Recombinant Human IL-1Rrp2/IL-1R6 Fc Avi-tag Protein, CF
Recombinant Human IL-1Rrp2/IL-1R6 Fc Avi-tag Protein, CF Summary
Learn more about Avi-tag Biotinylated ProteinsProduct Specifications
Human IL-1 R6 (Asp20-Tyr337) Accession # Q9HB29.2 | DIEGRMD | Human IgG1 Fc (Pro100-Lys330) | Avi-tag |
N-terminus | C-terminus | ||
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.
AVI11116
Formulation | Lyophilized from a 0.2 μm filtered solution in PBS with Trehalose. |
Reconstitution | Reconstitute at 500 μg/mL in PBS. |
Shipping | The product is shipped with polar packs. 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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Scientific Data
When Recombinant Human IL-36 beta /IL-1F8 (6834-ILB/CF) is immobilized at 2 µg/mL (100 µL/well), Biotinylated Recombinant Human IL-1Rrp2/IL-1R6 Fc Chimera Avi-tag Protein (Catalog # AVI11116) binds with an ED50 of 1.50-15.0 μg/mL.
2 μg/lane of Biotinylated Recombinant Human IL-1Rrp2/IL-1R6 Fc Chimera Avi-tag Protein (Catalog # AVI11116) was resolved with SDS-PAGE under reducing (R) and non-reducing (NR) conditions and visualized by Coomassie® Blue staining, showing bands at 78-87 kDa and 156-174 kDa, respectively.
Reconstitution Calculator
Background: IL-1Rrp2/IL-1R6
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
- Boraschi, D. and A. Tagliabue (2006) Vitam. Horm. 74:229.
- Lovenberg, T. W. et al. (1996) J. Neuroimmunol. 70:113.
- Debets, R. et al. (2001) J. Immunol. 167:1440.
- Towne, J. E. et al. (2004) J. Biol. Chem. 279:13677.
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