, a preclinical security investigation of HNP1 gene remedy was carried out in non-human primates. Eleven cynomolgus monkeys had been divided into three teams of three to four animals every and obtained both repeated s.c. injections of pHNP1/cationic liposome complexes at low (0.625 mg/kg) or excessive (2.5 mg/kg) dose or glucose as management. Important HNP1 in vivo accumulation was detected after consecutive administrations. All primates reached the top of the research with good physique situations. Injection web site irritation was the one apparent poisonous response throughout commentary interval.

As well as, elevation of monocyte/macrophage and neutrophil in addition to decline of lymphocyte had been detected within the peripheral blood of pHNP1-treated primates. These alterations had been partially alleviated on the finish of commentary interval. In addition to, dose-related histopathological adjustments of the immune organs had been noticed at necropsy, together with a minimal thymic lymphocyte lower and a minimal-to-mild lymph node erythrocyte enhance, however which can’t be excluded from HNP1 induced immune reactions. Collectively, these information help future medical research of pHNP1-based native gene supply in tumor sufferers.

The downregulation of endogenous dhfr improved the effectivity of EBNA-1 amplification, as evidenced by a comparability with the amplification extent in cells missing shRNA expression on the similar MTX focus. The EBNA-1 expression ranges from the EBNA-1-amplified clones chosen on this research had been larger than these obtained from EBNA-1-amplified clones that had been generated utilizing the standard amplification in our earlier research. According to earlier research, EBNA-1 amplification improved the manufacturing of the Fc-fusion protein by a selected protein productiveness (qp)-enhancing impact, slightly than by bettering cell development or transfection effectivity.

Joint common modular plasmids (JUMP): a versatile vector platform for artificial biology

Technology of latest DNA constructs is an important course of in trendy life science and biotechnology. Modular cloning techniques based mostly on Golden Gate cloning, utilizing Kind IIS restriction endonucleases, permit meeting of complicated multipart constructs from reusable fundamental DNA components in a fast, dependable and automation-friendly manner. Many such toolkits can be found, with various levels of compatibility, most of that are aimed toward particular host organisms. Right here, we current a vector design which permits easy vector modification by utilizing modular cloning to assemble and add new capabilities in secondary websites flanking the primary insertion web site (used for typical modular cloning).

Preclinical safety evaluation of a recombinant plasmid vector encoding mature human neutrophil peptide-1 by repeated local administrations in nonhuman primates

Meeting in all websites is suitable with the PhytoBricks normal, and vectors are suitable with the Commonplace European Vector Structure (SEVA) in addition to BioBricks. We exhibit that this facilitates the development of vectors with tailor-made capabilities and simplifies the workflow for producing libraries of constructs with frequent components. We have now made out there a set of vectors with 10 totally different microbial replication origins, various in copy quantity and host vary, and permitting chromosomal integration, in addition to a choice of generally used fundamental components.

This design expands the vary of hosts which might be simply modified by modular cloning and acts as a toolkit which can be utilized to facilitate the technology of latest toolkits with particular capabilities required for focusing on additional hosts. The antigen produced by the described approach is appropriate for serological exams and subunit vaccine research. We developed a easy purification scheme that constantly yielded as much as 30 mg of RBD protein per liter of the easy shake flask cell tradition.

Excessive-level expression of the monomeric SARS-CoV-2 S protein RBD 320-537 in stably transfected CHO cells by the EEF1A1-based plasmid vector

The spike (S) protein is likely one of the three proteins forming the coronaviruses’ viral envelope. The S protein of the Extreme Acute Respiratory Syndrome Coronavirus 2 (SARS-CoV-2) has a spatial construction much like the S proteins of different mammalian coronaviruses, aside from a singular receptor-binding area (RBD), which is a big inducer of host immune response. Recombinant SARS-CoV-2 RBD is broadly used as a extremely particular minimal antigen for serological exams.

Right publicity of antigenic determinants has a big affect on the accuracy of such tests-the antigen must be appropriately folded, comprise no probably antigenic non-vertebrate glycans, and, ideally, ought to have a glycosylation sample much like the native S protein. Based mostly on the beforehand developed p1.1 vector, containing the regulatory sequences of the Eukaryotic translation elongation issue 1 alpha gene (EEF1A1) from Chinese language hamster, we created two expression constructs encoding SARS-CoV-2 RBD with C-terminal c-myc and polyhistidine tags.

Human Bone Morphogenetic Protein 4 (BMP4) ELISA Kit

DLR-BMP4-Hu-48T 48T
EUR 510
Description: A sandwich quantitative ELISA assay kit for detection of Human Bone Morphogenetic Protein 4 (BMP4) in samples from serum, plasma, tissue homogenates, cell lysates, cell culture supernates or other biological fluids.

Human Bone Morphogenetic Protein 4 (BMP4) ELISA Kit

DLR-BMP4-Hu-96T 96T
EUR 657.6
Description: A sandwich quantitative ELISA assay kit for detection of Human Bone Morphogenetic Protein 4 (BMP4) in samples from serum, plasma, tissue homogenates, cell lysates, cell culture supernates or other biological fluids.

Mouse Bone Morphogenetic Protein 4 (BMP4) ELISA Kit

DLR-BMP4-Mu-48T 48T
EUR 522
Description: A sandwich quantitative ELISA assay kit for detection of Mouse Bone Morphogenetic Protein 4 (BMP4) in samples from serum, plasma, tissue homogenates, cell lysates, cell culture supernates or other biological fluids.

Mouse Bone Morphogenetic Protein 4 (BMP4) ELISA Kit

DLR-BMP4-Mu-96T 96T
EUR 673.2
Description: A sandwich quantitative ELISA assay kit for detection of Mouse Bone Morphogenetic Protein 4 (BMP4) in samples from serum, plasma, tissue homogenates, cell lysates, cell culture supernates or other biological fluids.

Porcine Bone Morphogenetic Protein 4 (BMP4) ELISA Kit

DLR-BMP4-p-48T 48T
EUR 591.6
Description: A sandwich quantitative ELISA assay kit for detection of Porcine Bone Morphogenetic Protein 4 (BMP4) in samples from serum, plasma, tissue homogenates or other biological fluids.

Porcine Bone Morphogenetic Protein 4 (BMP4) ELISA Kit

DLR-BMP4-p-96T 96T
EUR 769.2
Description: A sandwich quantitative ELISA assay kit for detection of Porcine Bone Morphogenetic Protein 4 (BMP4) in samples from serum, plasma, tissue homogenates or other biological fluids.

Rat Bone Morphogenetic Protein 4 (BMP4) ELISA Kit

DLR-BMP4-Ra-48T 48T
EUR 544.8
Description: A sandwich quantitative ELISA assay kit for detection of Rat Bone Morphogenetic Protein 4 (BMP4) in samples from serum, plasma, tissue homogenates, cell lysates, cell culture supernates or other biological fluids.

Rat Bone Morphogenetic Protein 4 (BMP4) ELISA Kit

DLR-BMP4-Ra-96T 96T
EUR 704.4
Description: A sandwich quantitative ELISA assay kit for detection of Rat Bone Morphogenetic Protein 4 (BMP4) in samples from serum, plasma, tissue homogenates, cell lysates, cell culture supernates or other biological fluids.

Rabbit Bone Morphogenetic Protein 4 (BMP4) ELISA Kit

DLR-BMP4-Rb-48T 48T
EUR 544.8
Description: A sandwich quantitative ELISA assay kit for detection of Rabbit Bone Morphogenetic Protein 4 (BMP4) in samples from serum, plasma, tissue homogenates or other biological fluids.

