Analytical Data
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基因名
FN1
- Application
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别名
FN1；FN；Fibronectin
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种属
Human
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表达系统
E. coli
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标签
His tag N-Terminus
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纯度
Greater than 90% as determined by SDS-PAGE.
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蛋白编号
P02751
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表达区间
732-911aa
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氨基酸序列
TASSFVVSWVSASDTVSGFRVEYELSEEGDEPQYLDLPSTATSVNIPDLLPGRKYIVNVYQISEDGEQSLILSTSQTTAPDAPPDPTVDQVDDTSIVVRWSRPQAPITGYRIVYSPSVEGSSTELNLPETANSVTLSDLQPGVQYNITIYAVEENQESTPVVIQQETTGTPRSDTVPSPR
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分子量
23.6 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
FN1, or Fibronectin 1, is a glycoprotein that plays a crucial role in various biological processes, including cell adhesion, migration, and wound healing. It exists in two primary forms: soluble plasma fibronectin and insoluble extracellular matrix fibronectin. Research into FN1 has gained momentum due to its significant involvement in tumor progression and metastasis, where it facilitates cancer cell interactions with the extracellular matrix and immune system evasion. The reorganization of FN1 in the tumor microenvironment can influence cancer cell behavior and therapeutic responses. Additionally, FN1 is emerging as a potential biomarker for various diseases, with alterations in its expression patterns linked to conditions such as fibrosis, cardiovascular diseases, and certain cancers. Recent advances in recombinant protein technology have enabled the production of FN1 and its fragments, facilitating detailed studies of its structure-function relationships, interaction with other biomolecules, and role in cellular processes. Investigating FN1 as a therapeutic target or diagnostic tool continues to be a promising area of research, with potential implications for improving cancer treatment and understanding tissue repair mechanisms.
