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E8140

Sigma-Aldrich

Elastase from human leukocytes

lyophilized powder, ≥50 units/mg protein (Bradford)

Synonym(s):

Lysosomal elastase

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About This Item

CAS Number:
Enzyme Commission number:
MDL number:
UNSPSC Code:
12352204
NACRES:
NA.54

biological source

human leucocytes

Quality Level

form

lyophilized powder

specific activity

≥50 units/mg protein (Bradford)

mol wt

29 kDa

UniProt accession no.

shipped in

dry ice

storage temp.

−20°C

Gene Information

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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
Elastase has been used to digest fibronectin. The results were compared with fibronectin digestion by crude human leukocyte homogenate to examine the presence of fibronectin peptides in saliva of patients with Sjögren′s syndrome. It has also been used as a reference to determine the elastase activity in cell lysates. This study examined the effect of all-trans retinoic acid on procoagulant and fibrinolytic activities of cultured blast cells. These blast cells were from patients with acute promyelocytic leukemia.

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-L-alanine p-nitrophenyl ester at pH 6.5 at 37 °C.

Physical form

Lyophilized from 0.05 M sodium acetate (pH 5.5) and 0.6 M NaCl

Storage Class Code

13 - Non Combustible Solids

WGK

WGK 1

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable


Certificates of Analysis (COA)

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Yiming Shao et al.
Journal of cellular and molecular medicine, 26(7), 2089-2103 (2022-02-12)
Neutrophils release neutrophil extracellular traps (NETs) to capture and kill pathogens, but excessive NET release can damage the surrounding tissues. Myeloperoxidase (MPO) and neutrophil elastase (NE) are thought to be important in promoting histone depolymerization and DNA breakage in the
Emily J Meyer et al.
Protein science : a publication of the Protein Society, 29(12), 2495-2509 (2020-10-22)
Corticosteroid-binding globulin (CBG) transports cortisol and other steroids. High-affinity CBG (haCBG) undergoes proteolysis of the reactive center loop (RCL) by neutrophil elastase (NE) altering conformation to low-affinity CBG (laCBG). Elevated temperature reduces CBG:cortisol binding affinity. Surface plasmon resonance was used
Proteolytic Processing of the Epithelial Adherens Junction Molecule E-Cadherin by Neutrophil Elastase Generates Short Peptides With Novel Wound-Healing Bioactivity
Gordon MH, et al.
Cellular and molecular gastroenterology and hepatology, 7(2), 483-483 (2019)
Elastase: General Information1,2
Methods of Enzymatic Analysis, 2, 1041-1045 (1974)
Regulation of Dynein in Ciliary and Flagellar Movement
Dyneins, 366-393 (2012)

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