Recombinant Mouse CACHD1 Fc Chimera Protein, CF

Recombinant Mouse CACHD1 Fc Chimera Protein, CF Summary

Product Specifications

Product Datasheets

Carrier Free

CF stands for Carrier Free (CF). We typically add Bovine Serum Albumin (BSA) as a carrier protein to our recombinant proteins. Adding a carrier protein enhances protein stability, increases shelf-life, and allows the recombinant protein to be stored at a more dilute concentration. The carrier free version does not contain BSA.

In general, we advise purchasing the recombinant protein with BSA for use in cell or tissue culture, or as an ELISA standard. In contrast, the carrier free protein is recommended for applications, in which the presence of BSA could interfere.

Background: CACHD1

CACHD1 (Ca2+ channel and chemotaxis receptor Domain Containing 1) is a alpha 2δ-Like Protein that modulates CaV3 voltage-gated calcium channel activity (1, 2). Mature Mouse CACHD1 consists of a 1060 amino acid (aa) extracellular domain (ECD), a 21 aa transmembrane segment, and a 158 aa cytoplasmic domain. The ECD contains a von Willebrand factor A (VWA) domain and two bacterial chemosensory-like cache domains. Within the ECD, mouse CACHD1 shares 97.5% and 99.7% aa sequence identity with human and rat CACHD1, respectively. Diseases associated with CACHD1 include Cercarial Dermatitis and Hypertropia. CACHD1 increases the presence of CaV3.1 at the cell surface and causes an increase in channel open probability (2). CACHD1 is a new activity-modifying protein for voltage-gated calcium channels (2). Such physiological actions may have implications in targeting diseases involving aberrant neuronal firing, as CaV3 channels have been proposed as therapeutic targets to combat pain and epilepsy (2). CACHD1 and MDGA1 are novel in vivo substrates for beta-site APP cleaving enzyme 1 (BACE1), suggesting that cleavage of both proteins may contribute to the numerous functions of BACE1 in the nervous system (3). BACE1 inhibition is a major therapeutic approach for Alzheimer disease (3). CACHD1 closely interacts with voltage-gated calcium channels of the N-type58 and T-type59 at the cell surface and enhances the densities of their calcium currents (3). BACE1 cleavage is a mechanism to control CACHD1's function in calcium signaling and synaptic transmission (3). Expression of CACHD1 increased both CaV2.2 currents and cell surface trafficking in both cell lines and neurons (4). CACHD1 competed with a2d-1 for binding to CaV2.2 and for its functional effects and can therefore inhibit responses to a2d-1 (4). CACHD1 is widely expressed in many tissues, including the brain, lungs, and small intestine (4). CACHD1 contains a VWA domain that has a disrupted metal ion-dependent adhesion site (MIDAS) motif, a sequence that is conserved in the human, rat, mouse, and zebrafish CACHD1 proteins (4). At the Wnt Signaling Gordon Conference in August 2019, Yvonne Jones (Oxford) presented an unpublished crystal structure of the transmembrane proteins CACHD1 in a complex between LRP6 and Fz5. Their data suggest that CACHD1 is an inhibitor of Wnt signaling.