|Other Names||Homocysteine-responsive endoplasmic reticulum-resident ubiquitin-like domain member 1 protein, Methyl methanesulfonate (MMF)-inducible fragment protein 1, HERPUD1, HERP, KIAA0025, MIF1|
|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.|
|Synonyms||HERP, KIAA0025, MIF1|
|Function||Component of the endoplasmic reticulum quality control (ERQC) system also called ER-associated degradation (ERAD) involved in ubiquitin-dependent degradation of misfolded endoplasmic reticulum proteins. Could enhance presenilin-mediated beta-amyloid protein 40 generation. Binds to ubiquilins and this interaction is required for efficient degradation of CD3D via the ERAD pathway (PubMed:18307982).|
|Cellular Location||Endoplasmic reticulum membrane; Multi-pass membrane protein|
|Tissue Location||Widely expressed; in the brain, expression seems to be restricted to neurons and vascular smooth muscle cells. Present in activated microglia in senile plaques in the brain of patients with Alzheimer disease|
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The accumulation of unfolded proteins in the endoplasmicreticulum (ER) triggers the ER stress response. This responseincludes the inhibition of translation to prevent furtheraccumulation of unfolded proteins, the increased expression ofproteins involved in polypeptide folding, known as the unfoldedprotein response (UPR), and the destruction of misfolded proteinsby the ER-associated protein degradation (ERAD) system. This genemay play a role in both UPR and ERAD. Its expression is induced byUPR and it has an ER stress response element in its promoter regionwhile the encoded protein has an N-terminal ubiquitin-like domainwhich may interact with the ERAD system. This protein has beenshown to interact with presenilin proteins and to increase thelevel of amyloid-beta protein following its overexpression.Alternative splicing of this gene produces multiple transcriptvariants, some encoding different isoforms. The full-length natureof all transcript variants has not been determined. [provided byRefSeq].
Hirabayashi, Y., et al. J. Immunol. 184(6):3276-3283(2010)McLaughlin, M., et al. J. Biol. Chem. 285(10):6960-6969(2010)Zabaneh, D., et al. PLoS ONE 5 (8), E11961 (2010) :Ridker, P.M., et al. Circ Cardiovasc Genet 2(1):26-33(2009)Heid, I.M., et al. Circ Cardiovasc Genet 1(1):10-20(2008)
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