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Human Polyclonal SH3BP2 Primary Antibody for IP, ELISA - ABIN538209
Foucault, Liu, Bernard, Deckert: The chaperone protein 14-3-3 interacts with 3BP2/SH3BP2 and regulates its adapter function. in The Journal of biological chemistry 2003
Show all 3 Pubmed References
Human Monoclonal SH3BP2 Primary Antibody for IF, ELISA - ABIN562859
Matsumoto, La Rose, Kent, Wagner, Narimatsu, Levy, Omar, Tong, Krieger, Riggs, Storozhuk, Pasquale, Ventura, Yeganeh, Post, Moran, Grynpas, Wrana, Superti-Furga, Koleske, Pendergast, Rottapel: Reciprocal stabilization of ABL and TAZ regulates osteoblastogenesis through transcription factor RUNX2. in The Journal of clinical investigation 2016
All members featured a heterozygous missense c.1244G>C; p.Arg415Pro SH3BP2 mutation
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 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 and PLCgamma2.
No SH3BP2 gene mutation was found in PGCL.
Regulation of FcepsilonRI-mediated degranulation by an adaptor protein 3BP2 in rat basophilic leukemia RBL-2H3 cells.
3BP2 may regulate b cell receptor-mediated gene activation through Vav proteins.
Adaptor protein SH3BP2 regulates transcription factors through its tyrosine phosphorylation and SH2 domain.
CD244-3BP2 association regulates cytolytic function but not IFN-gamma release
no mutations...in giant cell granuloma
How SH3BP2 affects leukocyte signaling and influences cherubism
a novel A1517G missense mutation at the SH3BP2 gene in a Chinese family with multiple affected individuals with cherubism was identified
Mutated in a rare human disease involved in cranial-facial development called cherubism, suggesting a role for 3BP2 in regulating osteoclast and hematopoietic cell function. [REVIEW]
unexpected role of 3BP2 in endocytic and cytoskeletal regulation through its interaction with CIN85 and HIP-55
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 expressed in cherubism lesions and that SH3BP2 is a key regulator for TNF-alpha-induced osteoclastogenesis
3BP2 was needed for LPS-induced activation of macrophage signaling pathways. Having a single Sh3bp2 Gly418Arg allele and PAMP stimulation had a cooperative effect on macrophage activation and inflammatory responses.
Phosphorylation of SH3BP2 at Y183 is critical for the TNF-alpha production.
Gain-of-function of SH3BP2 augments inflammation and bone loss in the CIA model through increased macrophage activation and osteoclast formation.
Etanercept administration to neonatal SH3BP2 knock-in cherubism mice prevents TNF-alpha-induced inflammation and bone loss.
By participating in FcepsilonRI-mediated signal transduction, 3BP2 is an important regulator of human mast cell activation.
Adapter protein 3BP2 links chemoattractant fMLF-induced receptor signaling events to neutrophil actin cytoskeleton and NADPH oxidase 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/MT1-MMP signalling axis that explains the induction of adaptor protein 3BP2 and which may link protein binding partners together and stimulate oncogenic MSC migration.
critical role in osteoclastogenesis, potential target for suppression of pathologic bone resorption
3BP2 adapter protein has an unanticipated role in osteoblast function and in coordinating bone homeostatic signals in both osteoclast and osteoblast lineages
Data demonstrate for the first time that Sh3bp2 is important for bone formation and osteoblast differentiation and function.
The data, together with previous osteoclast studies, demonstrate a critical role of Sh3bp2 in bone remodeling and osteoblast differentiation.
3BP2 is a potential regulator of Lyn protein-tyrosine kinase as a ligand of its SH3/SH2 domains in FcepsilonRI-mediated signaling in mast cells
3BP2(-/-) mice had increased accumulation of pre-B cells in the bone marrow and a block in the progression of transitional B cells in the spleen from the T1 to the T2 stage, but normal numbers of mature B cells.
These results indicate that the mutant phenotype reflects gain of SH3BP2 function and suggests that SH3BP2 is a critical regulator of myeloid cell responses to M-CSF and RANKL stimulation.
3BP2 binds via its SH2 domain to the CD19 signaling complex and is required for optimum Syk phosphorylation and calcium flux.
SH3BP2 both increases nuclear NFATc1 in sRANKL treated RAW 264.7 preosteoclast cells and enhances expression of tartrate resistant acid phosphatase, a specific marker of osteoclast differentiation.
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