|Detection of Human, Mouse, and Rat CIB1 by Western Blot. Western blot shows lysates of human spleen tissue, mouse kidney tissue, and rat kidney tissue. PVDF membrane was probed with 1 µg/mL of Sheep Anti-Human/Mouse/Rat CIB1 Antigen Affinity-purified Polyclonal Antibody (Catalog # AF7557) followed by HRP-conjugated Anti-Sheep IgG Secondary Antibody (Catalog # HAF016). A specific band was detected for CIB1 at approximately 22 kDa (as indicated). This experiment was conducted under reducing conditions and using Immunoblot Buffer Group 1.|
CIB1 (Calcium and Integrin-Binding protein 1; also calmyrin, KIP and CIBP) is a 22-23 kDa, Ca++-binding member of the CIB family of proteins. It is widely expressed, being found in neurons, platelets/megakaryocytes, skeletal muscle myocytes and lymphocytes. CIB1 is associated with the cytosolic side of the plasma membrane, and has multiple binding partners, including InsP3R, GPIIb/ alpha IIb, presenilin 2, and NBR1 plus FEZ. When CIB1 binds InsP3R, this ER-embedded receptor is both activated, and later desensitized to subsequent ligand binding. Relative to GPIIb, CIB1 interaction with the alpha IIb beta 3 integrin on platelets following thrombin exposure appears to inhibit integrin activation, thus providing a tight control on subsequent platelet binding to fibrinogen. Human CIB1 is 191 amino acids (aa) in length. It contains a utilized myristoylation site at Gly2, followed by two EF-hand domains (aa 103-183). CIB1 is suggested to act as a monomer. There is at least one potential isoform variant that shows a 40 aa insertion after Lys29. Full-length human CIB1 (aa 1-191) shares 94% aa sequence identity with mouse CIB1.
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