Analytical Data
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基因名
LRP2/Megalin
- Application
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别名
DBS; gp330; Glycoprotein 330; Megalin; Low Density Lipoprotein-Related Protein 2
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种属
Human
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表达系统
E. coli
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标签
N-His
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纯度
Greater than 95% as determined by SDS-PAGE.
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蛋白编号
P98164
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表达区间
Gly4035~Leu4184
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分子量
25kDa
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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
LRP2, also known as Megalin, is a member of the low-density lipoprotein receptor (LDLR) family and plays a crucial role in endocytic processes, particularly in the kidney and brain. It functions as a multi-ligand receptor, mediating the uptake of various macromolecules, including hormones, vitamins, and drugs. Given its pivotal role in nutrient transport and homeostasis, research on LRP2/Megalin has gained significant attention, particularly in the context of renal function and developmental disorders. Mutations or dysfunctions in the LRP2 gene have been linked to several pathologies, including Donnai-Barrow syndrome and certain types of renal impairments, underscoring its importance in both health and disease. The recombinant protein of LRP2/Megalin has emerged as a valuable tool for studying its biological functions, receptor-ligand interactions, and potential therapeutic applications. By utilizing advanced molecular techniques, researchers aim to elucidate the precise mechanisms of LRP2 in cellular uptake processes, investigate its structural properties, and explore its role in various physiological and pathological scenarios. This research not only enhances our understanding of LRP2/Megalin's involvement in normal physiological functions but also opens avenues for developing targeted therapies for related disorders, making it a critical focus in biomedical research.
