Recombinant Cotton Rat IL-1 alpha/IL-1F1 Protein Summary
Product Specifications
Ser115-Pro269
Analysis
Product Datasheets
Carrier Free
CF stands for Carrier Free (CF). We typically add Bovine Serum Albumin (BSA) as a carrier protein to our recombinant proteins. Adding a carrier protein enhances protein stability, increases shelf-life, and allows the recombinant protein to be stored at a more dilute concentration. The carrier free version does not contain BSA.
In general, we advise purchasing the recombinant protein with BSA for use in cell or tissue culture, or as an ELISA standard. In contrast, the carrier free protein is recommended for applications, in which the presence of BSA could interfere.
552-R1
Formulation | Lyophilized from a 0.2 μm filtered solution in PBS with BSA as a carrier protein. |
Reconstitution | Reconstitute at 10 μg/mL in sterile PBS containing at least 0.1% human or bovine serum albumin. |
Shipping | The product is shipped at ambient temperature. Upon receipt, store it immediately at the temperature recommended below. |
Stability & Storage: | Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
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552-R1/CF
Formulation | Lyophilized from a 0.2 μm filtered solution in PBS. |
Reconstitution | Reconstitute at 100 μg/mL in sterile PBS. |
Shipping | The product is shipped at ambient temperature. Upon receipt, store it immediately at the temperature recommended below. |
Stability & Storage: | Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
|
Reconstitution Calculator
Background: IL-1 alpha/IL-1F1
Interleukin 1 (IL-1) is a name that designates two proteins, IL-1 alpha and IL-1 beta, that are the products of distinct genes, but show approximately 25% amino acid sequence identity and recognize the same cell surface receptors. Although IL-1 production is generally considered to be a consequence of inflammation, evidence suggests that IL-1 is also temporarily upregulated during bone formation and the menstrual cycle and can be induced in response to nervous system stimulation. In response to stimuli produced by inflammatory agents, infections, or microbial endotoxins, a dramatic increase in the production of IL-1 by macrophages and various other cells is seen. Cells in particular known to produce IL-1 include osteoblasts, monocytes, macrophages, keratinocytes, Kupffer cells, hepatocytes, thymic and salivary gland epithelium, Schwann cells, fibroblasts and glia (oligodendroglia, astrocytes and microglia).
IL-1 alpha and IL-1 beta are both synthesized as 31 kDa precursors that are subsequently cleaved into proteins with molecular weights of approximately 17,000 Daltons. Neither precursor contains a typical hydrophobic signal peptide sequence and most of the precursor form of IL-1 alpha remains in the cytosol of cells, although there is evidence for a membrane-bound form of the precursor form of IL-1 alpha. The IL-1 alpha precursor reportedly shows full biological activity in the EL-4 assay. Among various species, the amino acid sequence of mature IL-1 alpha is conserved 60% to 70% and human, porcine, rat and cotton rat IL-1 has been found to be biologically active on murine cell lines. Both forms of IL-1 bind to the same receptors, designated as type I and type II. Evidence suggests that only the type I receptor is capable of signal transduction and that the type II receptor may function as a decoy, binding IL-1 and thus preventing the binding of IL-1 to the type I receptor.
- Dower, S.K. and J.E. Sims (1994) Guidebook to Cytokines and their receptors, Nicole, N.A. (ed), Oxford University Press, New York, p. 17.
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