Calreticulin Mouse, Unlabeled, Clone: 16, BD

Description

• 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 Ca 2+ ;, Zn 2+ , 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 Ca 2+ ; storage, cell adhesion, and protein folding
• Immunofluorescence, Western Blotting