Overview
Product nameChlamydia Trachomatis HSP70 proteinSee all Chlamydia Trachomatis HSP70 proteins and peptides ...
Protein descriptionRecombinant fragment, corresponding to amino acids 549-660 of Chlamydia Trachomatis HSP70
Expression hostE. coli
Properties
Purity> 95
% by SDS-PAGE
Purification notesThis protein is >95% pure as determined by 10% PAGE (coomassie staining) and RP-HPLC. It was purified by proprietary chromatographic techniques.
Biological activityThis protein is immunoreactive with sera of Chlamydia Trachomatis infected individuals.
FormLiquid
Storage instructionsShipped at 4°C. Upon delivery aliquot and store at -20°C. Avoid freeze / thaw cycles.
Storage bufferPreservative: None
Constituents: 50% Glycerol, 8M Urea, 60mM Sodium chloride, 50mM Tris HCl, pH 8.0
Concentration information loading...
Research Areas
Applications
Our Abpromise guarantee covers the use of
ab67712
in the following tested applications.
The application notes include recommended starting dilutions; optimal dilutions/concentrations should be determined by the end user.
|
Application
|
Notes |
| ELISA |
ELISA: Use at an assay dependent dilution. |
| SDS-PAGE |
SDS-PAGE: Use at an assay dependent dilution. |
Protein info
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Alternative names
75 kDa membrane proteinChaperone proteinDnakHeat shock protein 70
RelevanceHSP70 is the eukaryotic analogue of prokaryotic DnaK. Heat-shock proteins applies to a group of proteins that assist in the assembly, folding, and translocation of other proteins. In addition, they protect the cell against heat injury or other forms of stress. All cells, prokaryotic and eukaryotic, are able to respond to different cellular stresses by synthesizing these proteins. Heat shock proteins are highly conserved, ubiquitously distributed, and involved in important aspects of viral and bacterial infections, autoimmune diseases, and in cancer immunity.
Two families of molecular chaperones have been identified. The members of the Hsp70 family (DnaK/DnaJ/GrpE) bind to the growing polypeptide chain and prevent its premature folding. The chaperonin family (GroEL and GroES) assists in correct folding when the complete polypeptide chain is formed and is transported into the cytosol or mitochondria. All the major heat shock proteins help to suppress irreversible unfolding reactions. These protein folding 'assistants' may have important functions in amyloid diseases where incorrectly folded proteins accumulate as folded aggregates.
References for Chlamydia Trachomatis HSP70 protein (ab67712)
ab67712
has not yet been referenced specifically in any publications.
Please note: All products are "FOR RESEARCH USE ONLY AND ARE NOT INTENDED FOR DIAGNOSTIC OR THERAPEUTIC USE"
