IMG-EN-AS-61315-01.jpg
Peptides

Cls Substrate, C2 (Abz/Dnp) - 1 mg

$228.00
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  • Cat.Number : AS-61315
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    In stock

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This peptide is a second complement component (C2), the physiological substrate for the proenzyme Cls, first complement component. The complement system is a central component of host defense but can also contribute to the inflammation seen in pathological conditions. The C1s protease of the C1 complex initiates the host defense pathway. This peptide employs 2Abz/Dnp FRET pair for quantitation of complement enzyme activity.

Specifications

Chemistry
Sequence one letter code
  • 2Abz-SLGRKIQIK(Dnp)-NH2
Sequence three letter code
  • 2Abz-Ser-Leu-Gly-Arg-Lys-Ile-Gln-Ile-Lys(Dnp)-NH2
Molecular Mass/ Weight
  • 1326.6
Properties
Absorbance (nm)
  • 320
Emission (nm)
  • 420
Modification
Conjugation type
  • Double dyes
Modification Name
Conjugation
  • Conjugated
Quantity & Purity
Purity
  • Peak Area by HPLC ≥95%
Storage & stability
Form
  • Lyophilized
Storage Conditions
  • - 20 °C Protected from light
Activity
Biomarker Target
Detection Method
Research Area
Sub-category Research Area
Usage
  • Research use
Source
Source / Species
  • synthetic

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Citations

Antimicrobial peptide conformation as a structural determinant of omptin protease specificity

J Bacteriol . 2015 Sep 08 ; 197 22 | DOI : 10.1128/JB.00469-15

  • RJ. Brannon

OmpT outer membrane proteases of enterohemorrhagic and enteropathogenic Escherichia coli contribute differently to the degradation ofhuman LL-37

Infect Immun . 2011 Dec 05 ; 80(2) 483 | DOI : 10.1128/​IAI.05674-11

  • JL. Thomassin

References

Cleavage of C2 by C1̄s̄ into the antigenically distinct fragments C2a and C2b: Demonstration of binding of C2b to C4b

PNAS . 1977 Jul 01 ; 74(7) 2998 | DOI : https://doi.org/10.1073/pnas.74.7.2998

  • S. Nagasawa
  • R. Stroud

Elucidation of the Substrate Specificity of the C1s Protease of the Classical Complement Pathway

J Biol Chem . 2005 Nov 01 ; 280(47) 39510 | DOI : https://doi.org/10.1074/jbc.M506131200

  • F. Kerr
  • et al