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Merck

F5135

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

collagenase substrate, chromogenic

Sinónimos:

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

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Fórmula empírica (notación de Hill):
C23H32N4O7
Número CAS:
78832-65-2
Peso molecular:
476.52
UNSPSC Code:
12352202
PubChem Substance ID:
329799652
NACRES:
NA.32
MDL number:
MFCD00133552

Documentos clave

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Nombre del producto

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

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

InChI key

ZLFQNOJSYZSINX-PVJKAEHXSA-N

UniProt accession no.

Q02111

storage temp.

−20°C

Quality Level

200

Gene Information

mouse ... Prkcq(18761)

General description

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.
Substrate for collagenase.

Application

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 Actions

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

Packaging

Bottomless glass bottle. Contents are inside inserted fused cone.

Clase de almacenamiento

11 - Combustible Solids

wgk

WGK 3

flash_point_f

Not applicable

flash_point_c

Not applicable

ppe

Eyeshields, Gloves, type N95 (US)

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Certificados de análisis (COA)

Lot/Batch Number
BCCP3919
BCCM1118
BCCK4776
BCCH9650
BCCG5673

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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
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
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
Z E Juarez et al.
Infection and immunity, 67(1), 271-278 (1998-12-24)
Streptococcus gordonii is a frequent cause of infective bacterial endocarditis, but its mechanisms of virulence are not well defined. In this study, streptococcal proteases were recovered from spent chemically defined medium (CDM) and fractionated by ammonium sulfate precipitation and by
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