The purity of recombinant mIL-17B was determined by SDS-PAGE of 6 µg reduced (+) and non-reduced (-) recombinant mIL-17B and staining overnight with Coomassie Blue.Learn more about how we get our images
The activity of mIL-17B was assessed by its ability to bind to IL-17RB in a functional ELISA.Learn more about how we get our images
Recombinant mouse IL-17B (mIL-17B) His21-Phe180 (Accession #NP_062381) was produced in E. coli at Cell Signaling Technology.
>98% as determined by SDS-PAGE of 6 μg reduced (+) and non-reduced (-) recombinant mIL-17B. All lots are greater than 98% pure.
Recombinant mIL-17B has a Met on the amino terminus and has a calculated MW of 18,186. DTT-reduced and non-reduced protein migrate as 19 kDa polypeptides. The expected amino-terminal MHPRN of recombinant mIL-17B was verified by amino acid sequencing.
The activity of mIL-17B was assessed by its ability to bind to IL-17RB in a functional ELISA. The concentration at which half-maximal binding was observed for each lot was 0.1-1.0 µg/ml.
Less than 0.01 ng endotoxin/1 μg mIL-17B.
With carrier: Lyophilized from a 0.22 μm filtered solution of PBS, pH 7.2 containing 20 μg BSA per 1 μg mIL-17B. Carrier free: Lyophilized from a 0.22 μm filtered solution of PBS, pH 7.2.
Stable in lyophilized state at 4°C for 1 year after receipt. Sterile stock solutions reconstituted with carrier protein are stable at 4°C for 2 months and at -20°C for 6 months. Avoid repeated freeze-thaw cycles.Maintain sterility. Storage at -20°C should be in a manual defrost freezer.
IL-17B is a member of the IL-17 family of structurally related proteins (1). Unlike other IL-17 family members, IL-17B is a non-covalently linked homodimer (1,2). IL-17B is expressed by chondrocytes and neurons, and binds to the IL-17RB receptor (1-4). Human IL-17B has been shown to induce TNF-α and IL-1β from monocytic THP-1 cells and may be involved in neutrophil recruitment in vivo (3). However, the exact biological functions of IL-17B remain elusive.
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