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>   首页   >   产品   >   一抗   >   细胞生物学   >   SUMO2/3 Antibody (N-term)   

SUMO2/3 Antibody (N-term)

Purified Rabbit Polyclonal Antibody (Pab)

     
  • 1 - SUMO2/3 Antibody (N-term) AP1223a
    All lanes : Anti-SUMO2/3 Antibody (M1) at 1:2000 dilution Lane 1: A549 whole cell lysates Lane 2: Hela whole cell lysates Lane 3: HepG2 whole cell lysates Lane 4: HL-60 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:
  • E=ELISA
  • WB=Western Blotting
  • IHC=Immunohistochemistry
  • IHC-P=Immunohistochemistry (Paraffin)
  • IP=Immunoprecipitation
  • IF=Immunofluorescence
  • IC=Immunochemistry
  • ICC=Immunocytochemistry
  • FC=Flow Cytometry
  • DB=Dot Blot
WB, E
Primary Accession P61956
Other Accession Q6KAQ7, Q8IYH5, Q5SSH7, O43149, A5H447, Q62523, Q15942, Q04584, G5EEM5, Q9GT24, A0JMZ3, Q5TYQ1, P21541, Q3UFS0, Q9C0D3, A2BFL2, Q6WRX3, Q8C8V1, Q2QGD7, P98169, P98168, A2CE44, Q8VIL3, Q9CQU5, O95229, Q2TBH8, Q6IRM9, Q8R060, Q9H900, Q9VA00, A5WWB6, Q95XP9
Reactivity Human, Rat, Mouse
Predicted Drosophila, C.Elegans, Bovine, Chicken, Human, Monkey, Mouse, Rat, Rabbit, Xenopus, Zebrafish, Yeast, Pig, Vaccinia Virus, Hamster, Neisseria Gonorrhoeae, SARS
Host Rabbit
Clonality Polyclonal
Isotype Rabbit IgG
Calculated MW 10871 Da
Additional Information
Gene ID 6613
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~~1:2000
E~~Use at an assay dependent concentration.
Format Purified monoclonal antibody supplied in PBS with 0.09% (W/V) sodium azide. This antibody is purified through a protein G column, 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.
PrecautionsSUMO2/3 Antibody (N-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..
Research Areas

For Research Use Only. Not For Use In Diagnostic Procedures.

BACKGROUND

SUMO2 and SUMO3 are members 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). Mannen, H., et al., Biochem. Biophys. Res. Commun. 222(1):178-180 (1996).

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