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Merck
모든 사진(2)

주요 문서

E6126

Sigma-Aldrich

Enolase from baker′s yeast (S. cerevisiae)

lyophilized powder, ≥50 units/mg protein

동의어(들):

2-Phospho-D-glycerate hydro-lyase, Phosphopyruvate hydratase

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500 UNITS
₩161,284
2500 UNITS
₩722,376
12500 UNITS
₩2,127,136

₩161,284


재고 있음세부사항

기존과 동일한 품질을 인하된 가격으로 - 어려운 예산 상황을 머크와 함께 극복하세요


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보기 변경
500 UNITS
₩161,284
2500 UNITS
₩722,376
12500 UNITS
₩2,127,136

About This Item

CAS Number:
효소 위원회 번호:
EC Number:
MDL number:
UNSPSC 코드:
12352204
NACRES:
NA.54

₩161,284


재고 있음세부사항

기존과 동일한 품질을 인하된 가격으로 - 어려운 예산 상황을 머크와 함께 극복하세요

양식

lyophilized powder

Quality Level

특이 활성도

≥50 units/mg protein

분자량

93 kDa

구성

Protein, 50-80% modified Warburg-Christian

solubility

15 mM Tris HCl, pH 7.4: soluble 1.0 mg/mL, clear

저장 온도

−20°C

일반 설명

Enolase (2-phosphoglycerate hydratase) is a cytosolic enzyme.[1] This cytosolic metalloenzyme is encoded by three homologous genes in mammals.[2] Enolase the from baker′s yeast is a homodimer containing two bound Mg2+ ions. The peptide consists of 436 amino acids and contains a single cysteine residue and corresponds to a molecular weight of 93 kDa. Two of the active site components include His191 and Arg414. Enolase is seen in archaea, bacteria and eukaryotes.[3]

애플리케이션

Enolase from baker′s yeast (S. cerevisiae) has been used as a supplement in assay buffer for phosphoglycerate mutase (PGM) enzyme assays.[4][5]
Enolase from baker′s yeast has been used in a study to investigate the contribution of the antibodies response induced by a low virulent Candida albicans strain in protection against systemic candidiasis. Enolase from baker′s yeast has also been used in a study to investigate the role of metal ions in catalysis by enolase.
The enzyme from Sigma has been used as an antigen during ELISA. the study used human granulocyte proteins to identify and characterize autoantibodies against catalase and α-enolase in patients with primary sclerosing cholangitis.[6] It has been used to study temperature- and denaturant-induced yeast enolase denaturation using fourier transform infrared spectroscopy.[7] It has also been used along with other proteins to study gradient chromatofocusing-mass spectrometry; a new technique for protein analysis.[8]

생화학적/생리학적 작용

Enolase is a metalloenzyme that catalyzes the interconversion of 2-phosphoglycerate to phosphoenolpyruvate. Enolase is essential for both glycolysis and gluconeogenesis.
Enolase plays a key role in glycolysis and gluconeogenesis. Enolase, found in the nucleus of mammalian cells plays a key role in transcriptional modulation of genes, which participates in morphological transformation and cell proliferation.[3]
The phosphorylated tyrosine residue present in yeast enolase forms a substrate for phosphorylation by tyrosine protein kinase.[9] Apart from Mg2+, the enzyme can be activated by Zn2+, Mn2+, and Cd2+.[10]

단위 정의

One unit will convert 1.0 μmole of 2-phosphoglycerate to phospho(enol)pyruvate per min at pH 7.4 at 25 °C.

물리적 형태

Lyophilized powder containing Tris buffer salts

Storage Class Code

11 - Combustible Solids

WGK

WGK 3

Flash Point (°F)

Not applicable

Flash Point (°C)

Not applicable

개인 보호 장비

Eyeshields, Gloves, type N95 (US)


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문서 라이브러리 방문

Thermal, chemical and chemothermal denaturation of yeast enolase.
Huang, Ping, and Aichun Dong.
Spectroscopy: An International Journal, 17(2), 453-467 (2003)
Cofactor-independent phosphoglycerate mutase has an essential role in Caenorhabditis elegans and is conserved in parasitic nematodes
Zhang Y, et al.
The Journal of biological chemistry, 279(35), 37185-37190 (2004)
Lian Shan et al.
Journal of the American Society for Mass Spectrometry, 19(8), 1132-1137 (2008-06-10)
A new analytical technique, gradient chromatofocusing-mass spectrometry (gCF-MS), was developed employing ion-exchange high-performance liquid chromatography (HPLC) interfaced to an electrospray-quadrupole mass spectrometer in the determination of proteins. There have been few reports, if any, of a HPLC-MS technique for proteins
Measurement of enolase activity in cell lysates
Test, 542, 115-124 (2014)
C C Chin et al.
The Journal of biological chemistry, 256(3), 1377-1384 (1981-02-10)
Automatic sequencing of yeast enolase and of its chemically and enzymatically produced peptide fragments has established the sequence of 416 of the 436 residues in the enolase subunits. The missing segments have been provided from results from sequencing the DNA

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