Recombinant Mouse Aen Protein, Myc/DDK-tagged
Cat.No. : | Aen-1546M |
Product Overview : | Purified recombinant protein of mouse full-length apoptosis enhancing nuclease (Aen), with C-terminal MYC/DDK tag, expressed in HEK293T cells. |
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Description : | Ubiquitous expression in ovary adult (RPKM 12.3), genital fat pad adult (RPKM 10.6) and 28 other tissues. |
Source : | HEK293T |
Species : | Mouse |
Tag : | Myc/DDK |
Molecular Mass : | 37.3 kDa |
Purity : | > 80% as determined by SDS-PAGE and Coomassie blue staining |
Stability : | Stable for 12 months from the date of receipt of the product under proper storage and handling conditions. Avoid repeated freeze-thaw cycles. |
Storage : | Store at -80 centigrade after receiving vials. |
Concentration : | >50 μg/mL as determined by microplate BCA method |
Storage Buffer : | 25 mM Tris.HCl, pH 7.3, 100 mM glycine, 10% glycerol. |
Gene Name : | Aen apoptosis enhancing nuclease [ Mus musculus (house mouse) ] |
Official Symbol : | Aen |
Synonyms : | AEN; apoptosis enhancing nuclease; apoptosis-enhancing nuclease; interferon-stimulated 20 kDa exonuclease-like 1; interferon stimulated exonuclease gene 20-like 1; Isg20l1; 2700083B06Rik |
Gene ID : | 68048 |
mRNA Refseq : | NM_026531 |
Protein Refseq : | NP_080807 |
UniProt ID : | Q9CZI9 |
Products Types
◆ Recombinant Protein | ||
AEN-372M | Recombinant Mouse AEN Protein, His (Fc)-Avi-tagged | +Inquiry |
AEN-207R | Recombinant Rat AEN Protein, His (Fc)-Avi-tagged | +Inquiry |
AEN-2438H | Recombinant Human AEN Protein, His (Fc)-Avi-tagged | +Inquiry |
AEN-553H | Recombinant Human AEN Protein, MYC/DDK-tagged | +Inquiry |
AEN-1066H | Recombinant Human AEN Protein (117-325 aa), His-SUMO-tagged | +Inquiry |
◆ Lysates | ||
AEN-8992HCL | Recombinant Human AEN 293 Cell Lysate | +Inquiry |
Related Gene
For Research Use Only. Not intended for any clinical use. No products from Creative BioMart may be resold, modified for resale or used to manufacture commercial products without prior written approval from Creative BioMart.
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Q&As (10)
Ask a questionThe subcellular localization of AEN protein is determined by specific mechanisms and targeting sequences, which facilitate its transport and localization to specific cellular compartments.
Dysregulation or dysfunction of AEN protein can disrupt cellular functions, such as impaired DNA repair or altered apoptotic responses, and contribute to the development of diseases like cancer or neurodegenerative disorders.
Genetic variations or mutations in the AEN gene may impact the expression or function of AEN protein, potentially influencing cellular processes or disease susceptibility.
AEN protein may interact with other proteins, such as DNA repair factors or apoptotic regulators, forming protein complexes that influence cellular processes such as DNA repair or cell death.
AEN protein is implicated in specific cellular processes such as DNA repair and apoptosis, where it may play a role in maintaining genomic stability or regulating cell survival.
Experimental techniques such as molecular biology, cell biology, and biochemical assays can be employed to investigate the functional significance of AEN protein, including DNA repair assays or apoptosis assays.
Post-translational modifications or regulatory factors that modulate the activity or stability of AEN protein are not currently identified. Further research is necessary to explore these regulatory mechanisms.
The specific structural features or domains critical for the function or interaction of AEN protein are currently unknown, and further studies are needed to determine their role in cellular processes and molecular interactions.
The enzymatic activity or molecular function of AEN protein is currently unknown, and further experimental assays are needed to investigate its activity and molecular roles.
The tissue-specific expression patterns of AEN protein vary across different organs and cell types. Factors regulating its expression levels include transcriptional control and signaling pathways.
Customer Reviews (3)
Write a reviewExploring protein-protein interactions involved in neurotransmitter signaling.
Characterizing protein-protein interactions involved in chromosomal organization.
Determining protein-protein interaction interfaces using F枚rster resonance energy transfer.
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