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anti-Mouse (Murine) PAG1 Anticorps:
anti-Rat (Rattus) PAG1 Anticorps:
anti-Human PAG1 Anticorps:
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Human Monoclonal PAG1 Primary Antibody pour FACS, IHC (p) - ABIN94272
Yerly, Ding, Tauzin, van Echten-Deckert, Borisch, Hoessli: The sphingolipid-rich rafts of ALK+ lymphomas downregulate the Lyn-Cbp/PAG signalosome. dans European journal of haematology 2010
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Human Monoclonal PAG1 Primary Antibody pour IHC (p), IP - ABIN94270
Baumgartner, Angelisová, Setterblad, Mooney, Werling, Horejsí, Langsley: Constitutive exclusion of Csk from Hck-positive membrane microdomains permits Src kinase-dependent proliferation of Theileria-transformed B lymphocytes. dans Blood 2003
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Cow (Bovine) Monoclonal PAG1 Primary Antibody pour IHC (p), IP - ABIN269119
Yamashita, Chattopadhyay, Fensterl, Zhang, Sen: A TRIF-independent branch of TLR3 signaling. dans Journal of immunology (Baltimore, Md. : 1950) 2012
our findings illustrate that Cbp is an important regulator of Csk recruitment to the SFK Lyn in Eporesponsive erythroid cells.
This study demonstrated that cbp increase in skeletal muscle in muscle atrophy.
PAG is constitutively phosphorylated in resting T cells and rapidly dephosphorylated once the TCR is engaged.
If Cbp enhances the interaction between c-Src and FAK, Cbp could promote c-Src function when lipid rafts are disrupted.
PAG can function as both a positive and a negative regulator of mast cell signaling, depending upon the signaling pathway involved. PAG is a positive regulator of passive systemic anaphylaxis.
Data show that the phosphoprotein associated with glycosphigolipid-enriched microdomains (PAG)/Csk binding protein (Cbp) modulates SFK activity in the brain.
Cbp plays a role in adult hematopoietic stem cell homeostasis.
regulates epithelial-mesenchymal transition in trophoblast stem cells
Cbp down-regulation is primarily mediated by epigenetic histone modifications via oncogenic MAPK/PI3K pathways in a subset of cancer cells.
expression of Cbp is downregulated during osteoclast differentiation, consequently inhibiting recruitment of Csk to lipid rafts and keeping c-Src activity high in osteoclasts. findings provide a novel paradigm that controls c-Src activity in osteoclasts.
CBP plays a role in transiently anchoring Thy-1 to the cytoskeleton.
PAG is a bona fide negative regulator of T-cell activation as a result of its capacity to recruit Csk.
Csk-binding protein is dispensable for the recruitment of carboxy-terminal Src kinase to the membrane [Csk-binding protein and carboxy-terminal Src kinase ]
PTPalpha-/- cells exhibit increased tyrosine phosphorylation of specific proteins, increased Fyn activity, and hyperphosphorylation of Cbp/PAG that promotes its association with C-terminal Src kinase
Pronounced, age-dependent reduction in PAG in CD4+ T cells' lipid rafts.
These findings indicate a potential role for Cbp as a suppressor of c-Src-mediated tumor progression.
PAG regulates PDGFR membrane partitioning and SRC family protein tyrosine kinases mitogenic signaling by modulating GM1 levels within caveolae independently from Csk.
Low PAG1 expression is associated neuroblastoma.
Our study highlights the underlying mechanism of cross interaction between ASCs and breast cancer cells, and indicates that PAG1/Cbp in breast cancer cell may modulate tumor progression and acquired chemoresistance in the ASCs-associated breast cancer microenvironment through Src and AKT/mTOR pathways.
Up-regulated expression of CBP in Jurkat cells could reduce cell homogeneity and promote cell apoptosis
No association Pag1 mutation with patient with Schizophrenia.
The risk-associated allele of rs2370615 predisposes to allergic disease by increasing PAG1 expression, which might promote B cell activation and have a pro-inflammatory effect.
CBP may decrease the metastasis of esophageal carcinoma by inhibiting the activation of Src.
The inhibitory function of novobiocin in disrupting the HIF1alpha/p300 complex might be important in tumor cell growth.
siRNA directed against PAG1 in a radioresistant (Hep-2max) cell line dramatically enhanced the radiosensitivity and IR-induced cell death.
expression of CBP gene is decreased in esophageal carcinoma, which might contribute to the tumorigenesis and progression.
findings support a negative regulatory function for Cbp/PAG in proximal B cell receptor signaling in normal and EBV-transformed B cells
An over-expression of PAG1 in PC-3M-1E8 cells effectively suppresses the activation of Ras and ERK, as well as the cyclin D1 expression, leading to an inhibition of the proliferation ability of tumor cells.
Results indicate that Cbp is required for the Csk-mediated inactivation of c-Src and may control the promotion of malignancy in NSCLC tumors that are characterized by c-Src upregulation.
PAG1 protein was downregulated in PC-3M-1E8 prostate cancer cell line.
In the membrane environment of ALK+ lymphoma rafts, where the glycosphingolipid to signaling protein ratio is higher than in B-NHL rafts, the Lyn activity is suboptimal and does not allow the formation of an efficient Lyn-Cbp/PAG signalosome
Study shows EGF-stimulation-induced Csk-binding protein (Cbp) tyrosine phosphorylation followed by Cbp-Csk association, in a SFK-dependent manner.
High PAG-binding ability with CSK in vitro as well as the human PAG structure characterized by 11 alpha-helix structures including a 3 kDa transmembrane domain are reported.
PAG negatively regulates Ras proteins, and by knocking down PAG there is enhanced Src kinase activity and Ras activation.
engagement of the SH2 domain on PAG renders FynT insensitive to Csk negative regulation
role in control of proliferation and survival in most B-non-Hodgkin lymphomas
The protein encoded by this gene is a type III transmembrane adaptor protein that binds to the tyrosine kinase csk protein. It is thought to be involved in the regulation of T cell activation.
, phosphoprotein associated with glycosphingolipid-enriched microdomains 1
, phosphoprotein transmembrane adaptor 1
, phosphoprotein-associated with GEMs
, transmembrane phosphoprotein Cbp
, Csk binding protein
, csk-binding protein
, transmembrane adapter protein PAG
, transmembrane adaptor protein PAG
, phosphoprotein associated with glycosphingolipid microdomains 1
, phosphoprotein associated with glycosphingolipid-enriched microdomains 1-like