Rabbit Bone Morphogenetic Protein 4 (BMP4) ELISA Kit

DLR-BMP4-Rb-96T 96T
EUR 704.4
Description: A sandwich quantitative ELISA assay kit for detection of Rabbit Bone Morphogenetic Protein 4 (BMP4) in samples from serum, plasma, tissue homogenates or other biological fluids.

Bovine Bone Morphogenetic Protein 4 (BMP4) ELISA Kit

RD-BMP4-b-48Tests 48 Tests
EUR 592.8

Bovine Bone Morphogenetic Protein 4 (BMP4) ELISA Kit

RD-BMP4-b-96Tests 96 Tests
EUR 820.8

Canine Bone Morphogenetic Protein 4 (BMP4) ELISA Kit

RD-BMP4-c-48Tests 48 Tests
EUR 566.4

Canine Bone Morphogenetic Protein 4 (BMP4) ELISA Kit

RD-BMP4-c-96Tests 96 Tests
EUR 783.6

Chicken Bone Morphogenetic Protein 4 (BMP4) ELISA Kit

RD-BMP4-Ch-48Tests 48 Tests
EUR 540

Chicken Bone Morphogenetic Protein 4 (BMP4) ELISA Kit

RD-BMP4-Ch-96Tests 96 Tests
EUR 746.4

Goat Bone Morphogenetic Protein 4 (BMP4) ELISA Kit

RD-BMP4-g-48Tests 48 Tests
EUR 606

Goat Bone Morphogenetic Protein 4 (BMP4) ELISA Kit

RD-BMP4-g-96Tests 96 Tests
EUR 840

Human Bone Morphogenetic Protein 4 (BMP4) ELISA Kit

RD-BMP4-Hu-48Tests 48 Tests
EUR 501.6

Human Bone Morphogenetic Protein 4 (BMP4) ELISA Kit

RD-BMP4-Hu-96Tests 96 Tests
EUR 690

Mouse Bone Morphogenetic Protein 4 (BMP4) ELISA Kit

RD-BMP4-Mu-48Tests 48 Tests
EUR 514.8

Mouse Bone Morphogenetic Protein 4 (BMP4) ELISA Kit

RD-BMP4-Mu-96Tests 96 Tests
EUR 709.2

Porcine Bone Morphogenetic Protein 4 (BMP4) ELISA Kit

RD-BMP4-p-48Tests 48 Tests
EUR 592.8

Porcine Bone Morphogenetic Protein 4 (BMP4) ELISA Kit

RD-BMP4-p-96Tests 96 Tests
EUR 820.8

Rat Bone Morphogenetic Protein 4 (BMP4) ELISA Kit

RD-BMP4-Ra-48Tests 48 Tests
EUR 540

Rat Bone Morphogenetic Protein 4 (BMP4) ELISA Kit

RD-BMP4-Ra-96Tests 96 Tests
EUR 746.4

Rabbit Bone Morphogenetic Protein 4 (BMP4) ELISA Kit

RD-BMP4-Rb-48Tests 48 Tests
EUR 540

Rabbit Bone Morphogenetic Protein 4 (BMP4) ELISA Kit

RD-BMP4-Rb-96Tests 96 Tests
EUR 746.4

Bovine Bone Morphogenetic Protein 4 (BMP4) ELISA Kit

RDR-BMP4-b-48Tests 48 Tests
EUR 619.2

Bovine Bone Morphogenetic Protein 4 (BMP4) ELISA Kit

RDR-BMP4-b-96Tests 96 Tests
EUR 859.2

Canine Bone Morphogenetic Protein 4 (BMP4) ELISA Kit

RDR-BMP4-c-48Tests 48 Tests
EUR 591.6

Canine Bone Morphogenetic Protein 4 (BMP4) ELISA Kit

RDR-BMP4-c-96Tests 96 Tests
EUR 819.6

Chicken Bone Morphogenetic Protein 4 (BMP4) ELISA Kit

RDR-BMP4-Ch-48Tests 48 Tests
EUR 564

Chicken Bone Morphogenetic Protein 4 (BMP4) ELISA Kit

RDR-BMP4-Ch-96Tests 96 Tests
EUR 781.2

Goat Bone Morphogenetic Protein 4 (BMP4) ELISA Kit

RDR-BMP4-g-48Tests 48 Tests
EUR 633.6

Goat Bone Morphogenetic Protein 4 (BMP4) ELISA Kit

RDR-BMP4-g-96Tests 96 Tests
EUR 879.6

Human Bone Morphogenetic Protein 4 (BMP4) ELISA Kit

RDR-BMP4-Hu-48Tests 48 Tests
EUR 523.2

Human Bone Morphogenetic Protein 4 (BMP4) ELISA Kit

RDR-BMP4-Hu-96Tests 96 Tests
EUR 721.2

Mouse Bone Morphogenetic Protein 4 (BMP4) ELISA Kit

RDR-BMP4-Mu-48Tests 48 Tests
EUR 536.4

Mouse Bone Morphogenetic Protein 4 (BMP4) ELISA Kit

RDR-BMP4-Mu-96Tests 96 Tests
EUR 741.6

Porcine Bone Morphogenetic Protein 4 (BMP4) ELISA Kit

RDR-BMP4-p-48Tests 48 Tests
EUR 619.2

Porcine Bone Morphogenetic Protein 4 (BMP4) ELISA Kit

RDR-BMP4-p-96Tests 96 Tests
EUR 859.2

Rat Bone Morphogenetic Protein 4 (BMP4) ELISA Kit

RDR-BMP4-Ra-48Tests 48 Tests
EUR 564

Rat Bone Morphogenetic Protein 4 (BMP4) ELISA Kit

RDR-BMP4-Ra-96Tests 96 Tests
EUR 781.2

Rabbit Bone Morphogenetic Protein 4 (BMP4) ELISA Kit

RDR-BMP4-Rb-48Tests 48 Tests
EUR 564

Rabbit Bone Morphogenetic Protein 4 (BMP4) ELISA Kit

RDR-BMP4-Rb-96Tests 96 Tests
EUR 781.2

Visitor Over Spectacle Clear

SAF1410 EACH
EUR 4.56

EP Reagent Biuret Reagent

1011601 1L
EUR 42.18

EP Reagent Iodoplatinate Reagent

1046300 200ML
EUR 360.24

EP Reagent Methoxyphenylacetic Reagent

1053601 100ML
EUR 354.54

EP Reagent Molybdovanadic Reagent

1056700 100ML
EUR 42.18

EP Reagent Phosphomolybdotungstic Reagent

1065000 100ML
EUR 161.88

Automatic CO2 Change Over Unit

INC6176 EACH
EUR 1288.2

Forceps Dissecting Turn Over End

D02129 EACH
EUR 4.67

Gas Change Over Unit 30Psi

GAS1000 EACH
EUR 904.02

Gas Change Over Unit 60Psi

GAS1002 EACH
EUR 905.16

Gas Change Over Unit 100Psi

GAS1004 EACH
EUR 922.26

Bolle TG10 Safety Over Glasses

SAF1106 EACH
EUR 8.39

EP Reagent Sulfomolybdic Reagent R3

1086500 1L
EUR 287.28

DURAN Over-Cap 45mm Black Phenolic

BOT2596 PK10
EUR 25.08

BOP reagent

5-02141 25g Ask for price

BOP reagent

5-02142 100g Ask for price

Chymase reagent

30C-CP1129 5 units
EUR 2622
Description: Purified native Human Chymase reagent

Traut's Reagent

2330-1000
EUR 418.8

Traut's Reagent

2330-500
EUR 248.4

MTS Reagent

2808-1000
EUR 1188

MTS Reagent

2808-250
EUR 438

MTT Reagent

2809-1G
EUR 216

MTT Reagent

2809-5G
EUR 652.8

BOP reagent

A7015-100000 100 g
EUR 240
Description: A peptide coupling reagent. Can be used in the preparation of phenyl esters of amino acids which have been shown to be valuable as blocked derivatives of amino acids in the field of peptide synthesis.

