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Aprotinin

Catalog No. T3359   CAS 9087-70-1
Synonyms: Bovine Pancreatic Trypsin Inhibitor, Traskolan, Antilysin

Aprotinin (Traskolan) a broad-spectrum serine protease inhibitor, inhibiting the activity of a number of different esterases and proteases, including trypsin, chymotrypsin, kallikrein, plasmin, tissue plasminogen activator, and tissue and leukocytic proteinases.

All products from TargetMol are for Research Use Only. Not for Human or Veterinary or Therapeutic Use.
Aprotinin Chemical Structure
Aprotinin, CAS 9087-70-1
Pack Size Availability Price/USD Quantity
5 mg In stock $ 39.00
10 mg In stock $ 54.00
25 mg In stock $ 117.00
50 mg In stock $ 198.00
100 mg In stock $ 328.00
200 mg In stock $ 493.00
500 mg In stock $ 789.00
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Potency: 6000U/mg
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Biological Description
Chemical Properties
Storage & Solubility Information
Description Aprotinin (Traskolan) a broad-spectrum serine protease inhibitor, inhibiting the activity of a number of different esterases and proteases, including trypsin, chymotrypsin, kallikrein, plasmin, tissue plasminogen activator, and tissue and leukocytic proteinases.
Targets&IC50 Trypsinogen:2 μM(Kd), Trypsin:0.06 pM(Kd), Kallikrein:0.8 nM(Kd), Chymotrypsin:9.5 nM(Kd)
In vitro Aprotinin is an antifibrinolytic molecule that inhibits trypsin and related proteolytic enzymes. In cell biology, aprotinin is used as an enzyme inhibitor to prevent protein degradation during lysis or homogenization of cells and tissues. In the presence of aprotinin, the fibrinolytic activity is inhibited concentration dependently and the coagulation time is prolonged. Aprotinin is an effective inhibitor of the contact (intrinsic) coagulation pathway in vitro[2].
In vivo Aprotinin inhibits clot lysis in vitro as well as rat-tail bleeding time in vivo and prolongs coagulation time in human plasma. In a rat arteriovenous shunt model, aprotinin reduces thrombus weight [2].
Kinase Assay Substrates and kinases are diluted in 50?mM Tris/HCl (pH?7.5), 0.1% 2-mercaptoethanol, 0.1?mM EGTA and 10?mM magnesium acetate. Reactions are initiated with [γ-32P]ATP (2500 c.p.m./pmol) to a final concentration of 0.1?mM and terminated after 15?min at 30°C by the addition of SDS and EDTA (pH?7.0) to final concentrations of 1.0% (w/v) and 20?mM respectively. After heating for 5?min at 100°C and separation by SDS/PAGE, the phosphorylated proteins are detected by autoradiography.
Cell Research Mouse G8-1 myoblasts are plated DMEM + 20% FBS (maintenance medium), in which they remain undifferentiated. When cells reach approximately 40-50% confluence, different protease inhibitors are added to the culture media and cells are incubated overnight. Cells are then switched to differentiation-promoting media (DMEM + 10% horse serum ± protease inhibitor) and incubated for 7 days. (Only for Reference)
Synonyms Bovine Pancreatic Trypsin Inhibitor, Traskolan, Antilysin
Molecular Weight 6511.51
Formula C284H432N84O79S7
CAS No. 9087-70-1

Storage

Powder: -20°C for 3 years | In solvent: -80°C for 1 year

Solubility Information

H2O: 100 mg/mL (15.36 mM), sonification is recommended.

TargetMolReferences and Literature

1. Capasso C, et al. J Mol Recognit. 1997, 10(1):26-35. 2. Sperzel M, et al. J Thromb Haemost. 2007, 5(10):2113-2118. 3. James M. Wells, et al. Development. 1994, 120:3639-3647. 4. Jiang T Y, Feng X F, Fang Z, et al. PTEN deficiency facilitates the therapeutic vulnerability to proteasome inhibitor bortezomib in gallbladder cancer[J]. Cancer Letters. 2020 5. Jiang T Y, Pan Y F, Wan Z H, et al. PTEN status determines chemosensitivity to proteasome inhibition in cholangiocarcinoma[J]. Science Translational Medicine. 2020, 12(562).

TargetMolCitations

1. Jiang T Y, Pan Y F, Wan Z H, et al. PTEN status determines chemosensitivity to proteasome inhibition in cholangiocarcinoma. Science Translational Medicine. 2020, 12(562). 2. Jiang T Y, Feng X F, Fang Z, et al. PTEN deficiency facilitates the therapeutic vulnerability to proteasome inhibitor bortezomib in gallbladder cancer. Cancer Letters. 2021, 501: 187-199. 3. Nie C, Zhou X A, Zhou J, et al.A transcription‐independent mechanism determines rapid periodic fluctuations of BRCA1 expression.The EMBO Journal.2023: e111951.

Related compound libraries

This product is contained In the following compound libraries:
Peptide Compound Library NO PAINS Compound Library Immunology/Inflammation Compound Library HIF-1 Signaling Pathway Compound Library Anti-Infection Compound Library Protease Inhibitor Library

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Keywords

Aprotinin 9087-70-1 Microbiology/Virology Others Proteases/Proteasome Ubiquitination Serine Protease Influenza Virus Proteasome Ser/Thr Protease Inhibitor Serine proteases Serine endopeptidases Bovine Pancreatic Trypsin Inhibitor inhibit Traskolan Threonine proteases Antilysin inhibitor

 

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