Analytical Data
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Gene name
HNRNPA3
- Application
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Alternative Names
HNRNPA3;HNRPA3;Heterogeneous nuclear ribonucleoProtein A3
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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
P51991
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Expression Region
1-378aa
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AA Sequence
MEVKPPPGRPQPDSGRRRRRRGEEGHDPKEPEQLRKLFIGGLSFETTDDSLREHFEKWGTLTDCVVMRDPQTKRSRGFGFVTYSCVEEVDAAMCARPHKVDGRVVEPKRAVSREDSVKPGAHLTVKKIFVGGIKEDTEEYNLRDYFEKYGKIETIEVMEDRQSGKKRGFAFVTFDDHDTVDKIVVQKYHTINGHNCEVKKALSKQEMQSAGSQRGRGGGSGNFMGRGGNFGGGGGNFGRGGNFGGRGGYGGGGGGSRGSYGGGDGGYNGFGGDGGNYGGGPGYSSRGGYGGGGPGYGNQGGGYGGGGGYDGYNEGGNFGGGNYGGGGNYNDFGNYSGQQQSNYGPMKGGSFGGRSSGSPYGGGYGSGGGSGGYGSRRF
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Molecular Weight
46.6 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
HNRNPA3, or heterogeneous nuclear ribonucleoprotein A3, is a member of the hnRNP family that plays a critical role in pre-mRNA processing, splicing, and regulation of gene expression. Recent studies have highlighted its involvement in various biological processes, including cellular stress responses, RNA metabolism, and cell differentiation. Dysregulation of HNRNPA3 has been associated with several diseases, particularly cancer, where it may influence tumor progression and metastasis through alteration of splicing patterns and gene expression profiles. The study of recombinant HNRNPA3 proteins has emerged as a crucial avenue for understanding its functional mechanisms and interactions at the molecular level. By producing HNRNPA3 in a recombinant form, researchers can investigate its structural properties, binding affinities with RNA substrates, and potential post-translational modifications. This research is essential for elucidating the pathogenic roles of HNRNPA3, as well as its potential as a therapeutic target. Understanding how HNRNPA3 interacts with other cellular components can provide insights into the regulatory networks governing cancer biology and may lead to the design of novel therapeutic strategies aimed at modulating its function in disease contexts. Overall, the exploration of recombinant HNRNPA3 not only advances the fundamental knowledge of RNA biology but also holds promise for clinical applications in oncology and other fields.