BOP reagent

A7015-25000 25 g
EUR 135.6
Description: A peptide coupling reagent. Can be used in the preparation of phenyl esters of amino acids which have been shown to be valuable as blocked derivatives of amino acids in the field of peptide synthesis.

Bradford reagent

BDE641 100ml
EUR 73.21

Bluing Reagent

BRT030 30 ml
EUR 72

Bluing Reagent

BRT125 125 ml
EUR 75.6

Bluing Reagent

BRT3800 1 Gal.
EUR 220.8

Bluing Reagent

BRT500 500 ml
EUR 91.2

Bluing Reagent

BRT999 1000 ml
EUR 105.6

Beaucage reagent

HY-100951 10mM/1mL
EUR 151.2

Phosphate Reagent

106199 PK100
EUR 61.29

Chromium Reagent

1206699 EACH
EUR 141.72

Ninhydrin Reagent

MIC6746 EACH
EUR 31.12

Nessler Reagent

NESSR 500ML
EUR 148.2

Thioacetamide Reagent

THIOR01 100ML
EUR 78.66

BMP4 antibody

70R-12408 100 ug
EUR 483.6
Description: Rabbit polyclonal BMP4 antibody

BMP4 antibody

70R-12409 100 ug
EUR 483.6
Description: Rabbit polyclonal BMP4 antibody

BMP4 Antibody

43852-100ul 100ul
EUR 302.4

BMP4 antibody

70R-16011 50 ul
EUR 522
Description: Rabbit polyclonal BMP4 antibody

BMP4 antibody

38256-100ul 100ul
EUR 302.4

BMP4 protein

30R-1255 100 ug
EUR 268.8
Description: Purified recombinant Human BMP4 protein

BMP4 protein

30R-2651 10 ug
EUR 409.2
Description: Purified recombinant Human BMP4 protein

BMP4 Antibody

35652-100ul 100ul
EUR 302.4

BMP4 antibody

20R-2936 100 ul
EUR 471.6
Description: Rabbit polyclonal BMP4 antibody

BMP4 protein

30R-AB029 5 ug
EUR 327.6
Description: Purified recombinant Human BMP4 protein

BMP4 antibody

10R-B119a 100 ug
EUR 950.4
Description: Mouse monoclonal BMP4 antibody

BMP4 antibody

10R-B119B 500 ug
EUR 327.6
Description: Mouse monoclonal BMP4 antibody

BMP4 antibody

10R-2148 100 ul
EUR 483.6
Description: Mouse monoclonal BMP4 antibody

BMP4 antibody

10R-3460 100 ul
EUR 829.2
Description: Mouse monoclonal BMP4 antibody

BMP4 Antibody

ABF5175 100 ug
EUR 525.6

BMP4 Antibody

ABD6461 100 ug
EUR 525.6

BMP4 siRNA

20-abx909174
  • EUR 661.20
  • EUR 878.40
  • 15 nmol
  • 30 nmol

BMP4 siRNA

20-abx909175
  • EUR 661.20
  • EUR 878.40
  • 15 nmol
  • 30 nmol

BMP4 Antibody

BF0696 200ul
EUR 540

BMP4 Antibody

1-CSB-PA763132
  • EUR 380.40
  • EUR 292.80
  • 100ul
  • 50ul
Description: A polyclonal antibody against BMP4. Recognizes BMP4 from Human, Mouse, Rat. This antibody is Unconjugated. Tested in the following application: ELISA, WB, IHC;ELISA:1:2000-1:5000, WB:1:500-1:2000, IHC:1:25-1:100

BMP4 Antibody

1-CSB-PA05799A0Rb
  • EUR 380.40
  • EUR 402.00
  • 100ug
  • 50ug
Description: A polyclonal antibody against BMP4. Recognizes BMP4 from Human, Mouse, Rat, Zebrafish. This antibody is Unconjugated. Tested in the following application: ELISA, WB, IHC; Recommended dilution: WB:1:500-1:5000, IHC:1:100-1:1000

BMP4 Antibody

DF6461 200ul
EUR 420

BMP4 Antibody

AF5175 200ul
EUR 420

BMP4 Antibody

1-CSB-PA212919
  • EUR 380.40
  • EUR 292.80
  • 100ul
  • 50ul
Description: A polyclonal antibody against BMP4. Recognizes BMP4 from Human, Mouse, Rat. This antibody is Unconjugated. Tested in the following application: ELISA, WB, IHC;ELISA:1:2000-1:5000, WB:1:500-1:2000, IHC:1:30-1:150

BMP4 Antibody

1-CSB-PA002740GA01HU
  • EUR 716.40
  • EUR 399.60
  • 150ul
  • 50ul
Description: A polyclonal antibody against BMP4. Recognizes BMP4 from Human, Mouse, Rat. This antibody is Unconjugated. Tested in the following application: ELISA, WB

anti-BMP4

LF-PA0093 100 ul
EUR 400.8
Description: Rabbit polyclonal to BMP4

pENTR223- BMP4

PVT10009 2 ug
EUR 319.2

pCDNA3.1- BMP4

PVT10207 2 ug
EUR 361.2

BMP4 Antibody

R31950 100 ug
EUR 419

BMP4 Antibody

R36461-100UG 100 ug
EUR 399

BMP4 Antibody

F45385-0.08ML 0.08 ml
EUR 165

BMP4 Antibody

F45385-0.4ML 0.4 ml
EUR 379

HEK-293T Telomerase Over-Expressing Cell Pellet

abx069991-1Pellet 1 Pellet
EUR 477.6

Visitor Eye Shield Over Specs - Portwest PW30

SAF1021 EACH
EUR 3.42

Esophagus Lysate

1365 0.1 mg
EUR 229.2
Description: Esophagus tissue lysate was prepared by homogenization in lysis buffer (10 mM HEPES pH7.9, 1.5 mM MgCl2, 10 mM KCl, 1 mM ethylenediaminetetraacetic acid, 10% glycerol, 1% NP-40, and a cocktail of protease inhibitors). Tissue and cell debris was removed by centrifugation. The product was boiled for 5 min in 1 x SDS sample buffer (50 mM Tris-HCl pH 6.8, 12.5% glycerol, 1% sodium dodecylsulfate, 0.01% bromophenol blue) containing 50 mM DTT.

Ileum Lysate

1367 0.1 mg
EUR 229.2
Description: Ileum tissue lysate was prepared by homogenization in lysis buffer (10 mM HEPES pH7.9, 1.5 mM MgCl2, 10 mM KCl, 1 mM ethylenediaminetetraacetic acid, 10% glycerol, 1% NP-40, and a cocktail of protease inhibitors). Tissue and cell debris was removed by centrifugation. The product was boiled for 5 min in 1 x SDS sample buffer (50 mM Tris-HCl pH 6.8, 12.5% glycerol, 1% sodium dodecylsulfate, 0.01% bromophenol blue) containing 50 mM DTT.

