Product Pathways - Protein Stability
Derlin-1 Antibody #8897
|8897S||100 µl (10 western blots)||---||In Stock||---|
|8897||carrier free and custom formulation / quantity||email request|
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|W||1:1000||Human, Mouse, Rat, Monkey||Endogenous||22||Rabbit|
Species cross-reactivity is determined by western blot.
Applications Key: W=Western Blotting, IP=Immunoprecipitation
Species predicted to react based on 100% sequence homology: Bovine, Dog, Pig, Guinea Pig, Horse.
Specificity / Sensitivity
Derlin-1 Antibody recognizes endogenous levels of total Derlin-1 protein. Based upon sequence alignment, this antibody is not predicted to cross-react with either Derlin-2 or Derlin-3.
Source / Purification
Polyclonal antibodies are produced by immunizing animals with a synthetic peptide corresponding to residues near the carboxy terminus of human Derlin-1 protein. Antibodies are purified by protein A and peptide affinity chromatography.
Western blot analysis of extracts from 293T cells, either mock transfected (-) or transfected with a Myc/DDK-tagged cDNA expression construct encoding full-length human Derlin-1 (hDerlin-1-Myc/DDK; +), using Derlin-1 Antibody.
Elimination of misfolded proteins from the endoplasmic reticulum (ER) occurs largely through the ER-associated degradation (ERAD) pathway and is an important physiological adaptation to ER stress. After insertion into the lumen of the ER, glycoproteins that fail to fold properly are destined for degradation. Through a process termed retro-translocation, misfolded proteins are deposited into the cytosol from the ER, where ubiquitination, deglycosylation, and proteasomal proteolysis lead to their degradation. Derlin-1 (Der1-like protein) corresponds to a homologue of yeast Der1p, a protein identified in a genetic screen for components required for the degradation of misfolded ER luminal proteins (1). Like yeast Der1p, mammalian Derlin-1 is an ER protein that is predicted to have four transmembrane segments with both the amino and carboxy termini exposed to the cytoplasmic compartment (2-4). Derlin-1 appears to be a central, evolutionarily conserved membrane component of the retro-translocation machinery associated with the ERAD pathway. Indeed, studies have shown that Derlin-1 expression is transcriptionally upregulated in response to ER stress (5-7) and associates with ER-anchored ubiquitin ligases, such as HRD1 and gp78/AMFR, via binding to p97/VCP and VCP-interacting membrane protein (VIMP) (5,8).
- Knop, M. et al. (1996) EMBO J 15, 753-63.
- Hitt, R. and Wolf, D.H. (2004) FEMS Yeast Res 4, 721-9.
- Lilley, B.N. and Ploegh, H.L. (2004) Nature 429, 834-40.
- Ye, Y. et al. (2004) Nature 429, 841-7.
- Lilley, B.N. and Ploegh, H.L. (2005) Proc Natl Acad Sci USA 102, 14296-301.
- Travers, K.J. et al. (2000) Cell 101, 249-58.
- Oda, Y. et al. (2006) J Cell Biol 172, 383-93.
- Ye, Y. et al. (2005) Proc Natl Acad Sci USA 102, 14132-8.
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For Research Use Only. Not For Use In Diagnostic Procedures.
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