CHORDC1 / Unconjugated /
Product Details
| Description | 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. | |
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| Conjugate | Unconjugated | |
| Clone | ||
| Target Species | Human, Mouse, Rat | |
| Applications | ELISA, ICC, WB | |
| Supplier | Aviva Systems Biology | |
| Catalog # | Sign in to view product details, citations, and spectra | |
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About CHORDC1
Enables Hsp90 protein binding activity. Predicted to be involved in centrosome duplication; chaperone-mediated protein folding; and regulation of cellular response to heat. [provided by Alliance of Genome Resources, Apr 2022]
Enables Hsp90 protein binding activity. Predicted to be involved in centrosome duplication; chaperone-mediated protein folding; and regulation of cellular response to heat. [provided by Alliance of Genome Resources, Apr 2022]
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