Foundational characteristics of cancer include proliferation, angiogenesis, migration, evasion of apoptosis, and cellular immortality. Find key markers for these cellular processes and antibodies to detect them.
The SUMOplot™ Analysis Program predicts and scores sumoylation sites in your protein. SUMOylation is a post-translational modification involved in various cellular processes, such as nuclear-cytosolic transport, transcriptional regulation, apoptosis, protein stability, response to stress, and progression through the cell cycle.
The Autophagy Receptor Motif Plotter predicts and scores autophagy receptor binding sites in your protein. Identifying proteins connected to this pathway is critical to understanding the role of autophagy in physiological as well as pathological processes such as development, differentiation, neurodegenerative diseases, stress, infection, and cancer.
SMURF2 Antibody (N-term)
Purified Rabbit Polyclonal Antibody (Pab)
- SPECIFICATION
- CITATIONS: 2
- PROTOCOLS
- BACKGROUND
Application 
| IHC-P, WB, E |
|---|---|
| Primary Accession | Q9HAU4 |
| Other Accession | A2A5Z6, A9JRZ0, NP_073576 |
| Reactivity | Human, Mouse |
| Predicted | Zebrafish |
| Host | Rabbit |
| Clonality | Polyclonal |
| Isotype | Rabbit IgG |
| Calculated MW | 86196 Da |
| Antigen Region | 6-36 aa |
| Gene ID | 64750 |
|---|---|
| Other Names | E3 ubiquitin-protein ligase SMURF2, hSMURF2, 632-, SMAD ubiquitination regulatory factor 2, SMAD-specific E3 ubiquitin-protein ligase 2, SMURF2 |
| Target/Specificity | This SMURF2 antibody is generated from rabbits immunized with a KLH conjugated synthetic peptide between 6-36 amino acids from the N-terminal region of human SMURF2. |
| Dilution | WB~~1:1000 IHC-P~~1:50~100 |
| Format | Purified polyclonal antibody supplied in PBS with 0.09% (W/V) sodium azide. This antibody is prepared by Saturated Ammonium Sulfate (SAS) precipitation followed by dialysis against PBS. |
| Storage | Maintain refrigerated at 2-8°C for up to 2 weeks. For long term storage store at -20°C in small aliquots to prevent freeze-thaw cycles. |
| Precautions | SMURF2 Antibody (N-term) is for research use only and not for use in diagnostic or therapeutic procedures. |
| Name | SMURF2 (HGNC:16809) |
|---|---|
| Function | E3 ubiquitin-protein ligase which accepts ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a thioester and then directly transfers the ubiquitin to targeted substrates (PubMed:11016919). Interacts with SMAD7 to trigger SMAD7-mediated transforming growth factor beta/TGF-beta receptor ubiquitin-dependent degradation, thereby down-regulating TGF-beta signaling (PubMed:11163210, PubMed:12717440, PubMed:21791611). In addition, interaction with SMAD7 activates autocatalytic degradation, which is prevented by interaction with AIMP1 (PubMed:18448069). Also forms a stable complex with TGF-beta receptor-mediated phosphorylated SMAD1, SMAD2 and SMAD3, and targets SMAD1 and SMAD2 for ubiquitination and proteasome-mediated degradation (PubMed:11016919, PubMed:11158580, PubMed:11389444). SMAD2 may recruit substrates, such as SNON, for ubiquitin-dependent degradation (PubMed:11389444). Negatively regulates TGFB1-induced epithelial-mesenchymal transition and myofibroblast differentiation (PubMed:30696809). |
| Cellular Location | Nucleus. Cytoplasm. Cell membrane. Membrane raft. Note=Cytoplasmic in the presence of SMAD7. Colocalizes with CAV1, SMAD7 and TGF-beta receptor in membrane rafts |
| Tissue Location | Widely expressed. |
Provided below are standard protocols that you may find useful for product applications.
Background
SMURF2, a 748-amino acid ubiquitin E3 ligase that is 83% identical to SMURF1, codes for a C2-WW-HECT domain ubiquitin ligase that associates constitutively with SMAD7. Binding to SMAD7 induces export of SMURF2 and recruitment to the activated transforming growth factor-beta receptor (TGFBR), where it causes receptor and SMAD7 degradation. A strong interaction of second and third SMURF2 WW domains has been identified with SMAD1, SMAD2, and SMAD3, but not SMAD4. Western blot analysis showed that SMURF2 selectively downregulates the transcription of SMAD2 and SMAD1, but not SMAD3. The nuclear SMURF2/phosphorylated SMAD2 interaction is requires TGFB1.
References
Zhang, Y., et al., Proc. Natl. Acad. Sci. U.S.A. 98(3):974-979 (2001).
Kavsak, P., et al., Mol. Cell 6(6):1365-1375 (2000).
Lin, X., et al., J. Biol. Chem. 275(47):36818-36822 (2000).
If you have used an Abcepta product and would like to share how it has performed, please click on the "Submit Review" button and provide the requested information. Our staff will examine and post your review and contact you if needed.
If you have any additional inquiries please email technical services at tech@abcepta.com.
Ordering Information
Other Products
Shipping Information
