P1869
Anti-Phosphotyrosine antibody, Mouse monoclonal
clone pT-154, purified from hybridoma cell culture
Synonym(s):
Phospho-Tyr, Phospho-tyrosine, p-Tyr
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About This Item
Recommended Products
conjugate
unconjugated
antibody form
purified immunoglobulin
antibody product type
primary antibodies
clone
pT-154, monoclonal
concentration
~2 mg/mL
technique(s)
direct ELISA: suitable
immunohistochemistry: suitable
microarray: suitable
western blot: 2-4 μg/mL using total extract of A431 cells stimulated by EGF
isotype
IgG2b
shipped in
dry ice
storage temp.
−20°C
target post-translational modification
unmodified
Related Categories
General description
Anti-Phosphotyrosine antibody, Mouse monoclonal (mouse IgG2b isotype) is derived from the pT-154 hybridoma produced by the fusion of mouse myeloma cells and splenocytes from BALB/c mice immunized with a tyrosine phosphorylated peptide. Members of protein-tyrosine kinases (PTKs) family consists of extra-cellular domain that is responsible for ligand binding, a trans-membrane domain, modular domain and an intracellular domain.
Immunogen
tyrosine phosphorylated peptide.
Application
Anti-Phosphotyrosine antibody, Mouse monoclonal has been used in:
- enzyme linked immunosorbent assay (ELISA)
- western blot
- immunohistochemistry
Biochem/physiol Actions
Protein phosphorylation is a post-translational modification that regulates signal transduction. Phosphorylation of tyrosine residues in proteins has been associated with oncogenesis, cell growth and survival . Monoclonal Anti-Phosphotyrosine antibody is specific for rat and human proteins/peptides that contain phosphotyrosine residues. As determined by competitive ELISA, the product does not bind to non-phosphorylated tyrosine, phosphorylated serine or threonine, ATP or AMP.
Protein-tyrosine kinases (PTKs) are enzymes that catalyze the transfer of Γ-phosphate of ATP to tyrosine residues of protein substrates. The PTKs are responsible for many biological processes like cell cycle, proliferation, oncogenesis and development. They are tightly regulated by other kinases and by autophosphorylation activity. Monoclonal antibodies specific for phosphotyrosine are essential tools for the study of tyrosine phosphorylation in post-translational modification in many biological processes.
Physical form
Solution in 0.01 M phosphate buffered saline, pH 7.4, containing 15 mM sodium azide.
Disclaimer
Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.
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Storage Class Code
10 - Combustible liquids
Flash Point(F)
Not applicable
Flash Point(C)
Not applicable
Certificates of Analysis (COA)
Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.
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Protein tyrosine kinase structure and function
Hubbard SR and Till JH
Annual Review of Biochemistry, 69(1), 373-398 (2000)
Shashikant Gupta et al.
Andrologia, 54(1), e14255-e14255 (2021-09-29)
In this study, the cryoprotective potential of natural antioxidant curcumin in Hariana bull semen was evaluated as an additive in a tris-based extender with the assessment of motility and motion parameters of spermatozoa, membrane intactness, progesterone-receptor binding, protein carbonyl content
Tyrosine kinase-role and significance in cancer
Paul MK and Mukhopadhyay AK
International Journal of Medical Sciences, 1(2), 101-101 (2004)
Debrup Sengupta et al.
The EMBO journal, 38(16), e99266-e99266 (2019-07-05)
During MHC-I-restricted antigen processing, peptides generated by cytosolic proteasomes are translocated by the transporter associated with antigen processing (TAP) into the endoplasmic reticulum, where they bind to newly synthesized MHC-I molecules. Dendritic cells and other cell types can also generate
S C Roy et al.
International journal of andrology, 31(1), 12-24 (2007-03-16)
The aim of the present study was to determine the effect of L-arginine on nitric oxide (NO*) synthesis, capacitation and protein tyrosine phosphorylation in buffalo spermatozoa. Ejaculated buffalo spermatozoa were capacitated in the absence or presence of heparin, or L-arginine
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