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Mouse IL-6 R alpha/CD126 Protein 2168

$315.00$1,050.00

Summary

  • Expression: HEK293
  • Pure: Yes (HPLC)
  • Amino Acid Range: Leu20-Pro364
SKU: 2168parent Categories: , Tag:
Weight1 lbs
Dimensions9 × 5 × 2 in
accession

P22272

express system

HEK293

product tag

C-His

purity

> 95% as determined by Tris-Bis PAGE;> 95% as determined by HPLC

background

The multifunctional factor interleukin 6 (IL-6) exerts its activities through binding to a high-affinity receptor complex consisting of two membrane glycoproteins: an 80 kDa component receptor that binds IL-6 with low affinity (IL-6R alpha) and a signal-transducing component of 130 kDa (gp130) that does not bind IL-6 by itself, but is required for high-affinity binding of IL-6 by the complex. Both components of the receptor complex, IL-6R alpha and gp130 have been cloned, sequenced, and expressed.

molecular weight

The protein has a predicted MW of 39.21 kDa. Due to glycosylation, the protein migrates to 60-70 kDa based on Tris-Bis PAGE result.

available size

100 µg, 500 µg

endotoxin

Less than 1EU per μg by the LAL method.

Mouse IL-6 R alpha/CD126 Protein 2168

protein
Size and concentration
100, 500µg and lyophilized
Form
Lyophilized
Storage Instructions
Valid for 12 months from date of receipt when stored at -80°C. Recommend to aliquot the protein into smaller quantities for optimal storage. Please minimize freeze-thaw cycles.
Storage buffer
Shipped at ambient temperature.
Purity
> 95% as determined by Tris-Bis PAGE
target relevance
The multifunctional factor interleukin 6 (IL-6) exerts its activities through binding to a high-affinity receptor complex consisting of two membrane glycoproteins: an 80 kDa component receptor that binds IL-6 with low affinity (IL-6R alpha) and a signal-transducing component of 130 kDa (gp130) that does not bind IL-6 by itself, but is required for high-affinity binding of IL-6 by the complex. Both components of the receptor complex, IL-6R alpha and gp130 have been cloned, sequenced, and expressed.
Protein names
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)]
Gene names
Il6ra,Il6ra Il6r
Protein family
Type I cytokine receptor family, Type 3 subfamily
Mass
10090Da
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 (PubMed:27893700).; [Soluble interleukin-6 receptor subunit alpha]: Soluble form of IL6 receptor (sIL6R) that acts as an agonist of IL6 activity (PubMed:11113088). 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 (By similarity). In complex with IL6, is required for induction of VEGF production (By similarity). Plays a protective role during liver injury, being required for maintenance of tissue regeneration (PubMed:11113088). 'Trans-signaling' in central nervous system regulates energy and glucose homeostasis (PubMed:28402851).
Subellular location
[Interleukin-6 receptor subunit alpha]: Cell membrane ; Single-pass type I membrane protein .; [Soluble interleukin-6 receptor subunit alpha]: Secreted .
Tissues
Expressed by dendritic cells.; [Soluble interleukin-6 receptor subunit alpha]: Detected in the cerebrospinal fluid.
Structure
Component of a hexamer of two molecules each of IL6, IL6R and IL6ST; first binds to IL6 to associate with the signaling subunit IL6ST (PubMed:28265003). Interacts (via N-terminal ectodomain) with SORL1; this interaction may affect IL6-binding to IL6R, hence decrease IL6 'classic-signaling' (PubMed:28265003).; [Soluble interleukin-6 receptor subunit alpha]: Also interacts with SORL1; this interaction leads to soluble IL6R internalization. May form a trimeric complex with the soluble SORL1 ectodomain and circulating IL6 receptor; this interaction might stabilize circulating IL6, hence promote IL6 'trans-signaling'.
Post-translational modification
A short soluble form is also released from the membrane by proteolysis (PubMed:26876177). The sIL6R is formed by limited proteolysis of membrane-bound receptors, a process referred to as ectodomain shedding (PubMed:26876177). mIL6R is cleaved by the proteases ADAM10 and ADAM17 (PubMed:26876177).; 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.
Domain
Th
Target Relevance information above includes information from UniProt accession: P22272
The UniProt Consortium

HPLC of Mouse IL-6 R alpha/CD126 Protein
The purity of Mouse IL-6 R alpha is greater than 95% as determined by SEC-HPLC.
SDS-PAGE gel of Mouse IL-6 R alpha/CD126 Protein
Mouse IL-6 R alpha on Tris-Bis PAGE under reduced condition. The purity is greater than 95%.

Publications

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We haven't added any publications to our database yet.
Published literature highly relevant to the biological target of this product and referencing this antibody or clone are retrieved from PubMed database provided by The United States National Library of Medicine at the National Institutes of Health.

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