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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 Proteins (5) and many more products for this protein.
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Disruption of the RIAM/lamellipodin (show RAPH1 Antibodies)-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 Antibodies) 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 Antibodies) 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 Antibodies) proteins during cell migration and spreading.
a minimized 50-residue Rap (show LRPAP1 Antibodies)-RIAM module containing the talin binding site of RIAM joined to the membrane-targeting sequence of Rap1A (show RAP1A Antibodies). This minimized Rap (show LRPAP1 Antibodies)-RIAM module was sufficient to target talin to the plasma membrane and to mediate integrin activation
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 Antibodies)-bound GTPase (show RACGAP1 Antibodies) domain of Rap1 (show TERF2IP Antibodies) in complex with the Ras association (RA)-pleckstrin (show PLEK Antibodies) 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 Antibodies) binding sites, which recruit vinculin (show VCL Antibodies) 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 Antibodies) 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