Human UDP-glucose dehydrogenase/UGDH protein (Recombinant) (His-Tag) (STJP016751)

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STJP016751
€161.40 - €886.20
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Short Description :Recombinant-Human UDP-glucose dehydrogenase/UGDH-His-Tag protein was developed from e.coli and has a target region of His-Tag. For use in research applications.
Applications:SDS-PAGE/Enzyme Activity
Host:E.coli
Note:STRICTLY FOR FURTHER SCIENTIFIC RESEARCH USE ONLY (RUO). MUST NOT TO BE USED IN DIAGNOSTIC OR THERAPEUTIC APPLICATIONS.
Concentration:0.5 mg/mL
Formulation:Liquid in 20mM Tris-HCl buffer (pH 8.0) containing 20% Glycerol, 1mM DTT, 0.1M NaCl, and 1mM EDTA
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 > 2500pmol/min/ug, and is defined as the amount of enzyme that convert 1.0pmole of UDP-glucose to UDP-glucuronate per minute at pH 8.7 at 37C.
Gene Symbol:UGDH
Gene ID:7358
Uniprot ID:UGDH_HUMAN
Accession Number:NP_003350.1
Immunogen:Human
Immunogen Region:1-494aa
Immunogen Sequence:M FEIKKICCIG AGYVGGPTCS VIAHMCPEIR VTVVDVNESR INAWNSPTLP IYEPGLKEVV ESCRGKNLFF STNIDDAIKE ADLVFISVNT PTKTYGMGKG RAADLKYIEA CARRIVQNSN GYKIVTEKST VPVRAAESIR RIFDANTKPN LNLQVLSNPE FLAEGTAIKD LKNPDRVLIG GDETPE
Tissue Specificity Detected in heart, placenta, liver, pancreas, spleen, thymus, prostate, ovary, small intestine and colon. Widely expressed.
Function Catalyzes the formation of UDP-alpha-D-glucuronate, a constituent of complex glycosaminoglycans. Required for the biosynthesis of chondroitin sulfate and heparan sulfate. Required for embryonic development via its role in the biosynthesis of glycosaminoglycans. Required for proper brain and neuronal development.
Protein Name Udp-Glucose 6-Dehydrogenase
Udp-Glc Dehydrogenase
Udp-Glcdh
Udpgdh
Database Links Reactome: R-HSA-173599
Cellular Localisation
Alternative Protein Names Udp-Glucose 6-Dehydrogenase protein
Udp-Glc Dehydrogenase protein
Udp-Glcdh protein
Udpgdh protein
UGDH protein

Information sourced from Uniprot.org