Analytical Data
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Gene name
GP1BA
- Application
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Alternative Names
GP1BA；Platelet glycoProtein Ib alpha chain
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Species
Human
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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
BC027955
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Expression Region
17-531aa
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AA Sequence
HPICEVSKVASHLEVNCDKRNLTALPPDLPKDTTILHLSENLLYTFSLATLMPYTRLTQLNLDRCELTKLQVDGTLPVLGTLDLSHNQLQSLPLLGQTLPALTVLDVSFNRLTSLPLGALRGLGELQELYLKGNELKTLPPGLLTPTPKLEKLSLANNNLTELPAGLLNGLENLDTLLLQENSLYTIPKGFFGSHLLPFAFLHGNPWLCNCEILYFRRWLQDNAENVYVWKQGVDVKAMTSNVASVQCDNSDKFPVYKYPGKGCPTLGDEGDTDLYDYYPEEDTEGDKVRATRTVVKFPTKAHTTPWGLFYSWSTASLDSQMPSSLHPTQESTKEQTTFPPRWTPNFTLHMESITFSKTPKSTTEPTPSPTTSEPVPEPAPNMTTLEPTPSPTTPEPTSEPAPSPTTPEPTPIPTIATSPTILVSATSLITPKSTFLTTTKPVSLLESTKKTIPELDQPPKLRGVLQGHLESSRNDPFLHPDFCCLLPLGFYVLGLFWLLFASVVLILLLSWVGH
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Molecular Weight
58.9 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
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Protein Description
The GP1BA protein, a critical component in the glycoprotein structure of certain pathogens, has garnered significant attention in the fields of virology and immunology. This protein plays a pivotal role in the entry mechanism of viruses into host cells, making it a key target for therapeutic interventions and vaccine development. Research into GP1BA has been spurred by the urgent need for effective countermeasures against viral diseases. Understanding the structure-function relationship of the GP1BA protein can facilitate the design of antiviral drugs and enhance vaccine efficacy by elucidating immune responses. Studies have revealed that variations in the GP1BA sequence can affect viral transmissibility and pathogenicity, leading to diverse outcomes in infected populations. The ability to produce recombinant forms of GP1BA has allowed researchers to investigate these properties in greater detail and develop potential diagnostic tools. Additionally, the exploration of GP1BA's interactions with host cell receptors holds promise for identifying novel therapeutic targets. As such, GP1BA represents a focal point in ongoing research aimed at combating viral infections, highlighting its significance in both basic and applied sciences. The insights gained from such studies may pave the way for innovative strategies to mitigate the impact of viral pathogens on public health.
