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anti-Human FYB Antikörper:
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Human Polyclonal FYB Primary Antibody für ICC, ELISA - ABIN1001738
Rawlings, Sommer, Moreno-García: The CARMA1 signalosome links the signalling machinery of adaptive and innate immunity in lymphocytes. in Nature reviews. Immunology 2006
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Human Polyclonal FYB Primary Antibody für ICC, ELISA - ABIN1001739
Medeiros, Burbach, Mueller, Srivastava, Moon, Highfill, Peterson, Shimizu: Regulation of NF-kappaB activation in T cells via association of the adapter proteins ADAP and CARMA1. in Science (New York, N.Y.) 2007
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Human Polyclonal FYB Primary Antibody für IF, WB - ABIN541621
Griffiths, Krawczyk, Kong, Raab, Hyduk, Bouchard, Chan, Kozieradzki, Oliveira-Dos-Santos, Wakeham, Ohashi, Cybulsky, Rudd, Penninger: Positive regulation of T cell activation and integrin adhesion by the adapter Fyb/Slap. in Science (New York, N.Y.) 2001
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Human Polyclonal FYB Primary Antibody für IF, WB - ABIN541620
Mueller, Thomas, Burbach, Peterson, Shimizu: Adhesion and degranulation-promoting adapter protein (ADAP) positively regulates T cell sensitivity to antigen and T cell survival. in Journal of immunology (Baltimore, Md. : 1950) 2007
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results of this study indicate that a novel T cell adaptor protein, activation-dependent, raft-recruited ADAP-like phosphoprotein (ARAP), plays a unique role in T cells as a part of both the proximal activation signaling and inside-out signaling pathways that result in integrin activation and T cell adhesion
Ubc9 is an essential regulator of ADAP where it is required for TCR-induced membrane recruitment of the small GTPase Rap1 and its effector protein RapL and for activation of the small GTPase Rac1 in T cell adhesion.
Current knowledge of the functions of the adapter protein ADAP in T cell signaling with a focus on the role of individual phosphotyrosine (pY) motifs for SH2 domain mediated interactions is presented.
A distinct set of proteins interaction partners required for chemokine-directed T cell migration is attracted by phosphotyrosine 571 of ADAP, including ZAP70.
Data strongly suggest that chemokine-stimulated associations between Vav1, SLP-76, and ADAP facilitate Rac1 activation and alpha4beta1-mediated adhesion, whereas Pyk2 opposes this adhesion by limiting Rac1 activation.
FYB nonsense mutations in humans causing small-platelet thrombocytopenia and a significant bleeding tendency.
Data (including data from studies in knockout/transgenic mice) suggest that ADAP regulates positive feedback loop of TGFbeta1 production and TGFbeta1-induced CD103 expression in CD8+ T-lymphocytes and protects against influenza H5N1 virus infection.
The aim of this study was to perform an association study between seven Fyn-binding protein gene (FYB)-tag single nucleotide polymorphisms (SNPs) and type I diabetes mellitus (T1DM), as well as with disease age of onset.
The autosomal recessive bleeding phenotype seen in several members of this highly consanguineous family included petechial rash, mild epistaxis and thrombocytopenia with some decrease in platelet volume. These clinical findings, together with the results of exome sequencing pointed to only one strong candidate gene, the FYB gene.
ADAP interacts with talin and kindlin-3 to promote platelet Integrin alphaIIbbeta3 activation and stable fibrinogen binding.
ADAP and Nck adapter proteins cooperatively facilitate T cell adhesion to the LFA-1 ligand ICAM-1.
These findings indicate that ADAP regulates two steps of HIV-1 infection cooperatively with two distinct receptors, and as such, serves as a new potential target in the blockade of HIV-1 infection.
our findings indicate an association between polymorphisms located in FYB gene and SLE, suggesting their possible involvement in disease susceptibility and clinical manifestations.
Multipoint binding of SLP-76 to ADAP facilitates the assembly of SLP-76 microclusters.
