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Canine IL-1 beta (IL-1F2) (Yeast-derived Recombinant Protein) - 100 micrograms

RP0085D-100
$900.00
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The IL-1 family of cytokines encompasses eleven proteins that each share a similar β-barrel structure and bind to Ig-like receptors. Several of the well characterized members of the IL-1-like cytokines play key roles in the development and regulation of inflammation. IL-1α (IL-1F1), IL-1β (IL-1F2), and IL-18 (IL-1F4) are well-known inflammatory cytokines active in the initiation of the inflammatory reaction and in driving Th1 and Th17 inflammatory responses. In contrast, IL-1 receptor antagonist (IL-1ra; IL-1F3) and IL-36 receptor antagonist (IL-36ra; IL-1F5) reduce inflammation by blocking the binding of the agonist receptor ligands. IL-33 (IL-1F11) is thought to function as an 'alarmin' released following cell necrosis to alerting the immune system to tissue damage or stress. The biological properties of IL-37 (IL-1F7) are mainly those of down-regulating inflammation.

Alternate Names - IL1B, IL-1, IL1-BETA, IL1F2, interleukin 1 beta, IL1beta

IL-1β Homology Across Species
Canis lupus familiaris (dog) IL-1β – 100%
Canis lupus dingo (dingo) IL-1β – 100%
Vulpes vulpes (red fox) IL-1β – 96%
More - https://blast.ncbi.nlm.nih.gov/

 

Canine IL-1 beta (IL-1F2) (Yeast-derived Recombinant Protein) - 100 micrograms
Catalog No.:
RP0085D-100
Quantity:
100 ug
Source:
The Canine IL-1 beta recombinant protein was produced in yeast and therefore does not have endotoxin, is naturally folded, and post-translationally modified.
MW:
The Canine IL-1 beta recombinant protein has a predicted molecular weight of 17.5 kDa.
Protein Sequence:
AAMQSVDCKL QDISHKYLVL SNSYELRALH LNGENVNKQV VFHMSFVHGD ESNNKIPVVL GIKQKNLYLS CVMKDGKPTL QLEKVDPKVY PKRKMEKRFV FNKIEIKNTV EFESSQYPNW YISTSQVEGM PVFLGNTRGG QDITDFTMEF SS (152)
Alias:
IL-1F2
Country of Origin:
USA
Applications:
The Canine IL-1 beta (IL-1F2) endotoxin-free recombinant protein can be used in cell culture, as an IL-1 beta 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


31536594

ERK1/ATF-2 signaling axis contributes to interleukin-1β-induced MMP-3 expression in dermal fibroblasts.

Kitanaka N, Nakano R, Sakai M, Kitanaka T, Namba S, Konno T, Nakayama T, Sugiya H.

PLoS One. 2019 Sep 19;14(9):e0222869. doi: 10.1371/journal.pone.0222869. eCollection 2019.

Applications: Stimulation of canine dermal fibroblasts.

Abstract

Matrix metalloproteinases (MMPs) play a pivotal role in tissue remodeling by degrading the extracellular matrix (ECM) components. This mechanism is implicated in a variety of physiological and pathological cellular processes including wound healing. One of the key proteins involved in this process is the proinflammatory cytokine interleukin-1β (IL-1β, which induces the expression of MMP-3 mRNA and the secretion of MMP-3 protein by dermal fibroblasts. In this study, we first investigated the contribution of activating transcription factor 2 (ATF-2) to IL-1β-induced MMP-3 expression in dermal fibroblasts. Our results showed that in cells transfected with ATF-2 siRNA or treated with the ATF-2 inhibitor SBI-0087702, IL-1β-induced MMP-3 mRNA expression was reduced. We also demonstrated that IL-1β stimulates the phosphorylation of ATF-2. These observations suggest that ATF-2 plays an important role in IL-1β-induced MMP-3 expression. Next, we investigated the role of MAPK signaling in ATF-2 activation. In cells treated with the extracellular signal-regulated kinase (ERK) inhibitor FR180240, as well as in cells transfected with ERK1 and ERK2 siRNAs, IL-1β-induced MMP-3 mRNA expression was reduced. In addition, we showed that IL-1β induced the phosphorylation of ERK1/2. These observations suggest that ERK1 and ERK2 are involved in IL-1β-induced MMP-3 expression. However, ERK1 and ERK2 do seem to play different roles. While the ERK inhibitor FR180204 inhibited IL-1β-induced ATF-2 phosphorylation, only in cells transfected with ERK1 siRNA, but not ERK2 siRNA, IL-1β-induced ATF-2 phosphorylation was reduced. These findings suggest that the ERK1/ATF-2 signaling axis contributes to IL-1β-induced MMP-3 expression in dermal fibroblasts.

 


31344106

Interleukin-1β promotes interleulin-6 expression via ERK1/2 signaling pathway in canine dermal fibroblasts.

Kitanaka N, Nakano R, Sugiura K, Kitanaka T, Namba S, Konno T, Nakayama T, Sugiya H.

PLoS One. 2019 Jul 25;14(7):e0220262. doi: 10.1371/journal.pone.0220262. eCollection 2019.

Applications: Simulation of dermal fibroblasts in culture

Abstract

Interleukin-6 (IL-6) is a pleiotropic cytokine involved in the regulation of the immune response and inflammation. In this study, we investigated effect of the proinflammatory cytokine interleukin-1β (IL-1β) on IL-6 expression in canine dermal fibroblasts. IL-1β induced IL-6 mRNA expression and protein release in a time- and dose-dependent manner. When cells were treated with inhibitors of mitogen-activated protein kinases (MAPKs), the extracellular signal-regulated kinase (ERK) inhibitor FR180240 inhibited IL-1β-induced IL-6 mRNA expression, but not SP600125 or SKF86002, which are c-Jun N-terminal kinase (JNK) and p38 MAPK inhibitors, respectively. In cells treated with U0126, an inhibitor of MAPK/ERK kinase (MEK), which activates ERK, IL-1β-induced IL-6 mRNA expression was also inhibited. IL-1β stimulated ERK1/2 phosphorylation. In cells transfected with ERK1 and ERK2 isoform siRNAs, IL-1β-induced IL-6 mRNA expression was reduced. These observations suggest that IL-1β induces IL-6 expression via ERK1/2 signaling pathway in canine dermal fibroblasts.


29743297

Interleukin-1β expression is increased in the duodenum of dogs with idiopathic inflammatory bowel disease.

Hawes M, Riddle A, Kirk J, Jergens A, Allenspach K.

Vet Rec. 2018 Nov 3;183(17):536. doi: 10.1136/vr.104495. Epub 2018 May 9.

Applications: Measurement of canine IL-1 beta in tissue homogenates supernatant in dogs with IBD by ELISA.


27357270

Cytokine and Growth Factor Concentrations in Canine Autologous Conditioned Serum.

Sawyere DM, Lanz OI, Dahlgren LA, Barry SL, Nichols AC, Werre SR.

Vet Surg. 2016 Jul;45(5):582-6. doi: 10.1111/vsu.12506.

Applications: Measurement of canine IL-1RA, IL-1 beta, and TNF alpha in serum and plasma by ELISA


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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