Recombinant Human Glutathione S-Transferase Kappa 1 (GSTK1) Protein (GST), Active

Beta LifeScience SKU/CAT #: BLC-05650P
Greater than 90% as determined by SDS-PAGE.
Greater than 90% as determined by SDS-PAGE.
Activity Measured by its binding ability in a functional ELISA. Immobilized HTR1B at 5 μg/ml can bind human GSTK1, the EC 50 of human GSTK1 protein is 159.40-218.50 ng/ml.
Activity Measured by its binding ability in a functional ELISA. Immobilized HTR1B at 5 μg/ml can bind human GSTK1, the EC 50 of human GSTK1 protein is 159.40-218.50 ng/ml.

Recombinant Human Glutathione S-Transferase Kappa 1 (GSTK1) Protein (GST), Active

Beta LifeScience SKU/CAT #: BLC-05650P
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Product Overview

Description Recombinant Human Glutathione S-Transferase Kappa 1 (GSTK1) Protein (GST), Active is produced by our E.coli expression system. This is a protein fragment.
Purity Greater than 90% as determined by SDS-PAGE.
Activity Measured by its binding ability in a functional ELISA. Immobilized HTR1B at 5 μg/ml can bind human GSTK1, the EC50 of human GSTK1 protein is 159.40-218.50 ng/ml.
Uniprotkb Q9Y2Q3
Target Symbol GSTK1
Synonyms EC 2.5.1.18; Glutathione S Transferase kappa 1; Glutathione S transferase subunit 13; Glutathione S-transferase k1; Glutathione S-transferase kappa 1; Glutathione S-transferase subunit 13; Glutathione S-transferase subunit 13 homolog; GST 13 13; GST 13-13; GST; GST class kappa; GST class-kappa; GST13; GST13-13; GSTK1 1; Gstk1; GSTK1-1; GSTK1_HUMAN; hGSTK1
Species Homo sapiens (Human)
Expression System E.coli
Tag N-GST
Target Protein Sequence GPLPRTVELFYDVLSPYSWLGFEILCRYQNIWNINLQLRPSLITGIMKDSGNKPPGLLPRKGLYMANDLKLLRHHLQIPIHFPKDFLSVMLEKGSLSAMRFLTAVNLEHPEMLEKASRELWMRVWSRNEDITEPQSILAAAEKAGMSAEQAQGLLEKIATPKVKNQLKETTEAACRYGAFGLPITVAHVDGQTHMLFGSDRMELLAHLLGEKWMGPIPPAVNARL
Expression Range 2-226aa
Protein Length Partial
Mol. Weight 52.4kDa
Research Area Tags & Cell Markers
Form Liquid or Lyophilized powder
Buffer Liquid form: default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol. Lyophilized powder form: the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, pH 8.0.
Reconstitution Briefly centrifuged the vial prior to opening to bring the contents to the bottom. Reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL. It is recommended to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20°C/-80°C. The default final concentration of glycerol is 50%.
Storage 1. Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. 2. Avoid repeated freeze-thaw cycles. 3. Store working aliquots at 4°C for up to one week. 4. In general, protein in liquid form is stable for up to 6 months at -20°C/-80°C. Protein in lyophilized powder form is stable for up to 12 months at -20°C/-80°C.
Notes Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.

Target Details

Target Function Significant glutathione conjugating activity is found only with the model substrate, 1-chloro-2,4-dinitrobenzene (CDNB).
Subcellular Location Peroxisome.
Protein Families GST superfamily, Kappa family
Database References
Tissue Specificity Ubiquitous.

