Reactivity | MuSpecies Glossary |
Applications | Binding Activity |
Format | Carrier-Free |
Details of Functionality | Measured by its binding ability in a functional ELISA. Immobilized rmIL-12 R beta 1 at 10 µg/mL (100 µL/well) can bind rmIL-12 with a linear range of 0.3-20 µg/mL. |
Source | Mouse myeloma cell line, NS0-derived mouse IL-12 R beta 1 protein Gln20-Glu561, with a C-terminal 6-His tag |
Accession # | |
N-terminal Sequence | No results obtained: Gln20 predicted |
Protein/Peptide Type | Recombinant Proteins |
Gene | Il12rb1 |
Purity | >90%, by SDS-PAGE under reducing conditions and visualized by silver stain |
Endotoxin Note | <0.01 EU per 1 μg of the protein by the LAL method. |
Dilutions |
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Theoretical MW | 61.3 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 | 95-110 kDa, 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. |
Purity | >90%, by SDS-PAGE under reducing conditions and visualized by silver stain |
Reconstitution Instructions | Reconstitute at 100 μg/mL in sterile PBS. |
IL-12 R beta 1 is a 100 kDa type I transmembrane protein that belongs to the gp130/G-CSF R family of cytokine receptors. IL-12 R beta 1 is a common subunit of both the IL-12 and IL-23 receptor complexes which play distinct but related roles in T cell mediated inflammatory reactions (1, 2). Mature mouse IL-12 R beta 1 contains a 546 amino acid (aa) extracellular domain (ECD) with five fibronectin type III repeats, and a 147 aa cytoplasmic domain (3). Within the ECD, mouse IL-12 R beta 1 shares 85% and 52% aa sequence identity with rat and human IL-12 R beta 1, respectively. It shares 16% - 21% aa sequence identity with the ECDs of mouse gp130, LIF R, G-CSF R, and IL-23 R. IL-12 and IL-23 are disulfide linked heterodimeric cytokines that share a common p40 subunit (1, 2). IL-12 R beta 1 interacts with p40 at low affinity but does not transmit signals (3). Increased ligand binding affinity and signaling capacity are gained by association of IL-12 R beta 1 with either IL-12 R beta 2 or IL-23 R (4 - 6). IL-12 R beta 2 and IL-23 R are the signal transducing components of these receptor complexes (4, 7). IL-12 R beta 1 is expressed on activated T cells, NK cells, B cells, macrophages, and microglia (8 - 10). IL-12 induced signaling promotes the development of naïve T cells into IFN-beta producing Th1 cells (11). IL-23 contributes to chronic inflammation by inducing the production of IL-17 by memory T cells (12). Naturally occurring homodimers of p40 can function as antagonists of IL-12 and IL-23 and can also induce macrophage chemotaxis in the absence of IL-12 R beta 2 (13, 14).
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