PTK2
Reaktivität: Human
WB, PLA
Wirt: Kaninchen
Polyclonal
unconjugated
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
The antibody was conjugated to Alexa Fluor® 488 under optimum conditions, and unreacted Alexa Fluor® 488 was removed. Store undiluted at 4°C and protected from prolonged exposure to light. Do not freeze.
Schlaepfer, Mitra, Ilic: "Control of motile and invasive cell phenotypes by focal adhesion kinase." in: Biochimica et biophysica acta, Vol. 1692, Issue 2-3, pp. 77-102, (2004) (PubMed).
Ma, Richardson, Schaefer, Parsons: "Serine phosphorylation of focal adhesion kinase in interphase and mitosis: a possible role in modulating binding to p130(Cas)." in: Molecular biology of the cell, Vol. 12, Issue 1, pp. 1-12, (2001) (PubMed).
Yamakita, Totsukawa, Yamashiro, Fry, Zhang, Hanks, Matsumura: "Dissociation of FAK/p130(CAS)/c-Src complex during mitosis: role of mitosis-specific serine phosphorylation of FAK." in: The Journal of cell biology, Vol. 144, Issue 2, pp. 315-24, (1999) (PubMed).
Target
FAK (PTK2)
(PTK2 Protein tyrosine Kinase 2 (PTK2))
Focal Adhesion Kinase (FAK) is a cytoplasmic tyrosine kinase that associates with integrins in focal adhesions. Its cellular localization is directed by a 125-amino acid sequence at the C terminus called the Focal Adhesion Targeting (FAT) domain, and the phosphorylation state of serine 910 (S910) in the FAT domain may regulate the assembly of focal adhesions. Furthermore, the binding of extracellular matrix ligands to integrins triggers tyrosine phosphorylations near FAK’s kinase domain that increase its kinase activity, and additional tyrosine phosphorylations near proline-rich motifs create binding sites for the SH2 domains of various adaptor proteins. FAK's ability to bind numerous structural and signaling proteins via a variety of interactions regulates FAK’s targeting to focal adhesions, modulates its kinase activity, and initiates intracellular signaling cascades. Thus, studies suggest that FAK may integrate cellular events controlling cell motility, growth, and invasiveness. The K73-480 monoclonal antibody recognizes the phosphorylated S910 of human FAK. The orthologous phosphorylation sites in mouse and rat FAK are S948 and S913, respectively.