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Canine IL-6 (Yeast-derived Recombinant Protein) - 5 micrograms

RP0103D-005
$150.00
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Bulk quantities of Canine IL-6 protein are available.
Please contact us for pricing.

Canine IL-6 Specifications

Molecular Weight (calculated) - 21.0kDa

Amino Acid Sequence - FPTPGPLAGD SKDDATSNSL PLTSANKVEE LIKYILGKIS ALRKEMCDKF NKCEDSKEAL AENNLHLPKL EGKDGCFQSG FNQETCLTRI TTGLVEFQLH LNILQNNYEG DKENVKSVHM STKILVQMLK SKVKNQDEVT TPDPTTDASL QAILQSQDEW LKHTTIHLIL RSLEDFLQFS LRAVRIM (187)

Gene ID - 403985

Homology Across Species
Canis lupus familiaris (dog) IL-6 – 100%
Canis lupus dingo (dingo) IL-6 – 100%
Vulpes lagopus (Arctic fox) IL-6 – 97%
Vulpes vulpes (red fox) IL-6 – 97%
More - https://blast.ncbi.nlm.nih.gov/

Endotoxin - Naturally endotoxin-free

Applications

Cell Culture, ELISA Standard, Western Blot Control

IL-6 Background

Interleukin-6 (IL-6) is an interleukin that acts as both a pro-inflammatory and anti-inflammatory cytokine. It is secreted by T cells and macrophages to stimulate immune response to trauma, especially burns or other tissue damage leading to inflammation. IL-6 is also produced from muscle, and is elevated in response to muscle contraction. It is significantly elevated with exercise, and precedes the appearance of other cytokines in the circulation. Osteoblasts secrete IL-6 to stimulate osteoclast formation. Smooth muscle cells in the tunica media of many blood vessels also produce IL-6 as a pro-inflammatory cytokine. The role of IL-6 as an anti-inflammatory cytokine is mediated through its inhibitory effects on TNF-alpha and IL-1, and activation of IL-1ra and IL-10.

Alternate Names - IL6, BSF2, HGF, HSF, IFNB2, IL-6, BSF-2, CDF, IFN-beta-2, interleukin 6

Canine IL-6 (Yeast-derived Recombinant Protein) - 5 micrograms
Catalog No.:
RP0103D-005
Quantity:
5 ug
Source:
The Canine IL-6 recombinant protein was produced in yeast and therefore does not have endotoxin, is naturally folded, and post-translationally modified.
MW:
The Canine IL-6 recombinant protein has a predicted molecular weight of 21.0 kDa.
Protein Sequence:
FPTPGPLAGD SKDDATSNSL PLTSANKVEE LIKYILGKIS ALRKEMCDKF NKCEDSKEAL AENNLHLPKL EGKDGCFQSG FNQETCLTRI TTGLVEFQLH LNILQNNYEG DKENVKSVHM STKILVQMLK SKVKNQDEVT TPDPTTDASL QAILQSQDEW LKHTTIHLIL RSLEDFLQFS LRAVRIM (187)
Country of Origin:
USA
Applications:
The Canine IL-6 endotoxin-free recombinant protein can be used in cell culture, as an IL-6 ELISA Standard, and as a Western Blot Control.

32058160

Elevated circulating Th2 but not group 2 innate lymphoid cell responses characterize canine atopic dermatitis.

Früh SP, Saikia M, Eule J, Mazulis CA, Miller JE, Cowulich JM, Oyesola OO, Webb LM, Peng SA, Cubitt RL, Danko CG, Miller WH, Tait Wojno ED.

Vet Immunol Immunopathol. 2020 Jan 24;221:110015. doi: 10.1016/j.vetimm.2020.110015. [Epub ahead of print]

Applications: In vitro culture of CD4+ T cells and CD25+ ILCs


26872054

Th17 Pathway As a Target for Multipotent Stromal Cell Therapy in Dogs: Implications for Translational Research.

Kol A, Walker NJ, Nordstrom M, Borjesson DL.

PLoS One. 2016 Feb 12;11(2):e0148568. doi: 10.1371/journal.pone.0148568. eCollection 2016.

Applications: Canine IL-6 and IL-1 beta proteins were use to stimulate T cells in culture.

Abstract

Detrimental Th17 driven inflammatory and autoimmune disease such as Crohn's disease, graft versus host disease and multiple sclerosis remain a significant cause of morbidity and mortality worldwide. Multipotent stromal/stem cell (MSC) inhibit Th17 polarization and activation in vitro and in rodent models. As such, MSC based therapeutic approaches are being investigated as novel therapeutic approaches to treat Th17 driven diseases in humans. The significance of naturally occurring diseases in dogs is increasingly recognized as a realistic platform to conduct pre-clinical testing of novel therapeutics. Full characterization of Th17 cells in dogs has not been completed. We have developed and validated a flow-cytometric method to detect Th17 cells in canine blood. We further demonstrate that Th17 and other IL17 producing cells are present in tissues of dogs with naturally occurring chronic inflammatory diseases. Finally, we have determined the kinetics of a canine specific Th17 polarization in vitro and demonstrate that canine MSC inhibit Th17 polarization in vitro, in a PGE2 independent mechanism. Our findings provide fundamental research tools and suggest that naturally occurring diseases in dogs, such as inflammatory bowel disease, may be harnessed to translate novel MSC based therapeutic strategies that target the Th17 pathway.

 


23141169

Interleukin-1β, tumour necrosis factor-α and lipopolysaccharide induce C-type natriuretic peptide from canine aortic endothelial cells.

Osterbur K, Yu DH, Declue AE.

Res Vet Sci. 2012 Nov 8. doi:pii: S0034-5288(12)00305-0. 10.1016/j.rvsc.2012.10.002.

Applications: Stimulation of canine aortic endothelial cells

Abstract
The N-terminal portion of pro C-type natriuretic peptide (NT-pCNP) has shown promise as a biomarker for sepsis in humans and dogs, however the mechanism of NT-pCNP production in dogs is unknown. Canine aortic endothelial cells were stimulated with lipopolysaccharide, lipoteichoic acid, peptidoglycan, TNF-α, IL-1β, IL-6, IL-10, IL-21, CXCL-8, IFN-γ, VEGF-A or control (PBS), and NT-pCNP production was measured. Lipopolysaccharide, TNF-α, and IL-1β significantly stimulated NT-pCNP production in a dose and time dependent manner; IL-1β resulted in the greatest NT-pCNP concentrations. The other stimulants did not result in significant NT-pCNP production. The addition of serum to the cell culture model did not alter lipopolysaccharide, lipoteichoic acid or peptidoglycan induced NT-pCNP production. These data indicate that lipopolysaccharide, TNF-α and IL-1β regulate CNP production from canine vascular endothelium and of the stimulants tested, IL-1β is the predominant inducing factor. These data provide some initial insight into the mechanisms of CNP regulation in dogs.


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