This PLC-gamma2-specific antibody conjugate may be used with conjugates of anti-PLC-gamma2 (pY759) mAb K86-689.37 to distinguish the expression of total versus phosphorylated PLC-gamma2. This antibody conjugate is suitable for intracellular staining of human whole blood and mouse splenocytes using the BD™ Phosflow Lyse/Fix Buffer and the BD™ Phosflow Perm Buffer II.
Probenmenge
20 μL
Beschränkungen
Nur für Forschungszwecke einsetzbar
Format
Liquid
Buffer
Aqueous buffered solution containing BSA and ≤0.09 % sodium azide.
Konservierungsmittel
Sodium azide
Vorsichtsmaßnahmen
This product contains Sodium azide: a POISONOUS AND HAZARDOUS SUBSTANCE which should be handled by trained staff only.
Lagerung
4 °C
Informationen zur Lagerung
Store undiluted at 4°C and protected from prolonged exposure to light. Do not freeze. The antibody was conjugated with R-PE under optimum conditions, and unconjugated antibody and free PE were removed.
Ozdener, Dangelmaier, Ashby, Kunapuli, Daniel: "Activation of phospholipase Cgamma2 by tyrosine phosphorylation." in: Molecular pharmacology, Vol. 62, Issue 3, pp. 672-9, (2002) (PubMed).
Wang, Feng, Wen, Marine, Sangster, Parganas, Hoffmeyer, Jackson, Cleveland, Murray, Ihle: "Phospholipase Cgamma2 is essential in the functions of B cell and several Fc receptors." in: Immunity, Vol. 13, Issue 1, pp. 25-35, (2000) (PubMed).
Target
PLC-g2
Hintergrund
The Phospholipase C (PLC) isozymes hydrolyze phosphatidyl inositol biphosphate to inositol triphosphate and diacylglycerol. The former causes release of calcium from the endoplasmic reticulum, while the latter is an activator of Protein Kinase C. Within the PLC family, PLC-g is the only member that contains SH2 and SH3 domains. These domains enable it to interact with receptor tyrosine kinases and become enzymatically activated via phosphorylation. It exists as two isoforms: 1) PLC-g1, which is ubiquitously expressed, and 2) PLCg2, found primarily in the lymphoid system. PLC-g is essential for growth factor-induced cell motility and mitogenesis. Overexpression of PLC-g is evident in several forms of cancer, and it has been identified as a key mediator of PDGF-dependent cellular transformation. Thus regulation of PLC-g activity by growth factors is involved in cell growth and transformation. Although the immunogen for generation of the K86-1161 monoclonal antibody was a phosphorylated peptide, peptide blocking studies demonstrated that the mAb recognizes PLC-g2 regardless of phosphorylation status. This antibody was raised to a unique region of PLC-gamma2 and is predicted not to crossreact with PLC-gamma1