• Rat anti-mouse IL-6R monoclonal antibody (MR16-1) (4 mg/mouse) was injected on day 10.

Mouse IL-6 Receptor (IL-6R) protein (Recombinant) (STJP000483)

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STJP000483

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Host: HEK293
Note: STRICTLY FOR FURTHER RESEARCH USE ONLY (RUO). MUST NOT TO BE USED IN DIAGNOSTIC OR THERAPEUTIC APPLICATIONS.
Short Description: Recombinant-Mouse IL-6 Receptor (IL-6R)-protein was developed from hek293. For use in research applications.
Conjugation: Unconjugated
Formulation: 0.2 Mu m filtered PBS solution, pH7.2.
Storage Instruction: Can be stored in working aliquots at 2°C-8°C C for one month, or at-20°C to-70°C for 1 year. Avoid repeated freeze/thaw cycles. NA
Endotoxin: Endotoxin content was assayed using a LAL gel clot method. Endotoxin level was found to be less than 0.1 ng/µg (1EU/µg). NA
Gene Symbol: Il6ra
Gene ID: 16194
Uniprot ID: IL6RA_MOUSE
Immunogen Region: ECD
Immunogen: Optimized DNA sequence encoding extracellular domain of mouse IL-6 receptor (CD126) including a C-terminal 6His tag was expressed in HEK293 cells. NA
Tissue Specificity Expressed by dendritic cells. Soluble interleukin-6 receptor subunit alpha: Detected in the cerebrospinal fluid.
Post Translational Modifications A short soluble form is also released from the membrane by proteolysis. The sIL6R is formed by limited proteolysis of membrane-bound receptors, a process referred to as ectodomain shedding. mIL6R is cleaved by the proteases ADAM10 and ADAM17. Glycosylated. Glycosylation is dispensable for transport, signaling, and cell-surface turnover. Glycosylation at Asn-55 is a protease-regulatory exosite. Glycosylation is required for ADAM17-mediated proteolysis.
Function Part of the receptor for interleukin 6. Binds to IL6 with low affinity, but does not transduce a signal. Signal activation necessitate an association with IL6ST. Activation leads to the regulation of the immune response, acute-phase reactions and hematopoiesis. The interaction with membrane-bound IL6R and IL6ST stimulates 'classic signaling', the restricted expression of the IL6R limits classic IL6 signaling to only a few tissues such as the liver and some cells of the immune system. Whereas the binding of IL6 and soluble IL6R to IL6ST stimulates 'trans-signaling'. Alternatively, 'cluster signaling' occurs when membrane-bound IL6:IL6R complexes on transmitter cells activate IL6ST receptors on neighboring receiver cells. Interleukin-6 receptor subunit alpha: Signaling via the membrane-bound IL6R is mostly regenerative and anti-inflammatory (Probable). Drives naive CD4(+) T cells to the Th17 lineage, through 'cluster signaling' by dendritic cells. Soluble interleukin-6 receptor subunit alpha: Soluble form of IL6 receptor (sIL6R) that acts as an agonist of IL6 activity. The IL6:sIL6R complex (hyper-IL6) binds to IL6ST/gp130 on cell surfaces and induces signaling also on cells that do not express membrane-bound IL6R in a process called IL6 'trans-signaling'. sIL6R is causative for the pro-inflammatory properties of IL6 and an important player in the development of chronic inflammatory diseases. In complex with IL6, is required for induction of VEGF production. Plays a protective role during liver injury, being required for maintenance of tissue regeneration. 'Trans-signaling' in central nervous system regulates energy and glucose homeostasis.
Protein Name Interleukin-6 Receptor Subunit Alpha
Il-6 Receptor Subunit Alpha
Il-6r Subunit Alpha
Il-6r-Alpha
Il-6ra
Il-6r 1
Cd Antigen Cd126 Cleaved Into - Soluble Interleukin-6 Receptor Subunit Alpha
Sil6r
Database Links Reactome: R-MMU-1059683
Reactome: -MMU-110056
Reactome: -MMU-112411
Cellular Localisation Interleukin-6 Receptor Subunit Alpha: Cell Membrane
Single-Pass Type I Membrane Protein
Soluble Interleukin-6 Receptor Subunit Alpha: Secreted
Alternative Protein Names Interleukin-6 Receptor Subunit Alpha protein
Il-6 Receptor Subunit Alpha protein
Il-6r Subunit Alpha protein
Il-6r-Alpha protein
Il-6ra protein
Il-6r 1 protein
Cd Antigen Cd126 Cleaved Into - Soluble Interleukin-6 Receptor Subunit Alpha protein
Sil6r protein
Il6ra protein
Il6r protein

Information sourced from Uniprot.org

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