Analytical Data
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Gene name
hasA
- Application
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Alternative Names
hasA;Hyaluronan synthase
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Species
Serratia
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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
Q54450
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Expression Region
1-188aa
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AA Sequence
MAFSVNYDSSFGGYSIHDYLGQWASTFGDVNHTNGNVTDANSGGFYGGSLSGSQYAISSTANQVTAFVAGGNLTYTLFNEPAHTLYGQLDSLSFGDGLSGGDTSPYSIQVPDVSFGGLNLSSLQAQGHDGVVHQVVYGLMSGDTGALETALNGILDDYGLSVNSTFDQVAAATAVGVQHADSPELLAA
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Molecular Weight
35.3 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 hasA recombinant proteins has gained significant attention in the field of microbiology and biotechnology due to their role in the synthesis of siderophores, which are critical for iron acquisition in various bacterial species, particularly in pathogenic strains. HasA, a hemophore produced by certain bacteria like *Pseudomonas aeruginosa*, facilitates the uptake of heme from host tissues, thus supporting bacterial survival and virulence. Its unique ability to bind heme makes hasA a valuable target for understanding bacterial iron metabolism and developing novel therapeutic strategies to combat infections. Researchers have focused on the recombinant expression of hasA to explore its structure-function relationships, investigate its interaction with host proteins, and evaluate its potential as a vaccine candidate or drug target. The advances in recombinant DNA technology and protein engineering have enabled the production of high quantities of hasA, aiding in comprehensive studies ranging from biochemical characterization to structural analysis. Moreover, understanding the ecological and evolutionary aspects of hasA can provide insights into bacterial adaptation and the development of antibiotic resistance. Overall, the research on hasA recombinant proteins not only enhances our knowledge of bacterial pathogenesis but also paves the way for innovative approaches in medical and environmental applications.











