Aprotinin CAS: 9087-70-1
MF: C284H432N84O79S7
MW: 6511.44
A reversible serine protease blocking and binding agent.

Aprotinin (CAS 9087-70-1)

Aprotinin | CAS 9087-70-1 is rated 5.0 out of 5 by 2.
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Synonym: Pancreatic Trypsin Inhibitor
Application: A reversible serine protease blocking and binding agent
CAS Number: 9087-70-1
Molecular Weight: 6511.44
Molecular Formula: C284H432N84O79S7
* Refer to Certificate of Analysis for lot specific data (including water content).
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Aprotinin is a single chain polypeptide (58 amino-acids) crosslinked by three disulfide bridges, showing competitive and reversible inhibiton of proteolytic and esterolytic activity. Aprotinin forms stable complexes and blocks the active sites of serine protease enzymes. Binding is reversible with most aprotinin-protease complexes dissociating at pH >10 or < 3 (optimum pH 5-7); effective concentration is equimolar with protease. Used as a proteolytic inhibitor in radioimmunoassays of polypeptide hormones.


References

1. Fritz, H., 1983. Arzneimittelforschung. 33: 479-494. PMID: 6191764
2. Hewlett, G. 1990. Biotechnology. 8: 565-6, 568. PMID: 1369990
3. Levy, J.H., et al. 2004. Orthopedics. 27: s653-s658. PMID: 15239552
4. Keesey, J. ed. 1987. Biochemica Information.1st Ed. Boehringer Mannheim Biochemicals. Indianapolis, IN. 1987. p. 111.

Usage :
STORAGE AND SOLUBILITY: Aprotinin is freely soluble in water (>10 mg/mL) and in aqueous buffers of low ionic strengths. Dilute solutions are generally less stable than concentrated ones. Aprotinin solutions are relatively stable, although solution stability is highly dependent on pH. Solutions can be stored at 4°C for up to one week. For long term storage; addition of a carrier protein (ex: 0.1% BSA) is recommended, store at -20°C. Avoid freeze-thaw cycles.

The Cys14-Cys38 disulfide bridge is readily split by reducing agents like b-mercaptoethanol. Due to its compact tertiary structure, aprotinin is relatively stable against denaturation due to high temperature, acids, alkalies, organic solvents or proteolytic degradation (only thermolysin has been found capable of degrading aprotinin after heating to 60-80°C). The high basicity of aprotinin causes it to adhere to commonly used dialysis tubing and even gel filtration matrices, but the use of acetylated materials and concentrated salt solutions minimizes the problem. Sterilization may be achieved by filtration through a 0.2 mm filter.
Appearance :
Lyophilized powder
Physical State :
Solid
Solubility :
Soluble in water (5 mg/ml) and in aqueous buffers of low ionic strengths..
Storage :
Store at 4° C
Ki Data :
Chymotrypsinoge pH 8.0: Ki= 9 nM (bovine); Elastase pH 8.0: Ki= 3.5 µM (human leukocytes); Kallikrein (pancreatic), pH 8.0: Ki= 1.0 nM; Kallikrein (tissue): Ki= 1 nM; Plasmin pH 7.8: Ki= 4.0 nM; Trypsin pH 8.0: Ki= 0.06 pM (bovine); Urokinase pH 8.8: Ki= 8.0 µM (human)
For Research Use Only. Not Intended for Diagnostic or Therapeutic Use.
WGK Germany :
1
RTECS :
YN5080000
PubChem CID :
16130295
Merck Index :
14: 757
MDL Number :
MFCD00130541
EC Number :
232-994-9
SMILES :
CC[[email protected]](C)[[email protected]]1C(=O)N[[email protected]](C(=O)N[[email protected]](C(=O)N[[email protected]](C(=O)N[[email protected]](C(=O)N[[email protected]](C(=O)N[[email protected]](C(=O)N[[email protected]](C(=O)N[[email protected]](C(=O)N[[email protected]](C(=O)NCC(=O)N[[email protected]](C(=O)N[[email protected]]2CSSC[[email protected]]3C(=O)N[[email protected]](C(=O)N[[email protected]](C(=O)N[[email protected]](C(=O)N[[email protected]@H](CSSC[[email protected]@H](C(=O)N[[email protected]](C(=O)N[[email protected]](C(=O)N4CCC[[email protected]]4C(=O)N5CCC[[email protected]]5C(=O)N[[email protected]](C(=O)N[[email protected]](C(=O)NCC(=O)N6CCC[[email protected]]6C(=O)N[[email protected]@H](CSSC[[email protected]@H](C(=O)N[[email protected]](C(=O)N[[email protected]](C(=O)N[[email protected]](C(=O)N[[email protected]](C(=O)N[[email protected]](C(=O)N[[email protected]](C(=O)N[[email protected]](C(=O)N[[email protected]](C(=O)N[[email protected]](C(=O)N[[email protected]](C(=O)N[[email protected]](C(=O)N[[email protected]](C(=O)N3)CC(=O)O)CCC(=O)O)C)CO)CCCCN)CC7=CC=CC=C7)CC(=O)N)CC(=O)N)CCCNC(=N)N)CCCCN)C)CCCNC(=N)N)NC(=O)CNC(=O)CNC(=O)[[email protected]@H](NC(=O)[[email protected]@H](NC(=O)[[email protected]@H](NC(=O)[[email protected]@H](NC(=O)[[email protected]@H](NC2=O)CCC(=O)N)[[email protected]@H](C)O)CC8=CC=CC=C8)C(C)C)CC9=CC=C(C=C9)O)C(=O)N[[email protected]](C(=O)N[[email protected]](C(=O)N[[email protected]](C(=O)N1)CCCNC(=N)N)C)CCCCN)[[email protected]@H](C)O)CC1=CC=C(C=C1)O)CCC(=O)O)CC(C)C)NC(=O)[[email protected]](CC1=CC=CC=C1)NC(=O)[[email protected]](CC(=O)O)NC(=O)[[email protected]@H]1CCCN1C(=O)[[email protected]](CCCNC(=N)N)N)C(=O)NCC(=O)NCC(=O)N[[email protected]@H](C)C(=O)O)[[email protected]@H](C)O)CCCNC(=N)N)CCSC)CC(C)C)C)CCCCN)C)CC(=O)N)CC1=CC=C(C=C1)O)CC1=CC=CC=C1)CC1=CC=C(C=C1)O)CCCNC(=N)N)[[email protected]@H](C)CC

