Recombinant Human SMURF2, GST-tagged

• Cat.No.: SMURF2-138H
• Product Overview: Recombinant human SMURF2 (amino acid residues 1-748), with N-terminal GST, was expressed in E.coli.

Specification

• Description: The enzymes of the ubiquitylation pathway play a pivotal role in a number of cellular processes including the regulated and targeted proteasome-dependent degradation of substrate proteins. Three classes of enzymes are involved in the process of ubiquitylation; activating enzymes (E1s), conjugating enzymes (E2s) and protein ligases (E3s). Smad-Specific E3 Ubiquitin Protein Ligase 1 (SMURF2) is a member of the E3 protein ligase family and cloning of the human gene was first described by Kavsak et al. (2000). SMURF2 is a HECT domain ubiquitin E3 ligase that has been shown to regulate cell polarity, senescence and tumor suppression (Blank et al., 2012).
• Source: E. coli
• Species: Human
• Tag: GST
• Form: 50 mM HEPES pH 7.5, 150 mM sodium chloride, 2 mM dithiothreitol, 10% glycerol
• Molecular Mass: ~114kDa
• Storage: 12 months at -70°C. Avoid multiple freeze/thaw cycles.
• Concentration: 0.5mg/ml

Gene Information

• Gene Name: SMURF2 SMAD specific E3 ubiquitin protein ligase 2 [ Homo sapiens ]
• Official Symbol: SMURF2
• Synonyms: SMURF2; SMAD specific E3 ubiquitin protein ligase 2; E3 ubiquitin-protein ligase SMURF2; hSMURF2; E3 ubiquitin ligase SMURF2; SMAD ubiquitination regulatory factor 2; SMAD-specific E3 ubiquitin-protein ligase 2; MGC138150; DKFZp686F0270
• Gene ID: 64750
• mRNA Refseq: NM_022739
• Protein Refseq: NP_073576
• MIM: 605532
• UniProt ID: Q9HAU4
• Chromosome Location: 17q22-q23
• Pathway: Adaptive Immune System, organism-specific biosystem; Antigen processing: Ubiquitination and Proteasome degradation, organism-specific biosystem; BMP receptor signaling, organism-specific biosystem; Class I MHC mediated antigen processing & presentation, organism-specific biosystem; Endocytosis, organism-specific biosystem
• Function: SMAD binding; acid-amino acid ligase activity; identical protein binding; ligase activity; protein binding; ubiquitin-protein ligase activity