FosB/G0S3 Recombinant Protein Antigen Summary
Description |
A recombinant protein antigen with a N-terminal His6-ABP tag corresponding to human FosB/G0S3. Source: E.coli Amino Acid Sequence: LPFQTSQDAPPNLTASLFTHSEVQVLGDPFPVVNPSYTSSFVLTCPEVSAF |
Source |
E. coli |
Protein/Peptide Type |
Recombinant Protein Antigen |
Gene |
FOSB |
Purity |
>80% by SDS-PAGE and Coomassie blue staining |
Applications/Dilutions
Dilutions |
- Antibody Competition 10 - 100 molar excess
|
Application Notes |
This peptide is useful as a blocking peptide for NBP2-56210 The protein was purified by IMAC chromatography and the expected concentration is greater than 0.5 mg/ml. This protein is produced on demand, estimated shipping date is 4 weeks after the order is placed. For further blocking peptide related information and a protocol, click here. |
Theoretical MW |
23 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 |
Notes
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.
Alternate Names for FosB/G0S3 Recombinant Protein Antigen
Background
Fos and Jun dimerize to form Activator Protein-1 (AP-1), a transcriptional factor that binds to the 12-O-tetradecanoylphorbol 13-acetate (TPA) response element (TRE) of several cellular and viral genes including human collagenase, metallothionein IIa, stromelysin, interleukin 2, SV40 and polyoma. Fos and Jun contain the 'leucine-zipper' motif that allows for dimerization and an adjacent basic domain required for biological activity. The functionally active form of Fos is in a heterodimer with a member of the Jun family. While Jun family members can form functional homodimers, studies indicate that Fos family members do not self-associate and therefore do not bind DNA on their own. The various dimers differ in their ability to transactivate AP-1 dependent genes.
Limitations
This product is for research use only and is not approved for use in humans or in clinical diagnosis. This product is
guaranteed for 1 year from date of receipt.
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