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Ca(2+)-binding protein that plays a key role in store- operated Ca(2+) entry (SOCE) in T-cells by regulating CRAC channel activation. Additionally we are shipping EF-Hand Calcium Binding Domain 4B Proteins (4) and and many more products for this protein.
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Results show the characterization of CRACR2A protein which encodes a large Rab GTPase containing multiple functional domains contrary to small Rab GTPases. It was found to play an unexpected role in regulating intracellular signaling pathways important for T cell activation.
GTP binding and prenylation of CRACR2A were associated with its localization near the Golgi and its stability
endothelial cells contain a long variant of CRACR2A which is an EF-hand-containing Rab protein that lacks impact on CRAC channels
CRACR2A interacts directly with Orai1 and STIM1, forming a ternary complex that dissociates at elevated Ca(2+) concentrations; is a key regulator of CRAC channel-mediated SOCE
Ca(2+)-binding protein that plays a key role in store- operated Ca(2+) entry (SOCE) in T-cells by regulating CRAC channel activation. Acts as a cytoplasmic calcium-sensor that facilitates the clustering of ORAI1 and STIM1 at the junctional regions between the plasma membrane and the endoplasmic reticulum upon low Ca(2+) concentration. It thereby regulates CRAC channel activation, including translocation and clustering of ORAI1 and STIM1. Upon increase of cytoplasmic Ca(2+) resulting from opening of CRAC channels, dissociates from ORAI1 and STIM1, thereby destabilizing the ORAI1-STIM1 complex (By similarity).
CRAC channel regulator 2A
, EF-hand calcium-binding domain-containing protein 4B
, calcium release-activated calcium channel regulator 2A