Analytical Data
-
基因名
FGF1
- Application
-
别名
FGF1；FGFA；Fibroblast growth factor 1
-
种属
Human
-
表达系统
E. coli
-
标签
N-6His
-
纯度
Greater than 90% as determined by SDS-PAGE.
-
蛋白编号
P05230
-
表达区间
1~155aa
-
分子量
55kDa
-
内毒素
< 1.0 EU per μg protein as determined by the LAL method.
-
性状
Freeze-dried powder
-
缓冲液
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
-
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
-
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.
-
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.
-
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
Related Products
Identification
Protein Description
Fibroblast growth factor 1 (FGF1) is a key member of the fibroblast growth factor family, known for its crucial role in various biological processes, including cell proliferation, differentiation, and angiogenesis. With its ability to promote wound healing and tissue regeneration, FGF1 has garnered significant attention in biomedical research and therapeutic development. Notably, studies have demonstrated its involvement in metabolic regulation, highlighting its potential in treating conditions such as obesity and diabetes. The recombinant protein form of FGF1 offers a promising avenue for exploring its therapeutic applications. Researchers have focused on optimizing its expression and purification to better understand its functional properties and mechanisms of action. Additionally, advancements in biotechnological methods have facilitated the production of recombinant FGF1 in sufficient quantities for preclinical and clinical research. Understanding the structure-function relationship of FGF1, as well as its interactions with specific receptors, is essential in designing effective interventions targeting various diseases. Thus, the ongoing investigation into FGF1 recombinant protein not only deepens our knowledge of growth factor biology but also paves the way for potential novel treatments in regenerative medicine and metabolic disorders.
