Analytical Data
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Gene name
H
- Application
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Alternative Names
H; Hemagglutinin glycoprotein
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Species
Measles virus
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Source
E. coli
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Tag
N- His
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P08362
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Expression Region
303-617aa
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Molecular Weight
39.3 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 research on H recombinant proteins has gained significant attention in the fields of biotechnology and medicine due to their potential applications in various therapeutic and diagnostic areas. H proteins, derived from viruses or other pathogenic organisms, play essential roles in processes such as viral entry, immune response, and cell signaling. These recombinant proteins can be used to generate specific antibodies, facilitating the development of vaccines and treatments against infectious diseases and cancers. Advances in genetic engineering techniques, such as recombinant DNA technology, have enabled the production of high-purity H proteins in various host systems, including bacterial, yeast, and mammalian cells. This progress has not only improved the efficiency and scalability of protein production but has also enhanced our understanding of the structural and functional characteristics of these proteins. Additionally, the study of H recombinant proteins allows for the exploration of their interactions with host immune systems, paving the way for innovative approaches to vaccine design that elicit strong and lasting immune responses. Overall, the ongoing research in this area holds promise for the development of novel therapeutic strategies and the enhancement of existing medical interventions, making H recombinant proteins a significant focus of contemporary scientific inquiry.
