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In this study, the authors identified that the ADAP (show APP Proteins)-SKAP55 signaling module reduced CD8 (show CD8A Proteins)(+) cytotoxic T lymphocyte cytotoxicity and enhanced PD-1 (show PDCD1 Proteins) expression in a Fyn (show FYN Proteins)-, Ca(2 (show CA2 Proteins)+)-, and NFATc1 (show NFATC1 Proteins)-dependent manner.
Data suggest that the presence or absence of associated SKAP55 defines functionally distinct pools of ADAP (show APP Proteins).
HPK1 (show MAP4K1 Proteins) associates with SKAP1 to negatively regulate Rap1 (show TERF2IP Proteins)-mediated B-lymphocyte (show AKAP17A Proteins) adhesion.
SKAP1 is dispensable for both CXCL12 (show CXCL12 Proteins) and CCL21 (show CCL21 Proteins) induced T-cell migration.
findings define a T cell receptor "inside-out" pathway via N-SKAP1-C-RapL (show RASSF5 Proteins) that regulates T cell adhesion, motility, and arrest times with dendritic cells in lymph nodes.
Results identify a clear effector role for SKAP-55 in LFA-1 adhesion in peripheral T cells and demonstrate that dependency on SKAP-55 and ADAP differs among T cells and differs with the strength of the TCR signal.
SKAP55 dimers stabilize SLP-76 (show LCP2 Proteins) microclusters, couple SLP-76 (show LCP2 Proteins) to the force-generating systems responsible for microcluster movement, and enable adhesion via the TCR by mechanisms independent of RIAM (show APBB1IP Proteins), talin, and beta1 integrins.
single-nucleotide polymorphisms in ARRDC3, FLT1 (show FLT1 Proteins), and SKAP1 were significant predictors for survival androgen-deprivation therapy in prostate cancer patients.
N-terminal myr-tagged SKAP1 for membrane binding facilitated constitutive RapL (show RASSF5 Proteins) membrane and Rap1 (show RABGEF1 Proteins) binding and effectively substituted for PI3K (show PIK3CA Proteins) and TCR ligation in the activation of LFA-1 (show ITGAL Proteins) in T cells.
Single nucleotide polymorphism in SKAP1 is associated with ovarian cancer.
SKAP55 coupled with CD45 (show PTPRC Proteins) positively regulates T-cell receptor-mediated gene transcription.
observation that adapter protein SKAP55 formed homodimers through its SH3 domain and SK region
SKAP-55 regulates integrin-mediated adhesion and conjugate formation between T cells and antigen-presenting cells
stimuli that signal for the stabilization of SKAP55 may play an important role in T cell adhesion and conjugate formation
This study reports on a RKXXY294 motif in SKAP-55 that mediates unique ADAP (show FYB Proteins) SH3c domain binding; it is necessary for LFA-1 (show ITGAL Proteins)-mediated adhesion and cytokine production.
This gene encodes a T cell adaptor protein, a class of intracellular molecules with modular domains capable of recruiting additional proteins but that exhibit no intrinsic enzymatic activity. The encoded protein contains a unique N-terminal region followed by a PH domain and C-terminal SH3 domain. Along with the adhesion and degranulation-promoting adaptor protein, the encoded protein plays a critical role in inside-out signaling by coupling T-cell antigen receptor stimulation to the activation of integrins.
ortholog of human src family associated phosphoprotein 1 SCAP1
, src family-associated phosphoprotein 1
, src kinase-associated phosphoprotein 1
, src family associated phosphoprotein 1
, src kinase-associated phosphoprotein of 55 kDa
, SKAP55 adapter protein
, SKAP55 adaptor protein