Analytical Data
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基因名
FGFR1
- Application
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别名
CD331; FLT2, KAL2; CEK; FLG; BFGFR, N-SAM,Basic Fibroblast Growth Factor Receptor 1; Fms-Related Tyrosine Kinase-2; Pfeiffer Syndrome
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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 97% as determined by reducing SDS-PAGE.
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蛋白编号
P11362
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表达区间
Tyr236~Leu362
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分子量
15kDa
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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
Fibroblast Growth Factor Receptor 1 (FGFR1) plays a critical role in various biological processes, including cell proliferation, differentiation, and survival, making it a significant focus in cancer research and developmental biology. Alterations in FGFR1 signaling are implicated in several pathologies, particularly in tumors where its overexpression or mutations contribute to oncogenesis. Given its importance, the production of recombinant FGFR1 proteins has garnered attention for elucidating the receptor's function and for developing therapeutic interventions targeting FGFR1-related diseases. These recombinant proteins allow researchers to study the molecular mechanisms of FGFR1 activation and its interactions with ligands and other cellular components. Furthermore, understanding the structure and function of FGFR1 through recombinant technology aids in identifying potential biomarkers and developing inhibitors for cancer treatment. As the landscape of targeted therapies continues to evolve, FGFR1 remains a promising candidate for innovative therapeutic strategies, emphasizing the relevance of recombinant FGFR1 protein studies in advancing medical research and treatment modalities.
