Analytical Data
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基因名
FABP12
- Application
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别名
Fatty acid-binding protein 12; FABP12; Homo sapiens; Human
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种属
Human
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表达系统
E. coli
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标签
Tag Free
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纯度
Greater than 90% as determined by SDS-PAGE.
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蛋白编号
A6NFH5
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表达区间
M1-S140
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蛋白长度
Full Length
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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
Fatty Acid Binding Protein 12 (FABP12), also known as adipocyte FABP or aP2, is a member of the FABP family, which plays a crucial role in intracellular lipid transport and metabolism. Recent studies have highlighted its significance in various metabolic disorders, including obesity, insulin resistance, and type 2 diabetes. FABP12 is primarily expressed in adipose tissue and is involved in the regulation of fatty acid uptake, storage, and oxidation, making it a potential therapeutic target for metabolic diseases. Research indicates that FABP12 influences the inflammatory responses related to lipid metabolism and is implicated in the function of macrophages and other immune cells. The recombinant expression of FABP12 provides a valuable tool to study its structural properties, binding affinities, and biological functions at a molecular level. Understanding the mechanisms by which FABP12 modulates lipid metabolism may offer insights into novel strategies for treating metabolic syndrome and associated conditions. As obesity continues to rise globally, elucidating the role of FABP12 through recombinant protein studies could pave the way for innovative therapeutic approaches aimed at improving metabolic health.
