| Clone: | MEM-255 |
|---|---|
| Isotype: | Mouse IgG2a |
| Specificity: | 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). |
| Immunogen: | Recombinant intracellular fragment (aa 97-432) of human Cbp (PAG). |
| Species Reactivity: | Human |
| Negative Species: | Mouse, Rat, Bovine |
| Application: |
Flow Cytometry
Recommended dilution:
2 μg/ml
Application note: intracellular staining, permeabilization required
Western Blotting
Application note:
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.
Immunohistochemistry (paraffin sections)
Positive tissue:tonsil, spleen
|
| Purity: | > 95% (by SDS-PAGE) |
| Purification: | Purified from ascites by protein-A affinity chromatography. |
| Concentration: | 1 mg/ml |
| Storage Buffer: | Phosphate buffered saline (PBS) with 15 mM sodium azide, approx. pH 7.4 |
| Storage / Stability: | Store at 2-8°C. Do not use after expiration date stamped on vial label. For long-term storage aliquot and store at -20°C. Avoid freeze/thaw cycles. |
| Expiration: | See vial label |
| Lot Number: | See vial label |
| Background: | 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. |
| References: |
*Horejsí V, Zhang W, Schraven B: Transmembrane adaptor proteins: organizers of immunoreceptor signalling. Nat Rev Immunol. 2004 Aug;4(8):603-16.
*Brdicka T, Pavlistova D, Leo A, Bruyns E, Korinek V, Angelisova P, Scherer J, Shevchenko A, Hilgert I, Cerny J, Drbal K, Kuramitsu Y, Kornacker B, Horejsi V, Schraven B: Phosphoprotein associated with glycosphingolipid-enriched microdomains (PAG), a
novel ubiquitously expressed transmembrane adaptor protein, binds the protein tyrosine kinase csk and is involved in regulation of T cell activation. J Exp Med. 2000 May 1;191(9):1591-604.
*Brdickova N, Brdicka T, Andera L, Spicka J, Angelisova P, Milgram SL, Horejsi V: Interaction between two adapter proteins, PAG and EBP50: a possible link between membrane rafts and actin cytoskeleton. FEBS Lett. 2001 Oct 26;507(2):133-6.
Semac I, Palomba C, Kulangara K, Klages N, van Echten-Deckert G, Borisch B, Hoessli DC: Anti-CD20 therapeutic antibody rituximab modifies the functional organization of rafts/microdomains of B lymphoma cells. Cancer Res. 2003 Jan 15;63(2):534-40.
*Davidson D, Bakinowski M, Thomas ML, Horejsi V, Veillette A: Phosphorylation-dependent regulation of T-cell activation by PAG/Cbp, a lipid raft-associated transmembrane adaptor.
Mol Cell Biol. 2003 Mar;23(6):2017-28.
*Tedoldi S, Paterson JC, Hansmann ML, Natkunam Y, Rudiger T, Angelisova P, Du MQ, Roberton H, Roncador G, Sanchez L, Pozzobon M, Masir N, Barry R, Pileri S, Mason DY, Marafioti T, Horejsi V: Transmembrane adaptor molecules: a new category of lymphoid-cell markers.
Blood. 2006 Jan 1;107(1):213-21. Epub 2005 Sep 13.
*Svec A, Velenská Z, Horejsí V: Expression pattern of adaptor protein PAG: correlation between secondary lymphatic follicle and histogenetically related malignant lymphomas. Immunol Lett. 2005 Aug 15;100(1):94-7.
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