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A1153
Aprotinin
3-8 TIU/mg solid, lyophilized powder
Synonym(s):
BPTI, Bovine pancreatic trypsin inhibitor, Trasylol, Trypsin inhibitor (basic)
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1 MG
449,00 kr.
5 MG
810,00 kr.
10 MG
1.130,00 kr.
25 MG
2.040,00 kr.
100 MG
7.310,00 kr.
250 MG
17.570,00 kr.
About This Item
Empirical Formula (Hill Notation):
C284H432N84O79S7
CAS Number:
Molecular Weight:
6511.44
UNSPSC Code:
12352202
NACRES:
NA.77
EC Number:
232-994-9
MDL number:
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Product Name
Aprotinin from bovine lung, lyophilized powder, 3-8 TIU/mg solid
SMILES string
S1SCC2NC(=O)CNC(=O)CNC(=O)C(NC(=O)C(NC(=O)C(NC(=O)C(NC(=O)C(NC(=O)C5NC(=O)C(NC(=O)CNC(=O)C(NC(=O)C(NC(=O)C(NC(=O)C(NC(=O)C(NC(=O)C(NC(=O)C(NC(=O)C(NC(=O)C(NC(=O)C(NC(=O)C(NC(=O)C(NC(=O)C(NC(=O)C(NC(=O)C9N(CCC9)C(=O)CNC(=O)C(NC(=O)C(NC(=O)C%11N(CCC%11)C(=O
InChI
1S/C284H432N84O79S7/c1-21-144(9)222-271(439)337-174(68-46-105-309-282(300)301)239(407)340-187(120-160-77-85-164(374)86-78-160)251(419)341-185(116-156-55-29-24-30-56-156)250(418)342-188(121-161-79-87-165(375)88-80-161)252(420)346-191(123-208(291)378)246(41
InChI key
ZPNFWUPYTFPOJU-UHFFFAOYSA-N
biological source
bovine lung
form
lyophilized powder
specific activity
3-8 TIU/mg solid
mol wt
~6,500
solubility
H2O: ≥5 mg/mL
UniProt accession no.
storage temp.
2-8°C
Quality Level
Gene Information
cow ... PTI(404172)
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1 of 4
This Item | A3886 | A1250000 | Y0001154 |
|---|---|---|---|
| biological source bovine lung | biological source bovine lung | biological source bovine | biological source - |
| Gene Information cow ... PTI(404172) | Gene Information cow ... PTI(404172) | Gene Information - | Gene Information - |
| Quality Level 300 | Quality Level 200 | Quality Level - | Quality Level - |
| form lyophilized powder | form powder | form - | form - |
| storage temp. 2-8°C | storage temp. −20°C | storage temp. 2-8°C | storage temp. 2-8°C |
| solubility H2O: ≥5 mg/mL | solubility glycerol: 3 mg/mL, clear, colorless (equilibration buffer containing 5% glycerol) | solubility - | solubility - |
Application
Aprotinin from bovine lung has been used:
- as a protease inhibitor in radioimmunoprecipitation assay buffer (RIPA) for the homogenization of cardiac microvascular endothelial cells (CMECs)(4) and mammary epithelial cells[1]
- in angiogenesis assay for fibroblast[2]
- in the proteomic stabilization of saliva supernatant[3]
Aprotinin is largely used as an inhibitor of trypsin.
Biochem/physiol Actions
Aprotinin inhibits proteases like trypsin, plasmin, chymotrypsin and thrombin. It blocks the bradykinin synthesis from kininogen.[4] It is useful for treating blood loss during surgery.[5]
Aprotinin is a competitive serine protease inhibitor that forms stable complexes with and blocks the active sites of enzyme. This binding is reversible, and most aprotinin-protease complexes will dissociate at extreme pH levels >10 or <3. Structurally, Aprotinin is a monomeric globular protein derived from bovine lung that consists of 58 amino acids, arranged in a single polypeptide chain with three crosslinking disulfide bridges.
