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Interleukinα (IL-1α), mouse

*This product has been discontinued!*
IL-1α is distinct from the other agonist member of the IL-1 family, IL-1β. Although IL-1α triggers the same IL-1 receptor and although many of the biological effects of IL-1α are similar to those of IL-1α, in humans IL-1α is predominantly an intracellular molecule. In fact, there is evidence that IL-1α has both intracellular functions as a precursor molecule due to a nuclear localization sequence. IL-1α as an unprocessed precursor is biologically as active as the processed form. IL-1α is also found constitutively in epithelial cells, whereas constitutive expression of IL-1β is rare. In many ways, IL-1α appears to be closer to the fibroblast growth factor family than the secreted IL-1β form. Therapeutic strategies for blocking IL-1β predominate over those for blocking IL-1α. Many humans have circulating neutralizing antibodies to IL-1α but not IL-1β. GenScript Interleukin (IL)-1α, mouse, produced in E. coli, is a non-glycosylated polypeptide chain containing 156 amino acids and having a molecular mass of 18,000 Da.
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Purity The purity of GenScript Recombinant Mouse IL-1 Alpha is greater than 98% as determined by the following methods:
(a) RP-HPLC analysis
(b) Anion-exchange FPLC
(c) Reducing and non-reducing SDS-PAGE silver-stained gel analysis
Endotoxin Level The endotoxin level of GenScript Recombinant Mouse IL-1 Alpha is below 0.1 ng/µg (1 IEU/µg) of IL-1α.
Formulation The protein was lyophilized after extensive dialysis against 50mM Tris-HCl, pH8.0, 200mM NaCl buffer.
Reconstitution It is recommended that the lyophilized GenScript Recombinant Mouse IL-1 Alpha be reconstituted in sterile 18 MΩ-cm H2O not less than 100 µg/ml, which can then be further diluted to other aqueous solutions.
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Target Background IL-1α is distinct from the other agonist member of the IL-1 family, IL-1β. Although IL-1α triggers the same IL-1 receptor and although many of the biological effects of IL-1α are similar to those of IL-1α, in humans IL-1α is predominantly an intracellular molecule. In fact, there is evidence that IL-1α has both intracellular functions as a precursor molecule due to a nuclear localization sequence. IL-1α as an unprocessed precursor is biologically as active as the processed form. IL-1α is also found constitutively in epithelial cells, whereas constitutive expression of IL-1β is rare. In many ways, IL-1α appears to be closer to the fibroblast growth factor family than the secreted IL-1β form. Therapeutic strategies for blocking IL-1β predominate over those for blocking IL-1α. Many humans have circulating neutralizing antibodies to IL-1α but not IL-1β.
GenScript Interleukin (IL)-1α, mouse, produced in E. coli, is a non-glycosylated polypeptide chain containing 156 amino acids and having a molecular mass of 18,000 Da.
Synonyms Interleukin (IL)-1α, mouse;
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