Analytical Data
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Gene name
PCA
- Application
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Alternative Names
PCA;LDLP;Leupaxin
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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
O60711
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Expression Region
1-386aa
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AA Sequence
MEELDALLEELERSTLQDSDEYSNPAPLPLDQHSRKETNLDETSEILSIQDNTSPLPAQLVYTTNIQELNVYSEAQEPKESPPPSKTSAAAQLDELMAHLTEMQAKVAVRADAGKKHLPDKQDHKASLDSMLGGLEQELQDLGIATVPKGHCASCQKPIAGKVIHALGQSWHPEHFVCTHCKEEIGSSPFFERSGLAYCPNDYHQLFSPRCAYCAAPILDKVLTAMNQTWHPEHFFCSHCGEVFGAEGFHEKDKKPYCRKDFLAMFSPKCGGCNRPVLENYLSAMDTVWHPECFVCGDCFTSFSTGSFFELDGRPFCELHYHHRRGTLCHGCGQPITGRCISAMGYKFHPEHFVCAFCLTQLSKGIFREQNDKTYCQPCFNKLFPL
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Molecular Weight
43.3 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
PCA (Protein Complementation Assay) recombinant proteins have emerged as a powerful tool in molecular biology, primarily for studying protein-protein interactions, cellular localization, and functional analysis of proteins in living cells. The technique is based on the principle that two non-fluorescent protein fragments can complement each other to form a functional protein when brought into close proximity, thus allowing researchers to visualize interactions in real-time. This method offers significant advantages over traditional co-immunoprecipitation or pull-down assays, as it enables the detection of interactions in their native cellular environment without the need for overexpression of the proteins involved. Furthermore, PCA can be adapted for use in high-throughput screening applications, facilitating the identification of novel protein interactions on a large scale. The continual refinement of PCA techniques, coupled with advances in recombinant protein technology, has revolutionized our understanding of cellular processes and the complex networks of protein interactions that underpin them. As research delves deeper into the roles of specific proteins in various biological pathways, PCA recombinant proteins are becoming invaluable in elucidating the mechanisms of diseases, developing targeted therapies, and advancing synthetic biology. This burgeoning field promises to uncover new insights into the dynamic nature of cellular functions and the intricate choreography of molecular interactions that sustain life.











