F5135
N-[3-(2-Furyl)acryloyl]-Leu-Gly-Pro-Ala
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:
Poids moléculaire :
476.52
UNSPSC Code:
12352202
PubChem Substance ID:
NACRES:
NA.32
MDL number:
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Laissez-nous vous aiderNom du produit
N-[3-(2-Furyl)acryloyl]-Leu-Gly-Pro-Ala,
Quality Level
UniProt accession no.
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)
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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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
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