Recombinant Human Hydroxyacylglutathione Hydrolase, Mitochondrial (HAGH) Protein (GST)

Name: Recombinant Human Hydroxyacylglutathione Hydrolase, Mitochondrial (HAGH) Protein (GST)
Brand: Beta LifeScience
SKU: BLC-03572P
Availability: InStock

Greater than 90% as determined by SDS-PAGE.

Based on the SEQUEST from database of E.coli host and target protein, the LC-MS/MS Analysis result of this product could indicate that this peptide derived from E.coli-expressed Homo sapiens (Human) HAGH.

Collections: High-quality recombinant proteins, Other recombinant proteins

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Product Overview

Description	Recombinant Human Hydroxyacylglutathione Hydrolase, Mitochondrial (HAGH) Protein (GST) is produced by our E.coli expression system. This is a protein fragment.
Purity	Greater than 90% as determined by SDS-PAGE.
Uniprotkb	Q16775
Target Symbol	HAGH
Synonyms	HAGH; GLO2; HAGH1Hydroxyacylglutathione hydrolase; mitochondrial; EC 3.1.2.6; Glyoxalase II; Glx II
Species	Homo sapiens (Human)
Expression System	E.coli
Tag	N-GST
Target Protein Sequence	KVEVLPALTDNYMYLVIDDETKEAAIVDPVQPQKVVDAARKHGVKLTTVLTTHHHWDHAGGNEKLVKLESGLKVYGGDDRIGALTHKITHLSTLQVGSLNVKCLATPCHTSGHICYFVSKPGGSEPPAVFTGDTLFVAGCGKFYEGTADEMCKALLEVLGRLPPDTRVYCGHEYTINNLKFARHVEPGNAAIREKLAWAKEKYSIGEPTVPSTLAEEFTYNPFMRVREKTVQQHAGETDPVTTMRAVRREKDQFKMPRD
Expression Range	50-308aa
Protein Length	Partial
Mol. Weight	55.7kDa
Research Area	Metabolism
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.
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	Thiolesterase that catalyzes the hydrolysis of S-D-lactoyl-glutathione to form glutathione and D-lactic acid.
Subcellular Location	[Isoform 1]: Mitochondrion matrix.; [Isoform 2]: Cytoplasm.
Protein Families	Metallo-beta-lactamase superfamily, Glyoxalase II family
Database References	HGNC: 4805 OMIM: 138760 KEGG: hsa:3029 STRING: 9606.ENSP00000380514 UniGene: Hs.157394
Tissue Specificity	Expressed in liver and kidney.

Gene Functions References

Down regulation of Glyoxalase II was observed in cases of diabetic retinopathy as compared to controls. PMID: 29950256
The critical role of glyoxalases as regulators of tumorigenesis in the prostate through modulation of various critical signaling pathways, and an overview of the current knowledge on glyoxalases in bladder, kidney and testis cancers is reviewed. (GLO1, GLO2) PMID: 29385039
epidermal expression stronger in older skin donors PMID: 26914966
Glo2, together with Glo1, represents a novel mechanism in prostate cancer progression as part of a pathway driven by PTEN/PI3K/AKT/mTOR signaling. PMID: 27696457
This article reports for the first time a possible additional role of Glo2 that, after interacting with a target protein, is able to promote S-glutathionylation. PMID: 27935136
This study suggested that HAGH, rs11859266 and rs3743852 showed significant associations with schizophrenia in males at allelic and genotype levels. PMID: 25645869
No association between genetic variants of the HAGH gene and autism spectrum disorder was found. PMID: 24671236
hydroxyacylglutathione hydrolase (HAGH) gene encodes both cytosolic and mitochondrial forms of glyoxalase II PMID: 15117945
Overexpression of glyoxalase II is associated with kidney tumor PMID: 16803681
Data show that the GLX2 gene, which encodes glyoxalase II enzyme, is up-regulated by p63 and p73. PMID: 16831876
In androgen-dependent prostate cancer cells, testosterone upregulates GLO2 mRNA levels. In androgen-independent prostate cancer cells, it downregulates GLO2 mRNA. PMID: 18344682
Human glyoxalase II contains an Fe(II)Zn(II) center but is active as a mononuclear Zn(II) enzyme PMID: 19413286

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.