Recombinant E. coli Ecotin protein (ab92769)
Key features and details
- Expression system: Escherichia coli
- Purity: > 95% SDS-PAGE
- Active: Yes
- Suitable for: SDS-PAGE
Description
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Product name
Recombinant E. coli Ecotin protein
See all Ecotin proteins and peptides -
Biological activity
Kinetic Data: 1:1 inhibition of trypsin (mole per mole) -
Purity
> 95 % SDS-PAGE.
ab92769 is at least 98 percent pure as determined by SDS-PAGE. -
Expression system
Escherichia coli -
Protein length
Full length protein -
Animal free
No -
Nature
Recombinant -
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Species
Escherichia coli
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Description
Recombinant E. coli Ecotin protein
Specifications
Our Abpromise guarantee covers the use of ab92769 in the following tested applications.
The application notes include recommended starting dilutions; optimal dilutions/concentrations should be determined by the end user.
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Applications
SDS-PAGE
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Form
Liquid -
Additional notes
Kinetic Data: 1:1 inhibition of trypsin (mole per mole)Previously labelled as E. coli serine protease inhibitor.
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Concentration information loading...
Preparation and Storage
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Stability and Storage
Shipped on dry ice. Upon delivery aliquot and store at -80ºC. Avoid freeze / thaw cycles.
pH: 3
Constituent: 0.0036% Hydrochloric acidThis product is an active protein and may elicit a biological response in vivo, handle with caution.
General Info
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Alternative names
- E. coli serine protease inhibitor
- ECK2201
- Ecotin
see all -
Relevance
E. coli serine protease inhibitor (Ecotin) inhibits pancreatic serine proteases: inhibits chymotrypsin, trypsin, elastases, factor X, kallikrein as well as a variety of other proteases. The strength of inhibition does not appear to be correlated with a particular protease specificity. -
Cellular localization
Periplasm.
Protocols
To our knowledge, customised protocols are not required for this product. Please try the standard protocols listed below and let us know how you get on.
Datasheets and documents
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Datasheet download
References (0)
ab92769 has not yet been referenced specifically in any publications.