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GEE70092Y

Shrimp Alkaline Phosphatase

Cytiva E70092Y, pack of 500 U

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About This Item

Código UNSPSC:
12352204
NACRES:
NA.54
Preço e disponibilidade não estão disponíveis no momento.

fonte biológica

shrimp

Formulário

liquid

peso molecular

155 kDa

embalagem

pack of 500 U

fabricante/nome comercial

Cytiva E70092Y

Condições de expedição

dry ice

temperatura de armazenamento

−20°C

Categorias relacionadas

Descrição geral

Shrimp alkaline phosphatase (SAP) has a high specific activity and is a heat-labile alkaline phosphatase.[1] It can be inactivated by a short rise in temperature to 65 °C. SAP is a 155,000Da homodimeric protein with dimensions of about 95 Å×65 Å×50 Å and mol. wt of 155,000.[1][2]
Completely and irreversibly inactivated in Tris buffers at pH 8.0-8.5 by heating for 15 min at 65°C. No further treatment is necessary.

Ações bioquímicas/fisiológicas

Shrimp alkaline phosphatase (SAP) catalyzes the in vitro dephosphorylation of DNA or deoxynucleotides (dNTPs).[3] The enzyme activity can be completely inhibited by ethylenediaminetetraacetic acid (EDTA), but the activity can be restored to a large degree by zinc.[4]
Shrimp alkaline phosphatase (SAP) catalyzes the in vitro dephosphorylation of DNA or deoxynucleotides (dNTPs).[1] The enzyme activity can be completely inhibited by ethylenediaminetetraacetic acid (EDTA), but the activity can be restored to a large degree by zinc.[2]

Características e benefícios

  • Removing 5′-phosphates from DNA and RNA.
  • Easily inactivated by heat.

Armazenamento e estabilidade

Please be aware this product may be shipped 90 days before the expiration date. For more information on the batch specific expiration date, please contact technical service.

Nota de análise

To view the Certificate of Analysis for this product, please visit www.cytiva.com.

Código de classe de armazenamento

12 - Non Combustible Liquids

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Certificados de análise (COA)

Lot/Batch Number

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Alkaline phophatase from the hepatopancreas of shrimp (Pandalus borealis): a dimeric enzyme with catalytically active subunits.
Olsen R L, et val.
Comparative Biochemistry and Physiology. B, Comparative Biochemistry, 99(4), 755-761 (1991)
The 1.9 ? crystal structure of heat-labile shrimp alkaline phosphatase.
de Backer M, et al.
Journal of Molecular Biology, 318(5), 1265-1274 (2002)
Alkaline phophatase from the hepatopancreas of shrimp (Pandalus borealis): A dimeric enzyme with catalytically active subunits
Olsen RL, et al.
Comp. Biochem. Physiol., B: Comp. Biochem., 99, 755- 761 (2003)
The 1.9 A crystal structure of heat-labile shrimp alkaline phosphatase.
de Backer M, et al.
Journal of Molecular Biology, 318, 1265-1274 (2002)
Exploring alternative pathways for the in vitro establishment of the HOPAC cycle for synthetic CO2 fixation.
McLean, et al.
Science Advances, 9, eadh4299-eadh4299 (2023)

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