HSPA2 Recombinant Protein Antigen Summary
| Description |
A recombinant protein antigen with a N-terminal His6-ABP tag corresponding to human HSPA2. Source: E. coli
Amino Acid Sequence: ILNVTAADKSTGKENKITITNDKGRLSKDDIDRMVQEAERYKSEDEANRDRVAAKNALESYTYNIKQTVEDEKLRGKISEQDKNKILDKCQEVINWLDRNQMAEKDEYEHKQKELERVCNPIISKLYQGGPGGGSGGGGSGASGGPTIEE Fusion Tag: N-terminal His6ABP (ABP = Albumin Binding Protein derived from Streptococcal Protein G)
This product is intended to be used as a blocking antigen for antibody competition assays. Any other use of this antigen is done at the risk of the user. The use of this product for commercial production is strictly prohibited. Please contact technical support if you have any questions. |
| Source |
E. coli |
| Protein/Peptide Type |
Recombinant Protein Antigen |
| Gene |
HSPA2 |
| Purity |
>80% by SDS-PAGE and Coomassie blue staining |
Applications/Dilutions
| Dilutions |
- Antibody Competition 10 - 100 molar excess
|
| Application Notes |
This recombinant antigen is only intended to be used as a blocking agent to confirm antibody specificity with the corresponding antibody, catalog number NBP1-86185. It is purified by IMAC chromatography, and the expected concentration is greater than 0.5 mg/ml. For current lot information, including availability, please contact our technical support team click nb-technical@bio-techne.com |
| Theoretical MW |
34 kDa. Disclaimer note: The observed molecular weight of the protein may vary from the listed predicted molecular weight due to post translational modifications, post translation cleavages, relative charges, and other experimental factors. |
Packaging, Storage & Formulations
| Storage |
Store at -20C. Avoid freeze-thaw cycles. |
| Buffer |
PBS and 1M Urea, pH 7.4. |
| Preservative |
No Preservative |
| Purity |
>80% by SDS-PAGE and Coomassie blue staining |
Alternate Names for HSPA2 Recombinant Protein Antigen
Background
In cooperation with other chaperones, Hsp70s stabilize preexistent proteins against aggregation and mediatethe folding of newly translated polypeptides in the cytosol as well as within organelles. These chaperones participatein all these processes through their ability to recognize nonnative conformations of other proteins. They bindextended peptide segments with a net hydrophobic character exposed by polypeptides during translation and membranetranslocation, or following stress-induced damage
Limitations
This product is for research use only and is not approved for use in humans or in clinical diagnosis. Peptides and proteins are
guaranteed for 1 year from date of receipt.
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