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Ubiquitin-Conjugating Enzyme E2I Human Recombinant ( UBE2I Human )

DescriptionUbiquitin-Conjugating Enzyme E2I Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 154 amino acids & having a molecular mass of 17.9 kDa.SourceEscherichia Coli.Physical AppearanceSterile

$193.00

Data sheet

Formulation The protein (1 mg/ml) contains 50mM HEPES (pH7.5) 150mM NaCl, 1mM DTT, and 10% glycerol.
Purity Greater than 95.0% as determined by(a) Analysis by RP-HPLC.(b) Analysis by SDS-PAGE.
Description Ubiquitin-Conjugating Enzyme E2I Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 154 amino acids & having a molecular mass of 17.9 kDa.
Protein Background Human Ubc9 is homologous to ubiquitin-conjugating enzymes (E2s). However, instead of conjugating ubiquitin, it conjugates a ubiquitin homologue, small ubiquitin-like modifier 1(SUMO-1). And hUbc9 retains striking structural and functional conservation with yeast Ubc9. The ubiquitin-dependent protein degradation system has been recognized as a complete enzymatic pathway that is responsible for the selective degradation of abnormal and short-lived proteins. The conjugation of ubiquitin requires the activities of ubiquitin-activating (E1) and conjugating (E2) enzymes.
Expression host Escherichia Coli.
Synonyms SUMO-conjugating enzyme UBC9, EC 6.3.2.-, SUMO-protein ligase, Ubiquitin-conjugating enzyme E2 I, Ubiquitin-protein ligase I, Ubiquitin carrier protein I, Ubiquitin carrier protein 9, p18, UBC9, C358B7.1.
Reagent Appearance Sterile filtered colorless solution.
Stability Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
Amino acid sequence MSGIALSRLA QERKAWRKDH PFGFVAVPTK NPDGTMNLMN WECAIPGKKG TPWEGGLFKL RMLFKDDYPS SPPKCKFEPP LFHPNVYPSG TVCLSILEED KDWRPAITIK QILLGIQELL NEPNIQDPAQ AEAYTIYCQN RVEYEKRVRA QAKKFAPS.

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