Rectum Lysate

1373 0.1 mg
EUR 229.2
Description: Rectum tissue lysate was prepared by homogenization in homogenization in lysis buffer (10 mM HEPES pH7.9, 1.5 mM MgCl2, 10 mM KCl, 1 mM ethylenediaminetetraacetic acid, 10% glycerol, 1% NP-40, and a cocktail of protease inhibitors). Tissue and cell debris was removed by centrifugation. The product was boiled for 5 min in 1 x SDS sample buffer (50 mM Tris-HCl pH 6.8, 12.5% glycerol, 1% sodium dodecylsulfate, 0.01% bromophenol blue) containing 50 mM DTT.

Skin Lysate

1376 0.1 mg
EUR 229.2
Description: Skin tissue lysate was prepared by homogenization in lysis buffer (10 mM HEPES pH7.9, 1.5 mM MgCl2, 10 mM KCl, 1 mM ethylenediaminetetraacetic acid, 10% glycerol, 1% NP-40, and a cocktail of protease inhibitors). Tissue and cell debris was removed by centrifugation. The product was boiled for 5 min in 1 x SDS sample buffer (50 mM Tris-HCl pH 6.8, 12.5% glycerol, 1% sodium dodecylsulfate, 0.01% bromophenol blue) containing 50 mM DTT.

Thyroid Lysate

1380 0.1 mg
EUR 229.2
Description: Thyroid tissue lysate was prepared by homogenization in lysis buffer (10 mM HEPES pH7.9, 1.5 mM MgCl2, 10 mM KCl, 1 mM ethylenediaminetetraacetic acid, 10% glycerol, 1% NP-40, and a cocktail of protease inhibitors). Tissue and cell debris was removed by centrifugation. The product was boiled for 5 min in 1 x SDS sample buffer (50 mM Tris-HCl pH 6.8, 12.5% glycerol, 1% sodium dodecylsulfate, 0.01% bromophenol blue) containing 50 mM DTT.

Spleen Lysate

1406 0.1 mg
EUR 229.2
Description: Spleen tissue lysate was prepared by homogenization in modified RIPA buffer (150 mM sodium chloride, 50 mM Tris-HCl, pH 7.4, 1 mM ethylenediaminetetraacetic acid, 1 mM phenylmethylsulfonyl fluoride, 1% Triton X-100, 1% sodium deoxycholic acid, 0.1% sodium dodecylsulfate, 5 μg/ml of aprotinin, 5 μg/ml of leupeptin. Tissue and cell debris was removed by centrifugation. Protein concentration was determined with Bio-Rad protein assay. The product was boiled for 5 min in 1 x SDS sample buffer (50 mM Tris-HCl pH 6.8, 12.5% glycerol, 1% sodium dodecylsulfate, 0.01% bromophenol blue) containing 50 mM DTT.

Bladder Lysate

1410 0.1 mg
EUR 229.2
Description: Bladder tissue lysate was prepared by homogenization in modified RIPA buffer (150 mM sodium chloride, 50 mM Tris-HCl, pH 7.4, 1 mM ethylenediaminetetraacetic acid, 1 mM phenylmethylsulfonyl fluoride, 1% Triton X-100, 1% sodium deoxycholic acid, 0.1% sodium dodecylsulfate, 5 μg/ml of aprotinin, 5 μg/ml of leupeptin. Tissue and cell debris was removed by centrifugation. Protein concentration was determined with Bio-Rad protein assay. The product was boiled for 5 min in 1 x SDS sample buffer (50 mM Tris-HCl pH 6.8, 12.5% glycerol, 1% sodium dodecylsulfate, 0.01% bromophenol blue) containing 50 mM DTT.

Cerebellum Lysate

1412 0.1 mg
EUR 229.2
Description: Cerebellum tissue lysate was prepared by homogenization in modified RIPA buffer (150 mM sodium chloride, 50 mM Tris-HCl, pH 7.4, 1 mM ethylenediaminetetraacetic acid, 1 mM phenylmethylsulfonyl fluoride, 1% Triton X-100, 1% sodium deoxycholic acid, 0.1% sodium dodecylsulfate, 5 μg/ml of aprotinin, 5 μg/ml of leupeptin. Tissue and cell debris was removed by centrifugation. Protein concentration was determined with Bio-Rad protein assay. The product was boiled for 5 min in 1 x SDS sample buffer (50 mM Tris-HCl pH 6.8, 12.5% glycerol, 1% sodium dodecylsulfate, 0.01% bromophenol blue) containing 50 mM DTT.

Cerebrum Lysate

1413 0.1 mg
EUR 229.2
Description: Cerebrum tissue lysate was prepared by homogenization in modified RIPA buffer (150 mM sodium chloride, 50 mM Tris-HCl, pH 7.4, 1 mM ethylenediaminetetraacetic acid, 1 mM phenylmethylsulfonyl fluoride, 1% Triton X-100, 1% sodium deoxycholic acid, 0.1% sodium dodecylsulfate, 5 μg/ml of aprotinin, 5 μg/ml of leupeptin. Tissue and cell debris was removed by centrifugation. Protein concentration was determined with Bio-Rad protein assay. The product was boiled for 5 min in 1 x SDS sample buffer (50 mM Tris-HCl pH 6.8, 12.5% glycerol, 1% sodium dodecylsulfate, 0.01% bromophenol blue) containing 50 mM DTT.

Pancreas Lysate

1414 0.1 mg
EUR 229.2
Description: Pancreas tissue lysate was prepared by homogenization in modified RIPA buffer (150 mM sodium chloride, 50 mM Tris-HCl, pH 7.4, 1 mM ethylenediaminetetraacetic acid, 1 mM phenylmethylsulfonyl fluoride, 1% Triton X-100, 1% sodium deoxycholic acid, 0.1% sodium dodecylsulfate, 5 μg/ml of aprotinin, 5 μg/ml of leupeptin. Tissue and cell debris was removed by centrifugation. Protein concentration was determined with Bio-Rad protein assay. The product was boiled for 5 min in 1 x SDS sample buffer (50 mM Tris-HCl pH 6.8, 12.5% glycerol, 1% sodium dodecylsulfate, 0.01% bromophenol blue) containing 50 mM DTT.

Stomach Lysate

1415 0.1 mg
EUR 229.2
Description: Stomach tissue lysate was prepared by homogenization in modified RIPA buffer (150 mM sodium chloride, 50 mM Tris-HCl, pH 7.4, 1 mM ethylenediaminetetraacetic acid, 1 mM phenylmethylsulfonyl fluoride, 1% Triton X-100, 1% sodium deoxycholic acid, 0.1% sodium dodecylsulfate, 5 μg/ml of aprotinin, 5 μg/ml of leupeptin. Tissue and cell debris was removed by centrifugation. Protein concentration was determined with Bio-Rad protein assay. The product was boiled for 5 min in 1 x SDS sample buffer (50 mM Tris-HCl pH 6.8, 12.5% glycerol, 1% sodium dodecylsulfate, 0.01% bromophenol blue) containing 50 mM DTT.

Testis Lysate

1416 0.1 mg
EUR 229.2
Description: Testis tissue lysate was prepared by homogenization in modified RIPA buffer (150 mM sodium chloride, 50 mM Tris-HCl, pH 7.4, 1 mM ethylenediaminetetraacetic acid, 1 mM phenylmethylsulfonyl fluoride, 1% Triton X-100, 1% sodium deoxycholic acid, 0.1% sodium dodecylsulfate, 5 μg/ml of aprotinin, 5 μg/ml of leupeptin. Tissue and cell debris was removed by centrifugation. Protein concentration was determined with Bio-Rad protein assay. The product was boiled for 5 min in 1 x SDS sample buffer (50 mM Tris-HCl pH 6.8, 12.5% glycerol, 1% sodium dodecylsulfate, 0.01% bromophenol blue) containing 50 mM DTT.

