Analytical Data
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基因名
ARPC2
- Application
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别名
ARPC2；ARC34；Actin-related Protein 2/3 complex subunit 2
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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
O15144
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表达区间
1-300aa
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氨基酸序列
MGSSHHHHHH SSGLVPRGSH MGSMILLEVN NRIIEETLAL KFENAAAGNK PEAVEVTFAD FDGVLYHISN PNGDKTKVMV SISLKFYKEL QAHGADELLK RVYGSFLVNP ESGYNVSLLY DLENLPASKD SIVHQAGMLK RNCFASVFEK YFQFQEEGKE GENRAVIHYR DDETMYVESK KDRVTVVFST VFKDDDDVVI GKVFMQEFKE GRRASHTAPQ VLFSHREPPL ELKDTDAAVG DNIGYITFVL FPRHTNASAR DNTINLIHTF RDYLHYHIKC SKAYIHTRMR AKTSDFLKVL NRARPDAEKK EMKTITGKTF SSR
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分子量
37 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
ARPC2, a vital component of the Arp2/3 complex, plays a significant role in actin polymerization and cytoskeletal dynamics, which are crucial for various cellular processes including cell motility, shape maintenance, and cytokinesis. Research on ARPC2 recombinant proteins has garnered interest due to its implications in understanding cellular functions and disease mechanisms. Recent studies have suggested that mutations or dysregulation of ARPC2 can contribute to various diseases, including cancer, where altered cell migration and proliferation are observed. The generation of ARPC2 recombinant proteins allows for in-depth structural and functional analyses, facilitating the exploration of its interactions with other cellular proteins and its regulation within the context of the Arp2/3 complex. Techniques such as X-ray crystallography and cryo-electron microscopy have been employed to elucidate the molecular mechanisms by which ARPC2 influences actin dynamics. Understanding the biochemical properties of ARPC2 can also pave the way for potential therapeutic strategies targeting actin-associated disorders. Overall, the study of ARPC2 recombinant proteins not only enhances our knowledge of cellular mechanics but also holds promise for future biomedical applications.
