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219474 Cathepsin G Substrate IV, Fluorogenic - Calbiochem

An internally quenched fluorogenic peptide substrate (Mca/Anb as fluorophore/quencher) that is preferentially cleaved by cathepsin G between Gnf and Ser with high efficiency and selectivity.

Cathepsin G Substrate IV, Fluorogenic - Calbiochem MSDS (material safety data sheet) or SDS, CoA and CoQ, dossiers, brochures and other available documents.

Synonyms: Mca-FVT-Gnf-SW-Anb-NH₂

219474
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Przegląd

Replacement Information

Products

Numer katalogowyOpakowanie Ilość/opak.
219474-1MG Ampulka plastikowa 1 mg
Description
OverviewAn internally quenched fluorogenic peptide substrate (Mca/Anb as fluorophore/quencher) that is preferentially cleaved by cathepsin G between Gnf and Ser with high efficiency and selectivity (kcat = 0.524 s-1; KM = 2.08 µM; kcat/KM = 252,000 M-1s-1) as well as sensitivity (≤70 pM Cath G; [subsrate] = 3.3 µM). Human neutrophil elastase and proteinase 3 are found to cleave the peptide between Val and Thr with a much slower kinetics (no detectable cleavage in 1 h) and lower efficiency (10% and 23% cleavage, respectively, after 24 h). Excitation max: 325 nm; emission max: 400 nm.
Mca = 7-Methoxycoumarin-4-yl acetyl; Gnf = 4-Guanidine-L-phenylalanine; Anb = Amino nitrobenzoic acid.
Catalogue Number219474
Brand Family Calbiochem®
SynonymsMca-FVT-Gnf-SW-Anb-NH₂
References
ReferencesLesner, A., et al. 2008. Anal. Biochem. 375, 306.
Product Information
FormLyophilized solid
FormulationSupplied as a trifluoroacetate salt
Hill FormulaC₆₁H₆₇N₁₃O₁₅
Chemical formulaC₆₁H₆₇N₁₃O₁₅
Hygroscopic Hygroscopic
Quality LevelMQ100
Applications
Biological Information
Purity≥97% by HPLC
Physicochemical Information
Emission max.
Excitation max.
Peptide SequenceMca-Phe-Val-Thr-Gnf~Ser-Trp-Anb-NH₂
Dimensions
Materials Information
Toxicological Information
Safety Information according to GHS
Safety Information
Product Usage Statements
Storage and Shipping Information
Ship Code Shipped with Blue Ice or with Dry Ice
Toxicity Standard Handling
Storage -20°C
Protect from Light Protect from light
Hygroscopic Hygroscopic
Do not freeze Ok to freeze
Special InstructionsFollowing reconstitution, aliquot and freeze (-20°C). Stock solutions are stable for up to 6 months at -20°C.
Packaging Information
Packaged under inert gas Packaged under inert gas
Transport Information
Supplemental Information
Specifications
Global Trade Item Number
Numer katalogowy GTIN
219474-1MG 04055977218510

Documentation

Cathepsin G Substrate IV, Fluorogenic - Calbiochem Certificates of Analysis

TitleLot Number
219474

References

Przegląd literatury
Lesner, A., et al. 2008. Anal. Biochem. 375, 306.
Data Sheet

Note that this data sheet is not lot-specific and is representative of the current specifications for this product. Please consult the vial label and the certificate of analysis for information on specific lots. Also note that shipping conditions may differ from storage conditions.

Revision28-July-2020 JSW
SynonymsMca-FVT-Gnf-SW-Anb-NH₂
DescriptionAn internally quenched fluorogenic peptide substrate (Mca/Anb as fluorophore/quencher) that is preferentially cleaved by cathepsin G between Gnf and Ser with high efficiency and selectivity (kcat = 0.524 s-1; KM = 2.08 µM; kcat/KM = 252,000 M-1s-1) as well as sensitivity (≤70 pM Cath G; [subsrate] = 3.3 µM). Human neutrophil elastase and proteinase 3 are found to cleave the peptide between Val and Thr with a much slower kinetics (no detectable cleavage in 1 h) and lower efficiency (10% and 23% cleavage, respectively, after 24 h). Excitation max: 325 nm; Emission max: 400 nm
FormLyophilized solid
FormulationSupplied as a trifluoroacetate salt
Intert gas (Yes/No) Packaged under inert gas
Chemical formulaC₆₁H₆₇N₁₃O₁₅
Peptide SequenceMca-Phe-Val-Thr-Gnf~Ser-Trp-Anb-NH₂
Purity≥97% by HPLC
SolubilityDMSO (10 mg/ml)
Storage Protect from light
-20°C
Hygroscopic
Do Not Freeze Ok to freeze
Special InstructionsFollowing reconstitution, aliquot and freeze (-20°C). Stock solutions are stable for up to 6 months at -20°C.
Toxicity Standard Handling
ReferencesLesner, A., et al. 2008. Anal. Biochem. 375, 306.