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324699

Sigma-Aldrich

Elastase Substrate IV, Colorimetric

A specific substrate for pancreatic elastase.

别名:

Elastase Substrate IV, Colorimetric

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About This Item

经验公式(希尔记法):
C25H34N6O9
分子量:
562.57
分類程式碼代碼:
12352200
NACRES:
NA.54

品質等級

化驗

≥95% (HPLC)

形狀

lyophilized solid

製造商/商標名

Calbiochem®

儲存條件

OK to freeze
avoid repeated freeze/thaw cycles
desiccated

顏色

white to off-white

溶解度

ethanol: 1 mg/mL
water: soluble

運輸包裝

ambient

儲存溫度

−20°C

一般說明

A specific substrate for pancreatic elastase (Km = 100 µM; Kcat/Km = 35,000 s-1 M-1 for rat pancreatic elastase; Km = 30 µM; Kcat/Km = 351,000 s-1 M-1 for porcine pancreatic elastase). Cleavage of substrate can be monitored at ~405 nm.



Suggested protocol: see Largman, C. (1983)
A specific substrate for pancreatic elastase (km = 100 µM; kcat/ Km = 35,000 M-1 s-1 for rat pancreatic elastase, Km = 30 µM; kcat/Km = 35,000 M-1 s-1 for porcine). Cleavage of substrate can be monitored at ~405 nm.

生化/生理作用

Cell permeable: no
Primary Target
A specific substrate for pancreatic elastase
Product does not compete with ATP.
Reversible: no
km = 100 µM; kcat/ Km = 35,000 M-1 s-1 for rat pancreatic elastase; Km = 30 µM; kcat/Km = 35,000 M-1 s-1 for porcine

警告

Toxicity: Standard Handling (A)

序列

Suc-Ala-Ala-Pro-Abu-pNA (Abu = L-α-Aminobutyric Acid)

外觀

45 mg D-mannitol and 5 mg substrate. Sold on the basis of substrate content.

重構

Following reconstitution, store in the refrigerator (4°C). Stock solutions are stable for up to 3 months at 4°C.

其他說明

Largman, L. 1983. Biochemistry22, 3763.
Del Mar, E.G., et al. 1980. Biochemistry19, 468.

法律資訊

CALBIOCHEM is a registered trademark of Merck KGaA, Darmstadt, Germany

儲存類別代碼

11 - Combustible Solids

水污染物質分類(WGK)

WGK 1

閃點(°F)

Not applicable

閃點(°C)

Not applicable


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C Largman
Biochemistry, 22(16), 3763-3770 (1983-08-02)
Proelastase has been purified to homogeneity from rat pancreatic tissue by a combination of CM-Sephadex and immobilized protease inhibitor affinity resins. Trypsin activation yields an elastolytic enzyme that possesses a specificity toward small hydrophobic residues in synthetic amide substrates, similar
E G Del Mar et al.
Biochemistry, 19(3), 468-472 (1980-02-05)
The substrate specificity of human pancreatic elastase 2 was investigated by using a series of peptide p-nitroanilides. The kinetic constants, kcat and Km, for the hydrolysis of these peptides revealed that this serine protease preferentially hydrolyzes peptides containing P1 amino

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