Anti-Derlin-2 antibody produced in rabbit

Derlin-1, Derlin-2, and Derlin-3 are the mammalian homologues of yeast Der1p, a transmembrane protein required for yeast endoplasmic reticulum-associated degradation (ERAD). Derlin-2 is approximately 30% identical to Derlin-1. In rat Derlin-2 is present to the endoplasmic reticulum(ER) membrane and forms a multisubunit complex with other proteins.

synthetic peptide corresponding to amino acid residues 223-239 of human derlin-2 conjugated to KLH via an N-terminal added cysteine residue. The corresponding sequence is identical in mouse.

Anti-Derlin-2 antibody produced in rabbit has been used in immunoblotting and immunofluorescence.

Derlin-2, also known as F-LANa, is involved in the degradation of misfolded glycoproteins in the ER. Derlin-2 shares ~30% sequence identity with Derlin-1 and spans the lipid bilayer of the ER four times, showing structural similarity to Derlin-1. It is a component of the mammalian ER-associated degradation (ERAD) mechanism and is upregulated by unfolded protein response (UPR). Overexpression of this gene leads to increase in degradation of misfolded glycoprotein, whereas its knockdown blocks degradation. Derlin-2 also interacts with the mammalian orthologs of the yeast Hrd1p/Hrd3p ubiquitin-ligase complex.

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

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