Recombinant Human Ubiquitin-conjugating Enzyme E2 I, His

Synonyms SUMO-protein Ligase, Ubiquitin Carrier Protein 9, Ubiquitin Carrier Protein I, Ubiquitin-conjugating Enzyme E2 I, Ubiquitin-protein Ligase I, p18

Source Escherichia coli.

Molecular Weight Approximately 19.5 kDa, a single non-glycosylated polypeptide chain containing 158 amino acids (a.a.) of human UBE2I/UBC9 and 8 a.a. vector sequence including 6 × His tag at N-terminus.

Quantity 10µg/50µg/1mg

AA Sequence MHHHHHHAMG TLNMSGIALS RLAQERKAWR KDHPFGFVAV PTKNPDGTMN LMNWECAIPG KKGTPWEGGL FKLRMLFKDD YPSSPPKCKF EPPLFHPNVY PSGTVCLSIL EEDKDWRPAI TIKQILLGIQ ELLNEPNIQD PAQAEAYTIY CQNRVEYEKR VRAQAKKFAP S

Concentration See label.

Purity > 95 % by SDS-PAGE and HPLC analyses.

Biological Activity Data is not available.

Physical Appearance Sterile Colorless liquid.

Formulation A 0.2 µm filtered concentrated solution in 50 mM HEPES, pH 7.6, with 125 mM NaCl, 10 % Glycerol, 1 mM DTT.

Endotoxin Less than 1 EU/µg of rHuUBC9, His as determined by LAL method.

Stability & Storage Use a manual defrost freezer and avoid repeated freeze-thaw cycles.

- 6 months from date of receipt, -20 to -70 °C as supplied.

- 3 months, -20 to -70 °C under sterile conditions after opening.

Usage This material is offered by Shanghai PrimeGene Bio-Tech for research, laboratory or further evaluation purposes. NOT FOR HUMAN USE.

SDS-PAGE

Reference 1. Yukita A, Hosoya A, Ito Y, et al. 2012. Bone, 50: 1092-9.

2. Duan X, Trent JO, Ye H. 2009. Anticancer Agents Med Chem, 9: 51-4.

3. Niedenthal R. 2009. Methods Mol Biol, 497: 63-79.

4. Shang Q, Xu C, Zhang J, et al. 2009. Proteins, 76: 266-9.

Background SUMO-Conjugating Enzyme UBC9 belongs to the ubiquitin-conjugating enzyme family and is encoded by the UBE2I gene in humans. The ubiquitin-conjugating enzymes, also known as E2 enzymes and more rarely as ubiquitin-carrier enzymes, take part in the second step in the ubiquitination reaction. In this reaction, E1 activates the ubiquitin by covalently attaching the molecule to its active site cysteine residue. The activated ubiquitin is then transferred to an E2 cysteine and then the E2 molecule binds E3 via a structurally conserved binding region. The UBC9 accepts the ubiquitin-like proteins SUMO1-4 from the UBLE1A-UBLE1B E1 complex and catalyzes their covalent attachment to other proteins with the help of an E3 ligase such as RANBP2 or CBX4. Additionally, It takes parts in catalysis the formation of poly-SUMO chains, sumoylation of FOXL2 and KAT5, and the segregation of nuclear architecture and chromosome.