Analytical Data
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Gene name
HELLS
- Application
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Alternative Names
FLJ10339; Helicase lymphoid specific; Hells; HELLS_HUMAN; LSH; Lymphoid specific helicase; Lymphoid-specific helicase; Nbla10143; PASG; Proliferation associated SNF2 like protein; Proliferation-associated SNF2-like protein
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Species
Human
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Source
E. coli
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Tag
GST-tag at N-terminal
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q9NRZ9
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Expression Region
1-348aa
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AA Sequence
MFGSSEKETIELSPTGRPKRRTRKSINYSKIDDFPNELEKLISQIQPEVDRERAVVEVNIPVESEVNLKLQNIMMLLRKCCNHPYLIEYPIDPVTQEFKIDEELVTNSGKFLILDRMLPELKKRGHKVLLFSQMTSMLDILMDYCHLRDFNFSRLDGSMSYSEREKNMHSFNTDPEVFIFLVSTRAGGLGINLTAADTVIIYDSDWNPQSDLQAQDRCHRIGQTKPVVVYRLVTANTIDQKIVERAAAKRKLEKLIIHKNHFKGGQSGLNLSKNFLDPKELMELLKSRDYEREIKGSREKVISDKDLELLLDRSDLIDQMNASGPIKEKMGIFKILENSEDSSPECLF
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Molecular Weight
63.8 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
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Protein Description
The Hells protein, also known as PIF1 helicase, is an essential member of the family of helicases that play critical roles in various cellular processes, including DNA replication, repair, and transcription. Its function is particularly significant in the context of maintaining genomic stability, as it unwinds DNA strands, facilitating access for various enzymatic activities. The study of Hells has gained momentum in recent years due to its involvement in key biological processes and its potential links to various diseases, including cancer. Research indicates that dysregulation of Hells can affect cellular proliferation and stress responses, highlighting its importance in tumorigenesis. Moreover, understanding the molecular mechanisms underlying Hells activity may provide insights into novel therapeutic strategies. Its characterization, including the identification of binding partners and regulatory mechanisms, has become a focal point for researchers aiming to elucidate the intricate network of cellular events influenced by this protein. Consequently, Hells serves as a compelling target for studies aimed at unraveling fundamental biological processes and addressing the implications of its dysfunction in human health.
