Analytical Data
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Gene name
HELQ
- Application
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Alternative Names
HELQ；HEL308；Helicase POLQ-like
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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
Q8TDG4
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Expression Region
350-726aa
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AA Sequence
QERKNLIYSLPTSGGKTLVAEILMLQELLCCRKDVLMILPYVAIVQEKISGLSSFGIELGFFVEEYAGSKGRFPPTKRREKKSLYIATIEKGHSLVNSLIETGRIDSLGLVVVDELHMIGEGSRGATLEMTLAKILYTSKTTQIIGMSATLNNVEDLQKFLQAEYYTSQFRPVELKEYLKINDTIYEVDSKAENGMTFSRLLNYKYSDTLKKMDPDHLVALVTEVIPNYSCLVFCPSKKNCENVAEMICKFLSKEYLKHKEKEKCEVIKNLKNIGNGNLCPVLKRTIPFGVAYHHSGLTSDERKLLEEAYSTGVLCLFTCTSTLAAGVNLPARRVILRAPYVAKEFLKRNQYKQMIGRAGRAGIDTIGESILILQEK
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Molecular Weight
49.8 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
HELQ (HElicase-Related Ubiquitously expressed Protein) is a crucial member of the RecQ helicase family, playing a significant role in maintaining genomic stability and facilitating DNA repair processes. Mutations in HELQ have been associated with various human diseases, including cancer, emphasizing its importance in cellular responses to DNA damage. Research into HELQ has gained traction due to its potential as a therapeutic target for enhancing the efficacy of cancer treatments. The protein is believed to be involved in homologous recombination repair, a vital mechanism that cells use to repair double-strand breaks in DNA. Studies have indicated that HELQ interacts with multiple proteins involved in DNA repair pathways, suggesting it may have a regulatory role in these processes. Understanding its structure and function at the molecular level is essential for elucidating its contributions to DNA repair and the mechanisms underlying diseases associated with its dysfunction. Current research focuses on elucidating the biochemical properties of HELQ, characterizing its interactions, and exploring its potential in drug development strategies aimed at improving cancer therapy outcomes. By studying HELQ and its associated pathways, scientists hope to uncover novel insights into the processes that maintain genomic integrity and explore new avenues for treating cancers that exhibit defects in DNA repair mechanisms.
