Flagellin FliA (H)
Greater than 97.0% as determined by SDS-PAGE and HPLC analyses.
Description
Flagellin FliA (H) Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 302 amino acids and having a molecular mass of approximately 33.1kDa.
The Flagellin FliA (H) is purified by proprietary chromatographic techniques.
Product Specs
Flagellin FliA (H), also referred to as RNA polymerase sigma factor for flagellar operon, Sigma F, or Sigma-28, belongs to the FliA subfamily, a member of the sigma-70 factor family. This sigma factor plays a crucial role in controlling the expression of genes associated with flagella. Additionally, Flagellin FliA (H) regulates the expression of genes involved in virulence. As an initiation factor, it facilitates the binding of RNA polymerase to specific initiation sites, after which it is released.
Recombinant Flagellin FliA (H), produced in E.Coli, is a single-chain polypeptide that is not glycosylated. It comprises 302 amino acids, resulting in an approximate molecular mass of 33.1kDa. The purification of Flagellin FliA (H) is achieved through proprietary chromatographic methods.
To reconstitute the lyophilized Flagellin FliA (H), it is recommended to dissolve it in sterile 18MΩ-cm H2O to a concentration of at least 100µg/ml. This solution can be further diluted in other aqueous solutions as needed.
Lyophilized Flagellin FliA (H) remains stable at room temperature for up to 3 weeks; however, for long-term storage, it is recommended to store it desiccated below -18°C. Once reconstituted, Flagellin should be stored at 4°C for a period of 2-7 days. For extended storage, it should be kept below -18°C. It is important to avoid repeated cycles of freezing and thawing.
The purity of the product is determined to be greater than 97.0% based on SDS-PAGE and HPLC analyses.
MKGLKTGWIE KSVENIKTAY GIEPTGANKL KVTISDDGAY GVLASVTPKT GEFELHIDSS DFEKGDGESG NNIHGKLYDD RIIQHEMTHA VMNDALGIDK MNDLHDKNKL WFIEGTAEAM AGADERVKDI IGNDTQTGID NTKLSKLATR ADALLNGVSW NSSDEDYAAG YLMVKYIASK GIDLKAVMKE IKNTGASGLD NKIDLTNLKI DFKNNLENYI KDISKVHLDW DDDEKDVGSI LGSDHGHGDI KAEDVVKGTT PEKEQPLDKF KIIWPDDNSD NTTGKIQLQV GANEGQSITI LE
Product Science Overview
Flagellin is a globular protein that forms the filament structure of bacterial flagella, which are essential for bacterial motility. The flagellin protein is encoded by the fliC gene in many bacteria. Flagellin FliA (H) is a specific variant of this protein, often studied for its role in bacterial locomotion and its interaction with the host immune system. Recombinant flagellin FliA (H) is produced through genetic engineering techniques, allowing for detailed studies of its structure and function.
The preparation of recombinant Flagellin FliA (H) involves several key steps:
- Gene Cloning: The fliA (H) gene is cloned into an expression vector, which is then introduced into a suitable host organism, typically Escherichia coli.
- Protein Expression: The host cells are cultured under conditions that induce the expression of the recombinant flagellin protein.
- Protein Purification: The expressed protein is purified using techniques such as affinity chromatography, which isolates the flagellin protein from other cellular components.
- Verification: The purity and identity of the recombinant protein are verified using methods like SDS-PAGE and Western blotting.
Flagellin FliA (H) undergoes several post-translational modifications that can affect its function:
- Glycosylation: This modification involves the addition of sugar moieties to the protein, which can influence its stability and interaction with other molecules.
- Methylation: Methyl groups are added to specific amino acids, affecting the protein’s activity and interactions.
- Proteolytic Cleavage: The protein can be cleaved by proteases, which may regulate its activity and function.
The expression and activity of Flagellin FliA (H) are tightly regulated by several mechanisms:
- Transcriptional Regulation: The fliA (H) gene is regulated by transcription factors that respond to environmental signals, ensuring that flagellin is produced only when needed.
- Post-Translational Modifications: As mentioned earlier, modifications like glycosylation and methylation can regulate the protein’s function.
- Proteolytic Regulation: Proteases can cleave flagellin, modulating its activity and stability.
