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Merck

P5872

Anti-Phosphotyrosine antibody, Mouse monoclonal

clone PT-66, purified from hybridoma cell culture

Synonyme(s) :

Monoclonal Anti-Phosphotyrosine, Phospho-Tyr, Phospho-tyrosine, p-Tyr

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A propos de cet article

NACRES:
NA.44
UNSPSC Code:
12352203
Conjugate:
unconjugated
Clone:
PT-66, monoclonal
Application:
ELISA (i), FACS, ICC, IHC, IP, RIA, WB
Citations:
17
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biological source

mouse

Quality Level

conjugate

unconjugated

antibody form

purified immunoglobulin

antibody product type

primary antibodies

clone

PT-66, monoclonal

form

buffered aqueous solution

packaging

antibody small pack of 25 μL

concentration

~2 mg/mL

technique(s)

flow cytometry: suitable, immunocytochemistry: suitable, immunohistochemistry: suitable, immunoprecipitation (IP): suitable, indirect ELISA: 0.5-1.0 μg/mL using phosphotyrosine conjugated to BSA, radioimmunoassay: suitable, western blot: 0.25-0.5 μg/mL using total cell extract of human platelets

isotype

IgG1

shipped in

dry ice

storage temp.

−20°C

target post-translational modification

unmodified

General description

As determined by ELISA and competitive ELISA, the antibody reacts specifically with phosphorylated tyrosine, both as free amino acid or conjugated to carriers such as BSA or KLH. No cross-reactivity is observed with non-phosphorylated tyrosine, phosphothreonine, phosphoserine, AMP or ATP.
Monoclonal Anti-Phosphotyrosine (mouse IgG1 isotype) is derived from the PT-66 hybridoma produced by the fusion of mouse myeloma cells and splenocytes from BALB/c mice immunized with phosphotyrosine-BSA conjugate.

Immunogen

phosphotyrosine conjugated to BSA

Application

Monoclonal Anti-Phosphotyrosine has been used in
  • immunoblotting,
  • immunofluorescence,
  • immunohistochemistry
  • immunocytochemistry
  • flow cytometry
  • immunoprecipitation
  • enzyme linked immunosorbent assay (ELISA)
  • radio immunoassay (RIA)
  • immunoaffinity isolation

Biochem/physiol Actions

Monoclonal Anti-Phosphotyrosine is specific for phosphorylated tyrosine both as the free amino acid or when conjugated to carriers such as BSA or KLH. It does not react with non-phosphorylated tyrosine or other phosphorylated amino acids, including serine
Protein phosphorylation is a basic signaling mechanism that modifies protein function in eukaryotic cells. Serine, threonine, and tyrosine are the major phosphorylated amino acids in proteins. Tyrosine phosphorylation is a rare post-translational event in normal tissues, accounting for only 0.03% of phosphorylated amino acids. However, this phosphorylation increases several folds by various activation signals and the process is mediated by protein tyrosine kinases. 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.

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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Classe de stockage

12 - Non Combustible Liquids

wgk

WGK 2

flash_point_f

Not applicable

flash_point_c

Not applicable



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Contenu apparenté

Instructions


Cyclin D1 governs adhesion and motility of macrophages
Neumeister P, et al.
Molecular Biology of the Cell, 14(5), 2005-2015 (2003)
Dongwon Choi et al.
Circulation research, 120(9), 1426-1439 (2017-02-09)
Lymphatic vessels function to drain interstitial fluid from a variety of tissues. Although shear stress generated by fluid flow is known to trigger lymphatic expansion and remodeling, the molecular basis underlying flow-induced lymphatic growth is unknown. We aimed to gain
Amy M Nichols et al.
Methods in molecular biology (Clifton, N.J.), 492, 143-160 (2009-02-26)
Mass spectrometry-based analysis of protein phosphorylation has become increasingly powerful over the past decade and has been applied to many different biological systems. One of the most significant concerns facing the phosphoproteomics community and the proteomics field as a whole