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.
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Species : Human
Source : E.coli
Tag : GST
Protein Length : 1-748 a.a.
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).
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 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;

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