Invitrogen™ CD157 Monoclonal Antibody (eBioSY11B5 (SY11B5)), PE, eBioscience™, Invitrogen™

Beskrivning

Description: The eBioSY11B5 monoclonal antibody recognizes human CD157 (Mo5, BST-1). CD157 is a 42-45 kDa, GPI-anchored protein with structural and functional similarities with CD38. CD157 was initially cloned because of its expression on monocytes and macrophages, and was subsequently discovered to be the same protein named BST-1, discovered for its expression on bone marrow stromal cells and its ability to stimulate the proliferation of a mouse pre-B cell line. CD157 is a pleiotropic ectoenzyme and is thought to act independently as an enzyme and receptor. Similar to CD38, CD157 is involved in the metabolism of NAD+ and this activity may be involved in regulating intracellular Ca2+ levels. As a receptor, upon binding of its putative ligand, CD157 is thought to initiate a signal transduction cascade resulting in the phosphorylation of cytoplasmic proteins including focal adhesion kinase (FAK). The mechanism and functional significance of CD157-initiated signal transduction remain to be fully characterized. Applications Reported: This eBioSY11B5 (SY11B5) antibody has been reported for use in flow cytometric analysis. Applications Tested: This eBioSY11B5 (SY11B5) antibody has been pre-titrated and tested by flow cytometric analysis of normal human peripheral blood cells. This can be used at 5 μL (0.125 μg) per test. A test is defined as the amount (μg) of antibody that will stain a cell sample in a final volume of 100 μL.

CD157, also known as Bone Marrow Stromal Cell Antigen 1 (BST1), is a pleiotropic ectoenzyme and glycosylphosphatidylinositol-anchored molecule that functions both as an enzyme and a receptor. Similar to CD38, CD157 is involved in the metabolism of NAD+, which may play a role in regulating intracellular Ca2+ levels. As an enzyme, CD157 is also referred to as ADP-ribosyl cyclase 2 and DAMP-1, and it facilitates pre-B cell growth. As a receptor, CD157 is thought to initiate a signal transduction cascade upon binding to its putative ligand, leading to the phosphorylation of cytoplasmic proteins, including focal adhesion kinase (FAK). While the mechanism and functional significance of CD157-initiated signal transduction are not fully characterized, its role in cellular signaling is evident. BST1 expression is enhanced in bone marrow stromal cell lines derived from patients with rheumatoid arthritis, suggesting a link to polyclonal B cell abnormalities observed in the disease. This overexpression in the stromal cell population may contribute to the pathophysiology of rheumatoid arthritis, highlighting the importance of CD157/BST1 in both normal immune function and disease states.