Analytical Data
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Gene name
HEATR6
- Application
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Alternative Names
HEATR6；ABC1；HEAT repeat-containing Protein 6
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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
Q6AI08
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Expression Region
1052-1175aa
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AA Sequence
KSEDTIDFLEFKYCVSLRTQICQALIHLLSLASASDLPCMKETLELSGNMVQSYILQFLKSGAEGDDTGAPHSPQERDQMVRMALKHMGSIQAPTGDTARRAIMGFLEEILAVCFDSSGSQGAL
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Molecular Weight
18.5 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
HEATR6, a member of the HEAT repeat-containing protein family, has garnered significant interest in recent years due to its potential roles in cellular processes, such as chromatin remodeling and RNA metabolism. The HEAT repeats, structural motifs characterized by the presence of alternating alpha-helices and loops, contribute to the stability and functionality of proteins involved in critical cellular pathways. Research has indicated that HEATR6 may be involved in the regulation of gene expression and the maintenance of genome integrity. Its association with various human diseases, including cancer, highlights the necessity of understanding its biochemical properties and interactions. Effective study of HEATR6 requires the production of recombinant protein, allowing researchers to explore its structure-function relationships in vitro. The purification and characterization of HEATR6 as a recombinant protein can facilitate the investigation of its binding partners and functional mechanisms. Additionally, insights into its role in cellular response to stress and its involvement in signal transduction pathways may provide valuable information for therapeutic strategies targeting diseases related to HEATR6 dysregulation. Therefore, the ongoing research into HEATR6 recombinant protein is critical for elucidating the multifaceted roles of this protein in human health and disease.