Adrenal Lysate

1417 0.1 mg
EUR 229.2
Description: Adrenal tissue lysate was prepared by homogenization in modified RIPA buffer (150 mM sodium chloride, 50 mM Tris-HCl, pH 7.4, 1 mM ethylenediaminetetraacetic acid, 1 mM phenylmethylsulfonyl fluoride, 1% Triton X-100, 1% sodium deoxycholic acid, 0.1% sodium dodecylsulfate, 5 μg/ml of aprotinin, 5 μg/ml of leupeptin. Tissue and cell debris was removed by centrifugation. Protein concentration was determined with Bio-Rad protein assay. The product was boiled for 5 min in 1 x SDS sample buffer (50 mM Tris-HCl pH 6.8, 12.5% glycerol, 1% sodium dodecylsulfate, 0.01% bromophenol blue) containing 50 mM DTT.

Skin Lysate

1419 0.1 mg
EUR 229.2
Description: Skin tissue lysate was prepared by homogenization in modified RIPA buffer (150 mM sodium chloride, 50 mM Tris-HCl, pH 7.4, 1 mM ethylenediaminetetraacetic acid, 1 mM phenylmethylsulfonyl fluoride, 1% Triton X-100, 1% sodium deoxycholic acid, 0.1% sodium dodecylsulfate, 5 μg/ml of aprotinin, 5 μg/ml of leupeptin. Tissue and cell debris was removed by centrifugation. Protein concentration was determined with Bio-Rad protein assay. The product was boiled for 5 min in 1 x SDS sample buffer (50 mM Tris-HCl pH 6.8, 12.5% glycerol, 1% sodium dodecylsulfate, 0.01% bromophenol blue) containing 50 mM DTT.

Eye Lysate

1420 0.1 mg
EUR 229.2
Description: Eye tissue lysate was prepared by homogenization in modified RIPA buffer (150 mM sodium chloride, 50 mM Tris-HCl, pH 7.4, 1 mM ethylenediaminetetraacetic acid, 1 mM phenylmethylsulfonyl fluoride, 1% Triton X-100, 1% sodium deoxycholic acid, 0.1% sodium dodecylsulfate, 5 μg/ml of aprotinin, 5 μg/ml of leupeptin. Tissue and cell debris was removed by centrifugation. Protein concentration was determined with Bio-Rad protein assay. The product was boiled for 5 min in 1 x SDS sample buffer (50 mM Tris-HCl pH 6.8, 12.5% glycerol, 1% sodium dodecylsulfate, 0.01% bromophenol blue) containing 50 mM DTT.

Trachea Lysate

1422 0.1 mg
EUR 229.2
Description: Trachea tissue lysate was prepared by homogenization in modified RIPA buffer (150 mM sodium chloride, 50 mM Tris-HCl, pH 7.4, 1 mM ethylenediaminetetraacetic acid, 1 mM phenylmethylsulfonyl fluoride, 1% Triton X-100, 1% sodium deoxycholic acid, 0.1% sodium dodecylsulfate, 5 μg/ml of aprotinin, 5 μg/ml of leupeptin. Tissue and cell debris was removed by centrifugation. Protein concentration was determined with Bio-Rad protein assay. The product was boiled for 5 min in 1 x SDS sample buffer (50 mM Tris-HCl pH 6.8, 12.5% glycerol, 1% sodium dodecylsulfate, 0.01% bromophenol blue) containing 50 mM DTT.

Lung Lysate

1462 0.1 mg
EUR 229.2
Description: Lung tissue lysate was prepared by homogenization in modified RIPA buffer (150 mM sodium chloride, 50 mM Tris-HCl, pH 7.4, 1 mM ethylenediaminetetraacetic acid, 1 mM phenylmethylsulfonyl fluoride, 1% Triton X-100, 1% sodium deoxycholic acid, 0.1% sodium dodecylsulfate, 5 μg/ml of aprotinin, 5 μg/ml of leupeptin. Tissue and cell debris was removed by centrifugation. Protein concentration was determined with Bio-Rad protein assay. The product was boiled for 5 min in 1 x SDS sample buffer (50 mM Tris-HCl pH 6.8, 12.5% glycerol, 1% sodium dodecylsulfate, 0.01% bromophenol blue) containing 50 mM DTT.

Liver Lysate

1464 0.1 mg
EUR 229.2
Description: Liver tissue lysate was prepared by homogenization in modified RIPA buffer (150 mM sodium chloride, 50 mM Tris-HCl, pH 7.4, 1 mM ethylenediaminetetraacetic acid, 1 mM phenylmethylsulfonyl fluoride, 1% Triton X-100, 1% sodium deoxycholic acid, 0.1% sodium dodecylsulfate, 5 μg/ml of aprotinin, 5 μg/ml of leupeptin. Tissue and cell debris was removed by centrifugation. Protein concentration was determined with Bio-Rad protein assay. The product was boiled for 5 min in 1 x SDS sample buffer (50 mM Tris-HCl pH 6.8, 12.5% glycerol, 1% sodium dodecylsulfate, 0.01% bromophenol blue) containing 50 mM DTT.

Kidney Lysate

1465 0.1 mg
EUR 229.2
Description: Kidney tissue lysate was prepared by homogenization in modified RIPA buffer (150 mM sodium chloride, 50 mM Tris-HCl, pH 7.4, 1 mM ethylenediaminetetraacetic acid, 1 mM phenylmethylsulfonyl fluoride, 1% Triton X-100, 1% sodium deoxycholic acid, 0.1% sodium dodecylsulfate, 5 μg/ml of aprotinin, 5 μg/ml of leupeptin. Tissue and cell debris was removed by centrifugation. Protein concentration was determined with Bio-Rad protein assay. The product was boiled for 5 min in 1 x SDS sample buffer (50 mM Tris-HCl pH 6.8, 12.5% glycerol, 1% sodium dodecylsulfate, 0.01% bromophenol blue) containing 50 mM DTT.

Spleen Lysate

1466 0.1 mg
EUR 229.2
Description: Spleen tissue lysate was prepared by homogenization in modified RIPA buffer (150 mM sodium chloride, 50 mM Tris-HCl, pH 7.4, 1 mM ethylenediaminetetraacetic acid, 1 mM phenylmethylsulfonyl fluoride, 1% Triton X-100, 1% sodium deoxycholic acid, 0.1% sodium dodecylsulfate, 5 μg/ml of aprotinin, 5 μg/ml of leupeptin. Tissue and cell debris was removed by centrifugation. Protein concentration was determined with Bio-Rad protein assay. The product was boiled for 5 min in 1 x SDS sample buffer (50 mM Tris-HCl pH 6.8, 12.5% glycerol, 1% sodium dodecylsulfate, 0.01% bromophenol blue) containing 50 mM DTT.

L1210 Lysate

1284 0.1 mg
EUR 229.2
Description: L1210 lysate was prepared by homogenization in modified RIPA buffer (150 mM sodium chloride, 50 mM Tris-HCl, pH 7.4, 1 mM ethylenediaminetetraacetic acid, 1 mM phenylmethylsulfonyl fluoride, 1% Triton X-100, 1% sodium deoxycholic acid, 0.1% sodium dodecylsulfate, 5 μg/ml of aprotinin, 5 μg/ml of leupeptin. Cell debris was removed by centrifugation. Protein concentration was determined with Bio-Rad protein assay. The L1210 lysate was boiled for 5 min in 1 x SDS sample buffer (50 mM Tris-HCl pH 6.8, 12.5% glycerol, 1% sodium dodecylsulfate, 0.01% bromophenol blue) containing 50 mM DTT.

