Recombinant Human GSTK1 Protein

Name: Recombinant Human GSTK1 Protein
Brand: Beta LifeScience
SKU: BLPSN-2350
Availability: InStock

Collections: Other recombinant proteins, Recombinant proteins

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Product Overview

Tag	N/A
Host Species	Human
Accession	Q9Y2Q3
Synonym	GST, GST13, GST13-13, GSTK1-1, hGSTK1
Background	GSTK1 gene encodes a member of the kappa class of the glutathione transferase superfamily of enzymes that function in cellular detoxification. Glutathione S-transferases (GSTs) are a family of enzymes that catalyze a variety of reactions in both eukaryotes and prokaryotes. They catalyze the conjugation of reduced glutathione with potentially toxic, xenobiotic substrates, thus aiding excretion from the body. GSTK1(glutathione S-transferase kappa 1) is localized to the peroxisome and catalyzes the conjugation of glutathione to a wide range of hydrophobic substates facilitating the removal of these compounds from cells. GSTK1 functions in cellular detoxification.
Description	A DNA sequence encoding the mature form of human GSTK1 (Q9Y2Q3-1) (Gly2-Leu226) was expressed with a N-terminal Met.
Source	E.coli
Predicted N Terminal	Met
AA Sequence	Gly2-Leu226
Molecular Weight	The recombinant human GSTK1 consists of 226 a.a. and predicts a molecular mass of 25.5 KDa. It migrates as an approximately 25 KDa band in SDS-PAGE under reducing conditions.
Purity	>95% as determined by SDS-PAGE
Endotoxin	Please contact us for more information.
Bioactivity	Please contact us for detailed information
Formulation	Lyophilized from sterile 50mM Tris,10% glycerol, pH 8.0..
Stability	The recombinant proteins are stable for up to 1 year from date of receipt at -70°C.
Usage	For Research Use Only
Storage	Store the protein under sterile conditions at -20°C to -80°C. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.

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	HGNC: 16906 OMIM: 602321 KEGG: hsa:373156 UniGene: Hs.390667
Tissue Specificity	Ubiquitous.

Gene Functions References

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
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
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
GSTK1 T/T genotype may be a novel risk factor for the prediction of overweight status in SCZ male patients. PMID: 27010189
High glutathione-S-transferase is associated with type 2 diabetes mellitus. PMID: 27377684
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
we have optimized the GST-Nck1-SH2 pull-down procedure to obtain tyrosine-phosphorylated proteins in tumor tissues PMID: 23426619
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
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
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
structure and function characterization of a GST from human breast PMID: 14709161
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
crystal structure of hGSTK1 has been determined by the multiple-isomorphous replacement method and refined to 1.93 A resolution PMID: 16081649
Our results suggest that genetic polymorphisms of xenobiotic-metabolizing enzymes could play an important role in infertility. PMID: 18774560
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
Observational study of gene-disease association. (HuGE Navigator) PMID: 19225211
Observational study of gene-disease association. (HuGE Navigator) PMID: 17601350
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.