Aprotinin

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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 (Disulfide bridges: 5-5 | CAS No. 9087-70-1
Description: Competitive serine protease inhibitor
Datasheet
Citations (1)
Reviews

Biological Activity for Aprotinin

Aprotinin is a 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. Inhibits cytopathogenic effect of SARS-CoV-2 and double-stranded RNA formation in SARS-CoV-2-infected cells.

This product is from Bovine Lung.

Technical Data for Aprotinin

M. Wt 6511.48
Formula C284H432N84O79S7
Sequence RPDFCLEPPYTGPCKARIIRYFYNAKAGLCQTFVYGGCRAKRNNFKSAEDCMRTCGGA

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

Storage Store at +4°C
CAS Number 9087-70-1
PubChem ID 53487898
InChI Key ZPNFWUPYTFPOJU-YSFZTAPISA-N
Smiles [H]N[C@@H](CCCNC(N)=N)C(=O)N1CCC[C@H]1C(=O)N[C@@H](CC(O)=O)C(=O)N[C@@H](CC1=CC=CC=C1)C(=O)N[C@H]1CSSC[C@H](NC(=O)[C@@H](NC(=O)[C@H](CCCNC(N)=N)NC(=O)[C@H](CCSC)NC(=O)[C@@H]2CSSC[C@@H]3NC(=O)[C@H](CC(C)C)NC(=O)CNC(=O)[C@H](C)NC(=O)[C@H](CCCCN)NC(=O)[C@H](C)NC(=O)[C@H](CC(N)=O)NC(=O)[C@H](CC4=CC=C(O)C=C4)NC(=O)[C@H](CC4=CC=CC=C4)NC(=O)[C@H](CC4=CC=C(O)C=C4)NC(=O)[C@H](CCCNC(N)=N)NC(=O)[C@@H](NC(=O)[C@@H](NC(=O)[C@H](CCCNC(N)=N)NC(=O)[C@H](C)NC(=O)[C@H](CCCCN)NC(=O)[C@H](CSSC[C@H](NC(=O)CNC(=O)CNC(=O)[C@H](CC4=CC=C(O)C=C4)NC(=O)[C@@H](NC(=O)[C@H](CC4=CC=CC=C4)NC(=O)[C@@H](NC(=O)[C@H](CCC(N)=O)NC3=O)[C@@H](C)O)C(C)C)C(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@@H](C)C(=O)N[C@@H](CCCCN)C(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@@H](CC(N)=O)C(=O)N[C@@H](CC(N)=O)C(=O)N[C@@H](CC3=CC=CC=C3)C(=O)N[C@@H](CCCCN)C(=O)N[C@@H](CO)C(=O)N[C@@H](C)C(=O)N[C@@H](CCC(O)=O)C(=O)N[C@@H](CC(O)=O)C(=O)N2)NC(=O)[C@@H]2CCCN2C(=O)CNC(=O)[C@@H](NC(=O)[C@H](CC2=CC=C(O)C=C2)NC(=O)[C@@H]2CCCN2C(=O)[C@@H]2CCCN2C(=O)[C@H](CCC(O)=O)NC(=O)[C@H](CC(C)C)NC1=O)[C@@H](C)O)[C@@H](C)CC)[C@@H](C)CC)[C@@H](C)O)C(=O)NCC(=O)NCC(=O)N[C@@H](C)C(O)=O

The technical data provided above is for guidance only. For batch specific data refer to the Certificate of Analysis.

Tocris products are intended for laboratory research use only, unless stated otherwise.

Solubility Data for Aprotinin

Solubility Soluble to 10 mg/ml in water

Product Datasheets for Aprotinin

Certificate of Analysis / Product Datasheet
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References for Aprotinin

References are publications that support the biological activity of the product.

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

Bojkova et al (2020) SARS-CoV-2 and SARS-CoV differ in their cell tropism and drug sensitivity profiles. Bioinformatics 37 2282


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Keywords: Aprotinin, Aprotinin supplier, Aprotinin, serine, protease, inhibitors, inhibits, trypsin, plasmin, chymotrypsin, kallikrein, SARS-CoV-2, COVID-19, severe, acute, respiratory, syndrome, TMPRSS2, Other, Proteases, 4139, Tocris Bioscience

1 Citation for Aprotinin

Citations are publications that use Tocris products. Selected citations for Aprotinin include:

Berg et al (2019) Proteolytic and Opportunistic Breaching of the Basement Membrane Zone by Immune Cells during Tumor Initiation. Cell Rep 27 2837 PMID: 31167131


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