Analytical Data
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基因名
ARF4L
- Application
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别名
ADP ribosylation factor 4 like; ADP ribosylation factor like 4D; ADP ribosylation factor like 6
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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
P49703
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表达区间
2-201aa
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氨基酸序列
GNHLTEMAP TASSFLPHFQ ALHVVVIGLD SAGKTSLLYR LKFKEFVQSV PTKGFNTEKI RVPLGGSRGI TFQVWDVGGQ EKLRPLWRSY TRRTDGLVFV VDAAEAERLE EAKVELHRIS RASDNQGVPV LVLANKQDQP GALSAAEVEK RLAVRELAAA TLTHVQGCSA VDGLGLQQGL ERLYEMILKR KKAARGGKKR R
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分子量
22.1 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
ARF4L (ADP-Ribosylation Factor 4-Like) is a member of the ARF family of GTP-binding proteins, which play crucial roles in vesicular transport and intracellular trafficking. Research on ARF4L has gained prominence due to its implication in various cellular processes, including exocytosis, endocytosis, and lipid metabolism. Studies suggest that ARF4L may regulate the Golgi apparatus and influence the organization of the cytoskeleton. Abnormalities in ARF4L function have been linked to several disease states, such as cancer and neurodegenerative disorders, highlighting its potential as a therapeutic target. Recent advances in protein engineering and recombinant DNA technology have facilitated the production of ARF4L recombinant proteins, allowing for detailed structural and functional analyses. Understanding the molecular mechanisms underlying ARF4L activity could provide insights into its role in cell biology and disease mechanisms, paving the way for the development of novel therapeutic strategies. The exploration of ARF4L’s interactions with other cellular components, including its effectors and regulators, remains a significant focus, as it may reveal new pathways involved in cellular signaling and homeostasis. Overall, the study of ARF4L as a recombinant protein offers an exciting avenue for elucidating its biological roles and possible implications in human health.