C2C12 Lysate

1285 0.1 mg
EUR 229.2
Description: C2C12 lysate was prepared by homogenization in modified RIPA buffer (150 mM sodium chloride, 50 mM Tris-HCl, pH 7.4, 1 mM ethylenediaminetetraacetic acid, 1 mM phenylmethylsulfonyl fluoride, 1% Triton X-100, 1% sodium deoxycholic acid, 0.1% sodium dodecylsulfate, 5 μg/ml of aprotinin, 5 μg/ml of leupeptin. Cell debris was removed by centrifugation. Protein concentration was determined with Bio-Rad protein assay. The C2C12 lysate was boiled for 5 min in 1 x SDS sample buffer (50 mM Tris-HCl pH 6.8, 12.5% glycerol, 1% sodium dodecylsulfate, 0.01% bromophenol blue) containing 50 mM DTT.

P815 Lysate

1286 0.1 mg
EUR 229.2
Description: P815 lysate was prepared by homogenization in modified RIPA buffer (150 mM sodium chloride, 50 mM Tris-HCl, pH 7.4, 1 mM ethylenediaminetetraacetic acid, 1 mM phenylmethylsulfonyl fluoride, 1% Triton X-100, 1% sodium deoxycholic acid, 0.1% sodium dodecylsulfate, 5 μg/ml of aprotinin, 5 μg/ml of leupeptin. Cell debris was removed by centrifugation. Protein concentration was determined with Bio-Rad protein assay. The P815 lysate was boiled for 5 min in 1 x SDS sample buffer (50 mM Tris-HCl pH 6.8, 12.5% glycerol, 1% sodium dodecylsulfate, 0.01% bromophenol blue) containing 50 mM DTT.

EL4 Lysate

1287 0.1 mg
EUR 229.2
Description: EL4 lysate was prepared by homogenization in modified RIPA buffer (150 mM sodium chloride, 50 mM Tris-HCl, pH 7.4, 1 mM ethylenediaminetetraacetic acid, 1 mM phenylmethylsulfonyl fluoride, 1% Triton X-100, 1% sodium deoxycholic acid, 0.1% sodium dodecylsulfate, 5 μg/ml of aprotinin, 5 μg/ml of leupeptin. Cell debris was removed by centrifugation. Protein concentration was determined with Bio-Rad protein assay. The EL4 lysate was boiled for 5 min in 1 x SDS sample buffer (50 mM Tris-HCl pH 6.8, 12.5% glycerol, 1% sodium dodecylsulfate, 0.01% bromophenol blue) containing 50 mM DTT.

Lung Lysate

1302 0.1 mg
EUR 229.2
Description: Lung tissue lysate was prepared by homogenization in modified RIPA buffer (150 mM sodium chloride, 50 mM Tris-HCl, pH 7.4, 1 mM ethylenediaminetetraacetic acid, 1 mM phenylmethylsulfonyl fluoride, 1% Triton X-100, 1% sodium deoxycholic acid, 0.1% sodium dodecylsulfate, 5 μg/ml of aprotinin, 5 μg/ml of leupeptin. Tissue and cell debris was removed by centrifugation. Protein concentration was determined with Bio-Rad protein assay. The product was boiled for 5 min in 1 x SDS sample buffer (50 mM Tris-HCl pH 6.8, 12.5% glycerol, 1% sodium dodecylsulfate, 0.01% bromophenol blue) containing 50 mM DTT.

Spleen Lysate

1306 0.1 mg
EUR 229.2
Description: Spleen tissue lysate was prepared by homogenization in modified RIPA buffer (150 mM sodium chloride, 50 mM Tris-HCl, pH 7.4, 1 mM ethylenediaminetetraacetic acid, 1 mM phenylmethylsulfonyl fluoride, 1% Triton X-100, 1% sodium deoxycholic acid, 0.1% sodium dodecylsulfate, 5 μg/ml of aprotinin, 5 μg/ml of leupeptin. Tissue and cell debris was removed by centrifugation. Protein concentration was determined with Bio-Rad protein assay. The product was boiled for 5 min in 1 x SDS sample buffer (50 mM Tris-HCl pH 6.8, 12.5% glycerol, 1% sodium dodecylsulfate, 0.01% bromophenol blue) containing 50 mM DTT.

Placenta Lysate

1309 0.1 mg
EUR 229.2
Description: Placenta tissue lysate was prepared by homogenization in lysis buffer (10 mM HEPES pH7.9, 1.5 mM MgCl2, 10 mM KCl, 1 mM ethylenediaminetetraacetic acid, 10% glycerol, 1% NP-40, and a cocktail of protease inhibitors). Tissue and cell debris was removed by centrifugation. Protein concentration was determined with Bio-Rad protein assay. The product was boiled for 5 min in 1 x SDS sample buffer (50 mM Tris-HCl pH 6.8, 12.5% glycerol, 1% sodium dodecylsulfate, 0.01% bromophenol blue) containing 50 mM DTT.

Melanoma Lysate

20-101 0.1 mg
EUR 632.4
Description: Melanoma lysate was prepared by homogenization using a proprietary technique. The tissue was frozen in liquid nitrogen immediately after excision and then stored at -70°C. The human melanoma tissue total protein is provided in a buffer including HEPES (pH7.9), MgCl2, KCl, EDTA, Sucrose, Glycerol, Sodium deoxycholate, NP-40, and a cocktail of protease inhibitors. For quality control purposes, the melanoma tissue pattern on SDS-PAGE gel is shown to be consistent for each lot by visualization with coomassie blue staining. The melanoma tissue is then Western analyzed by either GAPDH or β-actin antibody, and the expression level is consistent with each lot.

Trachea Lysate

20-102 0.1 mg
EUR 500.1
Description: Human trachea lysate was prepared by homogenization using a proprietary technique. The tissue was frozen in liquid nitrogen immediately after excision and then stored at -70°C. The human trachea tissue total protein is provided in a buffer including HEPES (pH7.9), MgCl2, KCl, EDTA, Sucrose, Glycerol, Sodium deoxycholate, NP-40, and a cocktail of protease inhibitors. For quality control purposes, the trachea tissue pattern on SDS-PAGE gel is shown to be consistent for each lot by visualization with coomassie blue staining. The trachea tissue is then Western analyzed by either GAPDH or β-actin antibody, and the expression level is consistent with each lot.

Jurkat Lysate

1205 0.1 mg
EUR 229.2
Description: Jurkat lysate was prepared by homogenization in modified RIPA buffer (150 mM sodium chloride, 50 mM Tris-HCl, pH 7.4, 1 mM ethylenediaminetetraacetic acid, 1 mM phenylmethylsulfonyl fluoride, 1% Triton X-100, 1% sodium deoxycholic acid, 0.1% sodium dodecylsulfate, 5 μg/ml of aprotinin, 5 μg/ml of leupeptin. Cell debris was removed by centrifugation. Protein concentration was determined with Bio-Rad protein assay. The Jurkat lysate was boiled for 5 min in 1 x SDS sample buffer (50 mM Tris-HCl pH 6.8, 12.5% glycerol, 1% sodium dodecylsulfate, 0.01% bromophenol blue) containing 50 mM DTT.

