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Merck
모든 사진(4)

문서

A1153

Sigma-Aldrich

Aprotinin

3-8 TIU/mg solid, lyophilized powder

동의어(들):

BPTI, Bovine pancreatic trypsin inhibitor, Trasylol, Trypsin inhibitor (basic)

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About This Item

실험식(Hill 표기법):
C284H432N84O79S7
CAS Number:
Molecular Weight:
6511.44
EC Number:
MDL number:
UNSPSC 코드:
12352202
NACRES:
NA.77

product name

Aprotinin from bovine lung, lyophilized powder, 3-8 TIU/mg solid

생물학적 소스

bovine lung

형태

lyophilized powder

특이 활성도

3-8 TIU/mg solid

분자량

~6,500

solubility

H2O: ≥5 mg/mL

UniProt 수납 번호

저장 온도

2-8°C

InChI key

ZPNFWUPYTFPOJU-UHFFFAOYSA-N

유전자 정보

cow ... PTI(404172)

유사한 제품을 찾으십니까? 방문 제품 비교 안내

일반 설명

Aprotinin from bovine lung is a globular polypeptide monomer with a molecular weight of 6.5 kDa. 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. Aprotinin residues from amino acids 13 - 18 are essential for binding to serine proteases.

애플리케이션

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
  • in angiogenesis assay for fibroblast
  • in the proteomic stabilization of saliva supernatant

Aprotinin is largely used as an inhibitor of trypsin.

생화학적/생리학적 작용

Aprotinin inhibits proteases like trypsin, plasmin, chymotrypsin and thrombin. It blocks the bradykinin synthesis from kininogen. It is useful for treating blood loss during surgery.
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.

단위 정의

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.

제조 메모

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.

또한 이 제품과 함께 일반적으로 구입

Storage Class Code

11 - Combustible Solids

WGK

WGK 1

Flash Point (°F)

Not applicable

Flash Point (°C)

Not applicable

개인 보호 장비

Eyeshields, Gloves, type N95 (US)


시험 성적서(COA)

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문서 라이브러리 방문

이미 열람한 고객

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)
RNAPro? SAL: A device for rapid and standardized collection of saliva RNA and proteins
Chiang SH, et al.
Biotechniques, 58(2), 69-76 (2015)
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)
The effects of cell death-inducing DNA fragmentation factor-alpha-like effector C (CIDEC) on milk lipid synthesis in mammary glands of dairy cows
Yang Y, et al.
Journal of Dairy Science, 100(5), 4014-4024 (2017)

문서

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.

Elastase application index for understanding leukocyte elastase, a 29KDa serine endoprotease.

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.

Analytical Enzyme Chymotrypsin: Chymotrypsin is produced in the acinar cells of the pancreas as the inactive precursor, chymotrypsinogen.

프로토콜

Objective: To standardize a procedure for the enzymatic assay of Aprotinin.

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