Description_x000D_ General description_x000D_ STIM (stromal interaction molecule) proteins are conserved single-pass transmembrane protein. The three STIM proteins, STIM1, STIM2 and D-Stim, are ubiquitously expressed proteins composed of a single SAM (sterile α-motif) domain and an unpaired EF hand within the highly conserved extracellular region and coiled-coil domains that are conserved in structure and position within the cytoplasmic region. Significant divergence between these proteins was found only at the extreme C-termini. STIM proteins are modified by phosphorylation and N-linked glycosylation._x000D_ Immunogen_x000D_ synthetic peptide corresponding to amino acids 812-833 of human STIM2, conjugated to KLH. The corresponding sequence is identical in rat and mouse._x000D_ Application_x000D_ Anti-STIM2 antibody produced in rabbit has been used in western blotting._x000D_ Physical form_x000D_ Solution in 0.01 M phosphate buffered saline, pH 7.4, containing 15 mM sodium azide._x000D_ Disclaimer_x000D_ Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals._x000D_ Biochem/physiol Actions_x000D_ STIM (stromal interaction molecule) required for the regulation of store-operated Ca2+ influx. Store-operated calcium entry is mediated by Ca2+ release-activated Ca2+ (CRAC) channels, following Ca2+ depletion from the endoplasmic reticulum (ER) stores. This process is crucial for gene transcription, proliferation and cytokine release. STIM2 is an inhibitor of STIM1-mediated store-operated Ca2+ entry. STIM2 co-localizes with STIM1 in punctae upon store depletion, and coprecipitates with STIM1 from cell lysates, suggesting that they may play a coordinated role in controlling Ca2+ entry.