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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 many more products for this protein.
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Results show the characterization of CRACR2A protein which encodes a large Rab GTPase (show RAB6A Antibodies) containing multiple functional domains contrary to small Rab (show HRB Antibodies) GTPases. It was found to play an unexpected role in regulating intracellular signaling pathways important for T cell activation.
GTP binding (show RND2 Antibodies) 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 (show HRB Antibodies) protein that lacks impact on CRAC channels
CRACR2A interacts directly with Orai1 (show ORAI1 Antibodies) and STIM1 (show STIM1 Antibodies), forming a ternary complex that dissociates at elevated Ca(2 (show CA2 Antibodies)+) concentrations; is a key regulator of CRAC channel-mediated SOCE
GTP binding (show RND2 Antibodies) and prenylation of CRACR2A (show EFCAB4A Antibodies) were associated with its localization near the Golgi and its stability
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