Accéder au contenu
MilliporeSigma
Toutes les photos(1)

Documents

A5964

Sigma-Aldrich

Monoclonal Anti-Phosphotyrosine–Peroxidase antibody produced in mouse

clone PT-66, purified immunoglobulin, lyophilized powder

Synonyme(s) :

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

Se connecterpour consulter vos tarifs contractuels et ceux de votre entreprise/organisme


About This Item

Code UNSPSC :
12352203
Nomenclature NACRES :
NA.43

Source biologique

mouse

Niveau de qualité

Conjugué

peroxidase conjugate

Forme d'anticorps

purified immunoglobulin

Type de produit anticorps

primary antibodies

Clone

PT-66, monoclonal

Forme

lyophilized powder

Conditionnement

vial of 0.2 mL conjugate

Technique(s)

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

Isotype

IgG1

Température de stockage

2-8°C

Modification post-traductionnelle de la cible

unmodified

Vous recherchez des produits similaires ? Visite Guide de comparaison des produits

Catégories apparentées

Description générale

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.

Spécificité

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.

Immunogène

phosphotyrosine conjugated to BSA

Application

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

Actions biochimiques/physiologiques

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.

Forme physique

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

Clause de non-responsabilité

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.

Not finding the right product?  

Try our Outil de sélection de produits.

Code de la classe de stockage

13 - Non Combustible Solids

Classe de danger pour l'eau (WGK)

WGK 3

Point d'éclair (°F)

Not applicable

Point d'éclair (°C)

Not applicable


Certificats d'analyse (COA)

Recherchez un Certificats d'analyse (COA) en saisissant le numéro de lot du produit. Les numéros de lot figurent sur l'étiquette du produit après les mots "Lot" ou "Batch".

Déjà en possession de ce produit ?

Retrouvez la documentation relative aux produits que vous avez récemment achetés dans la Bibliothèque de documents.

Consulter la Bibliothèque de documents

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)
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
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
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]
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

Notre équipe de scientifiques dispose d'une expérience dans tous les secteurs de la recherche, notamment en sciences de la vie, science des matériaux, synthèse chimique, chromatographie, analyse et dans de nombreux autres domaines..

Contacter notre Service technique