MOLT4 Lysate

1206 0.1 mg
EUR 229.2
Description: MOLT4 lysate was prepared by homogenization in modified RIPA buffer (150 mM sodium chloride, 50 mM Tris-HCl, pH 7.4, 1 mM ethylenediaminetetraacetic acid, 1 mM phenylmethylsulfonyl fluoride, 1% Triton X-100, 1% sodium deoxycholic acid, 0.1% sodium dodecylsulfate, 5 μg/ml of aprotinin, 5 μg/ml of leupeptin. Cell debris was removed by centrifugation. Protein concentration was determined with Bio-Rad protein assay. The MOLT4 lysate was boiled for 5 min in 1 x SDS sample buffer (50 mM Tris-HCl pH 6.8, 12.5% glycerol, 1% sodium dodecylsulfate, 0.01% bromophenol blue) containing 50 mM DTT.

HL60 Lysate

1209 0.1 mg
EUR 229.2
Description: HL60 lysate was prepared by homogenization in modified RIPA buffer (150 mM sodium chloride, 50 mM Tris-HCl, pH 7.4, 1 mM ethylenediaminetetraacetic acid, 1 mM phenylmethylsulfonyl fluoride, 1% Triton X-100, 1% sodium deoxycholic acid, 0.1% sodium dodecylsulfate, 5 μg/ml of aprotinin, 5 μg/ml of leupeptin. Cell debris was removed by centrifugation. Protein concentration was determined with Bio-Rad protein assay. The HL60 lysate was boiled for 5 min in 1 x SDS sample buffer (50 mM Tris-HCl pH 6.8, 12.5% glycerol, 1% sodium dodecylsulfate, 0.01% bromophenol blue) containing 50 mM DTT.

T24 Lysate

1213 0.1 mg
EUR 229.2
Description: T24 lysate was prepared by homogenization in modified RIPA buffer (150 mM sodium chloride, 50 mM Tris-HCl, pH 7.4, 1 mM ethylenediaminetetraacetic acid, 1 mM phenylmethylsulfonyl fluoride, 1% Triton X-100, 1% sodium deoxycholic acid, 0.1% sodium dodecylsulfate, 5 μg/ml of aprotinin, 5 μg/ml of leupeptin. Cell debris was removed by centrifugation. Protein concentration was determined with Bio-Rad protein assay. The T24 lysate was boiled for 5 min in 1 x SDS sample buffer (50 mM Tris-HCl pH 6.8, 12.5% glycerol, 1% sodium dodecylsulfate, 0.01% bromophenol blue) containing 50 mM DTT.

U937 Lysate

1215 0.1 mg
EUR 229.2
Description: U937 lysate was prepared by homogenization in modified RIPA buffer (150 mM sodium chloride, 50 mM Tris-HCl, pH 7.4, 1 mM ethylenediaminetetraacetic acid, 1 mM phenylmethylsulfonyl fluoride, 1% Triton X-100, 1% sodium deoxycholic acid, 0.1% sodium dodecylsulfate, 5 μg/ml of aprotinin, 5 μg/ml of leupeptin. Cell debris was removed by centrifugation. Protein concentration was determined with Bio-Rad protein assay. The U937 lysate was boiled for 5 min in 1 x SDS sample buffer (50 mM Tris-HCl pH 6.8, 12.5% glycerol, 1% sodium dodecylsulfate, 0.01% bromophenol blue) containing 50 mM DTT.

MCF7 Lysate

1219 0.1 mg
EUR 229.2
Description: MCF7 lysate was prepared by homogenization in modified RIPA buffer (150 mM sodium chloride, 50 mM Tris-HCl, pH 7.4, 1 mM ethylenediaminetetraacetic acid, 1 mM phenylmethylsulfonyl fluoride, 1% Triton X-100, 1% sodium deoxycholic acid, 0.1% sodium dodecylsulfate, 5 μg/ml of aprotinin, 5 μg/ml of leupeptin. Cell debris was removed by centrifugation. Protein concentration was determined with Bio-Rad protein assay. The MCF7 lysate was boiled for 5 min in 1 x SDS sample buffer (50 mM Tris-HCl pH 6.8, 12.5% glycerol, 1% sodium dodecylsulfate, 0.01% bromophenol blue) containing 50 mM DTT.

Ramos Lysate

1225 0.1 mg
EUR 229.2
Description: Ramos lysate was prepared by homogenization in modified RIPA buffer (150 mM sodium chloride, 50 mM Tris-HCl, pH 7.4, 1 mM ethylenediaminetetraacetic acid, 1 mM phenylmethylsulfonyl fluoride, 1% Triton X-100, 1% sodium deoxycholic acid, 0.1% sodium dodecylsulfate, 5 μg/ml of aprotinin, 5 μg/ml of leupeptin. Cell debris was removed by centrifugation. Protein concentration was determined with Bio-Rad protein assay. The Ramos lysate was boiled for 5 min in 1 x SDS sample buffer (50 mM Tris-HCl pH 6.8, 12.5% glycerol, 1% sodium dodecylsulfate, 0.01% bromophenol blue) containing 50 mM DTT.

Kidney Lysate

21-104 0.1 mg
EUR 342.6
Description: Bovine kidney tissue lysate was prepared by homogenization using a proprietary technique. The tissue was frozen in liquid nitrogen immediately after excision and then stored at -70°C. The bovine kidney tissue total protein is provided in a buffer including HEPES (pH 7.9), MgCl2, KCl, EDTA, Sucrose, Glycerol, Sodium deoxycholate, NP-40, and a cocktail of protease inhibitors. For quality control purposes, the kidney tissue pattern on SDS-PAGE gel is shown to be consistent for each lot by visualization with coomassie blue staining. The kidney tissue is then Western analyzed by either GAPDH or β-actin antibody, and the expression level is consistent with each lot.

Liver Lysate

21-105 0.1 mg
EUR 342.6
Description: Bovine liver tissue lysate was prepared by homogenization using a proprietary technique. The tissue was frozen in liquid nitrogen immediately after excision and then stored at -70°C. The bovine liver tissue total protein is provided in a buffer including HEPES (pH 7.9), MgCl2, KCl, EDTA, Sucrose, Glycerol, Sodium deoxycholate, NP-40, and a cocktail of protease inhibitors. For quality control purposes, the liver tissue pattern on SDS-PAGE gel is shown to be consistent for each lot by visualization with coomassie blue staining. The liver tissue is then Western analyzed by either GAPDH or β-actin antibody, and the expression level is consistent with each lot.

Heart Lysate

21-115 0.1 mg
EUR 342.6
Description: Guinea Pig heart tissue lysate was prepared by homogenization using a proprietary technique. The tissue was frozen in liquid nitrogen immediately after excision and then stored at -70°C. The guinea pig heart tissue total protein is provided in a buffer including HEPES (pH 7.9), MgCl2, KCl, EDTA, Sucrose, Glycerol, Sodium deoxycholate, NP-40, and a cocktail of protease inhibitors. For quality control purposes, the heart tissue pattern on SDS-PAGE gel is shown to be consistent for each lot by visualization with coomassie blue staining. The heart tissue is then Western analyzed by either GAPDH or β-actin antibody, and the expression level is consistent with each lot.

Kidney Lysate

21-116 0.1 mg
EUR 342.6
Description: Guinea Pig kidney tissue lysate was prepared by homogenization using a proprietary technique. The tissue was frozen in liquid nitrogen immediately after excision and then stored at -70°C. The guinea pig kidney tissue total protein is provided in a buffer including HEPES (pH 7.9), MgCl2, KCl, EDTA, Sucrose, Glycerol, Sodium deoxycholate, NP-40, and a cocktail of protease inhibitors. For quality control purposes, the kidney tissue pattern on SDS-PAGE gel is shown to be consistent for each lot by visualization with coomassie blue staining. The kidney tissue is then Western analyzed by either GAPDH or β-actin antibody, and the expression level is consistent with each lot.

