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F5135

Sigma-Aldrich

N-[3-(2-Furyl)acryloyl]-Leu-Gly-Pro-Ala

collagenase substrate, chromogenic

Synonym(e):

N-[3-(2-Furyl)-acryloyl]-L-leucyl-glycyl-L-prolyl-L-alanin

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About This Item

Empirische Formel (Hill-System):
C23H32N4O7
CAS-Nummer:
Molekulargewicht:
476.52
MDL-Nummer:
UNSPSC-Code:
12352202
PubChem Substanz-ID:
NACRES:
NA.32

product name

N-[3-(2-Furyl)acryloyl]-Leu-Gly-Pro-Ala,

Qualitätsniveau

UniProt-Hinterlegungsnummer

Lagertemp.

−20°C

SMILES String

CC(C)C[C@H](NC(=O)\C=C\c1ccco1)C(=O)NCC(=O)N2CCC[C@H]2C(=O)N[C@@H](C)C(O)=O

InChI

1S/C23H32N4O7/c1-14(2)12-17(26-19(28)9-8-16-6-5-11-34-16)21(30)24-13-20(29)27-10-4-7-18(27)22(31)25-15(3)23(32)33/h5-6,8-9,11,14-15,17-18H,4,7,10,12-13H2,1-3H3,(H,24,30)(H,25,31)(H,26,28)(H,32,33)/b9-8+/t15-,17-,18-/m0/s1

InChIKey

ZLFQNOJSYZSINX-PVJKAEHXSA-N

Angaben zum Gen

mouse ... Prkcq(18761)

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Amino Acid Sequence

FA-Leu-Gly-Pro-Ala

Allgemeine Beschreibung

N-[3-(2-Furyl)acryloyl]-Leu-Gly-Pro-Ala or FALGPA is a synthetic substance which resemble the primary structure of collagen, and is hydrolyzed by all known collagenases.

Anwendung

N-[3-(2-Furyl)acryloyl]-Leu-Gly-Pro-Ala has been used for use in FALGPA assay performed using GBS (Group B Streptococci) USF704.

Biochem./physiol. Wirkung

N-[3-(2-Furyl)acryloyl]-Leu-Gly-Pro-Ala or FALGPA is hydrolyzed by collagenases and the optimum pH for hydrolysis is 7.4.

Verpackung

Bottomless glass bottle. Contents are inside inserted fused cone.

Substrate

Substrate for collagenase.

Lagerklassenschlüssel

11 - Combustible Solids

WGK

WGK 3

Flammpunkt (°F)

Not applicable

Flammpunkt (°C)

Not applicable

Persönliche Schutzausrüstung

Eyeshields, Gloves, type N95 (US)


Analysenzertifikate (COA)

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Die Dokumentenbibliothek aufrufen

M S Yu et al.
Microbiology (Reading, England), 145 ( Pt 1), 143-150 (1999-04-17)
The prtV gene, encoding a collagenase of Vibrio parahaemolyticus, was expressed in Escherichia coli and purified by affinity chromatography. The transformant E. coli BL21(DE3)(pPRT2) secreted the recombinant PrtV, and the highest enzyme activity was detected in the culture supernatant after
K K Mäkinen et al.
Medical microbiology and immunology, 185(1), 1-10 (1996-05-01)
Relatively scant chemical information has been available on the proteinases and peptidases of spirochetes in spite of the association of spirochetes with several serious infections known to plague humans and other animal species. This situation has partly resulted from difficulties
E Söderling et al.
Journal of periodontal research, 26(1), 17-23 (1991-01-01)
Four rough-surfaced (R) and three smooth-surfaced (S) clinical isolates of Capnocytophaga obtained from the subgingival plaque of periodontitis patients were studied for their peptidase and protease profiles. The results were compared with those obtained with C. gingivalis (which has a
Jadi Praveen Kumar et al.
Photochemical & photobiological sciences : Official journal of the European Photochemistry Association and the European Society for Photobiology, 18(5), 1259-1274 (2019-03-21)
Topical delivery of potent antioxidants maintain the redox balance of the skin, which leads to the downregulation of matrix metalloproteinase (MMP) expression and prevents UV radiation-induced photoaging. In this study, we aimed at investigating the inhibitory role of silk cocoon
R Gayatri et al.
Biochimica et biophysica acta, 1524(2-3), 228-237 (2000-12-13)
Bacterial collagenase has now been reacted with a select series of Cr(III) complexes and modifications in the activity of chromium-modified collagenase has been deduced from the extent of hydrolysis of (2-furanacryloyl-L-leucyl-glycyl-L-prolyl-L-alanine), FALGPA. A homologous series of Cr(III) complexes with dimeric

Protokolle

To measure collagenase activity, N-(3-[2-Furyl]acryloyl)-Leu-Gly-Pro-Ala is used in a continuous spectrophotometric rate determination at 345 nm. Collagenase hydrolyzes collagen peptide bonds.

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