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Chicken IFN gamma (Yeast-derived Recombinant Protein) - 5 micrograms

RP0115C-005
$150.00
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Interferon-gamma (IFN-gamma) is a dimerized soluble cytokine that is the only member of the type II class of interferons. This interferon was originally called macrophage-activating factor, a term now used to describe a larger family of proteins to which IFN-gamma belongs. IFN-gamma, or type II interferon, is a cytokine that is critical for innate and adaptive immunity against viral and intracellular bacterial infections and for tumor control. Aberrant IFN-gamma expression is associated with a number of autoinflammatory and autoimmune diseases. The importance of IFN-gamma in the immune system stems in part from its ability to inhibit viral replication directly, but, most important, derives from its immunostimulatory and immunomodulatory effects. IFN-gamma is produced predominantly by natural killer (NK) and natural killer T (NKT) cells as part of the innate immune response, and by CD4 and CD8 cytotoxic T lymphocyte (CTL) effector T cells once antigen-specific immunity develops.

Recombinant Chicken IFN gamma Catalog Number RP0115C contains a single amino acid substitution compared to NCBI reference sequence NP_990480.1 (Thr at position 93 in place of Ile). This amino acid substitution was corrected to match the published sequence. The corrected recombinant protein is available (Catalog Number RP0929C-005/RP0929C-025/RP0929C-100) (Ile present at position 93).

IFNγ Homology Across Species

Gallus gallus (chicken) IFNg – 99% (see above)
Meleagris gallopavo (turkey) IFNγ – 98%
Lagopus lagopus scotica(red grouse) IFNγ – 96%
More - https://blast.ncbi.nlm.nih.gov/

Chicken IFN gamma (Yeast-derived Recombinant Protein) - 5 micrograms
Catalog No.:
RP0115C-005
Quantity:
5 ug
Source:
The Chicken IFN gamma recombinant protein was produced in yeast and therefore does not have endotoxin, is naturally folded, and post-translationally modified.
MW:
The Chicken IFN gamma recombinant protein has a predicted molecular weight of 16.7 kDa.
Protein Sequence:
HTASSLNLVQ LQDDIDKLKA DFNSSHSDVA DGGPIIVEKL KNWTERNEKR IILSQIVSMY LEMLENTDKS KPHTKHISEE LYTLKNNLPD GVKKVKDIMD LAKLPMNDLR IQRKAANELF SILQKLVDPP SFKRKRSQSQ RRCNC (145)
Country of Origin:
USA
Applications:
The Chicken IFN gamma endotoxin-free recombinant protein can be used in cell culture, as an IFN gamma ELISA Standard, and as a Western Blot Control.

32183481

Chlamydia psittaci PmpD-N Exacerbated Chicken Macrophage Function by Triggering Th2 Polarization and the TLR2/MyD88/NF-κB Signaling Pathway

Chu J, Li X, Qu G, Wang Y, Li Q, Guo Y, Hou L, Liu J, Eko FO, He C.

Int J Mol Sci. 2020 Mar 15;21(6):2003. doi: 10.3390/ijms21062003.

Applications: Measurement of chicken IL-2, IL-6, IL-10, IL-12, and IFN-γ in cell culture supernatants by ELISA