Adrenal Lysate

21-160 0.1 mg
EUR 468.6
Description: Monkey (Cynomolgus) adrenal tissue lysate was prepared by homogenization using a proprietary technique. The tissue was frozen in liquid nitrogen immediately after excision and then stored at -70°C. The monkey (Cynomolgus) adrenal tissue total protein is provided in a buffer including HEPES (pH 7.9), MgCl2, KCl, EDTA, Sucrose, Glycerol, Sodium deoxycholate, NP-40, and a cocktail of protease inhibitors. For quality control purposes, the adrenal tissue pattern on SDS-PAGE gel is shown to be consistent for each lot by visualization with coomassie blue staining. The adrenal tissue is then Western analyzed by either GAPDH or β-actin antibody, and the expression level is consistent with each lot.

Colon Lysate

21-179 0.1 mg
EUR 342.6
Description: Monkey (Cynomolgus) colon tissue lysate was prepared by homogenization using a proprietary technique. The tissue was frozen in liquid nitrogen immediately after excision and then stored at -70°C. The monkey (Cynomolgus) colon tissue total protein is provided in a buffer including HEPES (pH 7.9), MgCl2, KCl, EDTA, Sucrose, Glycerol, Sodium deoxycholate, NP-40, and a cocktail of protease inhibitors. For quality control purposes, the colon tissue pattern on SDS-PAGE gel is shown to be consistent for each lot by visualization with coomassie blue staining. The colon tissue is then Western analyzed by either GAPDH or β-actin antibody, and the expression level is consistent with each lot.

Gallbladder Lysate

21-188 0.1 mg
EUR 468.6
Description: Monkey (Cynomolgus) gallbladder tissue lysate was prepared by homogenization using a proprietary technique. The tissue was frozen in liquid nitrogen immediately after excision and then stored at -70°C. The monkey (Cynomolgus) gallbladder tissue total protein is provided in a buffer including HEPES (pH 7.9), MgCl2, KCl, EDTA, Sucrose, Glycerol, Sodium deoxycholate, NP-40, and a cocktail of protease inhibitors. For quality control purposes, the gallbladder tissue pattern on SDS-PAGE gel is shown to be consistent for each lot by visualization with coomassie blue staining. The gallbladder tissue is then Western analyzed by either GAPDH or β-actin antibody, and the expression level is consistent with each lot.

Kidney Lysate

21-190 0.1 mg
EUR 342.6
Description: Monkey (Cynomolgus) kidney tissue lysate was prepared by homogenization using a proprietary technique. The tissue was frozen in liquid nitrogen immediately after excision and then stored at -70°C. The monkey (Cynomolgus) kidney tissue total protein is provided in a buffer including HEPES (pH 7.9), MgCl2, KCl, EDTA, Sucrose, Glycerol, Sodium deoxycholate, NP-40, and a cocktail of protease inhibitors. For quality control purposes, the kidney tissue pattern on SDS-PAGE gel is shown to be consistent for each lot by visualization with coomassie blue staining. The kidney tissue is then Western analyzed by either GAPDH or β-actin antibody, and the expression level is consistent with each lot.

Lung Lysate

21-194 0.1 mg
EUR 342.6
Description: Monkey (Cynomolgus) lung tissue lysate was prepared by homogenization using a proprietary technique. The tissue was frozen in liquid nitrogen immediately after excision and then stored at -70°C. The monkey (Cynomolgus) lung tissue total protein is provided in a buffer including HEPES (pH 7.9), MgCl2, KCl, EDTA, Sucrose, Glycerol, Sodium deoxycholate, NP-40, and a cocktail of protease inhibitors. For quality control purposes, the lung tissue pattern on SDS-PAGE gel is shown to be consistent for each lot by visualization with coomassie blue staining. The lung tissue is then Western analyzed by either GAPDH or β-actin antibody, and the expression level is consistent with each lot.

Skin Lysate

21-204 0.1 mg
EUR 468.6
Description: Monkey (Cynomolgus) skin tissue lysate was prepared by homogenization using a proprietary technique. The tissue was frozen in liquid nitrogen immediately after excision and then stored at -70°C. The monkey (Cynomolgus) skin tissue total protein is provided in a buffer including HEPES (pH 7.9), MgCl2, KCl, EDTA, Sucrose, Glycerol, Sodium deoxycholate, NP-40, and a cocktail of protease inhibitors. For quality control purposes, the skin tissue pattern on SDS-PAGE gel is shown to be consistent for each lot by visualization with coomassie blue staining. The skin tissue is then Western analyzed by either GAPDH or β-actin antibody, and the expression level is consistent with each lot.

Spleen Lysate

21-209 0.1 mg
EUR 342.6
Description: Monkey (Cynomolgus) spleen tissue lysate was prepared by homogenization using a proprietary technique. The tissue was frozen in liquid nitrogen immediately after excision and then stored at -70°C. The monkey (Cynomolgus) spleen tissue total protein is provided in a buffer including HEPES (pH 7.9), MgCl2, KCl, EDTA, Sucrose, Glycerol, Sodium deoxycholate, NP-40, and a cocktail of protease inhibitors. For quality control purposes, the spleen tissue pattern on SDS-PAGE gel is shown to be consistent for each lot by visualization with coomassie blue staining. The spleen tissue is then Western analyzed by either GAPDH or β-actin antibody, and the expression level is consistent with each lot.

Brain Lysate

21-272 0.1 mg
EUR 342.6
Description: Monkey (Rhesus) brain tissue lysate was prepared by homogenization using a proprietary technique. The tissue was frozen in liquid nitrogen immediately after excision and then stored at -70°C. The monkey (Rhesus) brain tissue total protein is provided in a buffer including HEPES (pH 7.9), MgCl2, KCl, EDTA, Sucrose, Glycerol, Sodium deoxycholate, NP-40, and a cocktail of protease inhibitors. For quality control purposes, the brain tissue pattern on SDS-PAGE gel is shown to be consistent for each lot by visualization with coomassie blue staining. The brain tissue is then Western analyzed by either GAPDH or β-actin antibody, and the expression level is consistent with each lot.

Colon Lysate

21-288 0.1 mg
EUR 342.6
Description: Monkey (Rhesus) colon tissue lysate was prepared by homogenization using a proprietary technique. The tissue was frozen in liquid nitrogen immediately after excision and then stored at -70°C. The monkey (Rhesus) colon tissue total protein is provided in a buffer including HEPES (pH 7.9), MgCl2, KCl, EDTA, Sucrose, Glycerol, Sodium deoxycholate, NP-40, and a cocktail of protease inhibitors. For quality control purposes, the colon tissue pattern on SDS-PAGE gel is shown to be consistent for each lot by visualization with coomassie blue staining. The colon tissue is then Western analyzed by either GAPDH or β-actin antibody, and the expression level is consistent with each lot.

RBDv1 contained a local viral sign peptide, RBDv2 -human tPA sign peptide. We transfected a CHO DG44 cell line, chosen stably transfected cells, and carried out just a few rounds of methotrexate-driven amplification of the genetic cassette within the genome. For the RBDv2 variant, a high-yield clonal producer cell line was obtained. Purified proteins had been analyzed by polyacrylamide gel electrophoresis in lowering and non-reducing situations and gel filtration; for RBDv2 protein, the monomeric type content material exceeded 90% for a number of sequence. Deglycosylation with PNGase F and mass spectrometry confirmed the presence of N-glycosylation.

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