Analytical Data
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基因名
PFKFB3
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简介
The PFKFB3 protein is a key player in cellular energy metabolism as it exerts dual functions by catalyzing the synthesis and degradation of fructose 2,6-bisphosphate (F-2,6-BP). F-2,6-BP is an important allosteric regulator of glycolysis, controlling glucose utilization for energy production. PFKFB3 Protein, Human (sf9, His-GST) is the recombinant human-derived PFKFB3 protein, expressed by Sf9 insect cells , with N-His, N-GST labeled tag.
- Application
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别名
IPFK2; PFK2; iPFK-2; PFK/FBPase 3
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种属
Human
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表达系统
Baculovirus
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标签
N-His;N-GST
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纯度
Greater than 90% as determined by SDS-PAGE.
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蛋白编号
Q16875-1
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表达区间
M1-H520
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蛋白长度
Full Length of Isoform-1
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分子量
75 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
PFKFB3, a member of the 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase family, plays a critical role in regulating glycolysis and gluconeogenesis by modulating the levels of fructose-2,6-bisphosphate, a potent allosteric activator of phosphofructokinase-1. The enzyme is intricately linked to cellular metabolism and energy homeostasis, making it a significant target for understanding metabolic disorders, including cancer and diabetes, where altered glycolytic pathways are often observed. Research has shown that PFKFB3 is upregulated in several cancers, contributing to the Warburg effect, where cancer cells preferentially utilize glycolysis for energy production, even in the presence of oxygen. This unique metabolic adaptation supports rapid cell proliferation and survival under hypoxic conditions. Consequently, the development of recombinant PFKFB3 proteins offers valuable insights into its structural and functional properties, enabling researchers to explore its potential as a therapeutic target. Studies utilizing recombinant PFKFB3 can elucidate its enzymatic mechanisms, interactome, and regulatory pathways, further illuminating its role in metabolic reprogramming within tumor microenvironments. Moreover, understanding the molecular basis of PFKFB3's function could lead to novel strategies for designing inhibitors, providing promising avenues for cancer treatment and management of metabolic diseases. Thus, the study of recombinant PFKFB3 not only enhances our understanding of fundamental metabolic processes but also opens doors for innovative therapeutic interventions.
