Cell based assay with Human IL-6 Protein 4455

Human IL-6 Protein 4455

$210.00 – $700.00

Summary

Expression: E.coli
Active: Yes (cell based assay)
Amino Acid Range: Val30-Met212

SKU: 4455parent Categories: proteins, Recombinant proteins Tag: active proteins

Weight	1 lbs
Dimensions	9 × 5 × 2 in
accession	P05231
express system	E.coli
product tag	No Tag
purity	> 95% as determined by Tris-Bis PAGE;> 90% as determined by HPLC
background	IL-6 (Interleukin-6) is a pleiotropic cytokine that acts in the acute phase reaction, inflammation, hematopoiesis, bone metabolism, and cancer progression.Interleukin 6 has been shown to interact with interleukin-6 receptor and glycoprotein.
molecular weight	The protein has a predicted 20.8 kDa same as Tris-Bis PAGE result.
available size	100 µg, 500 µg
endotoxin	Less than 0.05EU per μg by the LAL method.

Human IL-6 Protein 4455

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
IL-6 (Interleukin-6) is a pleiotropic cytokine that acts in the acute phase reaction, inflammation, hematopoiesis, bone metabolism, and cancer progression.Interleukin 6 has been shown to interact with interleukin-6 receptor and glycoprotein.
Protein names Interleukin-6 (IL-6) (B-cell stimulatory factor 2) (BSF-2) (CTL differentiation factor) (CDF) (Hybridoma growth factor) (Interferon beta-2) (IFN-beta-2)
Gene names IL6,IL6 IFNB2
Protein family IL-6 superfamily
Mass 9606Da
Function Cytokine with a wide variety of biological functions in immunity, tissue regeneration, and metabolism. Binds to IL6R, then the complex associates to the signaling subunit IL6ST/gp130 to trigger the intracellular IL6-signaling pathway (Probable). The interaction with the membrane-bound IL6R and IL6ST stimulates 'classic signaling', 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 (Probable).; IL6 is a potent inducer of the acute phase response. Rapid production of IL6 contributes to host defense during infection and tissue injury, but excessive IL6 synthesis is involved in disease pathology. In the innate immune response, is synthesized by myeloid cells, such as macrophages and dendritic cells, upon recognition of pathogens through toll-like receptors (TLRs) at the site of infection or tissue injury (Probable). In the adaptive immune response, is required for the differentiation of B cells into immunoglobulin-secreting cells. Plays a major role in the differentiation of CD4(+) T cell subsets. Essential factor for the development of T follicular helper (Tfh) cells that are required for the induction of germinal-center formation. Required to drive naive CD4(+) T cells to the Th17 lineage. Also required for proliferation of myeloma cells and the survival of plasmablast cells (By similarity).; Acts as an essential factor in bone homeostasis and on vessels directly or indirectly by induction of VEGF, resulting in increased angiogenesis activity and vascular permeability (PubMed:12794819, PubMed:17075861). Induces, through 'trans-signaling' and synergistically with IL1B and TNF, the production of VEGF (PubMed:12794819). Involved in metabolic controls, is discharged into the bloodstream after muscle contraction increasing lipolysis and improving insulin resistance (PubMed:20823453). 'Trans-signaling' in central nervous system also regulates energy and glucose homeostasis (By similarity). Mediates, through GLP-1, crosstalk between insulin-sensitive tissues, intestinal L cells and pancreatic islets to adapt to changes in insulin demand (By similarity). Also acts as a myokine (Probable). Plays a protective role during liver injury, being required for maintenance of tissue regeneration (By similarity). Also has a pivotal role in iron metabolism by regulating HAMP/hepcidin expression upon inflammation or bacterial infection (PubMed:15124018). Through activation of IL6ST-YAP-NOTCH pathway, induces inflammation-induced epithelial regeneration (By similarity).
Subellular location Secreted .
Tissues Produced by skeletal muscle.
Structure Component of a hexamer of two molecules each of IL6, IL6R and IL6ST; first binds to IL6R to associate with the signaling subunit IL6ST (PubMed:12829785). Interacts with IL6R (via the N-terminal ectodomain); this interaction may be affected by IL6R-binding with SORL1, hence decreasing IL6 cis signaling (PubMed:28265003). Interacts with SORL1 (via the N-terminal ectodomain); this interaction leads to IL6 internalization and lysosomal degradation (PubMed:28265003). May form a trimeric complex with the soluble SORL1 ectodomain and soluble IL6R receptor; this interaction might stabilize circulating IL6, hence promoting IL6 trans signaling (PubMed:28265003).
Post-translational modification N- and O-glycosylated.
Target Relevance information above includes information from UniProt accession: P05231
The UniProt Consortium

Data

Human IL-6 R alpha, His Tag captured on CM5 Chip via anti-his antibody can bind Human IL-6, No Tag with an affinity constant of 0.22 nM as determined in SPR assay (Biacore T200).

Immobilized Human IL-6 at 2µg/ml (100µl/Well) on the plate. Dose response curve for Human IL-6 R alpha, hFc Tag with the EC50 6.0ng/ml determined by ELISA

Cell based assay with Human IL-6 Protein

Measured in a cell proliferation assay using TF-1 human erythroleukemic cells. The ED50 for this effect is 0.1 - 0.5 ng/mL (QC Test).

The purity of Human IL-6 is greater than 90% as determined by SEC-HPLC.

Human IL-6 on Tris-Bis PAGE under reduced condition. The purity is greater than 95%.

Publications

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.