Product Specifications for Recombinant Human IL-1 beta/IL-1F2 Protein
E. coli-derived human IL-1 beta/IL-1F2 protein Ala117-Ser269
>97%, by SDS-PAGE under reducing conditions and visualized by silver stain.
<0.10 EU per 1 μg of the protein by the LAL method.
N-terminal sequence Analysis
Ala117 & Pro118
Predicted Molecular Mass
17 kDa, reducing conditions
Measured in a cell proliferation assay using D10.G4.1 mouse helper T cells. Symons, J.A. et al. (1987) in Lymphokines and Interferons, a Practical Approach. Clemens, M.J. et al. (eds): IRL Press. 272. The ED50 for this effect is <12 pg/mL.
Scientific Data Examples for Recombinant Human IL-1 beta/IL-1F2 Protein
Recombinant Human IL-1 beta/IL-1F2 Protein Bioactivity
Recombinant Human IL-1 beta /IL-1F2 (Catalog # 201-LB) stimulates cell proliferation of the D10.G4.1 mouse helper T cell line. The ED50 for this effect is <12 pg/mL.
Recombinant Human IL-1 beta/IL-1F2 Protein SDS-PAGE
1 μg/lane of Recombinant Human IL-1 beta /IL-1F2 was resolved with SDS-PAGE under reducing (R) conditions and visualized by silver staining, showing a single band at 17 kDa.
Formulation, Preparation and Storage
What does CF mean?
CF stands for Carrier Free (CF). We typically add Bovine Serum Albumin (BSA) as a carrier protein to our
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.
Lyophilized from a 0.2 μm filtered solution in PBS with BSA as a carrier protein. *1 mg pack size (01M) is supplied as a 0.2 µm filtered solution in PBS with BSA as a carrier protein.
Reconstitute at 50-200 μg/mL in sterile PBS containing at least 0.1% human or bovine serum albumin.
The product is shipped at ambient temperature. *The 1 mg pack size (01M) is shipped with dry ice or equivalent. Upon receipt, store it immediately at the temperature recommended below.
Stability & Storage:
Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
12 months from date of receipt, -20 to -70 °C as supplied.
1 month, 2 to 8 °C under sterile conditions after reconstitution.
3 months, -20 to -70 °C under sterile conditions after reconstitution.
*The 1 mg pack size (01M) can be stored for 1 month at 2 to 8 °C under sterile conditions after opening.
Lyophilized from a 0.2 μm filtered solution in PBS with Trehalose.
Reconstitute at 50-200 μg/mL in sterile PBS.
The product is shipped at ambient temperature. Upon receipt, store it immediately at the temperature recommended below.
Stability & Storage:
Background: IL-1 beta/IL-1F2
IL-1 is a name that designates two pleiotropic cytokines, IL-1 alpha (IL-1F1) and IL-1 beta (IL-1F2), which are the products of distinct genes. IL-1 alpha and IL-1 beta are structurally related polypeptides that share approximately 21% amino acid (aa) identity in human. Both proteins are produced by a wide variety of cells in response to inflammatory agents, infections, or microbial endotoxins. While IL-1 alpha and IL-1 beta are regulated independently, they bind to the same receptor and exert identical biological effects. IL-1 RI binds directly to IL-1 alpha or IL-1 beta and then associates with IL-1 R accessory protein (IL-1 R3/IL-1 R AcP) to form a high-affinity receptor complex that is competent for signal transduction. IL-1 RII has high affinity for IL-1 beta but functions as a decoy receptor and negative regulator of IL-1 beta activity. IL-1ra functions as a competitive antagonist by preventing IL-1 alpha and IL-1 beta from interacting with IL-1 RI (1-4). The human IL-1 beta cDNA encodes a 269 aa precursor. A 116 aa propeptide is cleaved intracellularly by the cysteine protease IL-1 beta -converting enzyme (Caspase-1/ICE) to generate the active cytokine (5-7). The 17 kDa mature human IL-1 beta shares 96% aa sequence identity with rhesus and 67%-78% with canine, cotton rat, equine, feline, mouse, porcine, and rat IL-1 beta.
Allan, S.M. et al. (2005) Nat. Rev. Immunol. 5:629.
Boraschi, D. and A. Tagliabue (2006) Vitam. Horm. 74:229.
Kornman, K.S. (2006) Am. J. Clin. Nutr. 83:475S.
Isoda, K. and F. Ohsuzu (2006) J. Atheroscler. Thromb. 13:21.
March, C.J. et al. (1985) Nature 315:641.
Auron, P.E. et al. (1984) Proc. Natl. Acad. Sci. 81:7907.
Martinon, F. and J. Tschopp (2007) Cell Death Differ. 14:10.