PAG1 Antibody (MEM-255) Summary
| Immunogen |
Recombinant intracellular fragment, corresponding to amino acids 97-432 of Human Cbp/PAG (NM_018440.3).
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| 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).
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| Isotype |
IgG2a
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| Clonality |
Monoclonal
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| Host |
Mouse
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| Gene |
PAG1
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| Purity |
Protein A purified
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Applications/Dilutions
| Dilutions |
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| Application Notes |
Purity is > 95% (by SDS-PAGE). Flow Cytometry – intracellular staining, permeabilization required Western Blot – 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.
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Packaging, Storage & Formulations
| Storage |
Store at 4C. Do not freeze.
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| Buffer |
PBS (pH 7.4)
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| Preservative |
15mM Sodium Azide
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| Concentration |
1.0 mg/ml
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| Purity |
Protein A purified
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Alternate Names for PAG1 Antibody (MEM-255)
- CBP
- CBPMGC138364
- Csk-binding protein
- PAG1
- PAGFLJ37858
- phosphoprotein associated with glycosphingolipid microdomains 1
- phosphoprotein associated with glycosphingolipid-enriched microdomains 1
- Transmembrane adapter protein PAG
- Transmembrane phosphoprotein Cbp
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.