Abstract

The polymorphic membrane protein D (PmpD) is a highly conserved outer membrane protein which plays an important role in pathogenesis during Chlamydia psittaci infection. In this study, we evaluated the ability of the N-terminus of PmpD (PmpD-N) to modulate the functions of chicken macrophages and the signaling pathway(s) involved in PmpD-N-induced Toll-like receptors (TLRs), as well as interleukin (IL)-6 and IL-10 cytokine secretions. Thus, HD11 macrophages were treated with exogenous and intracellular PmpD-N of C. psittaci. The chlamydial growth was evaluated by enumeration of chlamydial loads in the infected macrophages. The phagocytic function of macrophages following PmpD-N treatment was detected by fluorescein-labeled Escherichia coli (E. coli). The concentration of nitric oxide (NO) secreted by HD11 macrophages was measured by the amount of NO2- in the culture supernatant using the Griess method. The cytokine secretions were assessed using multiplex cytokine ELISA kits. Expression levels of TLRs, myeloid differentiation factor 88 (MyD88), and nuclear factor kappa B (NF-κB) were analyzed by a Western blotting assay, as well as a luciferase assay, while NF-κB p65 nuclear translocation was assessed by confocal microscopy. The nuclear translocation of the transcription factor NF-κB was confirmed by evaluating its ability to combine with the corresponding promoter using the electrophoretic mobility shift assay (EMSA). After treatment with exogenous or endogenous PmpD-N, chlamydial loads and phagocytic functions were reduced significantly compared with those of the plasmid vector group, while NO secretions were reduced significantly compared with those of the lipopolysaccharide (LPS) treatment. Stimulation of HD11 cells with PmpD-N provoked the secretion of the Th2 cytokines, IL-6, and IL-10 and upregulated the expression of TLR2, TLR4, MyD88, and NF-κB. Furthermore, inhibition of TLR2, MyD88, and NF-κB in HD11 cells significantly decreased IL-6 and IL-10 cytokine levels, while NO production and phagocytosis increased significantly, strongly suggesting their involvement in PmpD-N-induced Th2 cytokine secretion and macrophage dysfunction. Our data indicate that C. psittaci PmpD-N inhibited macrophage functions by activating the Th2 immune response and the TLR2/MyD88/NF-κB signaling pathway.

 


31518579

Chicken lines divergently selected on feather pecking differ in immune characteristics.

van der Eijk JAJ, Verwoolde MB, de Vries Reilingh G, Jansen CA, Rodenburg TB, Lammers A.

Physiol Behav. 2019 Dec 1;212:112680. doi: 10.1016/j.physbeh.2019.112680. Epub 2019 Sep 10.

Applications: Leukocyte stimulation


24067955

Chicken Interferon-Inducible Transmembrane Protein 3 Restricts Influenza Viruses and Lyssaviruses In Vitro

Smith SE, Gibson MS, Wash RS, Ferrara F, Wright E, Temperton N, Kellam P, Fife M.

J Virol. 2013 Dec;87(23):12957-66. doi: 10.1128/JVI.01443-13. Epub 2013 Sep 25.

Applications: Stimulation of DF-1 chicken cells in culture.

Abstract

Interferon-inducible transmembrane protein 3 (IFITM3) is an effector protein of the innate immune system. It confers potent, cell-intrinsic resistance to infection by diverse enveloped viruses both in vitro and in vivo, including influenza viruses, West Nile virus, and dengue virus. IFITM3 prevents cytosolic entry of these viruses by blocking complete virus envelope fusion with cell endosome membranes. Although the IFITM locus, which includes IFITM1, -2, -3, and -5, is present in mammalian species, this locus has not been unambiguously identified or functionally characterized in avian species. Here, we show that the IFITM locus exists in chickens and is syntenic with the IFITM locus in mammals. The chicken IFITM3 protein restricts cell infection by influenza A viruses and lyssaviruses to a similar level as its human orthologue. Furthermore, we show that chicken IFITM3 is functional in chicken cells and that knockdown of constitutive expression in chicken fibroblasts results in enhanced infection by influenza A virus. Chicken IFITM2 and -3 are constitutively expressed in all tissues examined, whereas IFITM1 is only expressed in the bursa of Fabricius, gastrointestinal tract, cecal tonsil, and trachea. Despite being highly divergent at the amino acid level, IFITM3 proteins of birds and mammals can restrict replication of viruses that are able to infect different host species, suggesting IFITM proteins may provide a crucial barrier for zoonotic infections.

 


Application of Ecklonia cava Kjellman by-product as a feed additive: enhancing weight gain, immunity and protection from Salmonella infection in chickens.

Park, Soyeon, Kim, Chung Yoh, Park, Bokyoung, Kim, Kiju, Park, Keun-Tae, Han, Jong Kwon, & Hahn, Tae-Wook.

대한수의학회지, vol. 56, no. 4, 대한수의학회, Dec. 2016, pp. 255–260, doi:10.14405/KJVR.2016.56.4.255.

Applications: Measurement of chicken IFN gamma in cell culture supernatants by ELISA


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