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Manufactured by BioVendor

Glutathione S-transferase kappa 1 Human E. coli

  • Regulatory status:RUO
  • Type:Recombinant protein
  • Source:E. coli
  • Other names:Disulfide-bond A oxidoreductase-like protein, glutathione S-transferase kappa 1, GSTK1, glutathione S-transferases, GST,
  • Species:Human
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Cat. No. Size Price

RD172357100 0.1 mg
PubMed Product Details
Technical Data


Recombinant protein


Total 235 AA. MW: 26.6 kDa (calculated). UniProtKB Q9Y2Q3 (Gly2-Leu226). N-terminal his-tag (10 extra AA). Protein identity confirmed by LC-MS/MS.

Amino Acid Sequence



E. coli


Purity as determined by densitometric image analysis: >95 %


14 % SDS-PAGE separation of Human DsbA-L:
1. M.W. marker – 14, 21, 31, 45, 66, 97 kDa
2. Reduced and boiled sample, 2.5 μg/lane
3. Non-reduced and non-boiled sample, 2.5 μg/lane


< 1.0 EU/μg


Filtered (0.4 μm) and lyophilized in phosphate buffered saline pH 7.0 + 5%(w/v) trehalose.


Add deionized water to prepare a working stock solution of approximately 0.5 mg/ml and let the lyophilized pellet dissolve completely. Filter sterilize your culture media/working solutions containing this non-sterile product before using in cell culture.


Western blotting, ELISA


At ambient temperature. Upon receipt, store the product at the temperature recommended below.


Store the lyophilized protein at –80 °C. Lyophilized protein remains stable until the expiry date when stored at –80 °C. Aliquot reconstituted protein to avoid repeated freezing/thawing cycles and store at –80 °C for long term storage. Reconstituted protein can be stored at 4 °C for a week.

Quality Control Test

BCA to determine quantity of the protein.

SDS PAGE to determine purity of the protein.

LAL to determine quantity of endotoxin.


This product is intended for research use only.


Research topic

Diabetology - Other Relevant Products, Energy metabolism and body weight regulation


Disulfide-bond A oxidoreductase-like protein (DsbA-L) is the enzyme, which used to be called glutathione S-transferase kappa 1 (GSTK1) in humans and belongs to superfamily of enzymes glutathione S-transferases (GST), which are mainly known for cellular detoxification. GSTK1 enzyme is a homodimer, molecular weight of each subunit being 27 kDa, and shares high sequence and secondary structure homology with bacterial DsbA. Based on this finding, the enzyme GSTK1 was renamed to DsbA-L.
Bacterial DsbA catalyzes disulfide bond formation during folding of secreted proteins and therefore DsbA-L might also have the ability to catalyze disulfide bond formation during protein assembling. DsbA-L is expressed in a number of mouse tissues such as liver, kidney, pancreas, heart and lung; the highest DsbA-L expression was observed in the adipose tissue. It has been shown that DsbA-L expression in adipocytes is negatively correlated with obesity in mice and humans. DsbA-L in adipocytes plays a critical role in regulation of adiponectin secretion and multimerization to form high molecular weight (HMW) complex. This HMW form of adiponectin is the active form of the hormone and has a relevant role in enhancing insulin sensitivity and in protecting against diabetes. Impairment in adiponectin multimerization leads to defects in adiponectin secretion and function and is associated with diabetes. These findings suggest that increasing the ratio of the HMW form rather than the total levels of adiponectin might provide an effective alternative therapeutic strategy.
Transgenic mice overexpressing DsbA-L in fat exhibited increased levels of total and HMW adiponectin compared with wild type mice. These mice also displayed suppression of diet-induced obesity, insulin resistance and hepatic steatosis compared with wild type mice; thus, upregulation of DsbA-L may be a new therapeutic approach to treatment of obesity and associated metabolic disorders.
Originally, DsbA-L was identified as a mitochondrial enzyme but recent investigation provides evidence that DsbA-L is also localized in endoplasmic reticulum (ER). In obesity, increased demands on ER function (protein folding) lead to ER stress which in turn downregulates cellular levels and secretion of adiponectin in 3T3-L1 adipocytes. Experiments with 3T3-L1 adipocytes have shown that DsbA-L localization in ER is critical for its promoting effect on adiponectin biosynthesis in adipocytes and for suppressing the negative effects of ER stress.

Summary References (8)

References to DsbA-L

  • Thomson RE, Bigley AL, Foster JR, Jowsey IR, Elcombe CR, Orton TC, Hayes JD: Tissue-specific expression and subcellular distribution of murine glutathione S-transferase class kappa. J Histochem Cytochem, 2004, 52(5):653-662
  • Liu M, Zhou L, Xu A, Lam KSL, Wetzel MD, Xiang R, Zhang J, Xin X, Dong LQ, Liu F: A disulfide-bond A oxidoreductase-like protein (DsbA-L) regulates adiponectin multimerization. PNAS 2008, 105(47):18302-18307
  • Gao F, Fang Q, Zhang R, Lu J, Lu H, Wang C, Ma X, Xu J, Jia W, Xiang K: Polymorphism of DsbA-L gene associates with insulin secretion and body fat distribution in Chinese population. Endocrine J 2009, 56(3):487:494
  • Shield AJ, Murray TP, Cappello JY, Coggan M, Board PG: Polymorphisms in the human glutathione transferase kappa (GSTK1) promoter alter gene expression. Genomics 2010, 95:299-305
  • Zhou L, Liu M, Zhang J, Chen H, Dong LQ, Liu F: DsbA-L alleviates endoplasmic reticulum stress-induced adiponectin downregulation. Diabetes 2010, 59:2809:2816
  • Blackburn AC, Coggan M, Shield AJ, Cappello J, Theodoratos A, Murray TP, Rooke M, Larter CZ, Koina ME, Dahlstrom JE, Matthaei KI, Board PG: Glutathione transferase kappa deficiency causes glomerular nephropathy without overt oxidative stress. Lab Investigation 2011, 91:1572-1583
  • Liu M, Xiang R, Wilk SA, Zhang N, Sloane LB, Azarnoush K, Zhou L, Chen H, Xiang G, Walter CA, Austad SN, Musi N, DeFronzo RA, Asmis R, Scherer PE, Dong LQ, Liu F: Fat-specific DsbA-L overexpression promotes adiponectin multimerization and protects mice from diet-induced obesity and insulin resistance. Diabetes 2012, 61:2776:2786
  • Liu M, Chen H, Wei L, Hu D, Dong K, Jia W, Dong LQ, Liu F: ER localization is critical for DsbA-L to suppress ER stress and adiponectin down-regulation in adipocytes. J Biol Chem 2015, 290(16): 10143–10148
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