Human Glyoxalase II protein (Recombinant) (His-Tag) (STJP016947)
SPECIFICATIONS
HostE.coli
ImmunogenHuman
General Information
| Short Description | Recombinant-Human Glyoxalase II-His-Tag protein was developed from e.coli and has a target region of His-Tag. For use in research applications. |
| Applications | Enzyme Activity/SDS-PAGE |
| Host | E.coli |
| Note | STRICTLY FOR FURTHER SCIENTIFIC RESEARCH USE ONLY (RUO). MUST NOT TO BE USED IN DIAGNOSTIC OR THERAPEUTIC APPLICATIONS. |
Product Properties
| Concentration | 0.5 mg/mL |
| Formulation | Liquid in 20mM Tris-HCl buffer (pH 8.5) containing 10% Glycerol |
| Storage Instruction | For short term storage, keep at +2C to +8C for up to 1 week. For long term storage, aliquot and store at-20C, and avoid repeat freeze-thaw cycles. |
| Immunoreactivity | Specific activity is > 500unit/mg, and is defined as the amount of enzyme that reduce 1.0 umole of 5, 5-Dithiobis (2-nitrobenzoic acid) (DTNB) with reduced glutathione per minute at pH 7.5 at 37C. |
Target Information
| Gene Symbol | HAGH |
| Gene ID | 3029 |
| Uniprot ID | GLO2_HUMAN |
| Accession Number | NP_001035517 |
| Immunogen | Human |
| Immunogen Region | 1-260aa |
| Immunogen Sequence | MGSSHHHHHH SSGLVPRGSH MGSHMKVEVL PALTDNYMYL VIDDETKEAA IVDPVQPQKV VDAARKHGVK LTTVLTTHHH WDHAGGNEKL VKLESGLKVY GGDDRIGALT HKITHLSTLQ VGSLNVKCLA TPCHTSGHIC YFVSKPGGSE PPAVFTGDTL FVAGCGKFYE GTADEMCKAL LEVLGRLPPD TRVYCGHEYT INNLKFARHV EPGNAAIREK LAWAKEKY |
Additional Info
| Tissue Specificity | Expressed in liver and kidney. |
| Function | Thiolesterase that catalyzes the hydrolysis of S-D-lactoyl-glutathione to form glutathione and D-lactic acid. |
| Protein Name | Hydroxyacylglutathione Hydrolase - MitochondrialGlyoxalase IiGlx Ii |
| Database Links | Reactome: R-HSA-70268 Q16775-2 |
| Cellular Localisation | Isoform 1: Mitochondrion MatrixIsoform 2: Cytoplasm |
| Alternative Protein Names | Hydroxyacylglutathione Hydrolase - Mitochondrial proteinGlyoxalase Ii proteinGlx Ii proteinHAGH proteinGLO2 proteinHAGH1 protein |
Information sourced from Uniprot.org