Human PGM2 protein (Recombinant) (His-Tag) (STJP019198)

SPECIFICATIONS
HostE.coli
ImmunogenHuman
STJP019198
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General Information

Short DescriptionRecombinant-Human PGM2-His-Tag protein was developed from e.coli and has a target region of His-Tag. For use in research applications.
ApplicationsSDS-PAGE
HostE.coli
NoteSTRICTLY FOR FURTHER SCIENTIFIC RESEARCH USE ONLY (RUO). MUST NOT TO BE USED IN DIAGNOSTIC OR THERAPEUTIC APPLICATIONS.

Product Properties

Concentration1 mg/mL
FormulationLiquid in phosphate-Buffered Saline (pH 7.4) containing 10% Glycerol
Storage InstructionFor 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.

Target Information

Gene SymbolPGM2
Gene ID55276
Uniprot IDPGM2_HUMAN
Accession NumberNP_060760
ImmunogenHuman
Immunogen Region1-612aa
Immunogen SequenceMGSSHHHHHH SSGLVPRGSH MGSMAAPEGS GLGEDARLDQ ETAQWLRWDK NSLTLEAVKR LIAEGNKEEL RKCFGARMEF GTAGLRAAMG PGISRMNDLT IIQTTQGFCR YLEKQFSDLK QKGIVISFDA RAHPSSGGSS RRFARLAATT FISQGIPVYL FSDITPTPFV PFTVSHLKLC AGIMITASHN PKQDNGYKVY WDNGAQIISP HDKGISQAIE ENLEPWPQ

Additional Info

Function Catalyzes the conversion of the nucleoside breakdown products ribose-1-phosphate and deoxyribose-1-phosphate to the corresponding 5-phosphopentoses. Catalyzes the reversible isomerization of alpha-D-glucose 1-phosphate to alpha-D-glucose 6-phosphate but with a lower catalytic efficiency. The mechanism proceeds via the intermediate compound alpha-D-glucose 1,6-bisphosphate. In vitro, also has a low glucose 1,6-bisphosphate synthase activity which is most probably not physiologically relevant.
Protein Name Phosphopentomutase
Glucose Phosphomutase 2
Phosphodeoxyribomutase
Phosphoglucomutase-2
Database Links Reactome: R-HSA-6798695
Reactome: R-HSA-71336
Cellular Localisation Cytoplasm
Cytosol
Alternative Protein Names Phosphopentomutase protein
Glucose Phosphomutase 2 protein
Phosphodeoxyribomutase protein
Phosphoglucomutase-2 protein
PGM2 protein
MSTP006 protein

Information sourced from Uniprot.org

Citations

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