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Merck
CN

AP5

Aprotinin−Agarose

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化学文摘社编号:
UNSPSC Code:
12171500
MDL number:
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column volume

2.5 mL

storage temp.

2-8°C

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Other Notes

One trypsin inhibitor unit (TIU) will decrease the activity of 2 trypsin units by 50% where one trypsin unit will hydrolyze 1.0 μmole of Nα-benzoyl-DL-arginine p-nitroanilide (BAPNA) per min at pH 7.8 at 25°C.
Prepacked columns

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产品编号
说明
化学品安全说明书

  • Aprotinin−Agarose, saline suspension 5 column化学品安全说明书

存储类别

13 - Non Combustible Solids

wgk

WGK 3

flash_point_f

Not applicable

flash_point_c

Not applicable

法规信息

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分析证书(COA)

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Bernhard Glotzbach et al.
Acta crystallographica. Section D, Biological crystallography, 69(Pt 1), 114-120 (2013-01-01)
In recent decades, several canonical serine protease inhibitor families have been classified and characterized. In contrast to most trypsin inhibitors, those from garden four o'clock (Mirabilis jalapa) and spinach (Spinacia oleracea) do not share sequence similarity and have been proposed
Ziv Beckerman et al.
The Journal of thoracic and cardiovascular surgery, 145(1), 243-248 (2012-10-18)
Cardiac surgery patients are treated with antifibrinolytic agents to reduce intra- and postoperative bleeding. Until 2007, lysine analogues (aminocaproic acid and tranexamic acid) and serine protease inhibitors (aprotinin) were recommended. In 2008, the U.S. Food and Drug Administration prohibited aprotinin
A F L Later et al.
Cytokine, 61(2), 438-444 (2012-11-29)
Antifibrinolytics, used in cardiac surgery to abate postoperative blood loss, share anti-inflammatory properties by suppression of pro-inflammatory D-dimer and plasmin levels. Additional drug specific immune modulating qualities are often mentioned in the discussion on which antifibrinolytic can best be used.
Zbigniew Dauter
Acta crystallographica. Section D, Biological crystallography, 69(Pt 1), 2-4 (2013-01-01)
To uniquely describe a crystal structure, it is sufficient to specify the crystal unit cell and symmetry, and describe the unique structural motif which is repeated by the space-group symmetry throughout the whole crystal. It is somewhat arbitrary how such
Andrew T Fenley et al.
Proceedings of the National Academy of Sciences of the United States of America, 109(49), 20006-20011 (2012-11-15)
Molecular dynamics simulations of unprecedented duration now can provide new insights into biomolecular mechanisms. Analysis of a 1-ms molecular dynamics simulation of the small protein bovine pancreatic trypsin inhibitor reveals that its main conformations have different thermodynamic profiles and that

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