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anti-Human GRAP2 Antibodies:
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Human Monoclonal GRAP2 Primary Antibody for FACS, IP - ABIN509570
Yankee, Draves, Ewings, Clark, Graves: CD95/Fas induces cleavage of the GrpL/Gads adaptor and desensitization of antigen receptor signaling. in Proceedings of the National Academy of Sciences of the United States of America 2001
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Human Polyclonal GRAP2 Primary Antibody for ELISA, WB - ABIN256936
Qiu, Hua, Agrawal, Li, Cai, Chan, Zhou, Luo, Liu: Molecular cloning and expression of human grap-2, a novel leukocyte-specific SH2- and SH3-containing adaptor-like protein that binds to gab-1. in Biochemical and biophysical research communications 1999
These data are consistent with a model in which bivalent recruitment of a GADS/SLP-76 complex is required for costimulation by CD6.
Following phosphorylation of the tyrosine, the proteins growth factor receptor-bound protein 2 (Grb2), Grb2-related adaptor downstream of Shc (Gads), and p85 subunit of phosphoinositide 3-kinase may bind to pYMNM (where pY is phosphotyrosine) via their Src homology 2 (SH2) domains, leading to downstream signaling to distinct immune pathways. These three adaptor proteins bind to the same site on CD28 with variable affinity
GADS deficient T cells displayed similar levels of T cell receptor -induced SLP-76 and PLC-gamma1 phosphorylation but exhibited substantial decrease in TCR-induced IL-2 and IFN-gamma release.
Gads was dispensable for TCR-induced phosphorylation of SLP-76, but was a dose-dependent amplifier of TCR-induced CD69 expression.
GADS mediates lymphoid disease downstream of BCR-ABL through the recruitment of specific signaling intermediates.
Histidine domain-protein tyrosine phosphatase interacts with Grb2 and GrpL
The results show that Bcr-Abl regulates the actin cytoskeleton and non-apoptotic membrane blebbing via a GADS/Slp-76/Nck1 adaptor protein pathway.
Upstream open reading frames regulate translation of this protein's mRNA in megakaryocytes.
Exogenous expression of GrpL in a GrpL-negative B cell line leads to enhanced antigen receptor-induced extracellular signal-related kinase and p38 mitogen-activated protein kinase phosphorylation.
AML-1 plays a role in driving Mona protein expression in T and myelomonocytic cells.
Plays a tissue-specific role as an inhibitor of RET receptor tyrosine kinase mitogenic signaling
Gads plays a dominant role in CD28-mediated IL-2 promoter activation.
The integrity of T-cell receptor signaling in vivo is sustained both by strong selection of SLP-76 for the Gads C-SH3 domain and by a capacity to buffer intrinsic crossreactivity.
Our findings define a pathway involving CD28 binding to Grb-2 and its co-operativity with Vav1 in the regulation of T-cell co-stimulation.
Consistent Grap-2 expression suggests a specific role for this adaptor in human medullary thyroid carcinoma, while qualitative alterations do not appear to influence RET signaling
High GADS expression is associated with neoplasms.
The combined loss of Gads and CD127 reveals a novel function of Gads prior to T cell receptor beta expression
Data show that the primary function of Gads is to regulate the sensitivity of the TCR to Ag ligation.
Induced expression and association of the Mona/Gads adapter and Gab3 scaffolding protein during monocyte/macrophage differentiation. (Gab3 scaffolding protein)
Results reveal the basis for preferential recognition of specific LAT sites by Gads.
Mona/Gads SH3C binding to hematopoietic progenitor kinase 1 (HPK1) combines an atypical SH3 binding motif, R/KXXK, with a classical PXXP motif embedded in a polyproline type II (PPII) helix
The Gads adaptor protein is critical for homeostasis of CD4(+) T cells.
Selective impairment of FcepsilonRI-mediated allergic reaction in Gads-deficient mice
Gads plays a key role in linking the adapter LAT to SLP-76 in response to weak activation of GPVI and CLEC-2 whereas LAT is required for full activation over a wider range of agonist concentrations.
This gene encodes a member of the GRB2/Sem5/Drk family. This member is an adaptor-like protein involved in leukocyte-specific protein-tyrosine kinase signaling. Like its related family member, GRB2-related adaptor protein (GRAP), this protein contains an SH2 domain flanked by two SH3 domains. This protein interacts with other proteins, such as GRB2-associated binding protein 1 (GAB1) and the SLP-76 leukocyte protein (LCP2), through its SH3 domains. Transcript variants utilizing alternative polyA sites exist.
GRB2-related adaptor protein 2
, GRB2-related adapter protein 2
, GRB-2-like protein
, GRB2-related protein with insert domain
, SH3-SH2-SH3 adapter Mona
, SH3-SH2-SH3 adaptor molecule
, adapter protein GRID
, grf40 adapter protein
, growth factor receptor-binding protein
, growth factor receptor-bound protein 2-related adaptor protein 2
, hematopoietic cell-associated adapter protein GrpL
, hematopoietic cell-associated adaptor protein GRPL
, GRB-2-related monocytic adapter protein
, Grb2-related adaptor downstream of Sch
, hematopoietic cell-associated adaptor protein GrpL
, monocytic adapter
, monocytic adaptor