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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:
78832-65-2
Molekulargewicht:
476.52
MDL-Nummer:
MFCD00133552
UNSPSC-Code:
12352202
PubChem Substanz-ID:
329799652
NACRES:
NA.32

product name

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

UniProt-Hinterlegungsnummer

Q02111

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)

Suchen Sie nach Analysenzertifikate (COA), indem Sie die Lot-/Chargennummer des Produkts eingeben. Lot- und Chargennummern sind auf dem Produktetikett hinter den Wörtern ‘Lot’ oder ‘Batch’ (Lot oder Charge) zu finden.

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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
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
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
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
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Protokolle

Enzymatic Assay of Collagenase (EC 3.4.24.3) using FALGPA (N-(3-[2-Furyl]acryloyl)-Leu-Gly-Pro-Ala)

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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