hchA recombinant protein

hchA, 1-283aa, E Coli, His tag, E Coli

Cat. Num. AAA204082

• Gene Names: hchA; ECK1963; gloC; JW1950; yedU; yzzC
• Applications: SDS-Page
• Purity: > 95% by SDS-PAGE
• Synonyms: hchA; 1-283aa; E Coli; His tag; Hsp31 molecular chaperone; ECK1963; JW1950; yedu; yzzC; hchA recombinant protein

• Host: E Coli
• Purity/Purification: > 95% by SDS-PAGE
• Form/Format: Liquid. 20mM Tris-HCl Buffer (pH 8.0) containing 20% glycerol, 0.1M NaCl, 1mM DTT
• Concentration: 1.0 mg/ml (determined by Bradford assay) (varies by lot)
• Sequence: MGSSHHHHHH SSGLVPRGSH MTVQTSKNPQ VDIAEDNAFF PSEYSLSQYT SPVSDLDGVD YPKPYRGKHK ILVIAADERY LPTDNGKLFS TGNHPIETLL PLYHLHAAGF EFEVATISGL MTKFEYWAMP HKDEKVMPFF EQHKSLFRNP KKLADVVASL NADSEYAAIF VPGGHGALIG LPESQDVAAA LQWAIKNDRF VISLCHGPAA FLALRHGDNP LNGYSICAFP DAADKQTPEI GYMPGHLTWY FGEELKKMGM NIINDDITGR VHKDRKLLTG DSPFAANALG KLAAQEMLAA YAG
• Sequence Length: 283

• Applicable Applications for hchA recombinant protein: SDS-PAGE
• Antigen Species: E Coli
• Tag Information: His-tag
• Preparation and Storage: Can be stored at 4 degree C short term (1-2 weeks).; For long term storage, aliquot and store at -20 degree C or -70 degree C.; Avoid repeated freezing and thawing cycles.

SDS-Page

Related Product Information for hchA recombinant protein

HchA, also known as, Escherichia coli Hsp31, is a homodimeric member of the ThiI/DJ-1/PfpI superfamily that combines molecular chaperone and aminopeptidase activities. It uses temperature-induced exposure of structured hydrophobic domains to capture and stabilize early unfolding protein intermediates under severe thermal stress. Recombinant E. coli hchA protein, fused to His-tag at N-terminus, was expressed in E Coli and purified by using conventional chromatography techniques.

Product Categories/Family for hchA recombinant protein

Heat Shock Proteins

References

Malki A. et al. (2003) Biochem. Biophys. Res. Commun. 301:430-436.

NCBI and Uniprot Product Information

• NCBI GI #: 16129913
• NCBI GeneID: 946481
• NCBI Accession #: NP_416476
• NCBI GenBank Nucleotide #: NC_000913.3
• UniProt Accession #: P31658; P76338
• Molecular Weight: 33.3 kDa (303aa) confirmed by MALDI-TOF
• NCBI Official Full Name: glyoxalase III and Hsp31 molecular chaperone
• NCBI Official Symbol: hchA
• NCBI Official Synonym Symbols: ECK1963; gloC; JW1950; yedU; yzzC
• NCBI Protein Information: glyoxalase III and Hsp31 molecular chaperone
• UniProt Protein Name: Protein/nucleic acid deglycase 1
• Protein Family: Protein deglycase
• UniProt Gene Name: hchA
• UniProt Synonym Gene Names: yedU; yzzC

NCBI Description

Important for the processing of 8-12mer peptides in vivo. [More information is available at EcoGene: EG11755]. Hsp31 (YedU) is a chaperone that is active as a homodimer . [More information is available at EcoCyc: G7055].

Uniprot Description

Protein and nucleotide deglycase that catalyzes the deglycation of the Maillard adducts formed between amino groups of proteins or nucleotides and reactive carbonyl groups of glyoxals (PubMed:26102038, PubMed:26774339, PubMed:28596309). Thus, functions as a protein deglycase that repairs methylglyoxal- and glyoxal-glycated proteins, and releases repaired proteins and lactate or glycolate, respectively. Deglycates cysteine, arginine and lysine residues in proteins, and thus reactivates these proteins by reversing glycation by glyoxals. Is able to repair glycated serum albumin, aspartate aminotransferase, glyceraldehyde-3-phosphate dehydrogenase, and fructose biphosphate aldolase. Acts on early glycation intermediates (hemithioacetals and aminocarbinols), preventing the formation of Schiff bases and advanced glycation endproducts (AGE) that cause irreversible damage (PubMed:26102038, PubMed:26774339). Also functions as a nucleotide deglycase able to repair glycated guanine in the free nucleotide pool (GTP, GDP, GMP, dGTP) and in DNA and RNA. Is thus involved in a major nucleotide repair system named guanine glycation repair (GG repair), dedicated to reversing methylglyoxal and glyoxal damage via nucleotide sanitization and direct nucleic acid repair (PubMed:28596309). Has been reported to display chaperone, peptidase and glutathione-independent glyoxalase activities (PubMed:12235139, PubMed:12565879, PubMed:14731284, PubMed:15550391, PubMed:7848303, PubMed:21696459). However, these apparently disparate activities are all recruited to execute its protein deglycase primary function (PubMed:26102038, PubMed:26774339). Plays an important role in protecting cells from carbonyl stress, severe heat shock and starvation, as well as in acid resistance of stationary-phase cells (PubMed:12235139, PubMed:16796689, PubMed:17158627).