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Description: Competitive serine protease inhibitor
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 4 mg/ml in water |
Product Datasheets for Aprotinin
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
If you know of a relevant reference for Aprotinin, please let us know.
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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
4 Citations for Aprotinin
Citations are publications that use Tocris products. Selected citations for Aprotinin include:
María Elena et al (2023) Induction of Apoptosis and Decrease of Autophagy in Colon Cancer Cells by an Extract of Lyophilized Mango Pulp. Int J Environ Res Public Health 20 PMID: 36901174
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
Simon C et al (2019) Poly(ethylene glycol)-crosslinked gelatin hydrogel substrates with conjugated bioactive peptides influence endothelial cell behavior. Biomaterials 201 99-112 PMID: 30807988
Yan et al (2022) Metabolic diversity within breast cancer brain-tropic cells determines metastatic fitness. Cell Metab 34 90-105.e7 PMID: 34986341
Do you know of a great paper that uses Aprotinin from Tocris? Please let us know.
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