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Key Documents

E8140

Sigma-Aldrich

Elastase from human leukocytes

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

Sinonimo/i:

Lysosomal elastase

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About This Item

Numero CAS:
Classificazione EC (Enzyme Commission):
Numero MDL:
Codice UNSPSC:
12352204
NACRES:
NA.54

Origine biologica

human leucocytes

Livello qualitativo

Forma fisica

lyophilized powder

Attività specifica

≥50 units/mg protein (Bradford)

PM

29 kDa

N° accesso UniProt

Condizioni di spedizione

dry ice

Temperatura di conservazione

−20°C

Informazioni sul gene

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Descrizione generale

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.

Applicazioni

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.

Azioni biochim/fisiol

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.

Proprietà fisiche

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

Definizione di unità

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.

Stato fisico

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

Applicazioni

N° Catalogo
Descrizione
Determinazione del prezzo

Codice della classe di stoccaggio

13 - Non Combustible Solids

Classe di pericolosità dell'acqua (WGK)

WGK 1

Punto d’infiammabilità (°F)

Not applicable

Punto d’infiammabilità (°C)

Not applicable


Certificati d'analisi (COA)

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Koichiro Mihara et al.
The Journal of biological chemistry, 288(46), 32979-32990 (2013-09-21)
Neutrophil proteinases released at sites of inflammation can affect tissue function by either activating or disarming signal transduction mediated by proteinase-activated receptors (PARs). Because PAR1 is expressed at sites where abundant neutrophil infiltration occurs, we hypothesized that neutrophil-derived enzymes might
Carey A Hobbs et al.
American journal of physiology. Lung cellular and molecular physiology, 305(12), L990-L1001 (2013-10-15)
The epithelial sodium channel (ENaC) is responsible for Na(+) and fluid absorption across colon, kidney, and airway epithelia. Short palate lung and nasal epithelial clone 1 (SPLUNC1) is a secreted, innate defense protein and an autocrine inhibitor of ENaC that
III - Hydrolases
Enzymes of the Arterial Wall, 208-390 (1969)
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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