Analytical Data
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Gene name
HNRNPD
- Application
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Alternative Names
AU-rich element RNA-binding protein 1
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Species
Human
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Source
E. coli
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Tag
N- GST
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q14103
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Expression Region
18-306aa
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Molecular Weight
58.3 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
Related Products
Protein Description
HNRNPD, or heterogeneous nuclear ribonucleoprotein D, is a key protein involved in various cellular processes, including pre-mRNA splicing, gene expression regulation, and RNA metabolism. It is a member of the hnRNP family, which plays crucial roles in the processing and transport of RNA. Research into HNRNPD has gained momentum due to its implications in several diseases, including cancer, neurodegenerative disorders, and viral infections. Its ability to interact with RNA and other proteins makes it a significant player in the post-transcriptional regulation of gene expression. The study of recombinant HNRNPD has become vital for understanding its structure-function relationships and for elucidating its role in cellular processes. Recombinant protein studies allow for detailed examination of HNRNPD's interactions and modifications, as well as its potential as a therapeutic target. Advances in techniques such as X-ray crystallography and NMR spectroscopy have facilitated the exploration of HNRNPD's functional mechanisms, providing insights into its role in RNA binding and protein-protein interactions. As research continues to uncover the complexities of HNRNPD's involvement in disease pathways, recombinant protein studies remain pivotal in characterizing this protein's properties and functionalities in the broader context of cellular biology.
