Calreticulin Mouse, Unlabeled, Clone: 16, Bd, Mouse Monoclonal Antibody, Each

Details:

Proteins undergo numerous modifications, including folding, translocation, and degradation. During such modifications, polypeptides are rarely in a native, stable state. Molecular chaperones are a diverse group of proteins that modulate polypeptide stability through atp-dependent folding. Many chaperone proteins are found in the endoplasmic reticulum (er). Calreticulin is a luminal er protein that is 39% homologous to the er chaperone protein, calnexin. Calreticulin contains a c-terminal kdel er retention signal, and can bind ca2+;, zn2+, atp, and the proteins, erp57 and protein disulfide isomerase. The molecular chaperone activities of calreticulin may include folding of both asn-linked glycoproteins and non-glycosylated proteins. In addition, calreticulin is a component of mhc i/transporter associated with ag presentation (tap) complex where it may function in peptide assembly onto nascent class i molecules. Calreticulin may also function in integrin signaling, since it binds a3-integrin subunits and regulates integrin-mediated metalloprotease secretion. Thus, calreticulin may be involved in ca2+; storage, cell adhesion, and protein folding.Immunofluorescence, western blotting