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Appears to function in the signal transduction from Ras activation to actin cytoskeletal remodeling. Additionally we are shipping Amyloid beta (A4) Precursor Protein-Binding, Family B, Member 1 Interacting Protein Antibodies (70) and Amyloid beta (A4) Precursor Protein-Binding, Family B, Member 1 Interacting Protein Proteins (6) and many more products for this protein.
The Rap1 (show RABGEF1 ELISA Kits)-RIAM-talin axis of integrin activation and blood cell function
Disruption of the RIAM/lamellipodin-integrin-talin complex markedly impairs cell migration.
RIAM is a critical component of the phagocytosis machinery downstream of Rap1 and mediates its function by recruiting talin to the phagocytic complement receptors.
integrin-triggered, RIAM-dependent MEK (show MAP2K1 ELISA Kits) activation represents a key feedback event required for efficient focal adhesion disassembly.
RIAM was recruited to the lymphocyte plasma membrane through its Ras association and pleckstrin (show PLEK ELISA Kits) homology domains, both of which were required for lymphocyte adhesion.
RIAM might contribute to the dissemination of melanoma cells.
by regulating the localization of PLC-gamma1, RIAM plays a central role in TCR signaling and the transcription of target genes.
all-trans-retinoic acid-inducible RARP1 selectively affects signal transduction and may contribute to myeloid and megakaryocytic differentiation.(RARP1)
Data pinpoint PREL1 as the first direct link between Ras signalling and cytoskeletal remodelling via Ena/VASP (show VASP ELISA Kits) proteins during cell migration and spreading.
a minimized 50-residue Rap (show LRPAP1 ELISA Kits)-RIAM module containing the talin binding site of RIAM joined to the membrane-targeting sequence of Rap1A (show RAP1A ELISA Kits). This minimized Rap (show LRPAP1 ELISA Kits)-RIAM module was sufficient to target talin to the plasma membrane and to mediate integrin activation
These data identify the requirement of RIAM for formation of immunological synapses and in resulting T cell functions in autoimmunity.
we show that leukocyte integrin activation critically depends on RIAM both in vitro and in vivo
These in vivo results confirm a role for RIAM in the regulation of some, but not all, leukocyte integrins and suggest that RIAM-regulated integrin activation is required for trafficking of lymphocytes
Conformational activation of talin by PREL-1 triggers integrin-mediated cell adhesion.
crystal structure of an active, GTP (show AK3 ELISA Kits)-bound GTPase (show RACGAP1 ELISA Kits) domain of Rap1 (show TERF2IP ELISA Kits) in complex with the Ras association (RA)-pleckstrin (show PLEK ELISA Kits) homology (PH) structural module of RIAM at 1.65 A, is reported.
generated RIAM-null mice and found that they are viable, fertile, and apparently healthy
As talin engages F-actin, force exerted on the R2R3 helical bundles disrupts RIAM binding and exposes the vinculin (show VCL ELISA Kits) binding sites, which recruit vinculin (show VCL ELISA Kits) to stabilize the complex.
Data demonstrate a novel mechanism by which alphavbeta3 integrin acts to locally suppress beta1 integrin activation and regulate VASP (show VASP ELISA Kits) and RIAM to control cell adhesion and migration.
Appears to function in the signal transduction from Ras activation to actin cytoskeletal remodeling.
amyloid beta A4 precursor protein-binding family B member 1-interacting protein
, APBB1-interacting protein 1
, Amyloid beta A4 precursor protein-binding family B member 1-interacting protein
, amyloid beta (A4) precursor protein-binding, family B, member 1 interacting protein
, amyloid beta A4 precursor protein-binding family B member 1-interacting protein-like
, Rap1-GTP-interacting adaptor molecule
, Rap1-interacting adaptor molecule
, proline rich EVH1 ligand 1
, proline-rich EVH1 ligand 1
, proline-rich protein 73
, rap1-GTP-interacting adapter molecule
, retinoic acid-responsive proline-rich protein 1
, proline-rich protein 48