| Reactivity | HuSpecies Glossary |
| Applications | Bioactivity |
| Format | Carrier-Free |
| Additional Information | Biotinylated |
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| Details of Functionality | Measured by its binding ability in a functional ELISA. When
Recombinant Human IL-36 beta /IL-1F8
(Catalog #
6834-ILB/CF) is
immobilized at 2 µg/mL (100 µL/well), Biotinylated Recombinant Human IL-1Rrp2/IL-1R6
Fc Chimera Avi-tag (Catalog # AVI11116) binds with an ED50 of 1.50-15.0
μg/mL. |
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| Source | Human embryonic kidney cell, HEK293-derived human IL-1Rrp2/IL-1R6 protein
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| Accession # | |||||||||
| N-terminal Sequence | Protein identity confirmed by mass spectrometry. |
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| Structure / Form | Disulfide-linked homodimer Biotinylated via Avi-tag |
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| Protein/Peptide Type | Recombinant Proteins |
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| Purity | >95%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining. |
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| Endotoxin Note | <0.10 EU per 1 μg of the protein by the LAL method. |
| Dilutions |
|
| Theoretical MW | 65 kDa (monomer). 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 | 78-87 kDa, under reducing conditions. |
| 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. |
The Interleukin 1 receptor family (IL-1 R) comprises at least eleven members including IL-1 RI (IL-1 R1), IL-1 RII (IL-1 R2), IL-1 RAcP (IL‑1 R3), ST2 (T1/IL-1 R4), IL-18 Ra (IL-1 Rrp/IL-1 R5), IL-1Rrp2 (IL-1 RL2/IL-1R6), IL-18 Rb (AcPL/IL-1 R7), IL-1RAPL‑1 (TIGIRR‑2/IL‑1 R8), and TIGIRR-1 (IL-1 R9) (1). All family members possess three immunoglobulin (Ig)-like domains in their extracellular region. Most members also have an intracellular TIR (Toll-like receptor/IL-1 receptor signaling) domain that is also conserved in the Toll-like receptor family. Related proteins, SIGIRR (single Ig domain-containing IL-1 R-related molecule) and IL-18BP, differ from the other members by having only one Ig domain (1). Human IL-1Rrp2 cDNA encodes a 561 amino acid (aa) residue precursor protein with a putative 19 aa signal peptide and a 318 aa extracellular domain. It shares 67% and 65% amino acid sequence identity with rat and mouse IL 1Rrp2, respectively. IL-1Rrp2 is expressed in lung epitheium, brain vasculature, kidney, testis, monocytes, skin-derived keratinocytes, fibroblasts and, to a lesser extent, endothelial cells (2, 3). IL-1Rrp2 has been shown to mediate the activation of the transcription factor NF kappa B by the IL-1 family ligands IL-1 F6, F8 or F9 (also known as IL-1 epsilon ), with IL-1RAcP as a cofactor (3, 4). Response to IL-1F9 is specifically antagonized by IL-1 F5 (also known as IL-1δ), an IL-1 family ligand that is most closely related to IL-1ra (3). IL-1Rrp2, IL-1 F5, and IL-1F9 are all up-regulated in lesional psoriasis skin, suggesting that the IL-1Rrp2 mediated signaling pathway may take part in local inflammatory responses (3). Our Avi-tag Biotinylated IL-1Rrp2 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
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