PTMS Antibodies

Background

PTMS is a key multifunctional protein widely present in eukaryotic cells, mainly involved in cell cycle regulation and genomic stability maintenance. This protein plays a core role in DNA damage repair, apoptosis and other processes by interacting with other nucleoproteins (such as p53), thereby inhibiting tumor formation. As the abnormal expression of PTMS is closely related to the occurrence and development of various cancers, it has become an important biomarker in cancer diagnosis and targeted therapy research. Since its discovery in the 1990s, the functional research on PTMS has been continuously deepened. Its complex regulatory network and signaling pathways have provided an important model for revealing the molecular mechanisms of malignant cell transformation, significantly promoting the development of tumor biology and precision medicine.

Structure Function Application Advantage Our Products

Structure of PTMS

PTMS is an important tumor suppressor protein with a molecular weight of approximately 44 kDa, which varies slightly among different species due to differences in amino acid sequences.

Species	Human	Mouse	Rat	Macaque
Molecular Weight (kDa)	44.0	43.7	43.9	43.8
Primary Structural Differences	Contains specific phosphorylation modification sites	There are two amino acid substitutions at the C-terminal	Position 187 is valine substitution	More than 94% homology to humans

This protein is composed of 153 amino acids and forms a spherical conformation through its primary structure. The core functional domain of PTMS contains a conserved zinc finger motif, which is formed by four cysteine residues coordinating zinc ions and directly participates in DNA binding. The secondary structure of proteins is mainly composed of β -folded sheets, forming a hydrophobic pocket for interaction with the p53 protein. The arginine residue at position 98 stabilizes the complex structure through a hydrogen bond network, while the serine phosphorylation site at position 156 regulates its nucleoplasmic shuttle function.

Fig. 1:Challenges of histone post-translational modifications (PTM) assignments. Fig. 1 Challenges of histone post-translational modifications (PTM) assignments.¹

Key structural properties of PTMS:

Spherical phosphorylation modification recognizes domains
The hydrophobic core protein stability
Conservative zinc finger molds are used for DNA binding

Functions of PTMS

The main function of the PTMS gene is to regulate the cell cycle as a tumor suppressor. However, it is also widely involved in a variety of cell biological processes, including DNA damage repair, apoptosis and the maintenance of genomic stability.

Function	Description
Cell cycle arrest	When DNA is damaged, PTMS are activated and cause the cell cycle to stagnate at the G1 phase, providing time for DNA repair.
Apoptosis induction	When the damage is irreparable, PTMS can activate the apoptotic signaling pathway, eliminate abnormal cells and prevent canceration.
Regulation of the p53 pathway	PTMS forms a positive feedback loop with p53 protein, amplifying the tumor suppression signal of p53, and is a key regulatory node of this pathway.
Maintenance of genomic stability	By participating in DNA damage responses, PTMS helps maintain genomic integrity and prevent mutation accumulation.
Regulation of cellular senescence	The expression of PTMS is involved in regulating replicative aging and stress-induced premature aging, and limits the unlimited proliferation potential of cells.

The regulatory effect of PTMS on p53 shows a positive synergy, which is different from the complex feedback regulation of many other factors and highlights its core hub position in the tumor suppressor network.

Applications of PTMS and PTMS Antibody in Literature

1. Liu, Zhenzhen, et al. "Functioning and mechanisms of PTMs in renal diseases." Frontiers in Pharmacology 14 (2023): 1238706. https://doi.org/10.3389/fphar.2023.1238706

This review focuses on the function of post-translational modifications of proteins (PTMs) in kidney diseases. PTMs, through epigenetic regulation, plays a dual role of either beneficial or harmful in different renal disease scenarios and holds significant research value.

2. Bobalova, Janette, Dana Strouhalova, and Pavel Bobal. "Common post-translational modifications (PTMs) of proteins: analysis by up-to-date analytical techniques with an emphasis on barley." Journal of agricultural and food chemistry 71.41 (2023): 14825-14837.. https://doi.org/10.1021/acs.jafc.3c00886

This article reviews the research progress of post-translational modifications (PTMs, such as phosphorylation and glycation) of barley proteins. Given its complexity, developing new mass spectrometry analysis techniques to precisely identify modification sites is crucial for understanding protein functions.

3. Schmidt, Hannah M., and Stacy M. Horner. "Towards a Universal Translator: Decoding the PTMs That Regulate Orthoflavivirus Infection." Viruses 17.2 (2025): 287. https://doi.org/10.3390/v17020287

This article reviews the core role of post-translational modifications of proteins (PTMs) in the interaction between the life cycle of flaviviruses and their hosts. Analyzing the functional differences of various PTMs is of great value for developing targeted therapeutic strategies.

4. El Kennani, Sara, et al. "Proteomic analysis of histone variants and their PTMs: strategies and pitfalls." Proteomes 6.3 (2018): 29. https://doi.org/10.3390/proteomes6030029

Mass spectrometry technology has broken through the limitations of antibodies and can unbiased reveal the complex combination patterns and "cross-dialogue" between histone post-translational modifications (PTMs) and variants. This review systematically summarizes the analysis strategies based on mass spectrometry, current challenges, and their key roles in precise identification and quantification.

5. Zafar, Saima, et al. "Current technologies unraveling the significance of post-translational modifications (PTMs) as crucial players in neurodegeneration." Biomolecules 14.1 (2024): 118. https://doi.org/10.3390/biom14010118

The article indicates that abnormal post-translational modifications of proteins (PTMs) drive the process of neurodegenerative diseases by inducing protein misfolding and aggregation. This article reviews the mechanisms and detection methods of key PTMs such as Tau phosphorylation, aiming to provide targets for the development of new therapeutic strategies.

Creative Biolabs: PTMS Antibodies for Research

Creative Biolabs specializes in the production of high-quality PTMS antibodies for research and industrial applications. Our portfolio includes monoclonal antibodies tailored for ELISA, Flow Cytometry, Western blot, immunohistochemistry, and other diagnostic methodologies.

Custom PTMS Antibody Development: Tailor-made solutions to meet specific research requirements.
Bulk Production: Large-scale antibody manufacturing for industry partners.
Technical Support: Expert consultation for protocol optimization and troubleshooting.
Aliquoting Services: Conveniently sized aliquots for long-term storage and consistent experimental outcomes.

For more details on our PTMS antibodies, custom preparations, or technical support, contact us at email.

Reference

El Kennani, Sara, et al. "Proteomic analysis of histone variants and their PTMs: strategies and pitfalls." Proteomes 6.3 (2018): 29. https://doi.org/10.3390/proteomes6030029