Analytical Data
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基因名
Fibrillin-1/Asprosin
- Application
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别名
FBN; MASS; MFS1; OCTD; SGS
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种属
Human
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表达系统
E. coli
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标签
N-His
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纯度
Greater than 90% as determined by SDS-PAGE.
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蛋白编号
P35555
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表达区间
Gly2727~Pro2835
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分子量
16kDa
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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
Fibrillin-1 is a key extracellular matrix protein crucial for maintaining tissue integrity and elasticity, while Asprosin is a recently identified hormone playing a significant role in glucose metabolism and energy homeostasis. Research into Fibrillin-1 has primarily focused on its association with Marfan syndrome, a connective tissue disorder characterized by cardiovascular, skeletal, and ocular abnormalities due to mutations that affect its structure and function. In contrast, Asprosin, secreted by adipose tissue, has been linked to insulin resistance and metabolic disorders, highlighting the importance of its regulatory role in energy balance. The exploration of recombinant Fibrillin-1/Asprosin fusion proteins aims to harness the beneficial properties of both entities, potentially providing therapeutic avenues for conditions related to connective tissue disorders and metabolic syndromes. Understanding the functional interplay between these proteins will not only advance basic science but also pave the way for innovative treatment strategies targeting diseases characterized by metabolic dysregulation and impaired connective tissue function. This research is essential for developing therapeutics that can improve patient outcomes in disorders such as diabetes, obesity, and heritable connective tissue diseases, emphasizing the need for a multidisciplinary approach in advancing the field of protein engineering and therapeutic protein development.
