WB, IP, IF, IHC, ICC
Host: Mouse
Monoclonal
G104
PE
Application Notes
Western blot (7): 2 μg/mL. ELISA (7): 0.5 μg/mL. Immunoprecipitation: 10 μg/mL sample. Immunohistochemistry. Other applications not tested. Optimal dilutions are dependent on conditions and should be determined by the user.
Restrictions
For Research Use only
Format
Liquid
Concentration
0.25 mg/mL
Buffer
PBS, pH 7, 0.01 % Sodium Azide
Preservative
Sodium azide
Precaution of Use
This product contains sodium azide: a POISONOUS AND HAZARDOUS SUBSTANCE which should be handled by trained staff only.
Handling Advice
Avoid repeated freezing and thawing.
Storage
4 °C/-20 °C
Storage Comment
Store undiluted at 2-8 °C for one month or (in aliquots) at -20 °C for longer.
Protein phosphorylation is an important posttranslational modification that serves many key functions to regulate a protein's activity, localization, and protein-protein interactions. Phosphorylation is catalyzed by various specific protein kinases, which involves removing a phosphate group from ATP and covalently attaching it to a recipient protein that acts as a substrate. Most kinases act on both serine and threonine, others act on tyrosine, and a number (dual specificity kinases) act on all three. Because phosphorylation can occur at multiple sites on any given protein, it can therefore change the function or localization of that protein at any time (1). Changing the function of these proteins has been linked to a number of diseases, including cancer, diabetes, heart disease, inflammation and neurological disorders (2-4). In particular, the phosphorylation of tyrosine is considered one of the key steps in signal transduction and regulation of enzymatic activity (5). Phosphotyrosine can be detected through specific antibodies, and are helpful in facilitating the identification of tyrosine kinase substrates (6).