ENOPH1 Human

Enolase-Phosphatase-1 Human Recombinant
Cat. No.
BT28574
Source
Escherichia Coli.
Synonyms
Enolase-phosphatase E1, 2,3-diketo-5-methylthio-1-phosphopentane phosphatase, MASA homolog, ENOPH1, MASA, E1, MST145, FLJ12594, DKFZp586M0524.
Appearance
Sterile Filtered colorless solution.
Purity
Greater than 90.0% 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.
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Description

ENOPH1 Human Recombinant fused with a 20 amino acid His tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 281 amino acids (1-261 a.a.) and having a molecular mass of 31kDa. The ENOPH1 is purified by proprietary chromatographic techniques.

Product Specs

Introduction
Enolase-phosphatase E1 (ENOPH1), a member of the MasA family within the HAD (halo-acid dehalogenase)-like hydrolase superfamily, exhibits dual functionality as both a phosphatase and an atypical enolase. This enzyme plays a crucial role in the ubiquitous methionine salvage pathway, a fundamental biochemical process present in all organisms that regulates cellular methionine levels.
Description
Recombinant human ENOPH1, expressed in E. coli, is a single, non-glycosylated polypeptide chain. This protein construct consists of 281 amino acids, including a 20 amino acid His tag at the N-terminus (1-261 a.a. of the ENOPH1 sequence), resulting in a molecular mass of 31 kDa. Purification of ENOPH1 is achieved through proprietary chromatographic techniques.
Physical Appearance
Clear, colorless solution, sterile filtered.
Formulation
The ENOPH1 solution is provided at a concentration of 1 mg/ml in a buffer consisting of 20mM Tris-HCl (pH 8.0), 1mM DTT, 10% glycerol, and 100mM NaCl.
Stability
For short-term storage (2-4 weeks), the ENOPH1 solution should be kept at 4°C. For extended storage, it is recommended to freeze the solution at -20°C. To ensure optimal stability during long-term storage, the addition of a carrier protein (0.1% HSA or BSA) is advised. Repeated freezing and thawing of the solution should be avoided.
Purity
The purity of ENOPH1 is determined to be greater than 90% by SDS-PAGE analysis.
Synonyms
Enolase-phosphatase E1, 2,3-diketo-5-methylthio-1-phosphopentane phosphatase, MASA homolog, ENOPH1, MASA, E1, MST145, FLJ12594, DKFZp586M0524.
Source
Escherichia Coli.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MVVLSVPAEV TVILLDIEGT TTPIAFVKDI LFPYIEENVK EYLQTHWEEE ECQQDVSLLR KQAEEDAHLD GAVPIPAASG NGVDDLQQMI QAVVDNVCWQ MSLDRKTTAL KQLQGHMWRA AFTAGRMKAE FFADVVPAVR KWREAGMKVY IYSSGSVEAQ KLLFGHSTEG DILELVDGHF DTKIGHKVES ESYRKIADSI GCSTNNILFL TDVTREASAA EEADVHVAVV VRPGNAGLTD DEKTYYSLIT SFSELYLPSS T.

Product Science Overview

Structure and Function

ENOPH1 is a protein-coding gene that encodes a multifunctional enzyme involved in the methionine salvage pathway and sulfur amino acid metabolism . The enzyme catalyzes the conversion of 2-phosphoglycerate to phosphoenolpyruvate during glycolysis, a critical step in energy production within cells . This reaction is essential for maintaining cellular energy homeostasis and supporting various metabolic processes.

Role in Cancer

Recent studies have highlighted the tumor-promoting properties of ENOPH1, particularly in breast cancer . ENOPH1 expression is significantly upregulated in breast cancer tissues compared to adjacent normal tissues, and its overexpression is associated with advanced cancer stages, node metastasis, and poor overall survival . Functional assays have demonstrated that ENOPH1 overexpression accelerates cancer cell proliferation, migration, and invasion, primarily through the activation of the NF-κB signaling pathway . This makes ENOPH1 a potential prognostic factor and therapeutic target for breast cancer treatment.

Clinical Implications

The overexpression of ENOPH1 in various cancers and its role in promoting tumor progression suggest that it could serve as a valuable biomarker for cancer diagnosis and prognosis . Additionally, targeting ENOPH1 with specific inhibitors could provide a novel therapeutic approach for treating cancers characterized by high ENOPH1 expression.

Research and Development

Human recombinant ENOPH1 is produced using advanced biotechnological methods to ensure high purity and activity. This recombinant enzyme is widely used in research to study its biochemical properties, regulatory mechanisms, and potential therapeutic applications. Ongoing research aims to further elucidate the molecular mechanisms underlying ENOPH1’s role in cancer and other diseases, paving the way for the development of targeted therapies.

In conclusion, Enolase-Phosphatase 1 (Human Recombinant) is a critical enzyme with significant implications in cellular metabolism and cancer progression. Its role as a potential biomarker and therapeutic target underscores the importance of continued research in this field.

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