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Documentos Principais

ROAPRO

Roche

Aprotinin

from bovine lung

Sinônimo(s):

Aprotinin, pancreatic trypsin inhibitor, trypsin inhibitor, pancreas type (bpti), trypsin-kallikrein inhibitor

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About This Item

Código UNSPSC:
12352204

fonte biológica

bovine lung

Nível de qualidade

Formulário

lyophilized

embalagem

pkg of 10 mg (10236624001)
pkg of 100 mg (11583794001)
pkg of 50 mg (10981532001)

fabricante/nome comercial

Roche

técnica(s)

electrophoresis: suitable
tissue culture: suitable

faixa de pH

3-10

solubilidade

water: soluble 10 mg/mL

Absorção

0.84 at 280 nm

Condições de expedição

wet ice

temperatura de armazenamento

2-8°C

Categorias relacionadas

Descrição geral

Trypsin inhibitor, pancreas type from bovine lung. It is known as Pancreatic trypsin inhibitor (BPTI). Aprotinin, also known as pancreatic trypsin inhibitor and trypsin-kallikrein inhibitor, is found to be expressed in lungs, spleen, liver, and pancreas. It is also found to be present in the free form in calf serum.

Especificidade

Aprotinin inhibits serine proteases. It inhibits kallikrein, the protease that releases hypotensive peptides such as kallidin and bradykinin (human plasma kallikrein: Ki = 3 ×10-8 M at pH 8.0, porcine pancreas kallikrein: Ki = 1 × 10-9 M at pH 8.0), trypsin (Ki = 2.8 × 10-11 M at pH 7.8, Ki = 2.6 × 10-9 M at pH 4.0, non-competetive), trypsinogen, chymotrypsin (Ki = 9 × 10-9 M at pH 8.0), bacterial fibrinolysin, and plasmin (Ki = 1 nM at pH 7.3).
Cathepsin G, acrosin, human leukocyte elastase, and human urokinase are weakly inhibited. Factor Xa, thrombin, subtilisin, papain, pepsin, angiotensin-converting enzyme (ACE), carboxypeptidase A and B, other metalloproteases, and thiolproteases are not inhibited.

Aplicação

Aprotinin is used for the protection of proteins and enzymes during isolation/purification. The inhibition of protease activity increases the lifetime of cells in cell and tissue culture studies.
  • Further applications: Purification of urokinase, trypsin, and chymotrypsin on immobilized aprotinin
  • Quantification of kallikrein activity in mixtures of esterases and proteases
  • Controlled degradation of substrates by avoiding nonspecific proteolysis in clinical chemical tests
  • Aprotinin as a model protein in protein-folding studies
  • Molecular weight marker in SDS-polyacrylamide gel electrophoresis

Sequência

Monomeric peptide of 58 amino acids held in conformation by three disulfide bonds.

Definição da unidade

One inhibitor unit (IU) is defined as the amount of aprotinin that completely inhibits 1 U trypsin in < 10 minutes at pH 6. (Trypsin activity determined at +25 °C, pH 8.0, BAEE as substrate).
One inhibitor unit (IU) (+25 °C, BAEE as substrate) corresponds to about 2.8 inhibitor units (+25 °C, Chromozym TRY as substrate).
One inhibitor unit (IU) (+25 °C, BAEE as substrate) corresponds to about 26 kallikrein inhibitor units (KIU) (+25 °C).
One inhibitor unit (IU) (+25 °C, BAEE as substrate) corresponds to about 0.067 inhibitor units (+25 °C; Bz-D,L-Arg-4-Na as substrate, trypsin determination at pH 7.8).
One kallikrein inhibitor unit = 0.17 μg crystalline aprotinin.

Nota de preparo

Working concentration: 0.06 to 2 μg/ml (0.01 - 0.3 μM)
Working solution: Soluble in water (10 mg/ml) or aqueous buffer solution (e.g., 0.1 M Tris, pH 8.0).
Note: To avoid adsorption of aprotinin onto negatively charged solid phases, e.g., chromatography gels, ultrafiltration membranes, the NaCl concentration should be above 0.1 M or other suitable salts should be added to all buffers used during the separation.
Storage conditions (working solution): -15 to -25 °C

Reconstituição

Freely soluble in water (10 mg/ml) or aqueous buffer solution (e.g., Tris, 0.1 M, pH 8.0). A solution adjusted to pH 7 to 8 is stable for approximately 1 week at 2 to 8 °C.
Aliquots stored at -15 to -25 °C are stable for approximately 6 months.
Note: Avoid repeated freezing and thawing and exposure to strongly alkaline solutions (inactive at pH > 12.8).

Outras notas

For life science research only. Not for use in diagnostic procedures.

Código de classe de armazenamento

11 - Combustible Solids

Classe de risco de água (WGK)

WGK 1

Ponto de fulgor (°F)

Not applicable

Ponto de fulgor (°C)

Not applicable


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[EXPERIMENTS ON THE ISOLATION OF THE KALLIKREIN INACTIVATOR. V. THE ISOLATION OF A KALLIKREIN INACTIVATOR FROM THE BOVINE LUNG AND ITS IDENTIFICATION WITH THE INHIBITOR FROM THE BOVINE PAROTID GLAND].
H KRAUT et al.
Hoppe-Seyler's Zeitschrift fur physiologische Chemie, 338, 231-237 (1964-01-01)
Kamlesh Shroff et al.
Langmuir : the ACS journal of surfaces and colloids, 28(3), 1858-1865 (2011-12-14)
In recent years, a variety of biomimetic constructs have emerged which mimic the bioactive sequences found in the natural extracellular matrix (ECM) proteins such as fibronectin (FN) that promote cell adhesion as well as proliferation on artificially functionalized interfaces. Much
Glucose Starvation Increases V-ATPase Assembly and Activity in Mammalian Cells through AMP
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The Journal of Biological Chemistry (2018)
Selecting protein N-terminal peptides by combined
fractional diagonal chromatography
An S, et al.
Nature Protocols (2011)
H Fritz et al.
Hoppe-Seyler's Zeitschrift fur physiologische Chemie, 360(3), 437-444 (1979-03-01)
Using the indirect immunofluorescence technique, the basic kallikrein-trypsin inhibitor of bovine organs, Trasylol, could be localized in tissue mast cells of bovine lung, liver, pancreas and parotid gland. Identification of cells exhibiting specific fluorescence as tissue mast cells was achieved

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