Analytical Data
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基因名
FLJ39155
- Application
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别名
Agrin-like protein; AGRINL; AGRNL; EGF-like; EGF-like; fibronectin type III and laminin G domains; EGF-like; fibronectin type-III and laminin G-like domain-containing protein; EGFLA_HUMAN; EGFLAM; fibronectin type-III and laminin G-like domain-containing protein; FLJ39155; Pikachurin
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种属
Human
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表达系统
E. coli
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标签
GST-tag at N-terminal
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纯度
Greater than 90% as determined by SDS-PAGE.
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蛋白编号
Q63HQ2
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表达区间
1-152aa
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氨基酸序列
MRFKTTAKDGLLLWRGDSPMRPNSDFISLGLRDGALVFSYNLGSGVASIMVNGSFNDGRWHRVKAVRDGQSGKITVDDYGARTGKSPGMMRQLNINGALYVGGMKEIALHTNRQYMRGLVGCISHFTLSTDYHISLVEDAVDGKNINTCGAK
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分子量
43 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
The FLJ39155 recombinant protein has garnered attention in the field of molecular biology and biomedical research due to its potential role in various cellular processes and diseases. Initially identified through genomic sequencing projects, FLJ39155 is hypothesized to be involved in significant biological functions, given its evolutionary conservation across multiple species. Studies have indicated that this protein may be linked to pathways such as cell signaling, apoptosis, and immune response, making it a candidate for further investigation in the context of cancer biology and autoimmune disorders. The expression and purification of FLJ39155 as a recombinant protein allow researchers to study its biochemical properties, interactions with other cellular molecules, and effects on cellular functions. Additionally, understanding the structure-function relationship of FLJ39155 could provide insight into its mechanisms of action, opening avenues for therapeutic applications. Overall, the study of FLJ39155 represents a promising frontier in the quest to elucidate the complexities of protein functions in health and disease.
