Analytical Data
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基因名
LRRC15
- Application
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别名
LIB; LRRC15
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种属
Human
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表达系统
HEK293
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标签
C-Avi;C-hFc
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纯度
Greater than 90% as determined by SDS-PAGE.
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蛋白编号
Q8TF66-1
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表达区间
Y22-G538
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分子量
95-110 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
LRRC15 (Leucine-Rich Repeat Containing 15) is a protein that has garnered attention in recent years due to its potential role in various biological processes and diseases. Initially discovered for its involvement in extracellular matrix interactions, LRRC15 has been implicated in pathophysiological conditions, particularly in cancers and fibrosis. Studies suggest that LRRC15 may play a critical role in tumor microenvironment regulation, influencing factors like cell adhesion, migration, and immune response. Its expression is often upregulated in tumors, making it a potential biomarker for cancer diagnosis and prognosis. Furthermore, the protein's function in fibrogenesis highlights its relevance in chronic inflammatory diseases. Researchers are increasingly interested in generating recombinant LRRC15 protein for the purpose of elucidating its structural and functional characteristics, which could pave the way for novel therapeutic strategies. Understanding the molecular mechanisms by which LRRC15 participates in disease pathways could offer insights into targeted treatments, particularly in conditions where current therapeutic options are limited. The development of LRRC15-based assays may also enhance our understanding of its biological significance in health and disease. Overall, the study of LRRC15 and its recombinant forms is crucial for unraveling its potential as a therapeutic target and for advancing our comprehension of its role in complex biological systems.
