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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. De plus, nous expédions EF-Hand Calcium Binding Domain 4B Anticorps (54) et et beaucoup plus de produits pour cette protéine.
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Results show the characterization of CRACR2A protein which encodes a large Rab GTPase (Montrer RAB6A Protéines) containing multiple functional domains contrary to small Rab (Montrer HRB Protéines) GTPases. It was found to play an unexpected role in regulating intracellular signaling pathways important for T cell activation.
GTP binding (Montrer RND2 Protéines) 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 (Montrer HRB Protéines) protein that lacks impact on CRAC channels
CRACR2A interacts directly with Orai1 and STIM1 (Montrer STIM1 Protéines), forming a ternary complex that dissociates at elevated Ca(2 (Montrer CA2 Protéines)+) concentrations; is a key regulator of CRAC channel-mediated SOCE
GTP binding (Montrer RND2 Protéines) and prenylation of CRACR2A (Montrer EFCAB4A Protéines) 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