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SUMO1 Antibody
Affinity Purified Rabbit Polyclonal Antibody (Pab)
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- CITATIONS
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- BACKGROUND
Application 
| WB, IF, FC, IHC-P, E |
|---|---|
| Primary Accession | P63165 |
| Reactivity | Human, Rat |
| Host | Rabbit |
| Clonality | Polyclonal |
| Isotype | Rabbit IgG |
| Calculated MW | 11557 Da |
| Gene ID | 7341 |
|---|---|
| Other Names | Small ubiquitin-related modifier 1, SUMO-1, GAP-modifying protein 1, GMP1, SMT3 homolog 3, Sentrin, Ubiquitin-homology domain protein PIC1, Ubiquitin-like protein SMT3C, Smt3C, Ubiquitin-like protein UBL1, SUMO1, SMT3C, SMT3H3, UBL1 |
| Target/Specificity | This SUMO1 antibody is generated from rabbits immunized with human SUMO1 recombinant protein. |
| Dilution | IF~~1:10~50 WB~~1:8000 IHC-P~~1:50~100 FC~~1:10~50 |
| Format | Purified polyclonal antibody supplied in PBS with 0.09% (W/V) sodium azide. This antibody is purified through a protein A column, followed by peptide affinity purification. |
| 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 | SUMO1 Antibody is for research use only and not for use in diagnostic or therapeutic procedures. |
| 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. Covalently attached to the voltage-gated potassium channel KCNB1; this modulates the gating characteristics of KCNB1 (PubMed:19223394). 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. Covalently attached to ZFHX3 (PubMed:24651376). |
| Cellular Location | Nucleus membrane. Nucleus speckle {ECO:0000250|UniProtKB:P63166}. Cytoplasm. Nucleus, PML body. Cell membrane. Nucleus. Note=Recruited by BCL11A into the nuclear body (By similarity). In the presence of ZFHX3, sequesterd to nuclear body (NB)-like dots in the nucleus some of which overlap or closely associate with PML body (PubMed:24651376) {ECO:0000250|UniProtKB:P63166, ECO:0000269|PubMed:24651376} |
Thousands of laboratories across the world have published research that depended on the performance of antibodies from Abcepta to advance their research. Check out links to articles that cite our products in major peer-reviewed journals, organized by research category.
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Provided below are standard protocols that you may find useful for product applications.
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).
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