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SUMO1 Antibody (C-term) Blocking PeptideSynthetic peptide
| Country | United States
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| Catalog # | Size | Availability | Price | |
| BP1222a | 0.1 mg 400 ul | In Stock | $ 45.00 | DISCONTINED INQUIRE CLICK INQUIRE Add to cart |
- Specification
- Citiations : 0
- Reviews
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- Backgrounds
SUMO1 Antibody (C-term) Blocking Peptide - Product info | |
| Primary Accession | P63165 |
| Clone Names | 2012302 |
| Calculated MW | 11557 Da |
SUMO1 Antibody (C-term) Blocking Peptide - Additional info | |
| Gene ID 7341 | |
| Target/Specificity The synthetic peptide sequence used to generate the antibody AP1222a was selected from the C-term region of human SUMO1. A 10 to 100 fold molar excess to antibody is recommended. Precise conditions should be optimized for a particular assay. | |
| Format The synthetic peptide was lyophilized with 100% acetonitrile and is supplied as a powder. Reconstitute with 0.1 ml deionized water for a final concentration of 1 mg/ml. | |
| Storage Maintain refrigerated at 2-8°C for up to 6 months. For long term storage store at -20°C. | |
| Precautions This product is for research use only. Not for use in diagnostic or therapeutic procedures. | |
SUMO1 Antibody (C-term) Blocking Peptide - Protein Information | |
| Name SUMO1 | |
| Synonyms SMT3C, SMT3H3, UBL1 | |
| Function Ubiquitin-like protein that can be covalently attached to proteins as a monomer or a lysine-linked polymer. Covalent attachment via an isopeptide bond to its substrates requires prior activation by the E1 complex SAE1-SAE2 and linkage to the E2 enzyme UBE2I, and can be promoted by E3 ligases such as PIAS1-4, RANBP2 or CBX4. This post-translational modification on lysine residues of proteins plays a crucial role in a number of cellular processes such as nuclear transport, DNA replication and repair, mitosis and signal transduction. Involved for instance in targeting RANGAP1 to the nuclear pore complex protein RANBP2 Polymeric SUMO1 chains are also susceptible to polyubiquitination which functions as a signal for proteasomal degradation of modified proteins. May also regulate a network of genes involved in palate development | |
| Cellular Location Nucleus membrane. Nucleus speckle. Cytoplasm. Note=Recruited by BCL11A into the nuclear body (By similarity) | |
SUMO1 Antibody (C-term) Blocking Peptide - Related products
AP1221a: SUMO1 Antibody (N-term)
AP1222a: SUMO1 Antibody (C-term)
AP1222c: SUMO1 Antibody (N-term A6)
AP1222d: SUMO1 Antibody (N-term E67)
RI15169: SUMO1 predesign siRNA
BP1221a: SUMO1 Antibody (N-term) Blocking Peptide
BP1222a: SUMO1 Antibody (C-term) Blocking Peptide
BP1222c: SUMO1 Antibody (N-term A6) Blocking Peptide
SUMO1 Antibody (C-term) Blocking Peptide - Research Areas
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BACKGROUND
Covalent attachment of one protein to another is one of the more prominent posttranslational modifications in respects to size and ubiquity ? to which eukaryotic proteins are subject. Ubiquitin is the most familiar of the protein modifiers and its activation and transfer to target proteins has been studied for over two decades. Recently a new group of ubiquitin-like (Ubl) proteins have come to light. One of the most intriguing of them is SUMO (small ubiquitin-like modifier, ~12kDa) also known as Sentrin. SUMO family has been described in vertebrates: SUMO-1 and the closest homologs SUMO-2 and SUMO-3. SUMO have been shown to bind and regulate mammalian SP-RINGs (such as Mdm2, PIAS and PML), RanGAP1, RanBP2, p53, p73, HIPK2, TEL, c-Jun, Fas, Daxx, TNFRI, Topo-I, Topo-II, WRN, Sp100, IkB-alpha, Androgen receptor (AR), GLUT1/4, Drosophila Ttk69, Dorsal, CaMK, yeast Septins, and viral CMV-IE1/2, EBV-BZLF1, HPV/BPV-E1. These bindings implicate SUMO in the stabilization of the target proteins and/or their localization to subcellular complexes. SUMO research enters now an exciting phase with a promise to help understanding how cells orchestrate the complexities of rapidly regulating protein level and activity.
REFERENCES
Yang, S.H., et al., Mol. Cell 13(4):611-617 (2004).Bailey, D., et al., J. Biol. Chem. 279(1):692-703 (2004).Ling, Y., et al., Nucleic Acids Res. 32(2):598-610 (2004).Pountney, D.L., et al., Exp. Neurol. 184(1):436-446 (2003).Ohshima, T., et al., J. Biol. Chem. 278(51):50833-50842 (2003).
