Analytical Data
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Gene name
FAIM
- Application
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Alternative Names
FAIM；FAIM1;Fas apoptotic inhibitory molecule 1
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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
Q9NVQ4
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Expression Region
2-179aa
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AA Sequence
TDLVAVWDV ALSDGVHKIE FEHGTTSGKR VVYVDGKEEI RKEWMFKLVG KETFYVGAAK TKATINIDAI SGFAYEYTLE INGKSLKKYM EDRSKTTNTW VLHMDGENFR IVLEKDAMDV WCNGKKLETA GEFVDDGTET HFSIGNHDCY IKAVSSGKRK EGIIHTLIVD NREIPEIAS
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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
FAIM (Fas Apoptosis Inhibitory Molecule) is a protein that plays a crucial role in regulating apoptosis, particularly in the context of immune responses and neuroprotection. Researchers have focused on FAIM due to its potential implications in various pathological conditions, including autoimmune diseases, neurodegeneration, and cancer. Understanding the structure and function of FAIM is vital, as it can interact with key signaling pathways, influencing cell survival and death. The protein is known to suppress Fas-mediated apoptosis, thereby promoting cell survival, which is particularly significant in the immune system where maintaining a balance between activation and inhibition is crucial. Recent studies have also suggested that FAIM may have a role in modulating inflammation and cellular responses under stress conditions. Given its involvement in critical cellular processes, FAIM is a promising target for therapeutic interventions aimed at modulating immune functions and addressing diseases associated with dysregulated apoptosis. Consequently, the research into FAIM's structure and potential as a biomarker or therapeutic target has gained momentum, with efforts directed towards understanding its mechanism of action, interactions with other proteins, and implications in disease contexts. This research can pave the way for developing innovative treatment strategies that harness the regulatory capabilities of FAIM to improve patient outcomes in various diseases characterized by apoptotic dysregulation.
