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AB9344

Anti-Phosphothreonine-Proline / Phosphoserine-Proline antibody

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(14 Publications)

Rabbit Polyclonal Phosphothreonine-Proline / Phosphoserine-Proline antibody. Suitable for ELISA, WB and reacts with Modified Amino Acid samples. Cited in 14 publications. Immunogen corresponding to Chemical / Small Molecule corresponding to Phosphothreonine-Proline / Phosphoserine-Proline.
1 Images
Western blot - Anti-Phosphothreonine-Proline / Phosphoserine-Proline antibody (AB9344)
  • WB

Unknown

Western blot - Anti-Phosphothreonine-Proline / Phosphoserine-Proline antibody (AB9344)

All lanes:

Western blot - Anti-Phosphothreonine-Proline / Phosphoserine-Proline antibody (ab9344)

Lane 1:

Phosphorprotein protein kinase A PKA

Lane 2:

Myelin Basic Protein (MBP)

false

Key facts

Host species

Rabbit

Clonality

Polyclonal

Isotype

IgG

Carrier free

No

Applications

ELISA, WB

applications

Specificity

This antibody specifically reacts to proteins containing phosphothreonine-proline motifs, it also reacts to the phosphoserine-proline motif to a similar degree (pT-P and pS-P motif). The antibody does not react to phosphothreonine, phosphoserine or phosphotyrosine. The antibody will selectively recognize the phosphothreonine-proline motif of MBP, which is the site of phosphorylation by ERK1/ERK2.

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AB117253

Anti-Phospho - (Ser/Thr) antibody

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Primary Antibodies

AB218195

Anti-Phosphothreonine antibody [EPR22006-23]

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Western blot - Anti-Phosphothreonine antibody [EPR22006-23] (AB218195)

  • 0
  • 0
Primary Antibodies

AB9337

Anti-Phosphothreonine antibody

Western blot - Anti-Phosphothreonine antibody (AB9337)

  • 4
  • 3
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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": "guaranteed", "ELISA-species-dilution-info": "", "ELISA-species-notes": "<p></p>", "WB-species-checked": "testedAndGuaranteed", "WB-species-dilution-info": "", "WB-species-notes": "<p></p>" } } }
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Product details

The antigen is based on N-acetyl-pT-K-pY-NH2. The pT-X-pY sequence is considered to be the motif for some active MAPKs.
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Properties and storage information

Form
Liquid
Purification technique
Affinity purification Immunogen
Purification notes
Immunoaffinity chromatography with phosphothreonine-proline on agarose, then immuno-absorption with threonine-proline-NH2 on agarose.
Storage buffer
pH: 6 - 8 Preservative: 0.02% Sodium azide
Shipped at conditions
Blue Ice
Appropriate short-term storage duration
1-2 weeks
Appropriate short-term storage conditions
+4°C
Appropriate long-term storage conditions
-20°C
Storage information
Avoid freeze / thaw cycle
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Supplementary information

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

Phosphothreonine-Proline and Phosphoserine-Proline are key post-translational modifications often involved in signaling pathways. These sites are characterized by the addition of a phosphate group to the hydroxyl group of threonine or serine residues adjacent to proline creating unique recognition motifs. They are especially significant in cell cycle regulation and various cellular processes. These motifs are recognized by specialized proteins like proline-directed kinases and peptidyl-prolyl isomerases. Expression occurs widely in tissues where active signal transduction is essential. The exact molecular mass varies depending on the protein context in which these motifs occur.
Biological function summary

These phosphorylation motifs play roles in regulating protein function and stability. Phosphothreonine-Proline and Phosphoserine-Proline facilitate interactions with proteins such as Pin1 a well-known peptidyl-prolyl isomerase. This interaction modulates protein folding and function. These motifs influence cell cycle progression apoptosis and cellular differentiation showing involvement in complex signal transduction networks. Their presence can alter the conformation and thereby the activity of signaling proteins.

Pathways

Phosphothreonine-Proline and Phosphoserine-Proline modifications integrate into major pathways like MAPK and PI3K/Akt. They regulate activities of proteins such as cyclin-dependent kinases (CDKs) and Akt impacting cellular responses to external signals. These signaling pathways are essential for cellular growth survival and metabolism. Modifications on threonine and serine residues can influence the phosphorylation status and activity of these downstream effectors creating a dynamic and responsive signaling network.

Alterations in these phosphorylation sites contribute to conditions like cancer and neurodegenerative diseases. Over- or under-phosphorylation can lead to disrupted cell cycle control and apoptosis conditions often linked to tumors. Abnormal phosphorylation patterns may also relate to pathologies like Alzheimer’s disease where proteins such as Tau show abnormal phosphorylation states. This highlights the connection between these phosphorylation motifs and protein dysfunctions associated with disease progression.
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Product protocols

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

See full target information Phosphothreonine-Proline / Phosphoserine-Proline
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Publications (14)

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

Cell reports 43:114831 PubMed39392755

2024

ERK1/2 interaction with DHPS regulates eIF5A deoxyhypusination independently of ERK kinase activity.

