RNF40 Antibody (monoclonal) (M09)
Mouse monoclonal antibody raised against a partial recombinant RNF40.
|Application ||WB, IF, E|
|Calculated MW||113650 Da|
|Other Names||E3 ubiquitin-protein ligase BRE1B, BRE1-B, 632-, 95 kDa retinoblastoma-associated protein, RBP95, RING finger protein 40, RNF40, BRE1B, KIAA0661|
|Target/Specificity||RNF40 (NP_055586, 102 a.a. ~ 200 a.a) partial recombinant protein with GST tag. MW of the GST tag alone is 26 KDa.|
|Format||Clear, colorless solution in phosphate buffered saline, pH 7.2 .|
|Storage||Store at -20°C or lower. Aliquot to avoid repeated freezing and thawing.|
|Precautions||RNF40 Antibody (monoclonal) (M09) is for research use only and not for use in diagnostic or therapeutic procedures.|
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Provided below are standard protocols that you may find useful for product applications.
The protein encoded by this gene contains a RING finger, a motif known to be involved in protein-protein and protein-DNA interactions. This protein was reported to interact with the tumor suppressor protein RB1. Studies of the rat counterpart suggested that this protein may function as an E3 ubiquitin-protein ligase, and facilitate the ubiquitination and degradation of syntaxin 1, which is an essential component of the neurotransmitter release machinery.
Defining the human deubiquitinating enzyme interaction landscape. Sowa ME, et al. Cell, 2009 Jul 23. PMID 19615732.RAD6-Mediated transcription-coupled H2B ubiquitylation directly stimulates H3K4 methylation in human cells. Kim J, et al. Cell, 2009 May 1. PMID 19410543.Global, in vivo, and site-specific phosphorylation dynamics in signaling networks. Olsen JV, et al. Cell, 2006 Nov 3. PMID 17081983.Monoubiquitination of human histone H2B: the factors involved and their roles in HOX gene regulation. Zhu B, et al. Mol Cell, 2005 Nov 23. PMID 16307923.Signal sequence and keyword trap in silico for selection of full-length human cDNAs encoding secretion or membrane proteins from oligo-capped cDNA libraries. Otsuki T, et al. DNA Res, 2005. PMID 16303743.
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