Analytical Data
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Gene name
PRUNE2
- Application
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Alternative Names
PRUNE2; BMCC1; BNIPXL; C9orf65; KIAA0367; Protein prune homolog 2; BNIP2 motif-containing molecule at the C-terminal region 1
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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
Q8WUY3
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Expression Region
1-191 aa
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AA Sequence
MDIPFEEGVLSPSAADMRPEPPNSLDLNDTHPRRIKLTAPNINLSLDQSEGSILSDDNLDSPDEIDINVDELDTPDEADSFEYTGHEDPTANKDSGQESESIPEYTAEEEREDNRLWRTVVIGEQEQRIDMKVIEPYRRVISHGGYYGDGLNAIIVFAACFLPDSSRADYHYVMENLFLYVISTFTLQPQS
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Molecular Weight
48 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
PRUNE2 is a member of the PRUNE family of proteins, which are implicated in various cellular processes, including cell proliferation, migration, and apoptosis. Research has highlighted its potential role in cancer biology, particularly in the context of tumor progression and metastasis. The expression of PRUNE2 is often dysregulated in several malignancies, suggesting that it may serve as a novel biomarker for cancer diagnosis and prognosis. Studies have shown that PRUNE2 interacts with key signaling pathways, influencing cell growth and survival, thereby affecting tumor behavior. Understanding the structure and function of PRUNE2 at the molecular level could provide insights into its mechanism of action and potential as a therapeutic target. Recent advances in recombinant protein production techniques have allowed for the detailed characterization of PRUNE2, facilitating the analysis of its biochemical properties and interaction with other cellular components. Investigating PRUNE2 not only enhances the understanding of its role in oncogenesis but also opens avenues for the development of targeted therapies that could improve treatment outcomes for cancer patients. Thus, ongoing research into PRUNE2 is critical for unveiling its potential implications in cancer biology and developing innovative therapeutic strategies.
