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Elastase Substrate IV, Colorimetric

A specific substrate for pancreatic elastase.

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Synonym(s):
Elastase Substrate IV, Colorimetric
Empirical Formula (Hill Notation):
C25H34N6O9
Molecular Weight:
562.57

Quality Level

assay

≥95% (HPLC)

form

lyophilized solid

manufacturer/tradename

Calbiochem®

storage condition

OK to freeze
avoid repeated freeze/thaw cycles
desiccated

color

white to off-white

solubility

ethanol: 1 mg/mL
water: soluble

shipped in

ambient

storage temp.

−20°C

General description

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.

Biochem/physiol Actions

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

Warning

Toxicity: Standard Handling (A)

Sequence

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

Physical form

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

Reconstitution

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

Other Notes

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

Legal Information

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

Storage Class

11 - Combustible Solids

wgk_germany

WGK 1

flash_point_f

Not applicable

flash_point_c

Not applicable


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Customers Also Viewed

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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