Analytical Data
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Gene name
LITAF
- Application
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Alternative Names
Small integral membrane protein of lysosome/late endosome p53-induced gene 7 protein
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Species
Human
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Source
E. coli
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Tag
N- GST
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q99732
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Expression Region
1-161aa
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Molecular Weight
44.1 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
Related Products
Protein Description
LITAF (lipopolysaccharide-induced TNF-alpha factor) is a pivotal protein involved in the regulation of inflammatory responses and the immune system. Research into LITAF's structure and function has gained momentum due to its critical role in various pathological conditions, including autoimmune diseases, chronic inflammation, and certain cancers. As a transcription factor, LITAF is known to enhance the expression of pro-inflammatory cytokines, particularly tumor necrosis factor-alpha (TNF-α), upon stimulation by lipopolysaccharides (LPS) and other inflammatory signals. The understanding of LITAF's mechanisms and interactions at the molecular level has broad implications for developing targeted therapies, especially in conditions characterized by excessive inflammation. Recent studies have focused on the recombinant expression of LITAF to facilitate functional analyses and structural characterization using techniques such as X-ray crystallography and NMR spectroscopy. The generated recombinant proteins can be utilized in a variety of assays, including binding studies and functional assays, to elucidate the biochemical pathways that LITAF influences. Moreover, understanding how LITAF is modulated in response to various stimuli offers insights into its potential as a therapeutic target. Thus, ongoing research into LITAF recombinant protein not only enhances our grasp of inflammatory processes but also opens avenues for novel interventions in immune-mediated diseases.
