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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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B Lin et al.
Infection and immunity, 64(8), 3401-3406 (1996-08-01)
Group B streptococci were recently reported to possess a cell-associated collagenase. Although the enzyme hydrolyzed the synthetic collagen-like substrate N-(3-[2-furyl]acryloyl)-Leu-Gly-Pro-Ala, we found that neither the highly purified enzyme nor crude group B streptococcal cell lysate solubilized a film of reconstituted
K K Mäkinen et al.
The Journal of biological chemistry, 267(20), 14285-14293 (1992-07-15)
An endopeptidase was purified to homogeneity from the cell extracts of Treponema denticola ATCC 35405 (a human oral spirochete) by a procedure that comprised dialysis, anion exchange fast protein liquid chromatography (FPLC), hydroxylapatite FPLC, immobilized metal affinity FPLC, FPLC chromatofocusing
Teisuke Takita et al.
Journal of biochemistry, 163(5), 425-431 (2018-02-15)
The collagenase produced by a gram-negative bacterium Grimontia hollisae strain 1706B (Ghcol) degrades collagen more efficiently than that produced by a gram-positive bacterium Clostridium histolyticum (Chcol), which is currently the most widely used collagenase in industry [Teramura et al. (Cloning
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
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

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