Analytical Data
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Gene name
CIAPIN1
- Application
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Alternative Names
CIAPIN1；Anamorsin
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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
Q6FI81
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Expression Region
1-312aa
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AA Sequence
MGSSHHHHHH SSGLVPRGSH MGSMADFGIS AGQFVAVVWD KSSPVEALKG LVDKLQALTG NEGRVSVENI KQLLQSAHKE SSFDIILSGL VPGSTTLHSA EILAEIARIL RPGGCLFLKE PVETAVDNNS KVKTASKLCS ALTLSGLVEV KELQREPLTP EEVQSVREHL GHESDNLLFV QITGKKPNFE VGSSRQLKLS ITKKSSPSVK PAVDPAAAKL WTLSANDMED DSMDLIDSDE LLDPEDLKKP DPASLRAASC GEGKKRKACK NCTCGLAEEL EKEKSREQMS SQPKSACGNC YLGDAFRCAS CPYLGMPAFK PGEKVLLSDS NLHDA
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Molecular Weight
36 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
CIAPIN1 (Cytokine-Inducible Apoptosis Inhibitor 1) is an intriguing protein that has garnered attention in the field of cancer research due to its role in regulating apoptosis and cellular survival. Initially identified as a gene whose expression is induced by pro-inflammatory cytokines, CIAPIN1 has been linked to various cellular processes, including cell proliferation, migration, and anti-apoptotic signaling pathways. Recent studies suggest that CIAPIN1 may play a significant role in the pathogenesis of cancer, as its upregulation is often associated with tumor progression and poor patient prognosis. This has prompted researchers to explore the potential of CIAPIN1 as a therapeutic target. The recombinant protein form of CIAPIN1 is essential for elucidating its biochemical properties and understanding its functional role at the molecular level. By producing recombinant CIAPIN1, scientists can investigate its interactions with other proteins, its effects on signaling pathways, and its impact on cell fate decisions under various conditions. Furthermore, characterizing the structure and function of this protein could unveil new insights into its mechanism of action, potentially leading to the development of novel therapeutic strategies aimed at manipulating its expression or activity in cancer cells. Overall, the research surrounding CIAPIN1 and its recombinant protein forms is pivotal in advancing our understanding of its contributions to tumor biology and the development of innovative cancer treatments.
