Phosphotyrosine antibody (HRP)
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- Target See all Phosphotyrosine products
- Phosphotyrosine
- Reactivity
- Please inquire
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Host
- Mouse
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Clonality
- Monoclonal
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Conjugate
- This Phosphotyrosine antibody is conjugated to HRP
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Application
- Western Blotting (WB), Immunoprecipitation (IP), Immunofluorescence (IF), Immunohistochemistry (IHC), Immunocytochemistry (ICC)
- Specificity
- Reacts with phosphotyrosine, and detects the presence of phosphotyrosine in both un-stimulated and stimulated cell lysates. Does not cross-react with phosphoserine or phosphothreonine.
- Purification
- Protein G Purified
- Immunogen
- Phosphotyrosine, alanine and glyceine in a 1:1:1 ratio polymerized in the presence of keyhole limpet hemocyanin with 1-ethyl-3-(3'-dimentrylaminopropyl) carbodiimide
- Clone
- G104
- Isotype
- IgG1
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- Application Notes
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- WB (1:1000)
- IHC (1:100)
- optimal dilutions for assays should be determined by the user.
- Comment
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1 μg/ml of ABIN2484578 was sufficient for detection of phosphorylated tyrosine residues in 10 μg of rat tissue lysate by colorimetric immunoblot analysis using Goat anti-rat IgG:HRP as the secondary antibody.
- Restrictions
- For Research Use only
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- Format
- Liquid
- Concentration
- 1 mg/mL
- Buffer
- PBS pH 7.4, 50 % glycerol, 0.09 % sodium azide, Storage buffer may change when conjugated
- Preservative
- Sodium azide
- Precaution of Use
- This product contains Sodium azide: a POISONOUS AND HAZARDOUS SUBSTANCE which should be handled by trained staff only.
- Storage
- 4 °C
- Storage Comment
- Conjugated antibodies should be stored at 4°C
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- Target
- Phosphotyrosine
- Abstract
- Phosphotyrosine Products
- Target Type
- Amino Acid
- Background
- 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 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 (3). Changing the function of these proteins has been linked to a number of diseases, including cancer, diabetes, heart disease, inflammation and neurological disorders (4-6). In particular, the phosphorylation of tyrosine is considered one of the key steps in signal transduction and regulation of enzymatic activity (7). Phosphotyrosine can be detected through specific antibodies, and are helpful in facilitating the identification of tyrosine kinase substrates (8).
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