Anti-Stromal interaction molecule 2 STIM2 Antibody

In T lymphocytes, the sole pathway for Ca++ entry following antigen-receptor binding is through store-operated Ca++-release-activated Ca++ (CRAC) channels. These channels are made up of the pore-forming subunit ORAI1 and the stromal interaction molecule 1 (STIM1), a protein that functions as a Ca++ sensor and activates the CRAC channels, migrating to the plasma membrane from endoplasmic reticulum (ER) -like sites which act as the Ca++ store. A related molecule, STIM2, acts to inhibit the STIM1-mediated store-operated Ca++ entry, and can form complexes with STIM1, suggesting they may play a coordinated role in controlling Ca++ entry. At least three isoforms of STIM2 are known to exist. This STIM2 antibody is predicted to have no cross-reactivity to STIM1.

STIM2 antibody was raised against a 18 amino acid synthetic peptide from near the carboxy terminus of human STIM2. The immunogen is located within the last 50 amino acids of STIM2.

Plays a role in mediating store-operated Ca (2+) entry (SOCE), a Ca (2+) influx following depletion of intracellular Ca (2+) stores. Functions as a highly sensitive Ca (2+) sensor in the endoplasmic reticulum which activates both store-operated and store-independent Ca (2+) -influx. Regulates basal cytosolic and endoplasmic reticulum Ca (2+) concentrations. Upon mild variations of the endoplasmic reticulum Ca (2+) concentration, translocates from the endoplasmic reticulum to the plasma membrane where it probably activates the Ca (2+) release-activated Ca (2+) (CRAC) channels ORAI1, ORAI2 and ORAI3. May inhibit STIM1-mediated Ca (2+) influx.