Analytical Data
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Gene name
PCLAF
- Application
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Alternative Names
PCLAF；Proliferating cell nuclear antigen
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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
Q15004
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Expression Region
1-111aa
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AA Sequence
MVRTKADSVPGTYRKVVAARAPRKVLGSSTSATNSTSVSSRKAENKYAGGNPVCVRPTPKWQKGIGEFFRLSPKDSEKENQIPEEAGSSGLGKAKRKACPLQPDHTNDEKE
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Molecular Weight
39.0 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
PCLAF (PCNA-Dependent Locus Associated Factor) is a crucial protein involved in the regulation of DNA replication and repair processes. Its interactions with the Proliferating Cell Nuclear Antigen (PCNA) highlight its role in maintaining genomic stability. Understanding PCLAF’s structure and function can provide insights into cellular responses to DNA damage and the mechanisms underlying cancer progression. Research on PCLAF has gained momentum due to its potential implications in therapeutic strategies for cancers characterized by defective DNA repair pathways. Recent studies have focused on the reconstitution of PCLAF in various model systems to elucidate its role in orchestrating replication and repair dynamics. With advancements in recombinant DNA technology, scientists can now produce PCLAF as a purified protein to investigate its biochemical activities and interaction networks. This work not only sheds light on PCLAF's specific contributions to the DNA damage response but also opens avenues for targeted drug design that can exploit its pathways in cancer cells, ultimately aiding in the development of novel therapeutic approaches to enhance the efficacy of existing treatments. The growing interest in PCLAF research underscores the importance of understanding DNA repair proteins in the context of cancer biology and treatment.
