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06880

Sigma-Aldrich

4-Aminobenzamidine dihydrochloride

BioReagent, suitable for fluorescence, ≥99.0% (TLC)

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5 G
1.700,00 kr.

1.700,00 kr.

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5 G
1.700,00 kr.

About This Item

Linear Formula:
H2NC6H4C(=NH)NH2·2HCl
CAS Number:
2498-50-2
Molecular Weight:
208.09
Beilstein:
3692927
EC Number:
219-692-2
MDL number:
MFCD00013001
UNSPSC Code:
12352100
PubChem Substance ID:
329748295
NACRES:
NA.32

1.700,00 kr.

Please contact Customer Service for Availability
Request a Bulk Order

product line

BioReagent

Assay

≥99.0% (TLC)

form

powder or crystals

mp

>300 °C (lit.)

fluorescence

λex >300 nm in H2O

suitability

suitable for fluorescence

storage temp.

2-8°C

SMILES string

Cl[H].Cl[H].NC(=N)c1ccc(N)cc1
Cl[H].Cl[H].NC(=N)c1ccc(N)cc1

InChI

1S/C7H9N3.2ClH/c8-6-3-1-5(2-4-6)7(9)10;;/h1-4H,8H2,(H3,9,10);2*1H

InChI key

GHEHNICLPWTXJC-UHFFFAOYSA-N

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Analysis Note

Emmax: none

Other Notes

Competitive inhibitor of serine proteases[1][2]; As a fluorescent probe for the active site of serine proteases[3]

replaced by

Product No.
Description
Pricing

Storage Class Code

11 - Combustible Solids

WGK

WGK 3

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable

Personal Protective Equipment

dust mask type N95 (US), Eyeshields, Gloves

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Certificates of Analysis (COA)

Lot/Batch Number
MKCB0554V
MKBV5530V
MKBZ0651V
MKBS8455V
MKBQ2732V

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Comparative studies on the inhibition of trypsin, plasmin, and thrombin by derivatives of benzylamine and benzamidine.
F Markwardt et al.
European journal of biochemistry, 6(4), 502-506 (1968-12-05)
STUDIES ON THE ACTIVE CENTER OF TRYPSIN. THE BINDING OF AMIDINES AND GUANIDINES AS MODELS OF THE SUBSTRATE SIDE CHAIN.
M MARES-GUIA et al.
The Journal of biological chemistry, 240, 1579-1585 (1965-04-01)
S A Evans et al.
The Journal of biological chemistry, 257(6), 3014-3017 (1982-03-25)
p-Aminobenzamidine is weakly fluorescent in neutral aqueous buffer, with excitation and emission maxima at 293 and 376 nm, respectively. Binding to trypsin results in a blue shift of the emission peak to 362 nm, and 50-fold fluorescence enhancement, while binding
Nathan J Alves et al.
Biochemical and biophysical research communications, 457(3), 358-362 (2015-01-13)
The potent fibrinolytic enzyme, plasmin has numerous clinical applications for recannulizing vessels obstructed by thrombus. Despite its diminutive size, 91 kDa, success in the recombinant expression of this serine protease has been limited. For this reason, a truncated non-glycosylated plasmin

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