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AB7851

Anti-Phosphoserine antibody [B106.1]

3

(1 Review)

|

(7 Publications)

Mouse Monoclonal Phosphoserine antibody. Suitable for WB and reacts with Modified Amino Acid samples. Cited in 7 publications. Immunogen corresponding to Chemical / Small Molecule corresponding to Phosphoserine.

View Alternative Names

PS, pSER, phospho-Ser

Key facts

Host species

Mouse

Clonality

Monoclonal

Clone number

B106.1

Isotype

IgG1

Light chain type

unknown

Carrier free

No

Applications

WB

applications

Specificity

This antibody detects free and conjugated phosphoserine as well as phosphoserine in modified cellular proteins. It does not cross react with nonphosphorylated serine or with phosphotyrosine or phosphothreonine, neither does it cross react with AMP or ATP. However, due to steric hinderance, certain proteins known to contain phosphorylated serine may not be recognized by this antibody.

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Reactivity data

{ "title": "Reactivity Data", "filters": { "stats": ["", "Species", "Dilution Info", "Notes"], "tabs": { "all-applications": {"fullname" : "All Applications", "shortname": "All Applications"}, "WB" : {"fullname" : "Western blot", "shortname":"WB"} }, "product-promise": { "all": "all", "testedAndGuaranteed": "tested", "guaranteed": "expected", "predicted": "predicted", "notRecommended": "not-recommended" } }, "values": { "Modified Amino Acid": { "WB-species-checked": "guaranteed", "WB-species-dilution-info": "1/50", "WB-species-notes": "<p>Do not use milk as a blocking agent or in diluents, as milk casein is phosphorylated at several serine residues. BSA is recommended instead.</p>" } } }
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Properties and storage information

Form
Liquid
Purification technique
Affinity purification Protein G
Storage buffer
pH: 7.4 Preservative: 0.1% Sodium azide Constituents: PBS
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.

Phosphoserine often referred to by its common alternate name "P-Ser" represents a phosphorylated form of the amino acid serine. This small molecule under a molecular mass of near 166 Daltons plays an important role in cellular signaling. It is expressed widely across various cell types particularly in tissues with high cell turnover. Phosphoserine results from the action of kinases which transfer a phosphate group from ATP to the serine's hydroxyl group. This phosphorylation process provides a critical modulatory mechanism that impacts protein function and cellular pathways.
Biological function summary

Phosphorylated serine residues are involved in controlling a multitude of cellular processes including cell cycle regulation and apoptosis. These phosphorylated regions form parts of protein kinases phosphatases and glycoproteins acting as switches for cellular signaling. Phosphoserine is often part of multi-protein complexes binding to other proteins and influencing their activity through changes in conformation. This active participation in biological pathways signifies its significant influence in maintaining cellular homeostasis.

Pathways

Phosphoserine plays a significant role in the MAPK signaling and PI3K/AKT pathways both important for cell growth and survival. It interacts with proteins like AKT and MAPK facilitating cellular responses to extracellular stimuli. This phosphorylation state dictates the activation or inactivation of these proteins effectively regulating key steps in signal transduction and transcriptional control. Such pathways highlight the importance of phosphoserine in coordinating complex cellular activities.

Aberrations in phosphoserine activity have been linked to conditions such as cancer and neurodegenerative diseases. In cancer dysregulation in its phosphorylation status may lead to uncontrolled cellular proliferation and resistance to apoptosis. Proteins such as p53 which plays a pivotal role in DNA repair and cell cycle arrest often show altered phosphorylation patterns in the presence of disease. Similarly in neurodegenerative disorders improper phosphorylation of tau proteins is a hallmark of conditions like Alzheimer's disease pointing to the critical involvement of phosphoserine and its associated pathways in disease pathology.
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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 Phosphoserine
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Publications (7)

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

EMBO reports 26:720-747 PubMed39747662

2025

HDAC6 deacetylates TRIM56 to negatively regulate cGAS-STING-mediated type I interferon responses.

Applications

Unspecified application

Species

Unspecified reactive species

Qiongzhen Zeng,Zixin Chen,Shan Li,Ziwei Huang,Zhe Ren,Cuifang Ye,Xiao Wang,Jun Zhou,Kaisheng Liu,Kai Zheng,Yifei Wang

Heliyon 10:e35303 PubMed39170313

2024

ITPKA phosphorylates PYCR1 and promotes the progression of glioma.

Applications

Unspecified application

Species

Unspecified reactive species

Xiangying Luo,Tao Chen,Junyi Deng,Ziyuan Liu,Changlong Bi,Song Lan

Science advances 9:eadg7112 PubMed37595040

2023

FOXA1 O-GlcNAcylation-mediated transcriptional switch governs metastasis capacity in breast cancer.

Applications

Unspecified application

Species

Unspecified reactive species

Yajie Liu,Kairan Yu,Xiaotian Kong,Keren Zhang,Lingyan Wang,Nana Zhang,Qiushi Chen,Mingshan Niu,Wenli Li,Xiaomin Zhong,Sijin Wu,Jianing Zhang,Yubo Liu

EMBO reports 24:e56458 PubMed37249035

2023

O-GlcNAcylation promotes topoisomerase IIα catalytic activity in breast cancer chemoresistance.

Applications

Unspecified application

Species

Unspecified reactive species

Yangzhi Liu,Kairan Yu,Keren Zhang,Mingshan Niu,Qiushi Chen,Yajie Liu,Lingyan Wang,Nana Zhang,Wenli Li,Xiaomin Zhong,Guohui Li,Sijin Wu,Jianing Zhang,Yubo Liu

Pflugers Archiv : European journal of physiology 475:583-593 PubMed36917272

2023

Calcineurin-dependent regulation of gap junction conductance and connexin phosphorylation in guinea pig left atrium.

Applications

Unspecified application

Species

Unspecified reactive species

R I Jabr,S C Salvage,F S Hatch,C H Fry

Nature medicine 21:373-82 PubMed25799226

2015

Activation of AMPKα2 in adipocytes is essential for nicotine-induced insulin resistance in vivo.

Applications

WB, IP

Species

Unspecified reactive species, Unspecified reactive species

Yue Wu,Ping Song,Wencheng Zhang,Junhui Liu,Xiaoyan Dai,Zhaoyu Liu,Qiulun Lu,Changhan Ouyang,Zhonglin Xie,Zhengxing Zhao,Xiaozhen Zhuo,Benoit Viollet,Marc Foretz,Jiliang Wu,Zuyi Yuan,Ming-Hui Zou

Small (Weinheim an der Bergstrasse, Germany) 6:1509-13 PubMed20578112

2010

Kinase-actuated immunoaggregation of Peptide-conjugated gold nanoparticles.

Applications

Unspecified application

Species

Unspecified reactive species

Shalini Gupta,Heiko Andresen,James E Ghadiali,Molly M Stevens
View all publications
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