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Aprotinin  Product Citations

See how others have used Aprotinin. Click on the entry to view the PubMed entry .

Citations 1 to 10 of 32 total

PMID: # 30389374  Virgolini, MJ.|Feliziani, C.|Cambiasso, MJ.|Lopez, PH.|Bollo, M.| et al. 2019. Biochim Biophys Acta Mol Cell Res. 1866: 225-239.

PMID: # 30770245  Arora, H. et al. 2019. Immunity.

PMID: # 31263181  Zhang, K.|Xie, Y.|Muñoz-Moreno, R.|Wang, J.|Zhang, L.|Esparza, M.|García-Sastre, A.|Fontoura, BMA.|Ren, Y.| et al. 2019. Nat Microbiol.

PMID: # 27760898  Mitsui, T.|Ishida, M.|Izawa, M.|Arita, J.| et al. 2017. Endocr. J. 64: 103-115.

PMID: # 26443826  Murphy, KC. et al. 2016. FASEB J. 30: 477-86.

PMID: # 27114691  Nardi, GM. et al. 2016. Pharmacognosy Res. 8: S42-9.

PMID: # 27297104  Okoro, EU. et al. 2016. Biochemical and biophysical research communications.

PMID: # 28101164  Zhang, Y.|Wang, LL.|Wu, Y.|Wang, N.|Wang, SM.|Zhang, B.|Shi, CG.|Zhang, SC.| et al. 2016. Exp Ther Med. 12: 3729-3734.

PMID: # 27999422  Yang, SX.|Chen, YX.|Xu, J.|Yang, ZH.| et al. 2016. Med. Sci. Monit. 22: 5028-5034.

PMID: # 26622683  Zhong, F. et al. 2015. Oncology letters. 10: 1416-1422.

Citations 1 to 10 of 32 total

How many mg of aprotinin is needed to convert to kiu?

Asked by: two2igm05
Thank you for your question. The activity of Aprotinin, sc-3595, is 6300 KIU/mg (on dry basis).
Answered by: Chemical Support 4
Date published: 2017-03-07

What is the shelf life of sc-3595? How long is it stable?

Asked by: Jz28sail
Thank you for your question. The shelf life of sc-3595, Aprotinin, is dependent on handling and storage. Solutions are less stable than the lyophilized powder, but Lyophilized Aprotinin, stored at 4&deg;C, is stable at least one year from date of purchase. If you have any further questions or concerns, please feel free to contact our Technical Service department by calling 800-457-3801 option 2, emailing [email protected], or using the Live Chat function on our website.
Answered by: Tech Service 8
Date published: 2017-01-23
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Rated 5 out of 5 by from Good protease inhibitor It works well for PCR purification! I am going to buy it again
Date published: 2016-11-29
Rated 5 out of 5 by from It has been reported in several publications It has been reported in several publications that product sc-3595 has been used as a reversible serine protease inhibitor in their lysis buffer. -SCBT Publication Review
Date published: 2015-03-24
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