Analytical Data
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Gene name
AVEN
- Application
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Alternative Names
MGC124011; OTTMUSP00000016129; PDCD12; Programmed cell death 12; RP23-52C15.2
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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
Q9NQS1
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Expression Region
1-362aa
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AA Sequence
MQAERGARGGRGRRPGRGRPGGDRHSERPGAAAAVARGGGGGGGGDGGGRRGRGRGRGFRGARGGRGGGGAPRGSRREPGGWGAGASAPVEDDSDAETYGEENDEQGNYSKRKIVSNWDRYQDIEKEVNNESGESQRGTDFSVLLSSAGDSFSQFRFAEEKEWDSEASCPKQNSAFYVDSELLVRALQELPLCLRLNVAAELVQGTVPLEVPQVKPKRTDDGKGLGMQLKGPLGPGGRGPIFELKSVAAGCPVLLGKDNPSPGPSRDSQKPTSPLQSAGDHLEEELDLLLNLDAPIKEGDNILPDQTSQDLKSKEDGEVVQEEEVCAKPSVTEEKNMEPEQPSTSKNVTEEELEDWLDSMIS
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Molecular Weight
64.9 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
AVEN (Apoptosis and Caspase Activation Inhibitor) is a protein that has garnered significant interest in the field of cancer research due to its role in regulating apoptosis and maintaining cell survival. Originally identified as a caspase inhibitor, AVEN is involved in cellular responses to stress and plays a critical role in the development and progression of various cancers. Studies have shown that AVEN can modulate apoptotic pathways, allowing cancer cells to evade programmed cell death, which contributes to tumor growth and resistance to therapy. Recent research has focused on the structural and functional characterization of AVEN, aiming to understand its molecular mechanisms and how it interacts with other proteins in apoptotic signaling pathways. This has led to explorations of AVEN as a potential therapeutic target; inhibiting its function might restore apoptotic processes in cancer cells, enhancing the efficacy of existing treatments. Furthermore, understanding AVEN's role could provide insights into resistance mechanisms in cancer therapies, paving the way for novel strategies in cancer treatment. Researchers are employing techniques such as recombinant protein expression and structural biology to elucidate AVEN's conformation and binding properties, which is critical for the development of small molecules or peptides that can disrupt its function. This emerging body of work highlights AVEN not only as a vital player in apoptosis regulation but also as a promising candidate for targeted cancer therapies, signifying a shift towards more personalized treatment options in oncology.











