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Merck

A5964

Sigma-Aldrich

Monoclonal Anti-Phosphotyrosine–Peroxidase antibody produced in mouse

clone PT-66, purified immunoglobulin, lyophilized powder

Szinonimák:

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

Bejelentkezésa Szervezeti és Szerződéses árazás megtekintéséhez


About This Item

UNSPSC kód:
12352203
NACRES:
NA.43
konjugátum:
peroxidase conjugate
application:
DB
ELISA (d)
klón:
PT-66, monoclonal
technika/technikák:
direct ELISA: 1:60,000 using Phosphotyrosine-BSA
dot blot: 1:40,000-1:200,000 using phosphotyrosine-BSA using chromogenic and chemiluminescent substrates, respectively
citations:
12

biológiai forrás

mouse

Minőségi szint

konjugátum

peroxidase conjugate

antitest forma

purified immunoglobulin

antitest terméktípus

primary antibodies

klón

PT-66, monoclonal

Forma

lyophilized powder

kiszerelés

vial of 0.2 mL conjugate

technika/technikák

direct ELISA: 1:60,000 using Phosphotyrosine-BSA
dot blot: 1:40,000-1:200,000 using phosphotyrosine-BSA using chromogenic and chemiluminescent substrates, respectively

izotípus

IgG1

tárolási hőmérséklet

2-8°C

célzott transzláció utáni módosítás

unmodified

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Általános leírás

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 a phosphotyrosine-BSA conjugate.

Egyediség

Mouse anti-phosphotyrosine-peroxidase antibody reacts specifically with phosphorylated tyrosine coupled to BSA. The product has shown no reactivity for other phosphorylated amino acids like phosphothreonine and phosphoserine.

Immunogén

phosphotyrosine conjugated to BSA

Alkalmazás

Monoclonal Anti-Phosphotyrosine-Peroxidase antibody has been used in
  • enzyme linked immunosorbent assay (ELISA)
  • dot blot
  • Chemiluminescence dot blot
  • kinase assay

Biokémiai/fiziológiai hatások

Reversible phosphorylation of proteins is an important post-translational modification that plays a regulatory role in the expression of most proteins in the cells. Reversible phosphorylation at multiple serine, tyrosine and threonine residues mediates numerous signalling pathways in both prokaryotic and eukaryotic cells . Cellular proteins with phosphorylated tyrosine increase many fold by the activation of tyrosine kinases. Most mitogenic receptor systems such as EGF, PDGF, insulin receptors contain serine/threonine/tyrosine kinase domains that undergo autophosphorylation when receptors bind to the respective ligands. Monoclonal anti-phosphotyrosine–peroxidase antibody can be used in kinase assay to visualize the fraction of phosphorylated substrate.

Fizikai forma

Lyophilized from a solution containing 1% bovine serum albumin and 0.05% MIT in 0.01 M sodium phosphate buffered saline.

Jogi nyilatkozat

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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Tárolási osztály kódja

13 - Non Combustible Solids

WGK

WGK 3

Lobbanási pont (F)

Not applicable

Lobbanási pont (C)

Not applicable


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Analitikai tanúsítványok (COA)

Lot/Batch Number

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Dokumentumtár megtekintése

Yuko Naito et al.
Molecular and cellular biology, 27(8), 3008-3022 (2007-02-14)
Sialic acid (Sia) is a family of acidic nine-carbon sugars that occupies the nonreducing terminus of glycan chains. Diversity of Sia is achieved by variation in the linkage to the underlying sugar and modification of the Sia molecule. Here we
Bobbi Xayarath et al.
Journal of bacteriology, 189(9), 3369-3381 (2007-02-27)
Extracellular polysaccharides of many bacteria are synthesized by the Wzy polymerase-dependent mechanism, where long-chain polymers are assembled from undecaprenyl-phosphate-linked repeat units on the outer face of the cytoplasmic membrane. In gram-positive bacteria, Wzy-dependent capsules remain largely cell associated via membrane
Identification and biophysical assessment of the molecular recognition mechanisms between the human haemopoietic cell kinase Src homology domain 3 and ALG-2-interacting protein X
Shi X, et al.
The Biochemical Journal, 431(1), 93-102 (2010)
Ana Izabel Silva Balbin Villaverde et al.
Molecular & cellular proteomics : MCP, 19(11), 1860-1875 (2020-08-26)
After ejaculation, mammalian spermatozoa must undergo a process known as capacitation in order to successfully fertilize the oocyte. Several post-translational modifications occur during capacitation, including sialylation, which despite being limited to a few proteins, seems to be essential for proper
Xiaoli Shi et al.
The Biochemical journal, 431(1), 93-102 (2010-07-31)
SFKs (Src family kinases) are central regulators of many signalling pathways. Their functions are tightly regulated through SH (Src homology) domain-mediated protein-protein interactions. A yeast two-hybrid screen using SH3 domains as bait identified Alix [ALG-2 (apoptosis-linked gene 2)-interacting protein X]

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