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Arg and c-Abl represent the mammalian members of the Abelson family of non-receptor protein-tyrosine kinases. Additionally we are shipping Sorbs2 Proteins (4) and Sorbs2 Kits (1) and many more products for this protein.
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Human Polyclonal Sorbs2 Primary Antibody for EIA, WB - ABIN453519
Yuan, Kim, Kaneko, Sussman, Bokoch, Kruh, Nicosia, Testa, Cheng: ArgBP2gamma interacts with Akt and p21-activated kinase-1 and promotes cell survival. in The Journal of biological chemistry 2005
Show all 3 references for ABIN453519
Human Polyclonal Sorbs2 Primary Antibody for FACS, IF - ABIN652279
Olsen, Blagoev, Gnad, Macek, Kumar, Mortensen, Mann: Global, in vivo, and site-specific phosphorylation dynamics in signaling networks. in Cell 2006
Show all 3 references for ABIN652279
Human Polyclonal Sorbs2 Primary Antibody for IF, WB - ABIN521930
Lamberti, Sanges, Chambery, Migliaccio, Rosso, Di Maro, Papale, Marra, Parente, Caraglia, Abbruzzese, Arcari: Analysis of interaction partners for eukaryotic translation elongation factor 1A M-domain by functional proteomics. in Biochimie 2011
SORBS2 transcription is activated by telomere position effect-over long distance upon telomere shortening in muscle cells from patients with facioscapulohumeral dystrophy
ArgBP2 inhibits proliferation, migration, and invasion of gastric cancer cells.MORC2 down-regulates the ArgBP2 via histone methylation in gastric cancer cells.
This study confirmed that SORBS2 as genetic modifiers of age at onset of Alzheimer disease.
ArgBP2 interaction with alpha-actinin and actin stress fibers inhibits cell migration
Tyrosine phosphorylation of ARGBP2 interferes with a SH3 mediated self-interaction, thereby controlling its panel of interacting partners and related functions.
SORBS2 and TLR3 (show TLR3 Antibodies) induce premature senescence in primary human fibroblasts and keratinocytes.
Sarcoplasmic sorbin and SH3 domain-containing protein 2 is released from damaged cardiac tissue into the bloodstream upon lethal acute myocardial infarction.
In epithelial NMuMG cells, immunofluorescence analyses revealed localization of ArgBP2 at tight junctions and mutation analyses found a second SH3 domain (show ITSN1 Antibodies) to be important for ArgBP2 localization to the cell-cell contact sites.
A co-localization of SORBS2 and eEF1A (show EEF1A1 Antibodies) was evidenced at level of plasma membrane, thus suggesting the involvement of eEF1A1 (show EEF1A1 Antibodies) in novel key signal transduction complexes.
Reconstitution of SORBS2 expression resulted significant reduction in cell proliferation, colony formation and anchorage-independent growth in CaSki, HPKII and HaCaT cells, whereby anchorage-independent growth could only be investigated for CaSki cells
The study screened CrkL (show CRKL Antibodies) binding proteins using RNA interference (RNAi) and identified Sorbs1 (show SORBS1 Antibodies) and Sorbs2 as two proteins that are enriched at AChR clusters and are required for the formation of AChR aggregation in vitro.
Arg and c-Abl represent the mammalian members of the Abelson family of non-receptor protein-tyrosine kinases. They interact with the Arg/Abl binding proteins via the SH3 domains present in the carboxy end of the latter group of proteins. This gene encodes the sorbin and SH3 domain containing 2 protein. It has three C-terminal SH3 domains and an N-terminal sorbin homology (SoHo) domain that interacts with lipid raft proteins. The subcellular localization of this protein in epithelial and cardiac muscle cells suggests that it functions as an adapter protein to assemble signaling complexes in stress fibers, and that it is a potential link between Abl family kinases and the actin cytoskeleton. Alternative splicing results in multiple transcript variants encoding different isoforms.
sorbin and SH3 domain containing 2
, sorbin and SH3 domain-containing protein 2
, sorbin and SH3 domain-containing protein 2-like
, Arg binding protein 2
, Arg/Abl-interacting protein 2
, Arg/Abl-interacting protein ArgBP2
, arg/Abl-interacting protein 2
, neural ArgBP2
, Sorbin and SH3 domain-containing protein 2
, sorbin polypeptide