Recombinant Human Glyoxalase II Protein (His Tag)

Name: Recombinant Human Glyoxalase II Protein (His Tag)
Brand: Beta LifeScience
SKU: BLPSN-2272
Availability: InStock

Collections: Other recombinant proteins, Recombinant proteins

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Product Overview

Tag	His
Host Species	Human
Accession	Q16775
Synonym	GLO2, GLX2, GLXII, HAGH1
Background	The human and rodent forms of glyoxalase II (Hydroxyacylglutathione hydrolase, HAGH) can readily be separated by starch gel electrophoretic procedures.
Description	A DNA sequence encoding the mature form of human HAGH isoform 2 (Q16775-2) (Met 1-Asp 260) was fused with a His tag at the C-terminus
Source	E.coli
Predicted N Terminal	Met
AA Sequence	Met 1-Asp 260
Molecular Weight	The recombinant human HAGH consisting of 270 a.a. and has a calculated molecular mass of 30.2 kDa. It migrates as an approximately 19 kDa band in SDS-PAGE under reducing conditions
Purity	>96% as determined by SDS-PAGE
Endotoxin	Please contact us for more information.
Bioactivity	Please contact us for detailed information
Formulation	Lyophilized from sterile 20mM Tris, 0.15 M NaCl, 10% glycerol, pH 7.5.
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	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.