Aprotinin

Cat. No. 4139

Aprotinin Arg-Pro-Asp-Phe-Cys-Leu-Glu-Pro-Pro-Tyr-Thr-Gly-Pro-Cys-Lys-Ala-Arg-Ile-Ile-Arg-Tyr-Phe-Tyr-Asn-Ala-Lys-Ala-Gly-Leu-Cys-Gln-Thr-Phe-Val-Tyr-Gly-Gly-Cys-Arg-Ala-Lys-Arg-Asn-Asn-Phe-Lys-Ser-Ala-Glu-Asp-Cys-Met-Arg-Thr-Cys-Gly-Gly-Ala

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Biological Activity

Competitive serine protease inhibitor. Reversibly binds to and blocks the enzymatic active site. Inhibits a range of serine proteases including trypsin, chymotrypsin, kallikrein and plasmin.

Technical Data

M.Wt:
6511.48
Formula:
C284H432N84O79S7
Sequence:
RPDFCLEPPYTGPCKARIIRYFYNAKAGLCQTFVYGGCRAKRNNFKSAEDCMRTCGGA

(Modifications: Disulfide bridge: 5-55, 14-38, 30-51)

Solubility:
Soluble to 10 mg/ml in water
Storage:
Store at +4°C
CAS No:
9087-70-1

The technical data provided above is for guidance only. For batch specific data refer to the Certificate of Analysis.
All Tocris products are intended for laboratory research use only.

Certificate of Analysis / Product Datasheet / Safety Datasheet

Certificate of Analysis / Product Datasheet
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References are publications that support the products' biological activity.

Parlee et al (2012) Elastase and tryptase govern TNFa-mediated production of active chemerin by adipocytes. PLoS ONE 7 e51072. PMID: 23227233.

Reichel et al (2011) Plasmin inhibitors prevent leukocyte accumulation and remodeling events in the postischemic microvasculature. PLoS ONE 6 e17229. PMID: 21364954.

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Keywords: Aprotinin, supplier, Aprotinin, serine, protease, inhibitors, inhibits, trypsin, plasmin, chymotrypsin, kallikrein, Tocris Bioscience, Other Protease Inhibitor products

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