General description
Aprotinin from bovine lung is a globular polypeptide monomer with a molecular weight of 6.5 kDa.[4] Commonly used as a non-specific serine protease inhibitor, aprotinin contains an antiparallel β sheet, N-terminal 310 helix and C-terminal and α helix.[6] Aprotinin residues from amino acids 13 - 18 are essential for binding to serine proteases.[5]
Other Notes
One Trypsin Inhibitor Unit (TIU) will decrease the activity of two trypsin units by 50%, where one trypsin unit will hydrolyze 1.0 μmole of N-alpha-benzoyl-DL-arginine p-nitroanilide per minute at pH 7.8 and 25°C. Another commonly used unit is the KIU, with 1 TIU = 1,300 KIU.
Preparation Note
This product is a lyophilized powder with activity of 3-8 TIU/mg of solid powder. Aprotinin is freely soluble in water (>10 mg/mL) and in aqueous buffers of low ionic strengths. Dilute solutions tend to be less stable than concentrated ones, though solution stability also depends on pH. Aprotinin is relatively stable against denaturation - only thermolysin has been found capable of degrading it at 60-80°C. Sterilizaiton of Aprotinin can be achieved through filtration by a 0.2 μm filter.
related product
Storage Class
11 - Combustible Solids
wgk
WGK 1
flash_point_f
Not applicable
flash_point_c
Not applicable
ppe
Eyeshields, Gloves, type N95 (US)
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Find documentation for the products that you have recently purchased in the Document Library.
RNAPro? SAL: A device for rapid and standardized collection of saliva RNA and proteins
Chiang SH, et al.
Biotechniques, 58(2), 69-76 (2015)
Aprotinin interacts with substrate-binding site of human dipeptidyl peptidase III
Agic D, et al.
Journal of Biomolecular Structure & Dynamics, 8(1), 1-11 (2019)
J Pyo et al.
Journal of dairy science, 103(5), 4236-4251 (2020-03-17)
This study evaluated how feeding colostrum- or a colostrum-milk mixture for 3 d postnatal affects plasma glucagon-like peptide-2 (GLP-2), serum insulin-like growth factor-1 (IGF-1), and small intestinal histomorphology in calves. Holstein bulls (n = 24) were fed colostrum at 2
Perioperative systemic haemostatic agents
Mahdy AM and Webster NR
British journal of anaesthesia, 93(6), 842-858 (2004)
Engineering of a biomimetic pericyte-covered 3D microvascular network
Kim J,
PLoS ONE, 10(7), e0133880-e0133880 (2015)
Articles
ReadyShield® phosphatase and protease inhibitor cocktail FAQ for sample protection in a variety of cell types and tissue extracts, including mammalian, plant, and microbial samples. Our ReadyShield® Protease Inhibitor Cocktail is a non-freezing solution that contains inhibitors with a broad specificity for serine, cysteine, acid proteases and aminopeptidases.
Elastase application index for understanding leukocyte elastase, a 29KDa serine endoprotease.
Analytical Enzyme Chymotrypsin: Chymotrypsin is produced in the acinar cells of the pancreas as the inactive precursor, chymotrypsinogen.
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.
Protocols
Objective: To standardize a procedure for the enzymatic assay of Aprotinin.
Related Content
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What is the exact TIU/mg for the product? The information gives a range (3-8TIU/mg) but I need the exact value in order to calculate what size I need to order based on my samples.
1 answer-
Helpful?
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What type of inhibitor is Aprotinin from bovine lung, Product A1153?
1 answer-
Aprotinin is a competitive serine protease inhibitor which forms stable complexes that block the active site of the enzyme.
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What are typical concentrations of Aprotinin from bovine lung, Product A1153, to use as a protease inhibitor?
1 answer-
Typical concentration of Aprotinin to be used as a protease inhibitor is 1 μM or approximately 6.5 μg/ml.
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Is Aprotinin from bovine lung, Product A1153, the same as Trasylol?
1 answer-
Trasylol is the Bayer AG registered trademark name for this material.
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When using Product A1153, Aprotinin from bovine lung, what is the conversion from KIU to TIU?
1 answer-
According to data from our labs here at Sigma, there are approximately 1300 KIU per 1 TIU. This, along with other useful information, can be found on the product information sheet available at our website: A1153 Product Information Sheet
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How should I store solutions of Aprotinin from bovine lung, Product A1153?
1 answer-
Sterile solutions of aprotinin may be stored at 4 °C or as frozen aliquots at -20 °C.
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What is the Department of Transportation shipping information for this product?
1 answer-
Transportation information can be found in Section 14 of the product's (M)SDS.To access the shipping information for this material, use the link on the product detail page for the product.
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