Analytical Data
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Gene name
HBXIP
- Application
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Alternative Names
Hepatitis B virus X-interacting protein
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Species
Human
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Source
E. coli
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Tag
N- GST
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
O43504
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Expression Region
1-91aa
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Molecular Weight
36.6 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
Related Products
Protein Description
HBXIP (Hepatitis B virus X-interacting protein) is an essential cellular co-factor known for its interaction with the HBx protein of the Hepatitis B virus (HBV), playing a significant role in viral replication and pathogenesis. The therapeutic implications of HBXIP have garnered attention due to its involvement in the progression of various cancers, particularly liver cancer, where it contributes to tumorigenesis by modulating cell proliferation and survival pathways. The study of recombinant HBXIP protein has become paramount in understanding its structural and functional roles, particularly in elucidating the mechanisms by which it interacts with HBx and other cellular partners. Advanced techniques such as molecular cloning and protein expression have facilitated the production of HBXIP in a laboratory setting, enabling researchers to conduct detailed assays to investigate its biochemical properties and interactions. This research not only aims to decipher the molecular underpinnings of HBXIP in the context of HBV infection but also explores its potential as a therapeutic target. The development of inhibitors that disrupt HBXIP-HBx interactions could provide new avenues for combating HBV-related diseases, including chronic hepatitis and hepatocellular carcinoma. Thus, the understanding and analysis of recombinant HBXIP is critical in the ongoing efforts to develop effective strategies for prevention and treatment of HBV and its associated complications, highlighting the importance of further investigations in this area of study.
