Anti-Derlin-1 antibody produced in rabbit

Derlin-1 is a 22kDa hydrophobic protein that spans the lipid bilayer of the ER four times with its amino- and carboxy-terminus in the cytosol. It is expressed with high levels in liver, spleen, pancreas, lung, thymus, and ovary.

Derlin-1 shares human homology with yeast Der1p.

a synthetic peptide corresponding to the C-terminal region of human Derlin-1 with N-terminal added cysteine, conjugated to KLH. The corresponding sequence is identical in mouse.

Anti-Derlin-1 antibody produced in rabbit has been used in:

• immunostaining
• co-immunoprecipitation
• immunofluorescence

Derlin-1 can interact with peptide:N-glycanase (PNGase), a deglycosylating enzyme, bringing it close to misfolding dislocating glycoproteins.

Derlin-1 is required for the dislocation of misfolded proteins from the ER lumen to the cytosol, where they are destroyed by the ubiquitin-proteasome system. It interacts with PNGase, a deglycosylating enzyme, bringing it close to misfolding dislocating glycoproteins. It forms a membrane protein complex with VIMP ( (VCP-interacting membrane protein) and this complex serves as a receptor for p97. p97 interacts with several ubiquitin ligases, thus recruiting them to Derlin-1.

Solution in 0.01 M phosphate buffered saline, pH 7.4, containing 15 mM sodium azide.

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