Analytical Data
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Gene name
ha17
- Application
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Alternative Names
ha17；H-2 class I histocompatibility antigen. Q7 alpha chain
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Species
Mouse
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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
P14429
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Expression Region
1-334aa
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AA Sequence
MALTMLLLLVAAALTLIETRAGQHSLQYFHTAVSRPGLGEPWFISVGYVDDTQFVRFDSDAENPRMEPRARWMEQEGPEYWERETQIAKGHEQSFRGSLRTAQSYYNQSKGGSHTLQWMYGCDMGSDGRLLRGYLQFAYEGRDYIALNEDLKTWTAVDMAAQITRRKWEQAGIAEKDQAYLEGTCMQSLRRYLQLGKETLLRTDPPKAHVTHHPRSYGAVTLRCWALGFYPADITLTWQLNGEELTQDMELVETRPAGDGTFQKWASVVVPLGKEQNYTCHVNHEGLPEPLTLRWGRWEPPPYTVSNMATIAVVVDLGAVAIIGAVVAFVMNRR
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Molecular Weight
37.9 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 the HA17 recombinant protein is significant within the field of virology and vaccine development, particularly concerning influenza. HA17, a specific variant of the hemagglutinin (HA) protein found on the surface of the influenza virus, plays a critical role in the virus's ability to infect host cells. Researching this protein is crucial for understanding the mechanisms of viral entry and immune response. Hemagglutinin is a primary target for neutralizing antibodies, making it essential for developing effective vaccines. The HA17 variant may exhibit distinct antigenic properties, influencing vaccine design, especially in the context of emerging and re-emerging influenza strains. Investigating HA17 can provide insights into the evolution of the virus and the potential escape from immune surveillance. Additionally, recombinant technology enables the production of HA17 for functional studies, enhancing our knowledge of antigenic variation and enabling the design of broadly protective vaccines. Overall, the exploration of HA17 contributes to global health by advancing strategies to mitigate influenza outbreaks and improve public health preparedness.
