Analytical Data
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基因名
SFXN1
- Application
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别名
TCC; Tricarboxylate carrier protein
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种属
Mouse
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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 90% as determined by SDS-PAGE.
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蛋白编号
Q99JR1
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表达区间
Ser2~Thr102
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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
SFXN1, or sideroflexin 1, is a mitochondrial protein that has garnered significant interest in the fields of biochemistry and molecular biology due to its role in iron metabolism and cellular energy production. This protein participates in the transport of metabolites across mitochondrial membranes, particularly in the context of iron-sulfur cluster biogenesis and cellular respiration. Mutations or dysregulation of SFXN1 have been implicated in various pathological conditions, including neurodegenerative diseases and metabolic disorders, making it a critical subject for research. Given its essential functions in mitochondrial health and iron homeostasis, recombinant SFXN1 protein is increasingly being produced and studied to elucidate its biochemical properties and interactions within the mitochondrial environment. Understanding the functional mechanisms of SFXN1 through recombinant protein studies may pave the way for novel therapeutic strategies to address diseases linked to mitochondrial dysfunction. As researchers continue to explore the complexities of iron metabolism and its implications for human health, SFXN1 remains a focal point that bridges fundamental biological processes with potential clinical applications.
