Enhancing immune responses by a novel multi-epitope ROP8 DNA vaccine plus interleukin-12 plasmid as a genetic adjuvant against acute Toxoplasma gondii infection in BALB/c mice
Background: Toxoplasmosis is a widespread zoonotic infection, caused by the obligate intracellular protozoan. The infection is often asymptomatic in immunocompetent individuals, although in people with impaired immune systems can cause severe complications and progressive. constant efforts scientists have made valuable discoveries in the development of Toxoplasma gondii (T. gondii) vaccine candidate. However, an effective vaccine has not been developed yet. In the current study, we tested the co-delivery of multi-epitope vaccine pcROP8 new plasmid DNA encoding IL-12 (pcIL-12) to assess immune responses in BALB / c mice against acute T. gondii infection.
Methods: BALB / c mice were immunized on days 0, 21, and 42. The immune response of the vaccinated and control groups were evaluated using measurements of cytokines and antibodies, lymphocyte proliferation test, and survival time.
Results: The findings show that immunization with a multi-epitope pcROP8 significantly increase the level of anti-T. gondii antibodies, cellular immune responses TH1-type, lymphocyte proliferation, and survival time is long, compared with the control group (P <0.05). Furthermore, the use of pcIL-12 as an adjuvant genetic causes enhancement of the immune response mentioned above BALB / c mice (P <0.05).
Conclusion: The co-administration of pcIL-12 with a multi-epitope vaccine pcROP8, can be managed to increase the level of protection. Thus, this immunization regimen may be an effective vaccine strategies against T. gondii acute infection.
Enhancing immune responses by a novel multi-epitope ROP8 DNA vaccine plus interleukin-12 plasmid as a genetic adjuvant against acute Toxoplasma gondii infection in BALB/c mice
Genetic Variants FOXP3 Do Not Impact Supply and Cervical Interleukin-10 Levels in Human Papillomavirus Infection in Women
Regulatory T cells (Treg) heredity plays a central role in the control of inflammation and autoimmunity. Interleukin-10 (IL-10) has been described as a pleiotropic cytokine that is mainly released by CD4 + CD25 + FOXP3 + Treg and has strong immunosuppressive activity. Forkhead box P3 (FOXP3) expression of the transcription factor is very important for Treg function as a suppressor cells and FOXP3 gene single nucleotide variants (SNVs) has been shown to influence the pathogenesis of the virus.
This study was conducted to evaluate the plasmatic and cervical level of IL-10 in patients papillomavirus infected and uninfected humans and investigate whether intron -1 FOXP3 SNVs rs3761548 and rs2232365 may alter IL-10 secretion. SNVs characterization genotyped by polymerase chain reaction (PCR) products based on a specific sequence of enzymatic cleavage using restriction fragment length polymorphism method (RFLP). IL-10 levels determined by quantitative enzyme-linked immunosorbent assay (ELISA). In conclusion, the data show that there is no relationship between FOXP3 and cervical SNVs and circulating IL-10 level. These findings provide a reason that the IL-10 gene activation is independent of the transcription factor FOXP3 activity on Treg cells.
Introduction: We aimed to determine the genetic polymorphism and serum levels of interleukin 18 in Fars ethnic groups.Material and methods: 226 Fars ethnic groups participate. ATP III criteria were used to assess components of MS. SNP of the IL-18 gene was determined by ARMS-PCR.Results: The GG, GC and CC genotypes of -137 is 50%, 40% and 10%. CC, CA and AA genotypes of -607 is 45%, 37%, and 18% ..
