Product Pathways - Protein Stability
SUMO-1 (C9H1) Rabbit mAb #4940
|W IP IHC-P||H M R Mk||Endogenous||Rabbit IgG|
Reactivity Key: H=Human M=Mouse R=Rat Mk=Monkey
Species cross-reactivity is determined by western blot. Species enclosed in parentheses are predicted to react based on 100% sequence homology.
Specificity / Sensitivity
SUMO-1 (C9H1) Rabbit mAb detects recombinant SUMO-1 and endogenous levels of sumoylated proteins (e.g. SUMO-1-RanGAP at 90 kD). This antibody does not detect recombinant SUMO-2 or SUMO-3.
Source / Purification
Monoclonal antibody is produced by immunizing animals with a synthetic peptide from the amino terminus of human SUMO-1.
Western blot analysis of recombinant GST-SUMO-1 protein (38 kDa) and extracts from Jurkat cells using SUMO-1 (C9H1) Rabbit mAb.
Small ubiquitin-related modifier 1, 2 and 3 (SUMO-1, -2 and -3) are members of the ubiquitin-like protein family (1). The covalent attachment of the SUMO-1, -2 or -3 (SUMOylation) to target proteins is analogous to ubiquitination. This post-translational modification is a reversible, multi-step process that is initiated by cleaving a precursor protein to a mature protein. Mature SUMO-1, -2 or -3 is then linked to the activating enzyme E1, conjugated to E2 and in conjunction with E3, SUMO-1, -2 or -3 is ligated to the target protein (2). Ubiquitin and the individual SUMO family members are all targeted to different proteins with diverse biological functions. Ubiquitin predominantly regulates degradation of its target (1). In contrast, SUMO-1 is conjugated to RanGAP, PML, p53 and IκB-α to regulate nuclear trafficking, formation of subnuclear structures, regulation of transcriptional activity and protein stability (3-7). SUMO-2/-3 forms poly-(SUMO) chains, is conjugated to topoisomerase II and APP, regulates chromosomal segregation and cellular responses to environmental stress, and plays a role in the progression of Alzheimer disease (8-11).
- Schwartz, D.C. and Hochstrasser, M. (2003) Trends Biochem. Sci. 28, 321-328.
- Kim, K.I. et al. (2002) J. Cell Physiol. 191, 257-268.
- Matunis, M.J. et al. (1996) J. Cell Biol. 135, 1457-1470.
- Duprez, E. et al. (1999) J. Cell Sci. 112, 381-393.
- Gostissa, M. et al. (1999) EMBO J. 18, 6462-6474.
- Rodriguez, M.S. et al. (1999) EMBO J. 18, 6455-6461.
- Desterro, J.M. et al. (1998) Mol. Cell 2, 233-239.
- Tatham, M.H. et al. (2001) J. Biol. Chem. 276, 35368-35374.
- Azuma, Y. et al. (2003) J. Cell Biol. 163, 477-487.
- Li, Y. et al. (2003) Proc. Natl. Acad. Sci. USA 100, 259-264.
- Saitoh, H. and Hinchey, J. (2000) J. Biol. Chem. 275, 6252-6258.
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For Research Use Only. Not For Use In Diagnostic Procedures.