Analytical Data
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基因名
IPP
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简介
IPP may organize the actin cytoskeleton, affecting the structural arrangement and dynamics of the cell's cytoskeletal network. It contributes to the organization of actin filaments, which is critical for cell morphology, movement and signaling. IPP Protein, Human (sf9) is the recombinant human-derived IPP protein, expressed by sf9 insect cells , with tag free.
- Application
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别名
IPP; Actin-binding protein IPP; Intracisternal A particle-promoted polypeptide; IPP; Kelch-like protein 27
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种属
Human
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表达系统
Baculovirus
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标签
Tag Free
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纯度
Greater than 90% as determined by SDS-PAGE.
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蛋白编号
Q9Y573
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表达区间
A2-L584
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蛋白长度
Partial
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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
The study of IPP (isoprenyl pyrophosphate) recombinant proteins has gained significant attention due to their key role in various biological processes, including cell signaling, protein modification, and lipid metabolism. Isoprenoids, a diverse class of organic compounds, are essential for the post-translational modification of proteins, particularly through farnesylation and geranylgeranylation mechanisms. These modifications are critical for protein function, influencing processes such as membrane localization, protein-protein interactions, and signal transduction pathways. Disruptions in isoprenoid metabolism have been linked to diseases, including cancer and cardiovascular diseases, making the understanding of IPP biology increasingly important. The advent of recombinant DNA technology allows for the generation of IPP proteins in a controlled manner, enabling researchers to investigate their structure-function relationships and molecular mechanisms in depth. Furthermore, recombinant expression systems facilitate the production of tagged or modified versions of IPP proteins, providing tools for biophysical analyses, enzymatic assays, and therapeutic applications. As such, the exploration of IPP recombinant proteins not only sheds light on fundamental cellular processes but also holds potential for novel biotechnological and pharmaceutical advancements.
