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The protein encoded by SH3BP2 has an N-terminal pleckstrin homology (PH) domain, an SH3-binding proline-rich region, and a C-terminal SH2 domain. Additionally we are shipping SH3-Domain Binding Protein 2 Kits (5) and SH3-Domain Binding Protein 2 Proteins (5) and many more products for this protein.
Showing 10 out of 52 products:
Human Polyclonal SH3BP2 Primary Antibody for EIA, WB - ABIN954791
Lietman, Yin, Levine: SH3BP2 mutations potentiate osteoclastogenesis via PLCγ. in Journal of orthopaedic research : official publication of the Orthopaedic Research Society 2010
Show all 3 references for 954791
Mouse (Murine) Polyclonal SH3BP2 Primary Antibody for WB - ABIN264981
Songyang, Shoelson, McGlade, Olivier, Pawson, Bustelo, Barbacid, Sabe, Hanafusa, Yi: Specific motifs recognized by the SH2 domains of Csk, 3BP2, fps/fes, GRB-2, HCP, SHC, Syk, and Vav. in Molecular and cellular biology 1994
Show all 2 references for 264981
Cow (Bovine) Polyclonal SH3BP2 Primary Antibody for IHC, WB - ABIN2786764
Idowu, Thomas, Frow, Diss, Flanagan: Mutations in SH3BP2, the cherubism gene, were not detected in central or peripheral giant cell tumours of the jaw. in The British journal of oral & maxillofacial surgery 2008
The adaptor 3BP2 is required for KIT receptor expression and human mast cell survival.
A c.1244G>A (p.Arg415Gln) mutation in SH3BP2 gene causes cherubism in a Turkish family
Authors conclude that a novel p.Asp419Tyr alteration in SH3BP2 to be a cherubism-causing mutation in a Turkish family.
In the first family, a missense mutation Arg415Gln was found in exon 9 of SH3BP2 in all affected individuals. The unaffected individuals did not have the mutation. In the second family, a missense mutation Pro418Thr was identified in exon 9 of the SH3BP2
These results demonstrate that PARP1 (show PARP1 Antibodies) regulates expression of SH3BP2.
P416R mutation of 3BP2 causes the gain of function in B cells by increasing the interaction with specific signaling molecules.
if a primary genetic defect is the cause for CGCG it is either located in SH3BP2 gene exons not yet related to cherubism or in a different gene.
The SH-3BP-2 mutation may participate in the differentiation and maturation of osteoclast-like cells in the lesion of cherubism.
over expression of SH3BP2 in RAW 264.7 cells potentiates sRANKL-stimulated phosphorylation of PLCgamma1 (show PLCG1 Antibodies) and PLCgamma2 (show PLCG2 Antibodies).
No SH3BP2 gene mutation was found in PGCL.
Bone marrow transplantation also ameliorated the inflammation and bone loss in 10-week-old Sh3bp2(knock in) mice.
These findings suggest that the SH3BP2 cherubism mutation can cause jawbone destruction by promoting osteoclast formation in response to TNF-alpha (show TNF Antibodies) expressed in cherubism lesions and that SH3BP2 is a key regulator for TNF-alpha (show TNF Antibodies)-induced osteoclastogenesis
3BP2 was needed for LPS (show TLR4 Antibodies)-induced activation of macrophage signaling pathways. Having a single Sh3bp2 Gly418Arg allele and PAMP (show ADM Antibodies) stimulation had a cooperative effect on macrophage activation and inflammatory responses.
Phosphorylation of SH3BP2 at Y183 is critical for the TNF-alpha (show TNF Antibodies) production.
Gain-of-function of SH3BP2 augments inflammation and bone loss in the CIA (show NCOA5 Antibodies) model through increased macrophage activation and osteoclast formation.
Etanercept administration to neonatal SH3BP2 knock-in cherubism mice prevents TNF-alpha (show TNF Antibodies)-induced inflammation and bone loss.
By participating in FcepsilonRI (show FCER1A Antibodies)-mediated signal transduction, 3BP2 is an important regulator of human mast cell activation.
Adapter protein (show GRB10 Antibodies) 3BP2 links chemoattractant fMLF-induced receptor signaling events to neutrophil actin cytoskeleton and NADPH oxidase (show NOX1 Antibodies) complex, a requirement for effective bactericidal function in vivo.
Study shows that TNKS2, regulates 3BP2 stability through ADP-ribosylation and subsequent ubiquitylation in osteoclasts; cherubism mutations uncouple 3BP2 from Tankyrase-mediated protein destruction.
Data provide evidence for a concerted HIF-1alpha (show HIF1A Antibodies)/MT1-MMP (show MMP14 Antibodies) signalling axis that explains the induction of adaptor protein 3BP2 and which may link protein (show HAPLN1 Antibodies) binding partners together and stimulate oncogenic MSC (show MSC Antibodies) migration.
The protein encoded by this gene has an N-terminal pleckstrin homology (PH) domain, an SH3-binding proline-rich region, and a C-terminal SH2 domain. The protein binds to the SH3 domains of several proteins including the ABL1 and SYK protein tyrosine kinases , and functions as a cytoplasmic adaptor protein to positively regulate transcriptional activity in T, natural killer (NK), and basophilic cells. Mutations in this gene result in cherubism. Multiple transcript variants encoding different isoforms have been found for this gene.
SH3-domain binding protein 2
, SH3 domain-binding protein 2
, Abl-SH3 binding protein 2
, TNFAIP3 interacting protein 2