A3401
Ala-Ala-Phe-7-amido-4-methylcoumarin
protease substrate
๋์์ด(๋ค):
H-Ala-Ala-Phe-AMC
์กฐ์ง ๋ฐ ๊ณ์ฝ ๊ฐ๊ฒฉ์ ๋ณด๋ ค๋ฉด ๋ก๊ทธ์ธ๋ฅผ ํด๋ฆญํฉ๋๋ค.
ํฌ๊ธฐ ์ ํ
๋ณด๊ธฐ ๋ณ๊ฒฝ
์ ํ์ ๋ณด (DICE ๋ฐฐ์ก ์ ๋น์ฉ ๋ณ๋)
์คํ์(Hill ํ๊ธฐ๋ฒ):
C25H28N4O5
CAS ๋ฒํธ:
Molecular Weight:
464.51
NACRES:
NA.32
PubChem Substance ID:
UNSPSC Code:
12352204
MDL number:
๊ธฐ์ ์๋น์ค
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๋์ ๋ฌธ์Quality Level
assay
≥98% (TLC)
form
powder
solubility
ethanol: 20 mg/mL, clear, colorless to light yellow
storage temp.
2-8ยฐC
SMILES string
CC(N)C(=O)NC(C)C(=O)NC(Cc1ccccc1)C(=O)Nc2ccc3C(C)=CC(=O)Oc3c2
InChI
1S/C25H28N4O5/c1-14-11-22(30)34-21-13-18(9-10-19(14)21)28-25(33)20(12-17-7-5-4-6-8-17)29-24(32)16(3)27-23(31)15(2)26/h4-11,13,15-16,20H,12,26H2,1-3H3,(H,27,31)(H,28,33)(H,29,32)
InChI key
FVRLYIFIDKXFHU-UHFFFAOYSA-N
General description
Substrate for chymotrypsin and tripeptidyl peptidaseII.
Ala-Ala-Phe-7-amido-4-methylcoumarin is a fluorogenic substrate for the proteolytic activity. It is a positively charged substrate molecule.
Application
Ala-Ala-Phe-7-amido-4-methylcoumarin has been used:
- in the preparation of the reaction mixture for enzymatic assays
- to initiate theย enzyme reaction in tripeptidyl peptidase-1 (TPP1) enzyme activity assay
- to initiate the assay reaction in lysosomal hydrolases activity assay
์ ์ฅ ๋ฑ๊ธ
11 - Combustible Solids
wgk
WGK 3
flash_point_f
Not applicable
flash_point_c
Not applicable
ppe
Eyeshields, Gloves, type N95 (US)
๊ฐ์ฅ ์ต์ ๋ฒ์ ์ค ํ๋๋ฅผ ์ ํํ์ธ์:
์ด ์ ํ์ ์ด๋ฏธ ๊ฐ์ง๊ณ ๊ณ์ญ๋๊น?
๋ฌธ์ ๋ผ์ด๋ธ๋ฌ๋ฆฌ์์ ์ต๊ทผ์ ๊ตฌ๋งคํ ์ ํ์ ๋ํ ๋ฌธ์๋ฅผ ์ฐพ์๋ณด์ธ์.
๋ฌธ์
Analytical Enzyme Chymotrypsin: Chymotrypsin is produced in the acinar cells of the pancreas as the inactive precursor, chymotrypsinogen.
Accumulation of polyubiquitylated proteins in response to Ala-Ala-Phe-chloromethylketone is independent of the inhibition of tripeptidyl peptidase II
Villasevil E M, et al.
Biochimica et Biophysica Acta - Molecular Cell Research, 1803(9), 1094-1105 (2010)
Raffaella Di Giacopo et al.
Journal of the neurological sciences, 356(1-2), 65-71 (2015-07-06)
This work investigated the molecular cause responsible for a late-onset parkinsonism-dystonia phenotype in three Italian siblings, and clinically characterize this condition. Extensive neurophysiological and neuroradiological exams were performed on the three sibs. Most frequent late-onset metabolic diseases were ruled out
R M Bรฅlรถw et al.
The Journal of biological chemistry, 261(5), 2409-2417 (1986-02-15)
An extralysosomal tripeptide-releasing aminopeptidase was recently discovered in rat liver (Bรฅlรถw, R.-M., Ragnarsson, U., and Zetterqvist, O. (1983) J. Biol. Chem. 258, 11622-11628). In the present work this tripeptidyl peptidase is shown to occur in several rat tissues and in
๊ตญ์ ๋ฌด์ญ ํ๋ชฉ ๋ฒํธ
| SKU | GTIN |
|---|---|
| A3401-25MG | 04061832904146 |