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F5135

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

Name: N-[3-(2-Furyl)acryloyl]-Leu-Gly-Pro-Ala
Brand: SIGMA

collagenase substrate, chromogenic

Synonyme(s) :

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

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A propos de cet article

Formule empirique (notation de Hill) :

C₂₃H₃₂N₄O₇

Numéro CAS:

78832-65-2

Poids moléculaire :

476.52

UNSPSC Code:

12352202

PubChem Substance ID:

329799652

NACRES:

NA.32

MDL number:

MFCD00133552

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Propriétés

Nom du produit

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

Quality Level

200

UniProt accession no.

Q02111

storage temp.

−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

InChI key

ZLFQNOJSYZSINX-PVJKAEHXSA-N

Gene Information

mouse ... Prkcq(18761)

Description

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.

Classe de stockage

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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Protocoles

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.

Inhibitory role of silk cocoon extract against elastase, hyaluronidase and UV radiation-induced matrix metalloproteinase expression in human dermal fibroblasts and keratinocytes.

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

Reduced synovial inflammation and inhibition of matrix metalloproteinases explicates anti-osteoarthritis activity of polyherbal formulations.

Dhanashri R Ingale et al.

Indian journal of pharmacology, 50(1), 22-29 (2018-06-05)

Current osteoarthritis (OA) research experiences an incline toward Ayurveda to attain a complete cure without notable adverse effects. Ayurveda uses natural products, which are known to perform the multi-faceted role, a much demanding approach for OA management. However, lack of

Metal content and biochemical analyses of a recombinant collagenase PrtV from Vibrio parahaemolyticus.

M S Yu et al.

Microbiology and immunology, 44(10), 805-813 (2000-12-29)

PrtV is an extracellular metalloprotease of Vibrio parahaemolyticus and regarded as a collagenase. Inductively coupled plasma-optical emission spectrometry analysis indicated that the recombinant PrtV contains 1 mol of zinc per mol of the native enzyme. On the basis of a

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Numéro d'article de commerce international

Référence	GTIN
F5135-100MG	04061833618080
F5135-25MG	04061833618097
F5135-5MG	04061833618103