Analytical Data
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基因名
LRP1B
- Application
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别名
LRP1B；LRPDIT；Low-density lipoProtein receptor-related Protein 1B
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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
Q9NZR2
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表达区间
111-200aa
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氨基酸序列
VHCQELLSNCQQLNCQYKCTMVRNSTRCYCEDGFEITEDGRSCKDQDECA VYGTCSQTCRNTHGSYTCSCVEGYLMQPDNRSCKAKIEPT
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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
LRP1B (lipoprotein receptor-related protein 1B) is a member of the low-density lipoprotein receptor family and has garnered significant attention in recent years due to its potential roles in various biological processes and diseases. Initially identified as a receptor involved in lipid metabolism, LRP1B has been implicated in cellular signaling pathways, neuronal function, and cancer progression. Its expression is often altered in several types of malignancies, suggesting that LRP1B might serve as a biomarker for cancer diagnosis and prognosis. Researchers have also focused on the development of recombinant LRP1B proteins to better understand its structure-function relationships and interactions with ligands, which could unveil novel therapeutic targets. The ability to produce and purify large quantities of LRP1B recombinant proteins is crucial for characterizing its biochemical properties and elucidating mechanisms of action in cellular contexts. Additionally, studying LRP1B's role in modulating the tumor microenvironment could provide insights into its therapeutic potential and applicability in targeted cancer therapies. Overall, the investigation of LRP1B, particularly through recombinant protein studies, holds promise for advancing our understanding of its functions and developing innovative strategies for disease intervention.
