Analytical Data
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Gene name
LITAF
- Application
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Alternative Names
LITAF;PIG7;SIMPLE;Lipopolysaccharide-induced tumor necrosis factor-alpha factor
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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
Q99732
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Expression Region
1-161aa
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AA Sequence
MGSSHHHHHH SSGLVPRGSH MSVPGPYQAA TGPSSAPSAP PSYEETVAVN SYYPTPPAPM PGPTTGLVTG PDGKGMNPPS YYTQPAPIPN NNPITVQTVY VQHPITFLDR PIQMCCPSCN KMIVSQLSYN AGALTWLSCG SLCLLGCIAG CCFIPFCVDA LQDVDHYCPN CRALLGTYKR L
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Molecular Weight
19 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
LITAF, or Lipopolysaccharide-Induced TNF-alpha Factor, is a protein that plays a significant role in the immune response and inflammation. It was initially identified as a transcription factor involved in the regulation of pro-inflammatory cytokines, particularly tumor necrosis factor-alpha (TNF-α), in response to lipopolysaccharide (LPS) stimulation, which mimics bacterial infection. The study of LITAF has gained importance due to its implications in various diseases, including autoimmune disorders, chronic inflammatory diseases, and certain cancers. Researchers have focused on the structural and functional characterization of LITAF to understand its mechanism of action and interactions with other cellular pathways. Notably, the LITAF protein has been linked to the regulation of gene expression in response to inflammatory stimuli, making it a potential therapeutic target. Additionally, studies have revealed that mutations in the LITAF gene can lead to disease, underscoring its role in human health. The reconstitution of LITAF as a recombinant protein has enabled detailed investigations into its function, binding partners, and the downstream signaling pathways it influences. This research is crucial for developing novel therapies aimed at modulating LITAF's activity to treat various inflammatory conditions effectively. Understanding LITAF's structure and function could pave the way for innovative strategies in managing inflammation-related diseases, enhancing our ability to design targeted interventions for improving patient outcomes.
