Analytical Data
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Gene name
HA-33
- Application
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Alternative Names
HA 33 kDa subunit HA1
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Species
Clostridium botulinum
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Source
E. coli
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Tag
N- His-SUMO & C- Myc
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P0DPR0
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Expression Region
2-286aa
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Molecular Weight
53.6 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 HA-33 recombinant protein, derived from the human pathogen, has garnered significant attention in recent years due to its potential applications in immunology and vaccine development. As a critical component of the host's immune response, HA-33 plays a crucial role in the recognition and signaling pathways of immune cells. Researchers have been investigating the protein's structure-function relationship to better understand its role in pathogen recognition and immune activation. This includes exploring its interactions with specific receptors on immune cells, which can inform the design of targeted therapies and vaccines. By utilizing recombinant DNA technology, scientists are able to produce HA-33 in various expression systems, allowing for detailed studies of its biochemical properties and immunological functions. Recent advancements in biotechnology have further propelled research into HA-33, enabling the development of more effective vaccines and therapeutic strategies against infectious diseases. Understanding the mechanisms by which HA-33 influences immune responses could ultimately lead to innovative approaches for managing and preventing infections, making it a focal point in current biomedical research.











