General description
Elastase is a proteolytic enzyme. It is a member of the subgroup named, peptidyl peptide hydrolases. It is a major anatomic constituent of arteries. It is mainly found in the pancreas and pancreatic juice of various birds and mammals. It is also present in human serum, granulocytes and erythrocytes.
Application
Elastase from human leukocytes has been used:
- to measure serum elastase activity
- in proteolytic digestion of fibronectin and salivary glands
- in neutrophil elastase (NE) activity assay
- cell-free NE digestion of E-cadherin
- scratch wound assay
- in a study that determined that fragments of Nle3-angiotensin(1-7) accelerate healing in dermal models
Biochem/physiol Actions
Elastase enzyme is capable of releasing soluble peptides from insoluble elastin fibers with the help of a proteolytic process. It can stimulate disintegration of the axoneme with the help of adenosine triphosphate (ATP). Unlike pancreatic elastase the leukocyte enzyme has a preferential cleavage for the carboxyl side of valine, but will also cleave to a lesser extent after alanine. Natural substrates include elastin, cartilage proteoglycans, collagen types I, II, II and IV, and fibronectin.
Physical properties
Leukocyte elastase is a 29 kDa serine endoprotease of the Proteinase S1 Family. It exists as a single 238 amino acid-peptide chain with four disulfide bonds. It contains two or thee N-linked glycans of variable composition which account for its three major isoforms.
Isoelectric point: pI = 8.77 - 9.55
Unit Definition
One unit will release one nanomole of p-nitrophenol per sec from BOC-
Physical form
Lyophilized from 0.05 M sodium acetate (pH 5.5) and 0.6 M NaCl
- UPC:
- 41116127
- Condition:
- New
- Weight:
- 1.00 Ounces
- HazmatClass:
- No
- WeightUOM:
- LB
- MPN:
- E8140-1UN
