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

Name: Recombinant Human Glutathione S-Transferase Kappa 1 (GSTK1) Protein (GST), Active
Brand: Beta LifeScience
SKU: BLC-05650P
Availability: InStock

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.

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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	HGNC: 16906 OMIM: 602321 KEGG: hsa:373156 UniGene: 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.