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Pan SUMO AntibodyPurified Rabbit Polyclonal Antibody (Pab)
| Country | United States
Ordering Information
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| Catalog # | Size | Availability | Price | |
| AP1290a | 0.1 mg 400 ul | In Stock | $ 255.00 | DISCONTINED INQUIRE CLICK INQUIRE Add to cart |
- Specification
- Citiations : 0
- Reviews
- Protocols
- Backgrounds
Pan SUMO Antibody - Product info | |
| Application | WB
|
| Primary Accession | P55854 |
| Reactivity | Human |
| Concentration | 0.25 mg/ml |
| Isotype | Rabbit Ig |
| Calculated MW | 11637 Da |
Pan SUMO Antibody - Additional info | |
| Gene ID 6612 | |
| Other Names SUMO3; SMT3B; SMT3H1; Small ubiquitin-related modifier 3; SMT3 homolog 1; SUMO-2; Ubiquitin-like protein SMT3B | |
| Target/Specificity "This Pan SUMO antibody recognizes all 3 SUMO isoforms, including human SUMO1, SUMO2 and SUMO3. This antibody is generated from rabbits immunized with a recombinant protein encoding full length human SUMO3." | |
| Dilution WB~~1:100~500WB~~1:1000 | |
| Format Purified polyclonal antibody supplied in PBS with 0.09% (W/V) sodium azide. This antibody is purified through a protein G column, eluted with high and low pH buffers and neutralized immediately, followed by dialysis against PBS. | |
| Storage Maintain refrigerated at 2-8°C for up to 6 months. For long term storage store at -20°C in small aliquots to prevent freeze-thaw cycles. | |
| Precautions Pan SUMO Antibody is for research use only and not for use in diagnostic or therapeutic procedures. | |
Pan SUMO Antibody - Protein Information | |
| Name SUMO3 | |
| Synonyms SMT3B, SMT3H1 | |
| Function Ubiquitin-like protein which can be covalently attached to target lysines either as a monomer or as a lysine-linked polymer. Does not seem to be involved in protein degradation and may function as an antagonist of ubiquitin in the degradation process. Plays a role in a number of cellular processes such as nuclear transport, DNA replication and repair, mitosis and signal transduction. Covalent attachment to its substrates requires prior activation by the E1 complex SAE1-SAE2 and linkage to the E2 enzyme UBE2I, and can be promoted by an E3 ligase such as PIAS1-4, RANBP2 or CBX4 | |
| Cellular Location Cytoplasm. | |
| Tissue Location Expressed predominantly in liver. | |
Pan SUMO Antibody - Related products
AP1223d: SUMO2/3 Antibody (Center)
AP1223e: SUMO2/3 Antibody (C-term E69)
AP1224a: SUMO2/3 Antibody (C-term)
AP1225a: SUMO3 Antibody (C-term)
AP1225b: SUMO3 Antibody (C-term P94)
RI15171: SUMO3 predesign siRNA
DC00016: Human SUMO3 cDNA Clone
LY11068a: SUMO3 Over-expression Lysate
BP1223d: SUMO2/3 Antibody (Center) Blocking Peptide
BP1223e: SUMO2/3 Antibody (C-term E69) Blocking Peptide
BP1224a: SUMO2/3 Antibody (C-term) Blocking Peptide
Pan SUMO Antibody - Application data
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Western blot analysis of SUMO (arrow) using rabbit polyclonal Pan SUMO Antibody (Cat.#AP1290a). 293 cell lysates (2 ug/lane) either nontransfected (Lane 1) or transiently transfected (Lane 2) with the SUMO gene.
Pan SUMO Antibody - Research Areas
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BACKGROUND
Covalent modification of target lysines by SUMO (small ubiquitin-like modifier) modulates processes such as protein localization, transcription, nuclear transport, mitosis, DNA replication and repair, signal transduction, and viral reproduction. SUMO does not seem to be involved in protein degradation and may in fact function as an antagonist of ubiquitin in the degradation process. The SUMO family consists of SUMO1 and closely related homologs SUMO2, SUMO3, and SUMO4. Sumoylation has been shown to regulate a wide range of proteins, including MDM2, PIAS, PML, RanGAP1, RanBP2, p53, p73, HIPK2, TEL, c-Jun, Fas, Daxx, TNFRI, Topo-I, Topo-II, PARK2, WRN, Sp100, IkB-alpha, Androgen receptor (AR), GLUT1/4, CaMK, DNMT3B, TDG, HIF1A, CHD3, EXOSC9, RAD51, and viral targets such as CMV-IE1/2, EBV-BZLF1, and HPV/BPV-E1.
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). Strausberg, R.L., et al., Proc. Natl. Acad. Sci. U.S.A. 99(26):16899-16903 (2002). Lapenta, V., et al., Genomics 40(2):362-366 (1997).
