PTPMT1 Human

Protein Tyrosine Phosphatase, Mitochondrial 1 Human Recombinant
Cat. No.
BT25663
Source
Escherichia Coli.
Synonyms
Protein-tyrosine phosphatase mitochondrial 1, PTEN-like phosphatase, Phosphoinositide lipid phosphatase, PTPMT1, MOSP, PLIP, DUSP23, PNAS-129.
Appearance
Sterile Filtered colorless solution.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Usage
THE BioTek's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
Shipped with Ice Packs
In Stock

Description

PTPMT1 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 199 amino acids (28-201) and having a molecular mass of 22.6kDa.
PTPMT1 is fused to a 25 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Product Specs

Introduction
Protein tyrosine phosphatase mitochondrial 1 (PTPMT1) is a protein tyrosine phosphatase found in the inner membrane of mitochondria. It is highly expressed in various tissues, including pancreatic beta cells. PTPMT1 plays a crucial role in regulating mitochondrial function, particularly ATP production, by dephosphorylating specific mitochondrial proteins. It exhibits a preference for phosphatidylinositol 5-phosphate, a lipid signaling molecule, as a substrate.
Description
Recombinant PTPMT1, derived from humans and expressed in E. coli, is a non-glycosylated polypeptide consisting of 199 amino acids (residues 28-201). It has a molecular weight of 22.6 kDa. This PTPMT1 protein includes a 25 amino acid His-tag at the N-terminus to facilitate purification by proprietary chromatographic techniques.
Physical Appearance
Clear, colorless, and sterile solution.
Formulation
PTPMT1 is supplied as a 1 mg/ml solution in a buffer consisting of 20mM Tris-HCl (pH 8.0), 10% glycerol, 1mM DTT, and 0.15M NaCl.
Stability
For short-term storage (up to 4 weeks), keep the PTPMT1 vial refrigerated at 4°C. For extended periods, store the protein frozen at -20°C. It is recommended to add a carrier protein like HSA or BSA (0.1%) for long-term storage. Avoid repeated freezing and thawing of the PTPMT1 solution.
Purity
The purity of PTPMT1 is greater than 95% as determined by SDS-PAGE analysis.
Synonyms
Protein-tyrosine phosphatase mitochondrial 1, PTEN-like phosphatase, Phosphoinositide lipid phosphatase, PTPMT1, MOSP, PLIP, DUSP23, PNAS-129.
Source
Escherichia Coli.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSHMKVPGR AHRDWYHRID PTVLLGALPL RSLTRQLVQD ENVRGVITMN EEYETRFLCN SSQEWKRLGV EQLRLSTVDM TGIPTLDNLQ KGVQFALKYQ SLGQCVYVHC KAGRSRSATM VAAYLIQVHK WSPEEAVRAI AKIRSYIHIR PGQLDVLKEF HKQITARATK DGTFVISKT.

Product Science Overview

Structure and Function

PTPMT1 is a mitochondrial protein that specifically mediates the dephosphorylation of mitochondrial proteins, thereby playing an essential role in ATP production . It has been shown to display phosphatase activity toward phosphoprotein substrates, which is critical for maintaining cellular energy homeostasis .

Biological Significance

PTPMT1 is involved in several metabolic pathways, including glycerophospholipid biosynthesis and general metabolism . Its activity is essential for the proper functioning of mitochondrial processes, which are vital for energy production and overall cellular health .

Expression Patterns and Tissue Distribution

PTPMT1 is ubiquitously expressed in various tissues, with significant roles in lymphoid tissue, bone marrow, testis, and skeletal muscle . It is also involved in immune responses and protein ubiquitination, highlighting its diverse functional roles in different biological contexts .

Clinical Relevance

Mutations or dysregulation of PTPMT1 have been associated with several diseases, including primary ciliary dyskinesia and Barth syndrome . Given its central role in mitochondrial function and energy production, PTPMT1 is a potential target for therapeutic interventions aimed at treating metabolic disorders and mitochondrial diseases .

Research and Therapeutic Potential

Ongoing research is focused on understanding the detailed mechanisms of PTPMT1’s action and its interactions with other proteins. This knowledge is crucial for developing specific inhibitors or modulators that can be used in clinical settings to treat diseases associated with mitochondrial dysfunction .

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