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AB6187

Anti-Phosphothreonine 抗体

Anti-Phosphothreonine antibody

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(1 Publication)

Rabbit Polyclonal Phosphothreonine antibody. Suitable for ELISA, WB and reacts with Modified Amino Acid samples. Cited in 1 publication.
1 Images
ELISA - Anti-Phosphothreonine antibody (AB6187)
  • ELISA

Unknown

ELISA - Anti-Phosphothreonine antibody (AB6187)

Key facts

宿主種

Rabbit

クローン性

Polyclonal

アイソタイプ

IgG

キャリアフリー

No

アプリケーション

ELISA, WB

applications

特異性

Reacts with phosphorylated threonine both as free amino acid or when conjugated to a carrier protein such as BSA. Also, cross reacts with phosphorylated tyrosine.

Reactivity data

{ "title": "Reactivity Data", "filters": { "stats": ["", "Species", "Dilution Info", "Notes"], "tabs": { "all-applications": {"fullname" : "All Applications", "shortname": "All Applications"}, "ELISA" : {"fullname" : "ELISA", "shortname":"ELISA"}, "WB" : {"fullname" : "Western blot", "shortname":"WB"} }, "product-promise": { "all": "all", "testedAndGuaranteed": "tested", "guaranteed": "expected", "predicted": "predicted", "notRecommended": "not-recommended" } }, "values": { "Modified Amino Acid": { "ELISA-species-checked": "testedAndGuaranteed", "ELISA-species-dilution-info": "", "ELISA-species-notes": "<p></p>", "WB-species-checked": "guaranteed", "WB-species-dilution-info": "", "WB-species-notes": "<p></p>" } } }

出荷温度及び保存条件

製品の状態
Liquid
精製度
Whole antiserum
バッファー組成
Constituents: Whole serum
出荷温度
Blue Ice
短期保存期間
1-2 weeks
短期保存温度
+4°C
長期保存温度
-20°C
分注に関する情報
Upon delivery aliquot
保管に関する情報
Avoid freeze / thaw cycle

補足情報

This supplementary information is collated from multiple sources and compiled automatically.

Phosphothreonine often called phospho-threonine refers to a modified amino acid where a phosphate group attaches to threonine. It usually forms during protein post-translational modifications. This modification commonly occurs in eukaryotic cells and plays a significant role in regulating protein function. The mass of phosphothreonine itself is approximately 181 Da. Phosphothreonine residues are found in various proteins where they serve as important components for controlling multiple cellular processes.
Biological function summary

Phosphorylation of threonine residues influences protein activity localization and interactions. These phosphorylated threonine residues often exist as part of a larger protein complex influencing the dynamics of protein interactions. In cellular signal transduction they act as key regulatory switches. The modification is a reversible process which allows dynamic control over protein functionality in response to cellular signals.

Pathways

Signaling cascades often rely on phosphorylation events involving threonine which includes pathways like MAPK and PI3K/AKT. These pathways are essential for cellular responses to external stimuli and involve several other proteins such as RAS and AKT themselves. Through such pathways the phosphorylation state of threonine residues affects decisions about cell survival proliferation or differentiation.

Dysregulation of threonine phosphorylation links to conditions like cancer and diabetes. Abnormal phosphorylation patterns can lead to unregulated cell growth and survival common in tumorigenesis. Proteins such as p53 and insulin receptor substrates interact with phosphorylated threonine residues in these contexts. Investigating these interactions provides insights into the pathological mechanisms and potential therapeutic targets.

製品プロトコール

For this product, it's our understanding that no specific protocols are required. You can visit:

文献 (1)

Recent publications for all applications. Explore the full list and refine your search

The Biochemical journal 450:537-46 PubMed23252429

2012

Polyphenols differentially inhibit degranulation of distinct subsets of vesicles in mast cells by specific interaction with granule-type-dependent SNARE complexes.

Applications

Unspecified application

Species

Unspecified reactive species

Yoosoo Yang,Jung-Mi Oh,Paul Heo,Jae Yoon Shin,Byoungjae Kong,Jonghyeok Shin,Ji-Chun Lee,Jeong Su Oh,Kye Won Park,Choong Hwan Lee,Yeon-Kyun Shin,Dae-Hyuk Kweon
View all publications

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