Description: Interleukin-2 Human Recombinant produced in E.Coli is a single, non-glycosylated, Polypeptide chain containing 133 amino acids fragment (21-153) having a molecular weight of 20kDa and fused with a 4.5kDa amino-terminal hexahistidine tag. _x000D_ The IL-2 His is purified by proprietary chromatographic techniques._x000D_
LIMITED QTY-rhIL-2 Recombinant Human Interleukin-2 (100 µg)
Description: Defensins (alpha and beta) are cationic peptides with a broad spectrum of antimicrobial activity that comprise an important arm of the innate immune system. The α-defensins are distinguished from the β-defensins by the pairing of their three disulfide bonds. To date, six human β-defensins have been identified; BD-1, BD-2, BD-3, BD-4, BD-5 and BD-6. β-defensins are expressed on some leukocytes and at epithelial surfaces. In addition to their direct antimicrobial activities, they can act as chemoattractants towards immature dendritic cells and memory T cells. The β-defensin proteins are expressed as the C-terminal portion of precursors and are released by proteolytic cleavage of a signal sequence and in some cases, a propeptide sequence. β-defensins contain a six-cysteine motif that forms three intra-molecular disulfide bonds. Recombinant human BD-2 is a 4.3 kDa protein containing 41 amino acid residues.
Description: Relaxin-2 is a peptide hormone structurally related to insulin, which is expressed in the placenta, decidua, prostate, and in the ovary during pregnancy. Of the three known relaxin genes, Relaxin-2 is the only relaxin known to circulate in the blood. Relaxin-2 binds specifically to the LGR7 and LGR8 receptors, previously identified as an “orphan” G protein coupled receptors. Signaling by Relaxin-2 through its target receptors enhances the growth of pubic ligaments and ripening of the cervix during birth. Recombinant Relaxin-2 is a nonglycosylated 6.0 kDa disulfide linked heterodimeric protein consisting of a 24 amino acid A-chain and a 29 amino acid B-chain.
Description: PAI-2 is an inhibitory serpin expressed mainly in keratinocytes, activated monocytes, and placental trophoblasts. It exists predominantly as a 47 kDa nonglycosylated intracellular protein which can be induced to be secreted as 60 kDa glycoprotein. The glycosylated and unglycosylated forms of PAI-2 are equally effective as inhibitors of urokinase-type plasminogen activator (uPA), the only established physiological target of this serpin. PAI-2 has a unique ability to form dormant polymers spontaneously and reversibly under physiological conditions. The physiological relevance of this property, which is neither a consequence of any mutation in the PAI-2 gene nor associated with any known disorder, is still unclear. However, it appears that the formation of intracellular dormant polymers may be important for the controlled release of the inhibitor from PAI-2 producing cells. Plasma levels of PAI-2 are usually low or undetectable, except during pregnancy and in some forms of monocytic leukemia. Secretion of PAI-2 from the placenta normally occurs during the third trimester of pregnancy and accounts for the dramatic increase in PAI-2 levels (up to 250 ng/ml), which are maintained at these levels until postpartum, and then rapidly decline. In addition to its vital role in protecting the placenta from degradation by uPA and/or uPA-activated proteases, PAI-2 has been shown to be essential for the prevention of metastatic spread of neck, lung and breast cancers. The beneficial effect of PAI-2 seen in these studies is presumed to stem from its ability to inhibit uPA-dependent cell dissemination. PAI-2 has also been reported to inhibit keratinocyte proliferation, and to participate in the innate immune response during viral infection. Recombinant human PAI-2 is a 415-residue nonglycosylated protein.
Description: Matrix metalloproteinases (MMPs) are a family of endoproteases that require zinc and calcium for expressing catalytic activity. These enzymes play a central role in the maintenance and remodeling of the extracellular matrix. Elevated expression of their activity, caused either by up-regulation of their expression or down-regulation of their cognate inhibitors, has been implicated in various degenerative disorders, including arthritis, cardiovascular disease, skeletal growth-plate disorders, and cancer metastasis. MMP-2 is a secreted collagenase with specificity toward Type IV, V, VII, and X collagens. Recombinant human MMP-2 is a 62.0 kDa protein containing the entire catalytic N-terminal domain and the C-terminal domain (552 amino acids).
Description: The Trefoil Factor peptides (TFF1, TFF2 and TFF3) are expressed in the gastrointestinal tract, and appear to play an important role in intestinal mucosal defense and repair. TFF2 has been shown to inhibit gastrointestinal motility and gastric acid secretion. Recent data suggests a potential role for TFF2 in acute and chronic asthma (Nikolaidis, N.M. et al. Am. Journal Respir. Cell Mol. Biol. (2003) 4: 458-464). Recombinant human TFF2 is a 12.0 kDa polypeptide of 107 amino acid residues, which includes a 40-amino acid trefoil motif containing three conserved intramolecular disulfide bonds.
