Analytical Data
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Gene name
IL-32
- Application
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Alternative Names
NK4; TAIF; TAIFb; TAIFd; Natural Killer Cell Transcript 4; Natural killer cells protein 4; Tumor necrosis factor alpha-inducing factor
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Species
Human
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Source
E. coli
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Tag
N-His
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Purity
> 80% as determined by SDS-PAGE.
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Uniprot
P24001
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Expression Region
Met1~Lys131
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Molecular Weight
45kDa
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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
IL-32, or Interleukin-32, is a pro-inflammatory cytokine that plays a significant role in various immune responses and inflammatory diseases. Discovered in 2005, IL-32 is primarily produced by activated immune cells such as T cells, monocytes, and macrophages in response to infections and inflammatory stimuli. Its diverse biological functions include the regulation of immune cell activation, induction of other pro-inflammatory cytokines, and modulation of apoptosis in infected or cancerous cells. The elucidation of IL-32's mechanisms has significant implications for understanding its role in diseases like rheumatoid arthritis, inflammatory bowel disease, and certain cancers. Consequently, research into IL-32 recombinant proteins has gained momentum, aiming to explore their therapeutic potential. By producing and studying IL-32 recombinant proteins, researchers aim to develop targeted therapies that can modulate inflammatory responses, offering new avenues for the treatment of chronic inflammatory conditions. Additionally, understanding the structure-function relationship of IL-32 could pave the way for designing novel immunotherapies, enhancing the efficacy of existing treatments, and minimizing side effects. Overall, IL-32 remains an intriguing focus within immunological research, with promising prospects for biomedical applications.
