Analytical Data
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基因名
FLNb
- Application
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别名
FLNb；FLN1L；FLN3；TABP；Filamin-B
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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
O75369
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表达区间
2503-2602aa
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氨基酸序列
SAIPKASSDASKVTSKGAGLSKAFVGQKSSFLVDCSKAGSNMLLIGVHGP TTPCEEVSMKHVGNQQYNVTYVVKERGDYVLAVKWGEEHIPGSPFHVTVP
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分子量
278 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
FLNb, or fibulin-5, is an extracellular matrix protein that plays a crucial role in various biological processes, including tissue development, angiogenesis, and cellular signaling. Research on FLNb has gained momentum due to its significant involvement in the structural integrity of elastic fibers and its implications in various pathologies, such as arterial diseases, cancer, and connective tissue disorders. Studies have shown that FLNb contributes to the assembly and stabilization of elastin fibers, which are vital for the elasticity and resilience of connective tissues. Moreover, alterations in FLNb expression and function have been linked to the progression of certain diseases. As a result, characterizing FLNb through recombinant protein techniques has become essential for understanding its function at the molecular level. This research aims to investigate the structural properties, interactions, and biological roles of FLNb in both physiological and pathological contexts, thereby providing insights into its potential as a therapeutic target. Developing recombinant FLNb allows for the exploration of its mechanism of action and potential applications in regenerative medicine and tissue engineering, highlighting the significance of this protein in health and disease.
