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E8140

Elastase from human leukocytes

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

Sinónimos:

Lysosomal elastase

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Número CAS:
UNSPSC Code:
12352204
NACRES:
NA.54
Número CE:
MDL number:
Specific activity:
≥50 units/mg protein (Bradford)
Biological source:
human leucocytes
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Quality Level

biological source

human leucocytes

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

General description

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
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[1]
  • 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.[1] 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.[2]

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 form

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

Other Notes

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.


Clase de almacenamiento

13 - Non Combustible Solids

wgk

WGK 1

flash_point_f

Not applicable

flash_point_c

Not applicable



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Número de artículo de comercio global

SKUGTIN
E8140-1UN04061833608630

Questions

1–4 of 4 Questions  
  1. How much does each vial contains? please answer me using gram and not activity unit.

    1 answer
    1. This product is assigned a minimum activity specification of 50 units per milligram protein. At the minimum activity of 50 units, one vial would contain 20 ug of protein. The activity and protein content are lot specific and reported in the product Certificate of Analysis. Please see the link below to review a sample or lot specific Certificate:
      https://www.sigmaaldrich.com/product/sigma/e8140#product-documentation

      Helpful?

  2. Combien de temps et à quelle température peut-on stocker des aliquôts de solution l'élastase reconstituée dans le tampon pH5.5, s'il vous plaît?

    1 answer
    1. This material is lyophilized from a solution containing 0.05 M sodium acetate (pH 5.5) and 0.6 M NaCl. The solution stability of this product has not been determined. However, reconstitution in water and snap-freezing in aliquots, then storing at -70°C, is recommended.

      Helpful?

  3. Is this the active form of the enzyme? or does it require activation by cathepsin?

    1 answer
    1. This product is not activated by cathepsin when tested for the activity of the enzyme. Please see the enzyme assay at the link below:
      https://www.sigmaaldrich.com/deepweb/assets/sigmaaldrich/product/documents/506/826/e8140enz.pdf

      Helpful?

  4. How much enzyme is contained in a single package?

    1 answer
    1. As provided, each vial contains one unit of Elastase enzyme activity, defined as the amount of enzyme required to catalyze the conversion of nanomole of p-nitrophenol per second from BOC-L-alanine p-nitrophenyl ester at pH 6.5 at 37 °C.

      Helpful?

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