The antibody MEM-255 recognizes an epitope (aa 235-280) of Csk-binding protein (Cbp) located in the cytoplasmic domain, also known as protein associated with glycosphingolipid-enriched microdomains (PAG).
Keine Kreuzreaktivität
Rind (Kuh), Maus, Ratte
Kreuzreaktivität (Details)
Human
Aufreinigung
Purified by protein-A affinity chromatography.
Reinheit
> 95 % (by SDS-PAGE)
Immunogen
Recombinant intracellular fragment (aa 97-432) of human Cbp (PAG).
Flow cytometry: Recommended dilution: 2 μg/mL. Intracellular staining. Immunohistochemistry (paraffin sections): Positive tissue: tonsil, spleen. Western blotting: Csk binding protein is an ubiquitously expressed 46 kDa transmembrane adaptor protein present in membrane microdomains (rafts), which, however, migrates on SDS-PAGE gels anomalously as an 80 kDa molecule.
Beschränkungen
Nur für Forschungszwecke einsetzbar
Konzentration
1 mg/mL
Buffer
Phosphate buffered saline (PBS), pH 7.4, 15 mM sodium azide
Konservierungsmittel
Sodium azide
Vorsichtsmaßnahmen
This product contains Sodium azide: a POISONOUS AND HAZARDOUS SUBSTANCE which should be handled by trained staff only.
Handhabung
Do not freeze.
Lagerung
4 °C
Informationen zur Lagerung
Store at 2-8°C. Do not freeze.
Schatzlmaier, Supper, Göschl, Zwirzitz, Eckerstorfer, Ellmeier, Huppa, Stockinger: "Rapid multiplex analysis of lipid raft components with single-cell resolution." in: Science signaling, Vol. 8, Issue 395, pp. rs11, (2015) (PubMed).
Yerly, Ding, Tauzin, van Echten-Deckert, Borisch, Hoessli: "The sphingolipid-rich rafts of ALK+ lymphomas downregulate the Lyn-Cbp/PAG signalosome." in: European journal of haematology, (2010) (PubMed).
Tedoldi, Paterson, Hansmann, Natkunam, Rüdiger, Angelisova, Du, Roberton, Roncador, Sanchez, Pozzobon, Masir, Barry, Pileri, Mason, Marafioti, Horejsí: "Transmembrane adaptor molecules: a new category of lymphoid-cell markers." in: Blood, Vol. 107, Issue 1, pp. 213-21, (2005) (PubMed).
Davidson, Bakinowski, Thomas, Horejsi, Veillette: "Phosphorylation-dependent regulation of T-cell activation by PAG/Cbp, a lipid raft-associated transmembrane adaptor." in: Molecular and cellular biology, Vol. 23, Issue 6, pp. 2017-28, (2003) (PubMed).
Brdicková, Brdicka, Andera, Spicka, Angelisová, Milgram, Horejsí: "Interaction between two adapter proteins, PAG and EBP50: a possible link between membrane rafts and actin cytoskeleton." in: FEBS letters, Vol. 507, Issue 2, pp. 133-6, (2001) (PubMed).
Target
PAG1
(phosphoprotein Associated with Glycosphingolipid Microdomains 1 (PAG1))
Phosphoprotein membrane anchor with glycosphingoli,PAG (phosphoprotein associated with GEMs), also known as Cbp (Csk-binding protein), is a ubiquitously expressed 46 kDa transmembrane adaptor protein present in membrane rafts (glycosphingolipid-enriched microdomains), which however migrates on SDS PAGE gels anomalously as an 80 kDa molecule. Following tyrosine phosphorylation by Src family kinases, PAG binds and thereby activates the protein tyrosine kinase Csk, the major negative regulator of the Src family kinases. Signaling via the B-cell receptor in B cells or high affinity IgE receptor (FcepsilonRI) in mast cells leads to PAG increased tyrosine phosphorylation and Csk binding, while T cell receptor signaling causes PAG dephosphorylation, loss of Csk binding and increased activation of the protein tyrosine kinase Lck.,CBP, PAG