Home
Protein
Recombinant Proteins
Recombinant Human Hydroxyacylglutathione hydrolase, mitochondrial (HAGH), partial

Recombinant Human Hydroxyacylglutathione hydrolase, mitochondrial (HAGH), partial

^{In Stock}

Code	CSB-EP624118HU1
Abbreviation	Recombinant Human HAGH protein, partial
MSDS	MSDS Datasheet
Size	$224
	Order now
Image	(Tris-Glycine gel) Discontinuous SDS-PAGE (reduced) with 5% enrichment gel and 15% separation gel. Based on the SEQUEST from database of E.coli host and target protein, the LC-MS/MS Analysis result of CSB-RP111954h could indicate that this peptide derived from E.coli-expressed Homo sapiens (Human) HAGH. Based on the SEQUEST from database of E.coli host and target protein, the LC-MS/MS Analysis result of CSB-RP111954h could indicate that this peptide derived from E.coli-expressed Homo sapiens (Human) HAGH.
Have Questions?	Leave a Message or Start an on-line Chat

Product Details
Related Products
Customer Reviews and Q&A
Target Background

Product Details

Purity

Greater than 90% as determined by SDS-PAGE.

Target Names

HAGH

Uniprot No.

Q16775

Research Area

Metabolism

Alternative Names

HAGH; GLO2; HAGH1Hydroxyacylglutathione hydrolase; mitochondrial; EC 3.1.2.6; Glyoxalase II; Glx II

Species

Homo sapiens (Human)

Source

E.coli

Expression Region

50-308aa

Target Protein Sequence

KVEVLPALTDNYMYLVIDDETKEAAIVDPVQPQKVVDAARKHGVKLTTVLTTHHHWDHAGGNEKLVKLESGLKVYGGDDRIGALTHKITHLSTLQVGSLNVKCLATPCHTSGHICYFVSKPGGSEPPAVFTGDTLFVAGCGKFYEGTADEMCKALLEVLGRLPPDTRVYCGHEYTINNLKFARHVEPGNAAIREKLAWAKEKYSIGEPTVPSTLAEEFTYNPFMRVREKTVQQHAGETDPVTTMRAVRREKDQFKMPRD
Note: The complete sequence may include tag sequence, target protein sequence, linker sequence and extra sequence that is translated with the protein sequence for the purpose(s) of secretion, stability, solubility, etc.
If the exact amino acid sequence of this recombinant protein is critical to your application, please explicitly request the full and complete sequence of this protein before ordering.

Mol. Weight

55.7kDa

Protein Length

Partial

Tag Info

N-terminal GST-tagged

Form

Liquid or Lyophilized powder
Note: We will preferentially ship the format that we have in stock, however, if you have any special requirement for the format, please remark your requirement when placing the order, we will prepare according to your demand.

Buffer

If the delivery form is liquid, the default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol.
Note: If you have any special requirement for the glycerol content, please remark when you place the order.
If the delivery form is lyophilized powder, the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose.

Troubleshooting and FAQs

Protein FAQs

Storage Condition

Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. Avoid repeated freeze-thaw cycles.

Shelf Life

The shelf life is related to many factors, storage state, buffer ingredients, storage temperature and the stability of the protein itself.
Generally, the shelf life of liquid form is 6 months at -20°C/-80°C. The shelf life of lyophilized form is 12 months at -20°C/-80°C.

Lead Time

3-7 business days

Notes

Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.

Datasheet & COA

Please contact us to get it.

Description

In e.coli cells, the generation of recombinant Human HAGH protein involves cloning a DNA fragment encoding the Human HAGH protein (50-308aa) into a plasmid vector, which is then transferred into the e.coli cells. Positive cells are selected, cultured, and induced to express the HAGH protein. A N-terminal GST tag is attached to the protein. Lysis of the cells allows for the harvest of the recombinant Human HAGH protein. The collected recombiant Human HAGH protein is subjected to affinity purification and is identified using SDS-PAGE and subsequent staining of the gel with Coomassie Brilliant Blue. Its purity is greater than 90%.

Customer Reviews and Q&A

■ Customer Reviews

There are currently no reviews for this product.

Submit a Review here

Target Background

Function

Thiolesterase that catalyzes the hydrolysis of S-D-lactoyl-glutathione to form glutathione and D-lactic acid.

Gene References into Functions

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