Analytical Data
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Gene name
ARPC2
- Application
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Alternative Names
ARPC2；ARC34；Actin-related Protein 2/3 complex subunit 2
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Species
Human
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Source
E. coli
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Tag
His tag N-Terminus
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
O15144
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Expression Region
1-300aa
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AA Sequence
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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Molecular Weight
37 kDa
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Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
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Form
Freeze-dried powder
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Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
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Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
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Stability Test
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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Storage & Shelf Life
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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Shipping
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
Related Products
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.
