Analytical Data
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Gene name
HBXIP
- Application
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Alternative Names
LAMTOR5;HBXIP;XIP;Ragulator complex Protein LAMTOR5
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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
O43504
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Expression Region
1-173aa
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AA Sequence
MGSSHHHHHH SSGLVPRGSH MGSHMEPGAG HLDGHRAGSP SLRQALCDGS AVMFSSKERG RCTVINFVPL EAPLRSTPRS RQVTEACGGE GRAVPLGSEP EWSVGGMEAT LEQHLEDTMK NPSIVGVLCT DSQGLNLGCR GTLSDEHAGV ISVLAQQAAK LTSDPTDIPV VCLESDNGNI MIQKHDGITV AVHKMAS
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Molecular Weight
21 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 a crucial molecular player associated with numerous biological processes, particularly in the context of hepatitis B virus (HBV) infection and cancer development. Research interest in HBXIP has surged due to its role as a coactivator of transcription, influencing gene expression and modulating pathways related to cell proliferation and apoptosis. This protein has been implicated in the progression of various cancers, making it a potential target for therapeutic intervention. Understanding the structure and function of HBXIP is pivotal for unraveling its mechanisms in HBV-related oncogenesis. The generation of recombinant HBXIP proteins has become a significant aspect of this research, enabling scientists to study its interactions at a molecular level, characterize its functional domains, and explore its potential as a biomarker or therapeutic target. By utilizing techniques such as gene cloning and protein expression systems, researchers aim to produce HBXIP in sufficient quantities to facilitate detailed biochemical analyses and to screen for inhibitors that could disrupt its oncogenic functions. Such studies not only enhance our understanding of HBV pathogenesis but also contribute to the broader field of cancer research, highlighting the importance of HBXIP in both virology and oncology.
