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GEE70092Y

Shrimp Alkaline Phosphatase

Cytiva E70092Y, pack of 500 U

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About This Item

Codice UNSPSC:
12352204
NACRES:
NA.54

Origine biologica

shrimp

Stato

liquid

PM

155 kDa

Confezionamento

pack of 500 U

Produttore/marchio commerciale

Cytiva E70092Y

Condizioni di spedizione

dry ice

Temperatura di conservazione

−20°C

Descrizione generale

Shrimp alkaline phosphatase (SAP) has a high specific activity and is a heat-labile alkaline phosphatase. 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.
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.

Azioni biochim/fisiol

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

Caratteristiche e vantaggi

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

Stoccaggio e stabilità

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.

Risultati analitici

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

Codice della classe di stoccaggio

12 - Non Combustible Liquids


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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)
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)

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