Anti-CHORDC1 Antibody

The cysteine and histidine-rich domain (CHORD) -containing protein (CHORDC1) is a member of a highly conserved protein family that contains the plant protein RAR1 and the mammalian protein melusin. In mammals, CHORDC1 is an ADP-dependent HSP90-interacting protein, and this interaction is dependent on the ability of HSP90 to bind nucleotides. Recent experiments indicate that CHORDC1 mRNA is diurnally regulated in mouse hypothalamus, and that this regulation alters during development, suggesting that CHORDC1 may play a role in circadian mechanisms in the mammalian brain.

CHORDC1 antibody was raised against a 21 amino acid synthetic peptide near the amino terminus of human CHORDC1. The immunogen is located within amino acids 50 - 100 of CHORDC1.

Regulates centrosome duplication, probably by inhibiting the kinase activity of ROCK2. Proposed to act as co-chaperone for HSP90. May play a role in the regulation of NOD1 via a HSP90 chaperone complex. In vitro, has intrinsic chaperone activity. This function may be achieved by inhibiting association of ROCK2 with NPM1. Involved in stress response. Prevents tumorigenesis.

CHORDC1 antibody can be stored at 4°C for three months and -20°C, stable for up to one year. Avoid repeated freeze-thaw cycles. Antibodies should not be exposed to prolonged high temperatures.