Applications

Unspecified application

Species

Unspecified reactive species

Andrew E Becker,Paweł Kochanowski,Pui-Kei Wu,Elżbieta Wątor,Wenjing Chen,Koushik Guchhait,Artur P Biela,Przemysław Grudnik,Jong-In Park

PLoS genetics 19:e1010804 PubMed37384599

2023

The CERV protein of Cer1, a C. elegans LTR retrotransposon, is required for nuclear export of viral genomic RNA and can form giant nuclear rods.

Applications

Unspecified application

Species

Unspecified reactive species

Bing Sun,Haram Kim,Craig C Mello,James R Priess

NPJ Parkinson's disease 8:46 PubMed35443760

2022

Cdk5 phosphorylation-induced SIRT2 nuclear translocation promotes the death of dopaminergic neurons in Parkinson's disease.

Applications

Unspecified application

Species

Unspecified reactive species

Jianguo Yan,Pei Zhang,Jie Tan,Mao Li,Xingfeng Xu,Xiaoyun Shao,Fang Fang,Zhenyou Zou,Yali Zhou,Bo Tian

Cell death & disease 12:608 PubMed34117217

2021

K63-linked ubiquitination of DYRK1A by TRAF2 alleviates Sprouty 2-mediated degradation of EGFR.

Applications

Unspecified application

Species

Unspecified reactive species

Pengshan Zhang,Zhe Zhang,Yinkun Fu,Ying Zhang,Michael P Washburn,Laurence Florens,Min Wu,Chen Huang,Zhaoyuan Hou,Man Mohan

Cancer research 79:4135-4148 PubMed31209060

2019

p38 Stabilizes Snail by Suppressing DYRK2-Mediated Phosphorylation That Is Required for GSK3β-βTrCP-Induced Snail Degradation.

Applications

Unspecified application

Species

Unspecified reactive species

Ki-Jun Ryu,Sun-Mi Park,Seung-Ho Park,In-Kyu Kim,Hyeontak Han,Hyo-Jin Kim,Seon-Hee Kim,Keun-Seok Hong,Hyemin Kim,Minju Kim,Sung-Jin Yoon,Killivalavan Asaithambi,Kon Ho Lee,Jae-Yong Park,Young-Sool Hah,Hee Jun Cho,Jong In Yook,Jung Wook Yang,Gyung-Hyuck Ko,Gyemin Lee,Yang Jae Kang,Cheol Hwangbo,Kwang Dong Kim,Young-Jun Park,Jiyun Yoo

The Journal of biological chemistry 293:10220-10234 PubMed29764937

2018

Cyclin-dependent kinase 1 (CDK1) and CDK2 have opposing roles in regulating interactions of splicing factor 3B1 with chromatin.

Applications

Unspecified application

Species

Unspecified reactive species

Tushar Murthy,Theresa Bluemn,Abhishek K Gupta,Michael Reimer,Sridhar Rao,Manoj M Pillai,Alex C Minella

Nature communications 9:1876 PubMed29760377

2018

Cyclin K regulates prereplicative complex assembly to promote mammalian cell proliferation.

Applications

Unspecified application

Species

Unspecified reactive species

Tingjun Lei,Peixuan Zhang,Xudong Zhang,Xue Xiao,Jingli Zhang,Tong Qiu,Qian Dai,Yujun Zhang,Ling Min,Qian Li,Rutie Yin,Ping Ding,Ni Li,Yi Qu,Dezhi Mu,Jun Qin,Xiaofeng Zhu,Zhi-Xiong Xiao,Qintong Li

Nature 546:426-430 PubMed28607489

2017

The metabolic function of cyclin D3-CDK6 kinase in cancer cell survival.

Applications

Unspecified application

Species

Unspecified reactive species

Haizhen Wang,Brandon N Nicolay,Joel M Chick,Xueliang Gao,Yan Geng,Hong Ren,Hui Gao,Guizhi Yang,Juliet A Williams,Jan M Suski,Mark A Keibler,Ewa Sicinska,Ulrike Gerdemann,W Nicholas Haining,Thomas M Roberts,Kornelia Polyak,Steven P Gygi,Nicholas J Dyson,Piotr Sicinski

Journal of experimental botany 68:1585-1597 PubMed28369656

2017

Two maize Kip-related proteins differentially interact with, inhibit and are phosphorylated by cyclin D-cyclin-dependent kinase complexes.

Applications

Unspecified application

Species

Unspecified reactive species

Silvia K Godínez-Palma,Fernando R Rosas-Bringas,Omar G Rosas-Bringas,Elpidio García-Ramírez,Jorge Zamora-Zaragoza,Jorge M Vázquez-Ramos

Nucleic acids research 44:7755-65 PubMed27402161

2016

Phosphorylation of Ku70 subunit by cell cycle kinases modulates the replication related function of Ku heterodimer.

Applications

IP

Species

Unspecified reactive species

Soumita Mukherjee,Prabal Chakraborty,Partha Saha
View all publications
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Product promise

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