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GEE70092Y

Shrimp Alkaline Phosphatase

Cytiva E70092Y, pack of 500 U

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About This Item

UNSPSC Code:
12352204
NACRES:
NA.54

biological source

shrimp

form

liquid

mol wt

155 kDa

packaging

pack of 500 U

manufacturer/tradename

Cytiva E70092Y

shipped in

dry ice

storage temp.

−20°C

Související kategorie

General description

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.

Biochem/physiol Actions

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.

Features and Benefits

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

Storage and Stability

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.

Analysis Note

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

Storage Class

12 - Non Combustible Liquids

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Osvědčení o analýze (COA)

Lot/Batch Number

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Navštívit knihovnu dokumentů

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)
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 RL, et al.
Comp. Biochem. Physiol., B: Comp. Biochem., 99, 755- 761 (2003)
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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