BMP-2 Bone Morphogenetic Protein-2 Human Recombinant Protein, Monomer
Description: Bone Morphogenetic Protein-2 Human Recombinant produced in E.Coli is a monomeric, non-glycosylated, Polypeptide chain containing 115 amino acids (283-396) and having a molecular mass of 13009 Dalton. ;The BMP-2 is purified by proprietary chromatographic techniques.
Description: ErbB-2 Human Recombinant is a 43.4 kDa protein containing 397 amino acid residues of the human Herstatin, and an extra Methionine at N-Terminal (underlined), produced in E.coli.
Nori® Human Angiopoietin-2 (ANG-2) ELISA Kit (2 plates)
Description: IL-2 is a powerful immunoregulatory lymphokine produced by T-cells in response to antigenic or mitogenic stimulation. IL-2/IL-2R signaling is required for T-cell proliferation and other fundamental functions which are essential for the immune response. IL-2 stimulates growth and differentiation of B-cells, NK cells, lymphokine activated killer cells, monocytes, macrophages and oligodendrocytes. Recombinant murine IL-2 is a 17.2 kDa protein, containing 149 amino acid residues.
Description: FGF basic (FGF2) is a multipotential fibroblast growth factor that stimulates and supports proliferation, migration and differentiation. Mouse FGF basic (FGF-2) Recombinant Protein is purified FGF basic (FGF-2) produced in yeast.
Description: Interleukin-2 (IL-2) is a cytokine produced by T-helper cells in response to antigenic or mitogenic stimulation. It is required for T-cell proliferation and other activities crucial to the regulation of the immune response. Chicken IL-2 Recombinant Protein is purified interleukin-2 produced in yeast.
IL15 Human, Interleukin-15 Human Recombinant Protein, HEK
Description: Interleukin-15 Human Recombinant produced in HEK cells is a glycosylated monomer, having a molecular weight of 12.8kDa due to glycosylation.;The IL15 is purified by proprietary chromatographic techniques.
IL17B Human, Interleukin-17B Human Recombinant Protein, Sf9
Description: IL17B Human Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 169 amino acids (21-180a.a.) and having a molecular mass of 19.2kDa (Molecular size on SDS-PAGE will appear at approximately 18-28kDa). IL17B is expressed with a 6 amino acid His-tag at C-Terminus and purified by proprietary chromatographic techniques.
Description: Interleukin-7 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 152 amino acids and having a molecular mass of 17.4 kDa. ;The IL-7 is purified by proprietary chromatographic techniques.
Description: Interleukin-10 Human Recombinant produced in E.coli is a single non-glycosylated polypeptide chains containing 161 amino acids each and having a molecular mass of 18.6kDa.;The IL-10 is purified by proprietary chromatographic techniques.
Description: The three mammalian isoforms of TGF-β, TGF-β1, β2, β3, signal through the same receptor and elicit similar biological responses. They are multifunctional cytokines that regulate cell proliferation, growth, differentiation and motility as well as synthesis and deposition of the extracellular matrix. They are involved in various physiological processes including embryogenesis, tissue remodeling and wound healing. They are secreted predominantly as latent complexes which are stored at the cell surface and in the extracellular matrix. The release of biologically active TGF-β isoform from a latent complex involves proteolytic processing of the complex and /or induction of conformational changes by proteins such as thrombospondin-1. TGF-β2 has been shown to exert suppressive effects on IL-2 dependent T-cell growth, and may also have an autocrine function in enhancing tumor growth by suppressing immuno-surveillance of tumor development. Recombinant human TGF-β2 is a 25.0 kDa protein composed of two identical 112 amino acid polypeptide chains linked by a single disulfide bond. * Manufactured using (BTI-Tn-5B1-4) cells under license from the Boyce Thompson Institute for Plant Research, Inc.
Description: Interleukin-1 alpha Human Recombinant produced in HEK cells is a glycosylated monomer, having a molecular weight of 18kDa due to glycosylation.;The IL1A is purified by proprietary chromatographic techniques.
