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SUMO1 Antibody (N-term)
Affinity Purified Rabbit Polyclonal Antibody (Pab)
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- BACKGROUND
Application 
| WB, IF, IHC-P, E |
|---|---|
| Primary Accession | P63165 |
| Other Accession | Q5I0H3, A7WLH8, P63166, Q5E9D1, NP_001005781.1, NP_003343.1 |
| Reactivity | Human |
| Predicted | Bovine, Mouse, Pig, Rat |
| Host | Rabbit |
| Clonality | Polyclonal |
| Isotype | Rabbit IgG |
| Calculated MW | 11557 Da |
| Antigen Region | 1-30 aa |
| 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 a KLH conjugated synthetic peptide between 1-30 amino acids from the N-terminal region of human SUMO1. |
| Dilution | IF~~1:10~50 WB~~1:1000 IHC-P~~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 (N-term) 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
This gene encodes a protein that is a member of the SUMO (small ubiquitin-like modifier) protein family. It functions in a manner similar to ubiquitin in that it is bound to target proteins as part of a post-translational modification system. However, unlike ubiquitin which targets proteins for degradation, this protein is involved in a variety of cellular processes, such as nuclear transport, transcriptional regulation, apoptosis, and protein stability. It is not active until the last four amino acids of the carboxy-terminus have been cleaved off. Several pseudogenes have been reported for this gene. Alternate transcriptional splice variants encoding different isoforms have been characterized.
References
Jia, Z.L., et al. DNA Cell Biol. 29(11):675-680(2010) Kang, X., et al. Oncogene 29(41):5568-5578(2010) Bailey, S.D., et al. Diabetes Care 33(10):2250-2253(2010) Cox, B., et al. PLoS ONE 5 (8), E11996 (2010) : Jugessur, A., et al. PLoS ONE 5 (7), E11493 (2010) :
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