ENO2 Human
Enolase-2 Human Recombinant
Cat. No.
BT16740
Source
Escherichia Coli.
Synonyms
Gamma-enolase, EC 4.2.1.11, 2-phospho-D-glycerate hydro-lyase, Neural enolase, Neuron-specific enolase, NSE, Enolase 2, ENO2.
Appearance
Sterile Filtered clear solution.
Purity
Greater than 95% 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
ENO2 Human Recombinant expressed in E. coli contains 434 amino acids and its Mw is 47 kDa.
The Enolase-2 is purified by proprietary chromatographic techniques.
The Enolase-2 is purified by proprietary chromatographic techniques.
Product Specs
Introduction
Neuron-specific enolase (NSE), also known as Enolase-2, is a glycolytic isoenzyme primarily found in central and peripheral neurons and neuroendocrine cells. NSE is released into the cerebrospinal fluid (CSF) following neural tissue injury. Additionally, neoplasms originating from neural or neuroendocrine tissue release NSE into the bloodstream. NSE serves as a valuable biomarker for detecting and monitoring various tumors, including neuroblastoma, small cell lung cancer, medullary thyroid cancer, carcinoid tumors, pancreatic endocrine tumors, and melanoma. As one of the three enolase isoenzymes present in mammals, NSE is specifically found in mature neurons and cells of neuronal origin. During the development of neural tissue in rats and primates, a transition from alpha enolase to gamma enolase (NSE) takes place.
Description
Recombinant human ENO2, expressed in E. coli, consists of 434 amino acids and exhibits a molecular weight of 47 kDa. The purification of Enolase-2 is achieved using proprietary chromatographic techniques.
Physical Appearance
Clear, sterile-filtered solution.
Formulation
Enolase 2 is provided in a buffer solution containing 20mM Tris (pH 7.5), 0.1M KCl, and 5mM MgSO4.
Stability
For short-term storage (1-2 weeks), the product should be kept at 4°C. For extended storage, it is recommended to freeze the product at -20°C. Repeated freeze-thaw cycles should be avoided.
Purity
The purity of the product is greater than 95%, as determined by SDS-PAGE analysis.
Synonyms
Gamma-enolase, EC 4.2.1.11, 2-phospho-D-glycerate hydro-lyase, Neural enolase, Neuron-specific enolase, NSE, Enolase 2, ENO2.
Source
Escherichia Coli.
Amino Acid Sequence
MSIEKIWARE ILDSRGNPTV EVDLYTAKGL FRAAVPSGAS TGIYEALELR DGDKQRYLGK GVLKAVDHIN STIAPALISS GLSVVEQEKL DNLMLELDGT ENKSKFGANA ILGVSLAVCK AGAAERELPL YRHIAQLAGN SDLILPVPAF NVINGGSHAG NKLAMQEFMI LPVGAESFRD AMRLGAEVYH TLKGVIKDKY GKDATNVGDE GGFAPNILEN SEALELVKEA IDKAGYTEKI VIGMDVAASE FYRDGKYDLD FKSPTDPSRY ITGDQLGALY QDFVRDYPVV SIEDPFDQDD WAAWSKFTAN VGIQIVGDDL TVTNPKRIER AVEEKACNCL LLKVNQIGSV TEAIQACKLA QENGWGVMVS HRSGETEDTF IADLVVGLCT GQIKTGAPCR SERLAKYNQL MRIEEELGDE ARFAGHNFRN PSVL.
Product Science Overview
Structure and Function
Recombinant Production
Recombinant Human Enolase-2 is typically produced in Escherichia coli (E. coli) expression systems. The recombinant protein is often tagged with a histidine (His) tag to facilitate purification. The protein is purified to a high degree, with a purity greater than 95% as determined by SDS-PAGE and visualized with silver staining .
Applications
Recombinant Enolase-2 is used in various research applications, including:
- Biochemical studies: Understanding the enzyme’s role in glycolysis and gluconeogenesis.
- Clinical diagnostics: Serving as a biomarker for neuronal damage and neuroendocrine tumors.
- Drug development: Screening for potential inhibitors or modulators of enolase activity.
Storage and Stability
Assay Procedure
The activity of recombinant Enolase-2 can be measured by its ability to convert phosphoglyceric acid to phosphoenolpyruvate. The specific activity is typically greater than 6,000 pmol/min/μg under the described conditions .
Enolase-2’s role in glycolysis and its specificity to neurons make it a significant enzyme for both basic research and clinical applications. Its recombinant form allows for detailed studies and potential therapeutic developments.
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