PLGF2 Human, Placenta Growth Factor-2 Human Recombinant Protein, CHO
Description: PLGF2 Human Recombinant (19-170 a.a.) produced in CHO is a disulfide-linked homodimeric, glycosylated, polypeptide chain containing 152 amino acids and having a molecular mass of 33kDa.;The PLGF-2 Human Recombinant protein is purified by proprietary chromatographic techniques.
B2M Human, Beta 2 Microglobulin Human Recombinant Protein, His Tag
Description: B2M Recombinant Human produced in E.Coli is a single, non-glycosylated polypeptide chain containing 120 amino acids (1-119 a.a.) and having a molecular mass of 14 kDa. The B2M is fused to a 21 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.
Description: Interleukin-4 Human Recombinant produced in CHO is a single, non-glycosylated polypeptide chain containing 129 amino acids and having a molecular mass of 14 kDa, the glycosilation of IL-4 migrates as 18 kDa on SDS-PAGE.;The IL-4 is purified by proprietary chromatographic techniques.
Description: Interleukin-3 Human Recombinant produced in insect cells is a single, glycosylated polypeptide chain containing 133 amino acids and having a molecular mass of 15000 Dalton. ;The IL-3 CSF is fused to a C-terminal His-tag (6x His) and purified by proprietary chromatographic techniques.
Description: IL-9 produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain (19-144 a.a.) including an 18 aa signal peptide (1-18 aa) and fused to a 6 aa His Tag at C-terminus containing a total of 150 amino acids and having a molecular mass of 14.5kDa.;IL9 shows multiple bands between 18-28kDa on SDS-PAGE, reducing conditions and purified by proprietary chromatographic techniques.
AHSG Alpha-2-HS-Glycoprotein Human Recombinant Protein HEK
Description: AHSG Human Recombinant produced by transfected human cells is a single polypeptide chain containing 357 amino acids (19-367). AHSG is fused to an 8 amino acid His-tag at C-terminus & purified by proprietary chromatographic techniques.
FGF-2 Fibroblast Growth Factor-Basic Human Recombinant Protein
Description: Fibroblast Growth Factor-2 Human Recombinant (FGF-2) produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 154 amino acids and having a molecular mass of 17.2kDa.;The FGF-b is purified by proprietary chromatographic techniques.
TIMP2 Tissue Inhibitor of Metalloprotease 2 Human Recombinant Protein
Description: TIMP2 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 194 amino acids and having a molecular mass of 21.8kDa.
RARRES2 Human, Retinoic Acid Receptor Responder 2 Human Recombinant Protein,Sf9
Description: RARRES2 produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 146 amino acids (21-157a.a.) and having a molecular mass of 16.9kDa. (Molecular size on SDS-PAGE will appear at approximately 18-28kDa). RARRES2 is expressed with a 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.
Nori Equine MMP-2/TIMP-2 Complex ELISA Kit (2 plates)
Description: Interleukin-12 p40 His Human Recombinant produced in E.Coli is single, a non-glycosylated, polypeptide chain containing 306 amino acids fragment (23-328) with an amino-terminal hexahistidine tag. ;The IL-12 p40 His is purified by proprietary chromatographic techniques.
IL-13-Variant Interleukin-13 Variant Human Recombinant Protein
Description: Interleukin-13 Variant Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 114 amino acids, with a substitution of Q for R at position 112 compared with the wild type IL-13, having a molecular mass of 12.5 kDa. ;The IL-13 Variant is purified by proprietary chromatographic techniques.
IL-16 Interleukin-16 Human Recombinant Protein, His Tag
Description: Interleukin-16 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain (502-631 a.a) containing 150 amino acids and having a molecular mass of 15.5kDa. The IL-16 is fused to a 20 a.a His-Tag at N-Terminus.;The IL-16 is purified by proprietary chromatographic techniques.
