|Other Names||Small ubiquitin-related modifier 4, SUMO-4, Small ubiquitin-like protein 4, SUMO4, SMT3H4|
|Format||Synthetic peptide was lyophilized with 100% acetonitrile and is supplied as a powder. Reconstitute with 0.1 ml DI water for a final concentration of 1 mg/ml.|
|Storage||Maintain refrigerated at 2-8°C for up to 6 months. For long term storage store at -20°C.|
|Precautions||This product is for research use only. Not for use in diagnostic or therapeutic procedures.|
|Function||Ubiquitin-like protein which can be covalently attached to target lysines as a monomer. Does not seem to be involved in protein degradation and may modulate protein subcellular localization, stability or activity. Upon oxidative stress, conjugates to various anti-oxidant enzymes, chaperones, and stress defense proteins. May also conjugate to NFKBIA, TFAP2A and FOS, negatively regulating their transcriptional activity, and to NR3C1, positively regulating its transcriptional activity. Covalent attachment to its substrates requires prior activation by the E1 complex SAE1-SAE2 and linkage to the E2 enzyme UBE2I.|
|Tissue Location||Expressed mainly in adult and embryonic kidney. Expressed at various levels in immune tissues, with the highest expression in the lymph node and spleen|
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Provided below are standard protocols that you may find useful for product applications.
SUMO4 is a member of the mucin family and encodes a membrane bound, glycosylated phosphoprotein. The protein is anchored to the apical surface of many epithelia by a transmembrane domain, with the degree of glycosylation varying with cell type. It also includes a 20 aa variable number tandem repeat (VNTR) domain, with the number of repeats varying from 20 to 120 in different individuals. The protein serves a protective function by binding to pathogens and also functions in a cell signaling capacity. Overexpression, aberrant intracellular localization, and changes in glycosylation of this protein have been associated with carcinomas.
Li, Y., et al. Am. J. Physiol. Lung Cell Mol. Physiol. 298 (4), L558-L563 (2010) Sachdeva, M., et al. Cancer Res. 70(1):378-387(2010)Ricci, A., et al. Sarcoidosis Vasc Diffuse Lung Dis 26(1):54-63(2009)
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