Anti-Derlin-1 pAb

WB - 1:1,000 (chemiluminescence detection system) IP - 1 uL/250 uL of cell extract from 5x106 cells ICC - 1:50

Many proteins of eukaryotic cells undergo folding and modification in the endoplasmic reticulum (ER). Properly folded polypeptides leave the ER along the secretory pathway, whereas misfolded proteins or unassembled protein complexes are retained. These proteins are eventually degraded by proteasomes and must therefore be transported back into the cytosol by a multi-step process called retro-translocation, dislocation, or ERAD (ER-associated protein degradation). The S. cerevisiae Der1 was identified in a genetic screen for components required for the degradation of misfolded luminal ER proteins and the Der1 homologue Derlin-1 is found in every eukaryotic organism. All species contain at least one other related protein, called Derlin-2, that belongs to a distinct group. Mammalian Derlin-1 is predicted to have four transmembrane segments with both the amino and carboxy termini in the cytosol.

100 ul volume of PBS containing 50% glycerol, pH 7.2. No preservative is contained.

Human: 79139

Derlin-1 C-terminal peptide binding KLH (239-251 aa)

This antibody reacts with Derlin-1 (28 kDa) on Western blotting.

1 year

This antibody was purified from rabbit serum using an ion exchange chromatography. The rabbit was immunized with KLH-conjugated Derlin-1 C-terminal peptides (239-251 aa).

Derlin-1