Analytical Data
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Gene name
IL3
- Application
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Alternative Names
IL3；Interleukin-3
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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
P08700
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Expression Region
20-152aa
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AA Sequence
APMTQTTSLKTSWVNCSNMIDEIITHLKQPPLPLLDFNNLNGEDQDILME NNLRRPNLEAFNRAVKSLQNASAIESILKNLLPCLPLATAAPTRHPIHIK DGDWNEFRRKLTFYLKTLENAQAQQTTLSLAIF
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Molecular Weight
15 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
The research on IL-3 (Interleukin-3) recombinant protein is rooted in its key role as a hematopoietic growth factor, which influences the proliferation and differentiation of various blood cells, particularly in the immune system. IL-3 has garnered significant attention due to its involvement in several biological processes, including the regulation of immune responses, tissue repair, and the modulation of allergic reactions. In pathophysiological contexts, elevated levels of IL-3 have been associated with various hematological disorders and cancers, making it a critical target for therapeutic intervention. The development of recombinant IL-3 facilitates the study of its biological functions and mechanisms of action, allowing for the exploration of its potential applications in regenerative medicine and immunotherapy. Additionally, the elucidation of IL-3's structure-function relationship is essential for designing specific inhibitors or agonists that could modulate its effects in clinical settings. The production of IL-3 as a recombinant protein also enables standardized research protocols, thereby improving the reproducibility of experimental results across different laboratories. Overall, the continued investigation into IL-3 recombinant protein provides valuable insights that may lead to novel treatment strategies for immune-related diseases and offers potential advancements in targeted therapies leveraging the protein's regulatory capacities.
