Recombinant Human AEN Protein (117-325 aa), His-SUMO-tagged
Cat.No. : | AEN-1066H |
Product Overview : | Recombinant Human AEN Protein (117-325 aa) is produced by E. coli expression system. This protein is fused with a 6xHis-SUMO tag at the N-terminal. Research Area: Cell Biology. Protein Description: Partial. |
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Description : | Exonuclease with activity against single- and double-stranded DNA and RNA. Mediates p53-induced apoptosis. When induced by p53 following DNA damage, digests double-stranded DNA to form single-stranded DNA and amplifies DNA damage signals, leading to enhancent of apoptosis. |
Source : | E. coli |
Species : | Human |
Tag : | His-SUMO |
Form : | Tris-based buffer, 50% glycerol |
Molecular Mass : | 40.1 kDa |
Protein length : | 117-325 aa |
AA Sequence : | MVGTGPRGRVSELARCSIVSYHGNV LYDKYIRPEMPIADYRTRWSGITRQ HMRKAVPFQVAQKEILKLLKGKVVV GHALHNDFQALKYVHPRSQTRDTTY VPNFLSEPGLHTRARVSLKDLALQL LHKKIQVGQHGHSSVEDATTAMELY RLVEVQWEQQEARSLWTCPEDREPD SSTDMEQYMEDQYWPDDLAHGSRGG AREAQDRRN |
Purity : | > 90% as determined by SDS-PAGE. |
Notes : | Repeated freezing and thawing is not recommended. Store working aliquots at 4 centigrade for up to one week. |
Storage : | The shelf life is related to many factors, storage state, buffer ingredients, storage temperature and the stability of the protein itself. Generally, the shelf life of liquid form is 6 months at -20 centigrade/-80 centigrade. The shelf life of lyophilized form is 12 months at -20 centigrade/-80 centigrade. |
Concentration : | A hardcopy of COA with concentration instruction is sent along with the products. |
SDS-PAGE: |
Gene Name : | AEN apoptosis enhancing nuclease [ Homo sapiens ] |
Official Symbol : | AEN |
Synonyms : | AEN; FLJ12484; FLJ12562; ISG20L1; pp12744; |
Gene ID : | 64782 |
mRNA Refseq : | NM_022767 |
Protein Refseq : | NP_073604 |
MIM : | 610177 |
UniProt ID : | Q8WTP8 |
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◆ Lysates | ||
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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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