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Aprotinin

from bovine lung

Sinonimo/i:

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

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10 mg
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CHF 240.00
50 mg
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CHF 485.00
100 mg
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CHF 858.00

Informazioni su questo articolo

UNSPSC Code:
12352204
NACRES:
NA.54

CHF 240.00


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biological source

bovine lung

form

lyophilized

packaging

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

manufacturer/tradename

Roche

technique(s)

electrophoresis: suitable, tissue culture: suitable

pH range

3-10

solubility

water: soluble 10 mg/mL

absorption

0.84 at 280 nm

shipped in

wet ice

storage temp.

2-8°C

General description

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.[1][2]

Application

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.[3][4]
  • 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

Biochem/physiol Actions

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.

Preparation Note

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
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).

Other Notes

For life science research only. Not for use in diagnostic procedures.
Monomeric peptide of 58 amino acids held in conformation by three disulfide bonds.
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.

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Questo articolo
A4529A6279A3428
Aprotinin from bovine lung

Roche

ROAPRO

Aprotinin

biological source

bovine lung

biological source

bovine lung

biological source

bovine

biological source

bovine lung

form

lyophilized

form

lyophilized powder

form

saline solution

form

lyophilized powder

solubility

water: soluble 10 mg/mL

solubility

H2O: >10 mg/mL

solubility

H2O: soluble >10 mg/mL

solubility

H2O: 5 mg/mL

storage temp.

2-8°C

storage temp.

2-8°C

storage temp.

2-8°C

storage temp.

2-8°C

shipped in

wet ice

shipped in

-

shipped in

-

shipped in

-

packaging

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

packaging

-

packaging

-

packaging

-


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Classe di stoccaggio

11 - Combustible Solids

wgk

WGK 1

flash_point_f

Not applicable

flash_point_c

Not applicable



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Articoli

While aprotinin and bovine pancreatic trypsin inhibitor (BPTI) are the same protein sequence, the term aprotinin is typically used when describing the protein derived from bovine lung.






Numero articolo commerciale globale

SKUGTIN
1098153200104061838690517
1023662400104061838669490
1158379400104061838703675