Analytical Data
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Gene name
ARPC1A
- Application
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Alternative Names
ARC1A_HUMAN; Arc40; ARPC1A; Epididymis luminal Protein 68; Epididymis secretory Protein Li 307
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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
Q92747
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Expression Region
1-370aa
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AA Sequence
MSLHQFLLEP ITCHAWNRDR TQIALSPNNH EVHIYKKNGS QWVKAHELKE HNGHITGIDW APKSDRIVTC GADRNAYVWS QKDGVWKPTL VILRINRAAT FVKWSPLENK FAVGSGARLI SVCYFESEND WWVSKHIKKP IRSTVLSLDW HPNNVLLAAG SCDFKCRVFS AYIKEVDEKP ASTPWGSKMP FGQLMSEFGG SGTGGWVHGV SFSASGSRLA WVSHDSTVSV ADASKSVQVS TLKTEFLPLL SVSFVSENSV VAAGHDCCPM LFNYDDRGCL TFVSKLDIPK QSIQRNMSAM ERFRNMDKRA TTEDRNTALE TLHQNSITQV SIYEVDKQDC RKFCTTGIDG AMTIWDFKTL ESSIQGLRIM
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Molecular Weight
66.44 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
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Protein Description
ARPC1A, a subunit of the Arp2/3 complex, plays a crucial role in actin dynamics and cytoskeletal organization in eukaryotic cells. This protein is essential for the nucleation of new actin filaments, which is vital for various cellular processes, including cell motility, division, and shape maintenance. Dysregulation of ARPC1A has been associated with several diseases, including cancer, where altered actin polymerization contributes to increased cell migration and invasion. Consequently, the study of recombinant ARPC1A protein has garnered significant interest in the field of cell biology and therapeutic development. Researchers are particularly focused on understanding the structural and functional properties of ARPC1A to elucidate its role in actin filament assembly and to explore its potential as a target for pharmacological intervention. The production of recombinant ARPC1A allows for detailed biochemical assays, structural characterization, and the investigation of interactions with other cellular proteins. This research not only enhances our understanding of the fundamental mechanisms of the cytoskeleton but also paves the way for developing strategies to manipulate actin dynamics in disease contexts, thus presenting a promising avenue for innovative therapeutic approaches.
