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Merck
모든 사진(3)

문서

SRE0045

Sigma-Aldrich

Luciferase from Photinus pyralis (firefly)

recombinant, expressed in E. coli, lyophilized powder, ≥10×1010 units/mg protein

동의어(들):

Luciferase firefly

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About This Item

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

재조합

expressed in E. coli

Quality Level

형태

lyophilized powder

특이 활성도

≥10×1010 units/mg protein

분자량

62 kDa

응용 분야

diagnostic assay manufacturing

저장 온도

−20°C

유사한 제품을 찾으십니까? 방문 제품 비교 안내

애플리케이션

Firefly luciferase is used extensively in molecular and cell biology, in particular for the efficient detection and quantitation of ATP and as a reporter for genetic function.

생화학적/생리학적 작용

Firefly luciferase is a 62 kDa protein that catalyzes the production of light. The enzyme requires ATP, molecular oxygen, and the heterocyclic compound, firefly luciferin, to generate light in a two-step process. The light producing reaction is initiated by luciferin activation (adenylation of its carboxylate group) and proceeds in the presence of molecular oxygen to yield a photon of yellow-green light.

단위 정의

One luciferase enzyme unit will produce one Relative Light Unit (RLU) at 20-25 °C over a 10 second period, measured in 100 μl assay mixture containing 40 pmol ATP and 15 nmol luciferin in Tris-glycine buffer, pH 7.6, using a GloMax 20/20 Luminometer.

Unit Definition Conversion Factor: There are approximately 9000 Relative Light Units (RLU) per one traditional Light Unit that uses a peak height equivalent to 0.02 μCi of 14C in a PPO/POPOP cocktail.

물리적 형태

Supplied as a lyophilized powder containing HEPES, pH 7.5, NaCl, MgCl2, EDTA, DTT and a carbohydrate stabilizer.
This product is a recombinant luciferase (62 kDa) from Photinus pyralis (American firefly) produced from the luc gene expressed in E. coli.

제조 메모

To obtain maximal solubility it is important to reconstitute the enzyme at a high salt concentration, such as 1 M Tris buffer with any counter ion at pH 7-8. The enzyme can be prepared at a concentration of up to 5 mg protein/ml. Do not vortex and avoid agitation.
After reconstitution, the enzyme solutions can kept at 4-8 °C for up to 2 days or frozen in working aliquots at -20°C for at least one month. Repeated freezing and thawing is not recommended.

픽토그램

Health hazardCorrosion

신호어

Danger

유해 및 위험 성명서

Hazard Classifications

Eye Dam. 1 - Resp. Sens. 1

Storage Class Code

11 - Combustible Solids

WGK

WGK 3

Flash Point (°F)

Not applicable

Flash Point (°C)

Not applicable


시험 성적서(COA)

제품의 로트/배치 번호를 입력하여 시험 성적서(COA)을 검색하십시오. 로트 및 배치 번호는 제품 라벨에 있는 ‘로트’ 또는 ‘배치’라는 용어 뒤에서 찾을 수 있습니다.

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Reactions involving the transfer of a phosphoryl (-PO32-) group are fundamental to cellular metabolism. These reactions are catalyzed by enzymes, often large and complex, belonging to the phosphate-binding loop (P-loop) nucleoside triphosphatase (NTPase) superfamily. Due to their critical importance in
S R Ford et al.
Journal of bioluminescence and chemiluminescence, 7(3), 185-193 (1992-07-01)
Commercially available crystalline native and recombinant firefly luciferases were compared. The two types of luciferase had indistinguishable responses to variation in ATP and luciferin concentrations and to omission of reaction components. The time courses of light production, the responses to
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Bioluminescent imaging (BLI) is one of the most powerful and widely used preclinical imaging modalities. However, the current technology relies on the use of transgenic luciferase-expressing cells and animals and therefore can only be applied to a limited number of

문서

Firefly luciferase is a sensitive reporter for gene studies due to its absence in mammalian cells or tissues.

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