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Merck

B7661

Sigma-Aldrich

Monoclonal Anti-Phosphothreonine−Biotin antibody produced in mouse

clone PTR-8, purified immunoglobulin, buffered aqueous solution

Synonym(e):

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

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About This Item

UNSPSC-Code:
12352203
NACRES:
NA.44

Biologische Quelle

mouse

Konjugat

biotin conjugate

Antikörperform

purified immunoglobulin

Antikörper-Produkttyp

primary antibodies

Klon

PTR-8, monoclonal

Form

buffered aqueous solution

Methode(n)

direct ELISA: 1:40,000 using phosphothreonine-BSA at 10 μg/ml, and using ExtrAvidin-HRP at 2 μg/ml
dot blot: 1:120,000

Isotyp

IgG2b

Versandbedingung

dry ice

Lagertemp.

−20°C

Posttranslationale Modifikation Target

unmodified

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Allgemeine Beschreibung

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 PTR-8 hybridoma produced by the fusion of mouse myeloma cells and splenocytes from BALB/c mice.

Immunogen

phosphothreonine conjugated to keyhole limpet hemocyanin (KLH).

Anwendung

Monoclonal Anti-Phosphothreonine−Biotin antibody produced in mouse has been used in phosphoprotein staining.

Biochem./physiol. Wirkung

Phosphorylation is a rare post-translational event in normal tissue. However, the abundance of phosphorylated cellular proteins increases several-fold following various activation processes. The residues phosphotyrosine, phosphoserine or phosphothreonine (p-Tyr/p-Ser/p-Thr) mediate such processes. Many signal transduction pathways, such as the epidermal growth factor (EGF) and insulin receptor systems, contain Tyr/Ser/Thr kinase which phosphorylates specific Tyr/Ser/Thr residues upon binding of ligands to their receptors. Monoclonal Anti-Phosphothreonine-Biotin may be used as an analytical tool for the identification and quantification of threonine-phosphorylated proteins

Physikalische Form

Solution in phosphate buffered saline containing 1% bovine serum albumin and 15 mM sodium azide

Lagerung und Haltbarkeit

For continuous use, store at 2-8 °C for up to one month. For extended storage, the solution may be frozen in working aliquots. Repeated freezing and thawing, or storage in "frost-free" freezers,is notrecommended. If slight turbidity occurs upon prolonged storage, clarify the solution by centrifugation before use.

Haftungsausschluss

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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Lagerklassenschlüssel

10 - Combustible liquids

WGK

nwg

Flammpunkt (°F)

Not applicable

Flammpunkt (°C)

Not applicable


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Die Dokumentenbibliothek aufrufen

Jennifer L Miller et al.
Journal of proteome research, 8(10), 4789-4798 (2009-08-26)
Mitochondria, the powerhouse of eukaryotic cells, have their own translation machinery that is solely responsible for synthesis of 13 mitochondrially encoded protein subunits of oxidative phosphorylation complexes. Phosphorylation is a well-known post-translational modification in regulation of many processes in mammalian
Ya-Wei Zhao et al.
Scientific reports, 6, 34817-34817 (2016-10-05)
Phosphorylation is one of the most important protein post-translation modifications. With the rapid development of high-throughput mass spectrometry, phosphorylation site data is rapidly accumulating, which provides us an opportunity to systematically investigate and predict phosphorylation in proteins. The phosphorylation of
Fatima Ardito et al.
International journal of molecular medicine, 40(2), 271-280 (2017-06-29)
Protein phosphorylation is an impo-rtant cellular regulatory mechanism as many enzymes and receptors are activated/deactivated by phosphorylation and dephosphorylation events, by means of kinases and phosph-atases. In particular, the protein kinases are responsible for cellular transduction signaling and their hyperactivity

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