Recombinant Human HSPA6 protein (ab89366)
Key features and details
- Expression system: Escherichia coli
- Purity: > 90% SDS-PAGE
- Suitable for: SDS-PAGE
Description
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Product name
Recombinant Human HSPA6 protein -
Purity
> 90 % SDS-PAGE.
ab89366 is purified using conventional chromatography techniques. -
Expression system
Escherichia coli -
Protein length
Full length protein -
Animal free
No -
Nature
Recombinant -
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Species
Human
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Associated products
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Related Products
Specifications
Our Abpromise guarantee covers the use of ab89366 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 -
Concentration information loading...
Preparation and Storage
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Stability and Storage
Shipped at 4°C. Upon delivery aliquot and store at -20°C or -80°C. Avoid repeated freeze / thaw cycles.
pH: 8.00
Constituents: 0.316% Tris HCl, 10% Glycerol (glycerin, glycerine), 0.58% Sodium chloride
General Info
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Alternative names
- Heat shock 70 kDa protein 6
- Heat shock 70 kDa protein B'
- Heat shock 70 kDa protein B''
see all -
Function
In cooperation with other chaperones, Hsp70s stabilize preexistent proteins against aggregation and mediate the folding of newly translated polypeptides in the cytosol as well as within organelles. These chaperones participate in all these processes through their ability to recognize nonnative conformations of other proteins. They bind extended peptide segments with a net hydrophobic character exposed by polypeptides during translation and membrane translocation, or following stress-induced damage. -
Sequence similarities
Belongs to the heat shock protein 70 family. - Information by UniProt
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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SDS download
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Datasheet download
References (0)
ab89366 has not yet been referenced specifically in any publications.