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SUMO2 Antibody (C-term)

Purified Rabbit Polyclonal Antibody (Pab)

     
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  • WB - SUMO2 Antibody (C-term) AW5458-U100
    All lanes : Anti-SUMO2 Antibody at 1:1000 dilution Lane 1: 293T whole cell lysates Lane 2: HL-60 whole cell lysates Lane 3: Jurkat whole cell lysates Lysates/proteins at 20 µg per lane. Secondary Goat Anti-Rabbit IgG, (H+L),Peroxidase conjugated at 1/10000 dilution Predicted band size : 11 kDa Blocking/Dilution buffer: 5% NFDM/TBST.
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Product Information
Application
  • Applications Legend:
  • WB=Western Blot
  • IHC=Immunohistochemistry
  • IHC-P=Immunohistochemistry (Paraffin-embedded Sections)
  • IHC-F=Immunohistochemistry (Frozen Sections)
  • IF=Immunofluorescence
  • FC=Flow Cytopmetry
  • IC=Immunochemistry
  • ICC=Immunocytochemistry
  • E=ELISA
  • IP=Immunoprecipitation
  • DB=Dot Blot
  • CHIP=Chromatin Immunoprecipitation
  • FA=Fluorescence Assay
  • IEM=Immuno electron microscopy
  • EIA=Enzyme Immunoassay
WB
Primary Accession P61956
Other Accession Q7SZ22, Q5XIF4, Q9Z172, P55854, Q6DI05, Q5ZHQ1, Q17QV3, P61959, P61958, P61957, Q2PFW2, Q6DHL4, Q6LDZ8, Q5ZJM9, P61955, Q6NV25, Q6GPW2, Q7ZTK7
Reactivity Human
Predicted Xenopus, Zebrafish, Bovine, Chicken, Hamster, Monkey, Mouse, Pig, Rat
Host Rabbit
Clonality Polyclonal
Calculated MW H=11;M=11;R=11 KDa
Isotype Rabbit IgG
Antigen Source HUMAN
Additional Information
Gene ID 6613
Antigen Region 63-93 aa
Other Names Small ubiquitin-related modifier 2, SUMO-2, HSMT3, SMT3 homolog 2 {ECO:0000312|HGNC:HGNC:11125}, SUMO-3, Sentrin-2, Ubiquitin-like protein SMT3B, Smt3B, SUMO2 (HGNC:11125)
Dilution WB~~1:1000
Target/Specificity This SUMO2 antibody is generated from rabbits immunized with a KLH conjugated synthetic peptide between 63-93 amino acids from the C-terminal region of human SUMO2.
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.
StorageMaintain 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.
PrecautionsSUMO2 Antibody (C-term) is for research use only and not for use in diagnostic or therapeutic procedures.
Protein Information
Name SUMO2 (HGNC:11125)
Function Ubiquitin-like protein that can be covalently attached to proteins as a monomer or as 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 an E3 ligase such as PIAS1-4, RANBP2, CBX4 or ZNF451 (PubMed:26524494). 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. Polymeric SUMO2 chains are also susceptible to polyubiquitination which functions as a signal for proteasomal degradation of modified proteins (PubMed:18408734, PubMed:18538659, PubMed:21965678, PubMed:9556629). Plays a role in the regulation of sumoylation status of SETX (PubMed:24105744).
Cellular Location Nucleus. Nucleus, PML body.
Tissue Location Broadly expressed..
Citations (0)
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Background

SUMO2 is a member of the SUMO (small ubiquitin-like modifier) protein family. This protein family 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. In vertebrates, three members of the SUMO family have been described, SUMO 1 and the functionally distinct homologues SUMO 2 and SUMO 3. SUMO modification sites present in the N terminal regions of SUMO 2 and SUMO 3 are utilized by SAE1/SAE2 (SUMO E1) and Ubc9 (SUMO E2) to form polymeric chains of SUMO 2 and SUMO 3 on protein substrates, a property not shared by SUMO 1.

References

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).

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$ 370.00
Cat# AW5458-U100
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