IL-17 Interleukin-17 Human Recombinant Protein, His Tag
Description: Interleukin-17A Human Recombinant produced in E.Coli is a single, non-glycosylated, Polypeptide chain containing 132 amino acids fragment (24-155) having a molecular weight of 19.62kDa and fused with a 4.5kDa amino-terminal hexahistidine tag. ;The IL-17A His is purified by proprietary chromatographic techniques.
IL-29 Interleukin-29 Human Recombinant Protein, His Tag
Description: IL 29 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 206 amino acids (20-200 a.a) and having a molecular mass of 22.7kDa.IL 29 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
IL-28A Interleukin-28A Human Recombinant Protein, His Tag
Description: IL 28A Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 198 amino acids (26-200 a.a.) and having a molecular mass of 22.1kDa. IL 28A is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
IL36G Interleukin-36 Gamma Human Recombinant Protein, His Tag
Description: IL36G Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 192 amino acids (1-169) and having a molecular mass of 21.1kDa.
TNFR2 Tumor Necrosis Factor Receptor Type 2 Human Recombinant Protein
Description: TNFR2 Human produced in E.Coli is a single, non-glycosylated polypeptide chain containing 184 amino acids and having a molecular mass of 20kDa. The TNFR2 is purified by proprietary chromatographic techniques.
LCN2 Neutrophil Gelatinase Associated Lipocalin/Lipocalin-2 Human Recombinant Protein
Description: LCN2 Human Recombinant produced in E.Coli is a homodimeric non-glycosylated polypeptide chains consisting of two 178 amino acids and having a molecular mass of 41.0kDa.
Description: IL 17F His Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 158 amino acids (31-163) and having a molecular mass of 17.6kDa.;IL 17F His is fused to a 25 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Description: Dynactin 2 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 426 amino acids (1-403 a.a) and having a molecular mass of 46.9kDa.;DCTN2 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Description: Sox2 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 330 amino acids (317 aa residues of the full length Sox2) and having a molecular mass of 36kDa.;Sox2 is fused to a 13 amino acid TAT peptide at C-terminus (GGYGRKKRRQRRR) & purified by proprietary chromatographic techniques.
Description: Soluble TNF-related apoptosis-inducing ligand Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 169 amino acids _x000D_ (114-281) and having a molecular mass of 19.6 kDa._x000D_ The sTRAIL is purified by proprietary chromatographic techniques.
IL-1-beta Interleukin-1 beta Human Recombinant Protein, His Tag
Description: Interleukin-1 beta His-Tag Human Recombinant produced in E.Coli is a single, non-glycosylated, Polypeptide chain containing 153 amino acids fragment (117-269) and having a total molecular mass of 21.88 kDa fused with an amino-terminal hexahistidine tag. ;The IL-1b His is purified by proprietary chromatographic techniques.
Human Pancreas PrimaCell 2: Pancreatic Epithelial Cells
Description: Interleukin-6 Mouse Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 193 amino acids (25-211a.a.) and having a molecular mass of 22.5kDa (Molecular size on SDS-PAGE will appear at approximately 18-28kDa). IL6 is expressed with a 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.
Description: Pegylated Interleukin-22 Mouse Recombinant produced in E.Coli is a single, non-glycosylated homodimeric polypeptide chain containing 147 amino acids and an aditional Ala amino acid at N-terminus having a molecular mass of 36 kDa as determioned by mass spectometry. However due to enlarged hydrodymanic volume it runs on the SDS-PAGE as a 50 kDa protein and in gel-filtration on Superdex 200 as over 200 kDa protein._x000D_ The Murine IL-22 is Mono-pegylated (with 20 kDa PEG) purified by proprietary chromatographic techniques. _x000D_
Description: Soluble VEGFR2 Fc Human Recombinant fused with the Fc part of human IgG1 produced in baculovirus is a disulfide-linked homodimeric, glycosylated, polypeptide containing 968 amino acids and having a molecular mass of 145 kDa. The soluble receptor protein contains only the first 7 extracellular domains, which contain all the information necessary for ligand binding.
Nori Equine MMP-2/TIMP-4 Complex ELISA Kit (2 plates)
Conclusion: IL-18 genes may differ in certain populations, different ethnic groups and geographic regions. IL-18 polymorphisms may not be used as a marker of metabolic syndrome.
