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SUMO2SUMO3 (Small ubiquitin-related modifier 2 and 3) (N-Term) antibody
Alternatives Immunohistochemistry (IHC), Western Blotting (WB)
|5 references available|
|Price||454.67 $ Plus shipping costs $45.00|
|Availability||Will be delivered in 7 to 8 Business Days|
|Immunogen||A synthetic peptide from the n-terminal of rat SUMO2 & SUMO3 (Small ubiquitin-related modifier 2 and 3) conjugated to an immunogenic carrier protein was used as the immunogen. The antigen is homologous in many species including human, mouse and chicken.|
|Description||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 Subcellular location: Nucleus Also known as: Small ubiquitin-related modifier 2, SUMO-2, Ubiquitin-like protein SMT3B, SMT3 homolog 2, Sentrin-2, Smt3b, Smt3h2; SUMO-3, SUMO 3, Small ubiquitin-related modifier 3.|
|Specificity||Appears to be specific for SUMO2 and SUMO3.|
|Application Notes||IHC, WB. A concentration of 10-50 µg/ml is recommended. The optimal concentration should be determined by the end user. Not yet tested in other applications.|
|Storage||Maintain the lyophilised/reconstituted antibodies frozen at -20°C for long term storage and refrigerated at 2-8°C for a shorter term. When reconstituting, glycerol (1:1) may be added for an additional stability. Avoid freeze and thaw cycles.|
|Restrictions||For Research Use only|
Chen, Mannen, Li: "Characterization of mouse ubiquitin-like SMT3A and SMT3B cDNAs and gene/pseudogenes." in: Biochemistry and molecular biology international, Vol. 46, Issue 6, pp. 1161-74, 1999 (PubMed).
Carninci, Kasukawa, Katayama et al.: "The transcriptional landscape of the mammalian genome." in: Science (New York, N.Y.), Vol. 309, Issue 5740, pp. 1559-63, 2005 (PubMed).
Rosendorff, Sakakibara, Lu et al.: "NXP-2 association with SUMO-2 depends on lysines required for transcriptional repression." in: Proceedings of the National Academy of Sciences of the United States of America, Vol. 103, Issue 14, pp. 5308-13, 2006 (PubMed).
Zody, Garber, Adams et al.: "DNA sequence of human chromosome 17 and analysis of rearrangement in the human lineage." in: Nature, Vol. 440, Issue 7087, pp. 1045-9, 2006 (PubMed).
Baba, Maita, Jee et al.: "Crystal structure of SUMO-3-modified thymine-DNA glycosylase." in: Journal of molecular biology, Vol. 359, Issue 1, pp. 137-47, 2006 (PubMed).