Analytical Data
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基因名
Lgals3
- Application
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别名
Lgals3；Galectin
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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
P17931
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表达区间
2-250aa
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氨基酸序列
ADNFSLHDAL SGSGNPNPQG WPGAWGNQPA GAGGYPGASY PGAYPGQAPP GAYPGQAPPG AYPGAPGAYP GAPAPGVYPG PPSGPGAYPS SGQPSATGAY PATGPYGAPA GPLIVPYNLP LPGGVVPRML ITILGTVKPN ANRIALDFQR GNDVAFHFNP RFNENNRRVI VCNTKLDNNW GREERQSVFP FESGKPFKIQ VLVEPDHFKV AVNDAHLLQY NHRVKKLNEI SKLGISGDID LTSASYTMI
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分子量
26.0 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
Galectin-3 (Lgals3) is a lectin protein that plays a crucial role in various biological processes, including cell adhesion, apoptosis, and immune response modulation. It is predominantly expressed in macrophages and is involved in the regulation of inflammation and fibrosis. Due to its significant role in disease pathogenesis, particularly in cancer metastasis and autoimmune disorders, Lgals3 has emerged as a potential therapeutic target. The ability to recombinantly produce Lgals3 has enabled researchers to investigate its structural and functional properties more thoroughly. Recombination techniques allow for the generation of large quantities of purified protein, which is essential for understanding its interactions with glycoproteins and other cellular components. This research not only enhances our understanding of Lgals3’s biological functions but also paves the way for the development of novel therapeutic strategies aimed at modulating its activity in disease contexts. As studies progress, they hold the promise of elucidating the pathways regulated by Lgals3, ultimately contributing to advances in targeted therapies for cancer and other diseases where Lgals3 is a key player.
