Analytical Data
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Gene name
hbhA
- Application
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Alternative Names
hbhA；Heparin-binding hemagglutinin
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Species
Mycobacterium tuberculosis
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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
P9WIP8
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Expression Region
2-199aa
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AA Sequence
AENSNIDDIKAPLLAALGAADLALATVNELITNLRERAEETRTDTRSRVEESRARLTKLQEDLPEQLTELREKFTAEELRKAAEGYLEAATSRYNELVERGEAALERLRSQQSFEEVSARAEGYVDQAVELTQEALGTVASQTRAVGERAAKLVGIELPKKAAPAKKAAPAKKAAPAKKAAAKKAPAKKAAAKKVTQK
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Molecular Weight
28.8 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
Related Products
Protein Description
The study of recombinant proteins, particularly hbhA, has gained significant attention due to its potential applications in various fields, including vaccine development, therapeutic proteins, and enzyme engineering. hbhA, encoded by the hbhA gene, is a component found in certain bacterial strains and is implicated in various biological processes, including pathogenicity and host interactions. Research has shown that hbhA plays a crucial role in the immune response, making it a valuable candidate for vaccine development against specific infectious diseases. By utilizing recombinant DNA technology, scientists can produce large quantities of hbhA protein in heterologous systems, allowing for detailed functional studies and potential therapeutic applications. Furthermore, understanding the structure-function relationship of hbhA can facilitate the design of more effective vaccines or therapeutics. The ability to manipulate and express hbhA in a controlled environment opens avenues for investigating its mechanisms of action and exploring its immunogenic properties. Recent advancements in proteomics and bioinformatics have also enhanced the understanding of hbhA's role and its interactions at the molecular level, promoting further research into its utility in medical science. Overall, the exploration of hbhA as a recombinant protein embodies a critical intersection of microbiology, immunology, and biotechnology, highlighting its promise in addressing pressing health challenges.