Gene Functions References

  1. Several biological properties of the GST-hNdCTR1 fusion protein were assessed. It was demonstrated that in cells, the protein was prone to oligomerization, formed inclusion bodies and displayed no toxicity. Treatment of E. coli cells with copper and silver ions reduced cell viability in a dose- and time-dependent manner PMID: 29099786
  2. we confirmed several existing chemoinformatic filters and more importantly extended them as well as added novel filters that specify compounds with anti-GST/GSH activity. Selected compounds were also tested using different antibody-based GST detection technologies and exhibited no interference clearly demonstrating specificity toward their GST/GSH interaction. PMID: 27044684
  3. Our findings indicate that the medical staff exposed to low IR levels were under risk of significant oxidative stress that was enhanced by their glutathione S-transferase (GST) polymorphisms. PMID: 28287017
  4. GSTK1 T/T genotype may be a novel risk factor for the prediction of overweight status in SCZ male patients. PMID: 27010189
  5. High glutathione-S-transferase is associated with type 2 diabetes mellitus. PMID: 27377684
  6. DsbA-L is localized in both the mitochondria and the endoplasmic reticulum (ER) in adipocytes; its ER localization plays a critical role in suppressing ER stress and promoting adiponectin biosynthesis and secretion. PMID: 25739441
  7. we have optimized the GST-Nck1-SH2 pull-down procedure to obtain tyrosine-phosphorylated proteins in tumor tissues PMID: 23426619
  8. drug resistance in three strains of tumor cells is associated with significant increase in hGSTP1 and hGSTA4 gene expression, whereas increased hGSTK1 gene expression was detected only in resistant erythroleukemia and mammary adenocarcinoma cells. PMID: 23330092
  9. This study does not give evidence of interaction between the GST polymorphisms and smoking may although this study provided sufficient statistical power to detect modest interaction. PMID: 20472488
  10. SNP-1308G/T (rs1917760) genotypes of DsbA-L gene might participate in insulin secretion and body fat distribution. It is possible that polymorphisms of DsbA-L gene associated with metabolic diseases[DsbA-L] PMID: 19225211
  11. structure and function characterization of a GST from human breast PMID: 14709161
  12. Gene and protein characterization; its subcellular localization in peroxisomes, suggesting a new function for this family of enzymes [glutathione S-transferase kappa (hGSTK1)] PMID: 14742434
  13. crystal structure of hGSTK1 has been determined by the multiple-isomorphous replacement method and refined to 1.93 A resolution PMID: 16081649
  14. Our results suggest that genetic polymorphisms of xenobiotic-metabolizing enzymes could play an important role in infertility. PMID: 18774560
  15. The objective of this study was to investigate the molecular mechanisms underlying Group B Streptococcus-human umbilical vein endothelial cells interaction, focusing specifically on the responsiveness of host protein tyrosine kinase (PTK). PMID: 19639233
  16. Observational study of gene-disease association. (HuGE Navigator) PMID: 19225211
  17. Observational study of gene-disease association. (HuGE Navigator) PMID: 17601350
  18. Presence of hGSTK1 in both peroxisomes and mitochondria. The C-terminus of hGSTK1 is essential for localization of the protein to peroxisomes, and the C-terminal sequence Ala-Arg-Leu represents a peroxisome targeting signal 1 (PTS1). PMID: 14742434

FAQs

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Proteins are sensitive to heat, and freeze-drying can preserve the activity of the majority of proteins. It improves protein stability, extends storage time, and reduces shipping costs. However, freeze-drying can also lead to the loss of the active portion of the protein and cause aggregation and denaturation issues. Nonetheless, these adverse effects can be minimized by incorporating protective agents such as stabilizers, additives, and excipients, and by carefully controlling various lyophilization conditions.

Commonly used protectant include saccharides, polyols, polymers, surfactants, some proteins and amino acids etc. We usually add 8% (mass ratio by volume) of trehalose and mannitol as lyoprotectant. Trehalose can significantly prevent the alter of the protein secondary structure, the extension and aggregation of proteins during freeze-drying process; mannitol is also a universal applied protectant and fillers, which can reduce the aggregation of certain proteins after lyophilization.

Our protein products do not contain carrier protein or other additives (such as bovine serum albumin (BSA), human serum albumin (HSA) and sucrose, etc., and when lyophilized with the solution with the lowest salt content, they often cannot form A white grid structure, but a small amount of protein is deposited in the tube during the freeze-drying process, forming a thin or invisible transparent protein layer.

Reminder: Before opening the tube cap, we recommend that you quickly centrifuge for 20-30 seconds in a small centrifuge, so that the protein attached to the tube cap or the tube wall can be aggregated at the bottom of the tube. Our quality control procedures ensure that each tube contains the correct amount of protein, and although sometimes you can't see the protein powder, the amount of protein in the tube is still very precise.

To learn more about how to properly dissolve the lyophilized recombinant protein, please visit Lyophilization FAQs.

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