Recombinant Human IL-18 BPa His-tag Avi-tag Protein, CF

Measured by its binding ability in a functional ELISA. In a Human IL‑18/IL‑1F4 Antibody (MAB91244) coated plate, Biotinylated Recombinant Human IL‑18 BPa His-tag Avi-tag Protein (Catalog # AVI11236) binds to Recombinant Human IL‑18/IL‑1F4 Protein (9124-IL) with an ED50 of 0.0800-0.800 ng/mL.

2 μg/lane of Recombinant Human IL-18 BPa His-tag Avi-tag Protein (Catalog # AVI11236) was resolved with SDS-PAGE under reducing (R) and non-reducing (NR) conditions and visualized by Coomassie® Blue staining, showing bands at 40-46 kDa.

• Applications: Bioactivity
• Format: Carrier-Free

Recombinant Human IL-18 BPa His-tag Avi-tag Protein, CF Summary

• Additional Information: Biotinylated
• Details of Functionality: Measured by its binding ability in a functional ELISA. In a Human IL‑18/IL‑1F4 Antibody (Catalog # MAB91244) coated plate, Biotinylated Recombinant Human IL‑18 BPa His-tag Avi-tag protein (Catalog # AVI11236) binds to Recombinant Human IL‑18/IL‑1F4 (Catalog # 9124-IL) with an ED₅₀ of 0.0800-0.800 ng/mL.
• Source: Chinese Hamster Ovary cell line, CHO-derived human IL-18 BPa protein
  

  Human IL-18 BPa (Thr31-Gly194) Accession # O95998.2	6-His tag	Avi-tag
  N-terminus		C-terminus

• Accession #: O95998.2
• N-terminal Sequence: Thr31
• Structure / Form: Biotinylated via Avi-tag
• Protein/Peptide Type: Recombinant Proteins
• Purity: >95%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.
• Endotoxin Note: <0.10 EU per 1 μg of the protein by the LAL method.

Applications/Dilutions

• Dilutions:
  • Bioactivity
• Theoretical MW: 20 kDa.
  Disclaimer note: The observed molecular weight of the protein may vary from the listed predicted molecular weight due to post translational modifications, post translation cleavages, relative charges, and other experimental factors.
• SDS-PAGE: 40-46 kDa, under reducing conditions.

Packaging, Storage & Formulations

• Storage: Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
• Buffer: Lyophilized from a 0.2 μm filtered solution in PBS with Trehalose.
• Purity: >95%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.
• Reconstitution Instructions: Reconstitute at 500 μg/mL in PBS.

Notes

This product is produced by and ships from R&D Systems, Inc., a Bio-Techne brand.

Alternate Names for Recombinant Human IL-18 BPa His-tag Avi-tag Protein, CF

• IL18 BPa
• IL-18 BPa
• IL18BP
• IL-18BP
• IL18BPa
• interleukin 18 binding protein
• interleukin-18-binding protein
• MC51L-53L-54L homolog gene product
• tadekinig-alfa

Background

Interleukin 18 binding protein (IL-18 BP) is a secreted glycoprotein, which functions as an IL-18 antagonist by binding to IL-18 and blocking its biological activity. IL‑18 BP bears no amino acid sequence homology to the membrane-associated IL-18 and IL-1 receptor proteins. The gene for human IL-18 BP has been localized to chromosome 11q13. It encodes for at least four isoforms by alternative splicing. The IL-18 BP isoforms a and c each contain one immunoglobulin (Ig)-like C2-type domain while isoforms b and d lack a complete Ig domain. The complete Ig domain has been shown to be essential to the binding and neutralizing properties of the binding proteins. Two isoforms of mouse IL18 BP (c and d) containing the complete Ig domain have also been isolated and shown to neutralize IL-18 bioactivity. Human and mouse IL-18 BPs share approximately 61% amino acid sequence identity. Several poxviruses also encode proteins with sequence similarity to the human and mouse IL-18 BP. Viral IL-18 BPs have been shown to bind and inhibit IL-18 responses and may be involved in modulating host immune responses. The expression of IL-18 BP is markedly up-regulated by IFN-gamma , suggesting that IL-18 activity is modulated by a negative feedback mechanism mediated by IL-18 BP. Our Avi-tag Biotinylated human IL-18 BPa His-tag Chimera features biotinylation at a single site contained within the Avi-tag, a unique 15 amino acid peptide. Protein orientation will be uniform when bound to streptavidin-coated surface due to the precise control of biotinylation and the rest of the protein is unchanged so there is no interference in the protein's bioactivity.

1. Mühl, H. et al. (2000) Biochem. Biophys. Res. Commun. 267:960.
2. Kim, S-H. et al. (2000) Proc. Nat. Acad. Sci. USA 97:1190.
3. Calderara, S. et al. (2001) Virology 279:22.

Bioinformatics

• Uniprot:
  • O95998.2()