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H9019

Sigma-Aldrich

Ac-Hirudin Fragment 55-65 non-sulfated

≥97% (HPLC)

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Empirical Formula (Hill Notation):
C66H92N12O25
CAS Number:
Molecular Weight:
1453.50
MDL number:
UNSPSC Code:
12352200
PubChem Substance ID:
NACRES:
NA.26

Quality Level

Assay

≥97% (HPLC)

storage temp.

−20°C

SMILES string

CCC(C)C(NC(=O)C(CCC(O)=O)NC(=O)C(CCC(O)=O)NC(=O)C(Cc1ccccc1)NC(=O)C(CC(O)=O)NC(C)=O)C(=O)N2CCCC2C(=O)NC(CCC(O)=O)C(=O)NC(CCC(O)=O)C(=O)NC(Cc3ccc(O)cc3)C(=O)NC(CC(C)C)C(=O)NC(CCC(N)=O)C(O)=O

InChI

1S/C66H92N12O25/c1-6-34(4)55(77-59(95)42(22-27-53(88)89)70-56(92)39(19-24-50(82)83)71-61(97)45(30-36-11-8-7-9-12-36)76-63(99)47(32-54(90)91)68-35(5)79)65(101)78-28-10-13-48(78)64(100)72-41(21-26-52(86)87)57(93)69-40(20-25-51(84)85)58(94)75-46(31-37-14-16-38(80)17-15-37)62(98)74-44(29-33(2)3)60(96)73-43(66(102)103)18-23-49(67)81/h7-9,11-12,14-17,33-34,39-48,55,80H,6,10,13,18-32H2,1-5H3,(H2,67,81)(H,68,79)(H,69,93)(H,70,92)(H,71,97)(H,72,100)(H,73,96)(H,74,98)(H,75,94)(H,76,99)(H,77,95)(H,82,83)(H,84,85)(H,86,87)(H,88,89)(H,90,91)(H,102,103)

InChI key

IEAUQSWIFZNYCL-UHFFFAOYSA-N

Amino Acid Sequence

Acetyl-Asp-Phe-Glu-Glu-Ile-Pro-Glu-Glu-Tyr-Leu-Gln

Application

Ac-Hirudin Fragment 55-65 non-sulfated is a C-terminal fragment (fibrinogen-recognition site binding) of the leech anticoagulant peptide hirudin. Ac-Hirudin Fragment 55-65 may be used with other C-terminal fragments to study optimal N-terminal and position 56 functionalities for C-terminal fragment analogues of hirudin.

WGK

WGK 3

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable

Personal Protective Equipment

dust mask type N95 (US), Eyeshields, Gloves

Regulatory Information

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T Pernerstorfer et al.
Blood, 95(5), 1729-1734 (2000-02-26)
During sepsis, lipopolysaccharide (LPS) triggers the development of disseminated intravascular coagulation (DIC) via the tissue factor-dependent pathway of coagulation resulting in massive thrombin generation and fibrin polymerization. Recently, animal studies demonstrated that hirudin reduced fibrin deposition in liver and kidney
K P Hopfner et al.
Biochemistry, 32(12), 2947-2953 (1993-03-30)
The binding energetics of eight synthetic peptides capable of interfering with thrombin function have been studied by steady-state measurements and clotting assays. The synthetic peptides are bifunctional inhibitors consisting of three domains: (i) a fragment of the C-terminus of recombinant
Bon-Hun Koo et al.
The Journal of biological chemistry, 285(53), 41270-41279 (2010-11-03)
Like most metalloproteases, matrix metalloprotease 2 (MMP-2) is synthesized as a zymogen. MMP-2 propeptide plays a role in inhibition of catalytic activity through a cysteine-zinc ion pairing, disruption of which results in full enzyme activation. A variety of proteases have

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