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Merck

GEE70092Y

Shrimp Alkaline Phosphatase

Cytiva E70092Y, pack of 500 U

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About This Item

分類程式碼代碼:
12352204
NACRES:
NA.54

生物源

shrimp

形狀

liquid

分子量

155 kDa

包裝

pack of 500 U

製造商/商標名

Cytiva E70092Y

運輸包裝

dry ice

儲存溫度

−20°C

相关类别

一般說明

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.

生化/生理作用

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.

特點和優勢

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

儲存和穩定性

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.

分析報告

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

儲存類別代碼

12 - Non Combustible Liquids


分析证书(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)
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)
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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