Human Calreticulin Alexa Fluor® 594-conjugated Antibody

Applications

Please Note: Optimal dilutions should be determined by each laboratory for each application. General Protocols are available in the Technical Information section on our website.

Preparation and Storage

Background: Calreticulin

Human Calreticulin is a 55‑60 kDa, 400 amino acid, variably glycosylated intra- and extracellular Ca⁺⁺-binding lectin that is ubiquitously expressed. It consists of three domains: a 180 aa N-terminal globular region, a 111 aa P-, or proline rich domain, and a 109 aa C-terminus. The 180 aa N-terminus (aa 18‑197) is termed Vasostatin. It is unclear if it is ever generated naturally via proteolytic processing. Vasostatin domain has many functions. It binds to RNA (aa 18‑27), has autocatalytic phosphorylase activity (aa 77‑197), binds to a KxFFKR motif on steroid hormone receptors, and serves as a lectin-type chaperone for ER-localized molecules. It also shows antiangiogenic activity, presumably by binding to laminin carbohydrates and blocking endothelial cell adhesion and proliferation. Human Calreticulin is 94% aa identical to mouse and rat Calreticulin.

Product Datasheets

Related Research Areas

• Calcium-binding Proteins and Related Molecules
• Focal Adhesions
• Granzyme-mediated Cell Death
• Platelet Immune Receptors