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Key Documents

P3555

Sigma-Aldrich

Monoclonal Anti-Phosphothreonine antibody produced in mouse

clone PTR-8, ascites fluid

Synonyme(s) :

Monoclonal Anti-Phosphothreonine, Phospho Thr, Phospho Threonine, Phospho−Thr, Phospho-Threonine, p-Thr

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About This Item

Code UNSPSC :
12352203
Nomenclature NACRES :
NA.44

Source biologique

mouse

Niveau de qualité

Conjugué

unconjugated

Forme d'anticorps

ascites fluid

Type de produit anticorps

primary antibodies

Clone

PTR-8, monoclonal

Contient

15 mM sodium azide

Technique(s)

indirect ELISA: 1:4,000
western blot: 1:50

Isotype

IgG2b

Conditions d'expédition

dry ice

Température de stockage

−20°C

Modification post-traductionnelle de la cible

unmodified

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Description générale

As determined by ELISA and dot blot, the antibody reacts specifically with phosphorylated threonine, both as free amino acid or conjugated to carriers such as BSA or KLH. No cross-reactivity is observed with non-phosphorylated threonine, phosphoserine, phosphotyrosine, AMP or ATP. This antibody has been used in immunoblotting for the localization of some phosphothreonine-containing proteins. Certain proteins known to contain phosphorylated threonine may not be recognized by this antibody due to steric hindrance of the recognition site.
Monoclonal Anti-Phosphothreonine (mouse IgG2b isotype) is derived from the hybridoma produced by the fusion of mouse myeloma cells and splenocytes from an immunized mouse.

Immunogène

phosphothreonine conjugated to keyhole limpet hemocyanin (KLH).

Application

Monoclonal Anti-Phosphothreonine antibody produced in mouse has been used in:immunoblotting, enzyme linked immuno sorbent assay (ELISA) ,dot blot.
Monoclonal and polyclonal antibodies directed against phosphorylated residues may be useful as analytical and preparative tools, by enabling the identification, quantification and immunoaffinity isolation of phosphorylated cellular proteins. Antibodies can be employed to monitor alterations in phosphorylation of specific proteins as they occur in intact organs or even whole animals.
Mouse monoclonal clone PTR-8 anti-phosphothreonine antibody may be used for the localization of phosphorylated threonine using various immunochemical assays such as ELISA, dot blot, and immunoblotting. Due to steric hindrance of the recognition site, this antibody may not recognize certain proteins known to contain phosphorylated threonine.
Mouse monoclonal clone PTR-8 anti-Phosphothreonine antibody reacts with phosphorylated threonine both as a free amino acid or when conjugated to carriers such as BSA or KLH, using ELISA and dot blot. It does not react with nonphosphorylated threonine, phosphorylated tyrosine or serine, AMP or ATP.

Actions biochimiques/physiologiques

Protein phosphorylation and dephosphorylation are basic mechanisms for the modification of protein function in eukaryotic cells. Phosphorylation is a rare post-translational event in normal tissue. However, the abundance of phosphorylated cellular proteins increases tenfold following various activation processes, which are mediated through phosphotyrosine, phosphoserine or phosphothreonine (p-Tyr/p-Ser/p-Thr). Many different mitogenic systems, such as the EGF, PDGF and insulin receptor systems, contain Tyr/Ser/Thr kinase domains that autophosphorylate specific Tyr/Ser/Thr residues upon binding of their ligands. T cell antigen receptor complex or receptors for some hemopoietic growth factors may stimulate associated kinases, and cells transformed by viral oncogenes contain elevated levels of phosphorylated Tyr/Ser/Thr. An understanding of transformation by oncogenes and mitogenic processes of growth factors depends on the identification of their substrate and a subsequent determination of how phosphorylation affects the properties of these proteins.

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.

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Produit(s) apparenté(s)

Réf. du produit
Description
Tarif

Code de la classe de stockage

10 - Combustible liquids

Classe de danger pour l'eau (WGK)

WGK 3

Point d'éclair (°F)

Not applicable

Point d'éclair (°C)

Not applicable


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Sijo V Chemmannur et al.
International journal of nanomedicine, 11, 2039-2051 (2016-06-09)
Owing to the suppression of immune responses and associated side effects, steroid based treatments for inflammatory encephalitis disease can be detrimental. Here, we demonstrate a novel carbon nanosphere (CNP) based treatment regime for encephalomyelitis in mice by exploiting the functional
S L Gaffen et al.
Proceedings of the National Academy of Sciences of the United States of America, 92(16), 7192-7196 (1995-08-01)
To explore the possible involvement of STAT factors ("signal transducers and activators of transcription") in the interleukin 2 receptor (IL-2R) signaling cascade, murine HT-2 cells expressing chimeric receptors composed of the extracellular domain of the erythropoietin receptor fused to the
Quantification of the Dynamic Phosphorylation Process Of ERK Using Stable Isotope Dilution Selective Reaction Monitoring Mass Spectrometry
Lee N, et al.
Proteomics, 1900086-1900086 (2019)
Clémence Rougeaux et al.
Cellular microbiology, 10(3), 632-654 (2007-11-06)
Human decay accelerating factor (hDAF, CD55) and members of the carcinoembryonic-antigen-related cell-adhesion molecules (hCEACAMs) family are recognized as receptors by Gram-negative, diffusely adhering Escherichia coli (DAEC) strains expressing Afa/Dr adhesins. We report here that hCEACAM1-4L has a key function in
Takeru Zama et al.
The Journal of biological chemistry, 277(26), 23909-23918 (2002-04-18)
Mitogen-activated protein kinases (MAPKs) are activated in response to various extracellular stimuli, and their activities are regulated by upstream activating kinases and protein phosphatases such as MAPK phosphatases (MKPs). We report the identification and characterization of a novel MKP termed

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