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Merck
CN

F5135

Sigma-Aldrich

N-[3-(2-呋喃基)丙烯酰基]-亮氨酸-甘氨酸-脯氨酸-丙氨酸

collagenase substrate, chromogenic

别名:

FALGPA, N-[3-(2-呋喃基)丙烯酰基]-L-亮氨酸-甘氨酸-L-脯氨酸-L-丙氨酸

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About This Item

经验公式(希尔记法):
C23H32N4O7
CAS号:
分子量:
476.52
MDL编号:
UNSPSC代码:
12352202
PubChem化学物质编号:
NACRES:
NA.32

product name

N-[3-(2-呋喃基)丙烯酰基]-亮氨酸-甘氨酸-脯氨酸-丙氨酸,

质量水平

UniProt登记号

储存温度

−20°C

SMILES字符串

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

基因信息

mouse ... Prkcq(18761)

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Amino Acid Sequence

FA-Leu-Gly-Pro-Ala

一般描述

N-[3-(2-呋喃基)丙烯酰基]-亮氨酸-甘氨酸-脯氨酸-丙氨酸或FALGPA是一种类似于胶原蛋白一级结构的合成物质,可以被所有已知的胶原酶水解。

应用

N-[3-(2-呋喃基)丙烯酰基]-亮氨酸-甘氨酸-脯氨酸-丙氨酸已用于采用GBS(B组链球菌)USF704进行的FALGPA检测。

生化/生理作用

N-[3-(2-呋喃基)丙烯酰基]-亮氨酸-甘氨酸-脯氨酸-丙氨酸或FALGPA可以被胶原酶水解,水解的最适pH为7.4。

包装

无底玻璃瓶。内含物在插入的融合锥体内。

底物

胶原酶的底物。

WGK

WGK 3

闪点(°F)

Not applicable

闪点(°C)

Not applicable

个人防护装备

Eyeshields, Gloves, type N95 (US)


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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
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
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
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

实验方案

在测定胶原酶活性时,使用N-(3-[2-呋喃基]丙烯酰基)-Leu-Gly-Pro-Ala在345nm处进行连续分光光度法测定。胶原酶水解胶原肽键。

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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