Analytical Data
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Gene name
fliC
- Application
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Alternative Names
fliC；DEF6；Defensin-6
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Species
E.coli
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Source
E. coli
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Tag
His tag N-Terminus
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P04949
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Expression Region
2-498aa
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AA Sequence
AQVINTNSLSLITQNNINKNQSALSSSIERLSSGLRINSAKDDAAGQAIANRFTSNIKGLTQAARNANDGISVAQTTEGALSEINNNLQRVRELTVQATTGTNSESDLSSIQDEIKSRLDEIDRVSGQTQFNGVNVLAKNGSMKIQVGANDNQTITIDLKQIDAKTLGLDGFSVKNNDTVTTSAPVTAFGATTTNNIKLTGITLSTEAATDTGGTNPASIEGVYTDNGNDYYAKITGGDNDGKYYAVTVANDGTVTMATGATANATVTDANTTKATTITSGGTPVQIDNTAGSATANLGAVSLVKLQDSKGNDTDTYALKDTNGNLYAADVNETTGAVSVKTITYTDSSGAASSPTAVKLGGDDGKTEVVDIDGKTYDSADLNGGNLQTGLTAGGEALTAVANGKTTDPLKALDDAIASVDKFRSSLGAVQNRLDSAVTNLNNTTTNLSEAQSRIQDADYATEVSNMSKAQIIQQAGNSVLAKANQVPQQVLSLLQG
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Molecular Weight
67.2 kDa
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Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
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Form
Freeze-dried powder
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Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
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Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
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Stability Test
The thermal stability is described by the loss rate. The loss rate was determined by accelerated thermal degradation test, that is, incubate the protein at 37℃ for 48h, and no obvious degradation and precipitation were observed. The loss rate isless than 8% within the expiration date under appropriate storage condition.
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Storage & Shelf Life
Samples are stable for up to twelve months from date of receipt at -20℃ to -80℃. Store it under sterile conditions at -20℃ to -80℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
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Shipping
In general, recombinant proteins are supplied as lyophilized powder and shipped at ambient temperature. For bulk packages, the proteins are provided as frozen liquid and shipped with blue ice, unless otherwise requested by the customer.
Quality inspection process
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Protein Description
The fliC gene encodes the flagellin protein, a key component of bacterial flagella, which is essential for motility and is involved in pathogenicity. Research on recombinant fliC protein has gained significant attention due to its potential applications in vaccine development and as a diagnostic tool. In many pathogenic bacteria, such as Salmonella and Escherichia coli, flagellin not only plays a crucial role in mobility but also acts as an effective immunogen, eliciting strong immune responses. By expressing fliC as a recombinant protein, researchers can study its structural and functional properties, as well as its interaction with the host immune system. Additionally, fliC-derived vaccines could harness the immunogenicity of flagellin to create effective preventive measures against bacterial infections. The production of recombinant fliC protein allows for the exploration of various post-translational modifications, enhancing our understanding of its immunological properties and enabling its use in various biotechnological applications. Investigating fliC also aids in understanding the mechanisms of bacterial virulence and the host's immune response, which is critical in the development of novel therapeutics and interventions. The ongoing research in this area underscores the importance of fliC in microbiology and immunology, signifying its potential to contribute to public health advancements.
