GEE70092Y
Shrimp Alkaline Phosphatase
Cytiva E70092Y, pack of 500 U
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UNSPSC Code:
12352204
NACRES:
NA.54
Recommended Products
biological source
shrimp
form
liquid
shelf life
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.
mol wt
155 kDa
packaging
pack of 500 U
manufacturer/tradename
Cytiva E70092Y
shipped in
dry ice
storage temp.
−20°C
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.
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.
Analysis Note
To view the Certificate of Analysis for this product, please visit www.cytiva.com.
Regulatory Information
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Certificates of Analysis (COA)
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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)
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)
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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