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Merck

P1869

Sigma-Aldrich

Anti-Phosphotyrosine antibody, Mouse monoclonal

clone pT-154, purified from hybridoma cell culture

Sinónimos:

Phospho-Tyr, Phospho-tyrosine, p-Tyr

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About This Item

MDL number:
UNSPSC Code:
12352203
NACRES:
NA.44

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conjugate

unconjugated

Quality Level

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

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

10 - Combustible liquids

flash_point_f

Not applicable

flash_point_c

Not applicable


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    Visite la Librería de documentos

    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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