Analytical Data
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基因名
FN
- Application
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别名
FN；Fructosamine-3-kinase
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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
P02751
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表达区间
全长
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氨基酸序列
full
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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
FN (fibronectin) is a high-molecular-weight glycoprotein that plays a pivotal role in various biological processes, including cell adhesion, migration, growth, and differentiation. Its structure consists of multiple domains that enable interactions with integrins, collagen, and other extracellular matrix components, making it crucial for tissue repair and embryogenesis. Research on FK recombinant proteins has gained momentum due to their potential applications in cell biology, tissue engineering, and regenerative medicine. Advances in genetic engineering and recombinant DNA technology have facilitated the production of FN fragments with specific functions, allowing scientists to study their roles in cellular contexts more precisely. Additionally, FN and its derivatives are being explored for therapeutic purposes, such as targeted drug delivery and the enhancement of cell-based therapies. Understanding the structure-function relationship of FN recombinant proteins is essential for developing effective biomaterials and therapeutic strategies that can improve outcomes in regenerative medicine and other clinical applications. Overall, the exploration of FN recombinant proteins presents a promising frontier in both basic research and translational medicine, aiming to leverage the functional properties of FN for innovative therapeutic solutions.
