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F5135

Sigma-Aldrich

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

collagenase substrate, chromogenic

Sinonimo/i:

FALGPA, N-[3-(2-Furyl)acryloyl]-L-leucyl-glycyl-L-prolyl-L-alanine

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About This Item

Formula empirica (notazione di Hill):
C23H32N4O7
Numero CAS:
78832-65-2
Peso molecolare:
476.52
Numero MDL:
MFCD00133552
Codice UNSPSC:
12352202
ID PubChem:
329799652
NACRES:
NA.32

Nome del prodotto

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

Livello qualitativo

200

N° accesso UniProt

Q02111

Temperatura di conservazione

−20°C

Stringa SMILE

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
ZLFQNOJSYZSINX-PVJKAEHXSA-N

Informazioni sul gene

mouse ... Prkcq(18761)

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Amino Acid Sequence

FA-Leu-Gly-Pro-Ala

Descrizione generale

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.

Applicazioni

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

Azioni biochim/fisiol

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

Confezionamento

Bottomless glass bottle. Contents are inside inserted fused cone.

Substrati

Substrate for collagenase.

Codice della classe di stoccaggio

11 - Combustible Solids

Classe di pericolosità dell'acqua (WGK)

WGK 3

Punto d’infiammabilità (°F)

Not applicable

Punto d’infiammabilità (°C)

Not applicable

Dispositivi di protezione individuale

Eyeshields, Gloves, type N95 (US)

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Certificati d'analisi (COA)

Lot/Batch Number
BCCM1118
BCCK4776
BCCH9650
BCCG5673
BCCB9549

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C8051

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Collagenasi Type IA, 0.5-5.0 FALGPA units/mg solid, ≥125 CDU/mg solid, For general use

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C9891

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Tirosinasi lyophilized powder, ≥1000 unit/mg solid

Sigma-Aldrich

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Sigma-Aldrich

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Sigma-Aldrich

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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
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
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
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
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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Protocolli

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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