|Application ||WB, E|
|Calculated MW||10820 Da|
|Antigen Region||1-30 aa|
|Other Names||Small ubiquitin-related modifier 2-A, SUMO-2-A, sumo2-a, smt3h2|
|Target/Specificity||This Xenopus SUMO2 antibody is generated from rabbits immunized with a KLH conjugated synthetic peptide between 1-30 amino acids from the N-terminal region of human Xenopus SUMO2.|
|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||Xenopus SUMO2 Antibody (N-term) is for research use only and not for use in diagnostic or therapeutic procedures.|
|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. 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.|
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Provided below are standard protocols that you may find useful for product applications.
SUMO2 is a ubiquitin-like protein which can be covalently attached to target lysines either as a monomer or as a lysine-linked polymer. SUMO2 does not seem to be involved in protein degradation and may function as an antagonist of ubiquitin in the degradation process. This protein 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 E3 ligases such as PIAS isoforms 1-4.
Muller S, et al., Nat Rev Mol Cell Biol. 2001 2(3):202-10 Review.
Hochstrasser M. Cell. 2001 107(1):5-8. Review.
Kahyo T, et al., Mol Cell. 2001 Sep;8(3):713-8.
Yeh ET, et al., Gene. 2000 May 2;248(1-2):1-14. Review.
Keane,M.M., et al., Oncogene 18 (22), 3365-3375 (1999)
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