质量水平
检测方案
≥95% (HPLC)
形式
lyophilized solid
制造商/商品名称
Calbiochem®
储存条件
OK to freeze
avoid repeated freeze/thaw cycles
desiccated
颜色
white to off-white
溶解性
ethanol: 1 mg/mL
water: soluble
运输
ambient
储存温度
−20°C
一般描述
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)
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
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)
外形
45 mg D-mannitol and 5 mg substrate. Sold on the basis of substrate content.
重悬
Following reconstitution, store in the refrigerator (4°C). Stock solutions are stable for up to 3 months at 4°C.
其他说明
Largman, L. 1983. Biochemistry22, 3763.
Del Mar, E.G., et al. 1980. Biochemistry19, 468.
Del Mar, E.G., et al. 1980. Biochemistry19, 468.
法律信息
CALBIOCHEM is a registered trademark of Merck KGaA, Darmstadt, Germany
WGK
WGK 1
闪点(°F)
Not applicable
闪点(°C)
Not applicable
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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