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Merck
모든 사진(2)

문서

C7688

Sigma-Aldrich

Chaperonin 60 from Escherichia coli

>95% (SDS-PAGE), recombinant, expressed in E. coli overproducing strain, lyophilized powder

동의어(들):

Cpn60, GroEL

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About This Item

MDL number:
UNSPSC 코드:
12352200
NACRES:
NA.32

생물학적 소스

Escherichia coli

Quality Level

재조합

expressed in E. coli overproducing strain

분석

>95% (SDS-PAGE)

형태

lyophilized powder

기술

electron microscopy: suitable
mass spectrometry (MS): suitable

적합성

passes test (Refolding (w/GroES))

UniProt 수납 번호

저장 온도

2-8°C

유전자 정보

human ... HSPD1(3329)

일반 설명

Research area: Cell Signaling

Chaperonin 60 (GroEL) and chaperonin 10 (GroES) belong to the ubiquitous family of heat-shock molecular chaperones found in prokaryotes and in eukaryotic organelles.

애플리케이션

Chaperonin 60 from Escherichia coli has been used:
  • in mass spectroscopy
  • in cryo-electron microscopy imaging as control for testing particle distribution
  • as standard in infrared spectrum measurements
  • as a protein sample for stability assessment and characterization studies using differential mobility analysis (DMA) and cryo-electron microscopy (cryo-EM).

생화학적/생리학적 작용

Apart from its role in facilitating protein folding, chaperonin 60 (Cpn60) serves as an extracellular signaling protein, showing functional similarities to certain proinflammatory cytokines. Furthermore, Cpn60 contributes to the inhibition of lipid accumulation and adipogenesis during the initial stages of cellular differentiation, thereby exerting anti-obesity effects.

포장

Package size based on protein content.

물리적 형태

Lyophilized powder containing Tris buffer salts, potassium chloride, magnesium chloride, dithiothreitol, and trehalose as stabilizer.

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)


시험 성적서(COA)

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문서 라이브러리 방문

Infrared irradiation in the collision cell of a hybrid tandem quadrupole/time-of-flight mass spectrometer for declustering and cleaning of nanoelectrosprayed protein complex ions
El-Faramawy A, et al.
Analytical Chemistry, 82(23), 9878-9884 (2010)
Self-assembled monolayers improve protein distribution on holey carbon cryo-EM supports
Meyerson JR, et al.
Scientific Reports, 4(2), 7084-7084 (2014)
Separating and visualising protein assemblies by means of preparative mass spectrometry and microscopy
Benesch JLP, et al.
Journal of Structural Biology, 172(2), 161-168 (2010)
Stéphane Erb et al.
Methods in molecular biology (Clifton, N.J.), 2247, 173-191 (2020-12-11)
By maintaining intact multi-protein complexes in the gas-phase, native mass spectrometry provides their molecular weight with very good accuracy compared to other methods (typically native PAGE or SEC-MALS) (Marcoux and Robinson, Structure 21:1541-1550, 2013). Besides, heterogeneous samples, in terms of
Zachary L VanAernum et al.
Nature protocols, 15(3), 1132-1157 (2020-02-02)
It is important to assess the identity and purity of proteins and protein complexes during and after protein purification to ensure that samples are of sufficient quality for further biochemical and structural characterization, as well as for use in consumer

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