Analytical Data
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基因名
HBXIP
- Application
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别名
LAMTOR5;HBXIP;XIP;Ragulator complex Protein LAMTOR5
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种属
Human
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表达系统
E. coli
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标签
His tag N-Terminus
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纯度
Greater than 90% as determined by SDS-PAGE.
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蛋白编号
O43504
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表达区间
1-173aa
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氨基酸序列
MGSSHHHHHH SSGLVPRGSH MGSHMEPGAG HLDGHRAGSP SLRQALCDGS AVMFSSKERG RCTVINFVPL EAPLRSTPRS RQVTEACGGE GRAVPLGSEP EWSVGGMEAT LEQHLEDTMK NPSIVGVLCT DSQGLNLGCR GTLSDEHAGV ISVLAQQAAK LTSDPTDIPV VCLESDNGNI MIQKHDGITV AVHKMAS
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分子量
21 kDa
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内毒素
< 1.0 EU per μg protein as determined by the LAL method.
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性状
Freeze-dried powder
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缓冲液
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
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复溶方法
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- 个性化定制
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稳定性测试
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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保存条件 & 期限
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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运输条件
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
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.
