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Recombinant Human IL1RAPL1 Protein, CF

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When Recombinant Human PTPRD Fc Chimera is coated at 1µg/mL, Recombinant Human IL1RAPL1 FcChimera binds with an ED50 of 5‑30 ng/mL.
2 μg/lane of Recombinant Human IL1RAPL1 was resolved with SDS-PAGE under reducing (R) and non-reducing (NR) conditions and visualized by Coomassie® blue staining, showing bands at 81-92 kDa and 160-180 kDa, ...read more

Product Details

Summary
Reactivity HuSpecies Glossary
Applications Bioactivity
Format
Carrier-Free

Order Details

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Recombinant Human IL1RAPL1 Protein, CF Summary

Details of Functionality
Measured by its binding ability in a functional ELISA. When Recombinant Human PTPRD Fc Chimera is coated at 1 µg/mL, 100 μL/well, Recombinant Human IL1RAPL1 binds with an ED50 of 5‑30 ng/mL.
Source
Chinese Hamster Ovary cell line, CHO-derived human IL1RAPL1 protein
Human IL1RAPL1
(Leu19-Thr357)
Accession # Q9NZN1
IEGRMD Human IgG1
(Pro100-Lys330)
N-terminusC-terminus
Accession #
N-terminal Sequence
Leu19
Structure / Form
Disulfide-linked homodimer
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
66 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
81-92 kDa, reducing conditions

Packaging, Storage & Formulations

Storage
Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
  • 12 months from date of receipt, ≤ -20 °C as supplied.
  • 1 month, 2 to 8 °C under sterile conditions after reconstitution.
  • 3 months, ≤ -20 °C under sterile conditions after reconstitution.
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 IL1RAPL1 Protein, CF

  • IL1R8IL1RAPL
  • IL-1R9
  • IL1RAPL1
  • IL-1RAPL1
  • IL-1-RAPL-1
  • IL-1RAPL-1
  • IL1RAPL-1
  • interleukin 1 receptor accessory protein-like 1
  • interleukin 1 receptor-8
  • interleukin-1 receptor accessory protein-like 1
  • mental retardation, X-linked 10
  • MRX10
  • MRX21
  • MRX34
  • oligophrenin-4
  • OPHN4mental retardation, X-linked 21
  • Three immunoglobulin domain-containing IL-1 receptor-related 2
  • TIGIRR-2
  • TIGIRR-2mental retardation, X-linked 34
  • X-linked interleukin-1 receptor accessory protein-like 1

Background

Interleukin 1 receptor accessory protein-like 1 (IL1RAPL1), also known as Oligophenin-4 (OPHN4) and three immunoglobulin domain containing IL-1 receptor-related 2 (TIGIRR-2) (1), is a member of the IL-1 receptor superfamily. IL1RAPL1 is a single pass type I membrane protein which contains an N-terminal signal peptide (aa 1-18 ), three extracellular immunoglobulin-like domains (aa 19-350), a transmembrane domain (aa 358-378 ), an intracellular Toll/IL-1R domain (aa 403-562), and a long C-terminal tail which interacts with multiple signaling molecules (aa 549-644 ) (2). High expression levels of IL1RAPL1 was found in post-natal hippocampus, and its expression is upregulated by neuronal activity (3). The extracellular domain of IL1RAPL1 can mediate synapse formation through trans-synaptic interaction with PTPRD (4, 5). In neurons, IL1RAPL1 interacts with PSD-95, a major scaffolding protein of excitatory synapses, and modulates its synaptic localization by regulating JNK activity and PSD-95 phosphorylation (3).  Mutation or deletion of IL1RAPL1 gene is associated with non-syndromic intellectual disability and autism spectrum disorder (5). Human IL1RAPL1 shares 98% and 99% aa sequence identity with mouse and rat IL1RAPL1, respectively.
  1. Born, T.L. et al. (2000) J. Biol. Chem. 275:29946.
  2. Bahi, N. et al. (2003) Hum. Mol. Gen. 12:1415.
  3. Pavlowsky, A. et al. (2010) Curr. Biol. 20:103.
  4. Yoshida, T. et al. (2011) J. Neurosci. 31:13485.
  5. Ramos-Brossier, M. et al. (2015) Hum Mol Genet. 24:1106.

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