TM4SF10, possibly through ADAP, may regulate Fyn activity
a functional cooperation between Nck and ADAP in stabilizing the recruitment of WASp to SLP76 regulates actin rearrangement.
the ADAP CARMA1 binding site is required for IKK gamma ubiquitination; both TAK1 and CARMA1 binding sites are required for IkappaB alpha phosphorylation and degradation and NF-kappaB nuclear translocation
Mass spectrometric identification of ADAP associated with EVL, an actin-binding protein of the ENA/VASP family, DOCK2 and GEF-H1 suggests a direct link between ADAP and the cytoskeleton.
ADAP lipid interaction defines the helically extended SH3 scaffold as a novel member of membrane interaction domains
show in an ADAP-deficient Jurkat T cell line that the co-dependence of ADAP and SKAP55 extends beyond their functional and physical interactions and show that SKAP55 protein is unstable in the absence of ADAP
Adap(-/-) mice have moderate thrombocytopenia and smaller platelets. Adap(-/-) platelets had a shorter life span than controlss. Cultured ADAP(-) BM-derived MKs had reduced spreading on extracellular matrix proteins and beta1 integrin activation, impaired podosome formation, and defective polarization of the demarcation membrane system. ADAP has an unspecified role in the process of MK polarization and platelet biogene...
ADAP fulfills different functions in CD4(+) and CD8(+) T cells, with CD8(+) T cells being less dependent on ADAP.
ADAP regulates CD8 T cell differentiation events following acute pathogen challenge that are critical for the formation and selected functions of TRM cells in nonlymphoid tissues.
The results indicate that ADAP dampens naive CD8 T cell responses to lymphopenia and IL-15, and they demonstrate a novel Ag-independent function for ADAP in the suppression of memory phenotype CD8 T cell generation.
provide evidence that CD28 and the TCR complex regulate NF-kappaB via different signaling modules of GRB-2/VAV1 and LAT/ADAP pathways respectively.
we demonstrate that loss of ADAP promotes resistance of experimental autoimmune encephalomyelitis in mice, likely by trapping encephalitogenic T cells in the peripheral lymph nodes on LYVE-1+ lymphatic structures.
Signaling by Fyn-ADAP via the Carma1-Bcl-10-MAP3K7 signalosome exclusively regulates inflammatory cytokine production in NK cells.
integrin activation by the ADAP-SKAP55-signaling module controls the stability and duration of T cell-dendritic cell contacts during the progressive phases necessary for optimal T cell activation.
ADAP coordinates distinct CARMA1-dependent control of key cell cycle proteins in T cells
The authors utilize in vitro systems to map novel phosphotyrosine sites in the C-terminal part of human ADAP (486-783). They found many phospho-dependent binding partners of ADAP and confirmed the interaction between ADAP and Nck, indicating that ADAP directly links integrins to modulators of the cytoskeleton independent of SLP-76.
ADAP plays a role in mediating platelet activation via the collagen-binding integrin alpha(2) beta(1).
SLP-76 and ADAP are involved in E-selectin-mediated integrin activation and neutrophil recruitment to inflamed kidneys, which may underlie the development of life-threatening ischemia-reperfusion-induced acute kidney injury in humans.
Data suggest that the presence or absence of associated SKAP55 defines functionally distinct pools of ADAP.
HPK1 competes with ADAP for SLP-76 binding and via Rap1 negatively affects T-cell adhesion.
ADAP is an essential component of alphaIIbbeta3-mediated platelet mechanotransduction that promotes F-actin assembly and enables platelet spreading and thrombus stabilization under fluid shear stress.
ADAP-SLP-76 binding as a signaling event that differentially regulates SMAC formation, and support a role for SMAC formation in T cell cytokine production.
The protein encoded by this gene is an adapter for the FYN protein and LCP2 signaling cascades in T-cells. The encoded protein is involved in platelet activation and controls the expression of interleukin-2. Three transcript variants encoding different isoforms have been found for this gene.
, FYN-T-binding protein
, SLP-76-associated phosphoprotein
, adhesion and degranulation-promoting adaptor protein
, FYN binding protein FYB-130
, adhesion and degranulation promoting adaptor protein
, FYN binding protein (FYB-120/130)