Search results for: anti-5-Methylcytosine (anti-5-meC) antibody mouse IgM (clone 5MC-CD) Antibodies
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Production of a Mouse Monoclonal Antibody Against Mortalin by Whole Cell Immunization.Pancreatic carcinoma is the fourth leading cause of cancer death and is characterized by early invasion and metastasis. Advances in molecular biology directed new strategies in targeted therapy using monoclonal antibodies. To identify new biomarkers, we generated a panel of monoclonal antibodies against the newly established cell line, Faraz-ICR, from a patient with acinar cell carcinoma. After immunization of BALB/c female mice with Faraz-ICR cell line and fusion of splenocytes with SP2/0 myeloma cell line, high reactive hybridoma producing antibodies to Faraz-ICR were detected using enzyme-linked immunosorbent assay, immunofluorescence staining and flow cytometry. Western blot and two-dimensional immunoblot were used for further characterization of the targets antibodies. Among high reactive clones, the reactivity of 1C11 clone was assessed with other epithelial tumors. The isotype of the antibody was revealed to be IgM, and the antibody reacted to a protein with a molecular weight of about 70 kDa in Western blot analysis. To further characterization of the target antigen, immunoproteome of the Faraz-ICR cell line was performed. By liquid chromatography-mass spectrometry (LC-MS) analysis, we identified that the target of 1C11 clone was HSP70. In conclusion, pancreatic cancer is a fatal malignancy with no reliable biomarker for early screening and diagnosis. In this study, by establishing a pancreatic cell line, a panel of monoclonal antibodies was generated aiming to explore specific or associated cancer targets. We then introduced 1C11 monoclonal antibody that can specifically recognize mortalin as a main tumor marker and may serve as a new tool for diagnostic kit and therapeutic strategies targeting this molecule.
2553 related Products with: Production of a Mouse Monoclonal Antibody Against Mortalin by Whole Cell Immunization.Monoclonal Anti-Cellulose Anti C Reactive Protein A MOUSE ANTI BOVINE ROTAVIR Anti AGO2 Mouse, Monoclon Anti AGO2 Mouse, Monoclon Anti AGO2 Mouse, Monoclon Anti AGO2 Mouse, Monoclon Anti AGO2 Mouse, Monoclon Anti AGO2 Mouse, Monoclon anti CD16 monoclonal anti anti CD20 monoclonal anti CD8 antibody, Monoclonal
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Human Secretory IgM Emerges from Plasma Cells Clonally Related to Gut Memory B Cells and Targets Highly Diverse Commensals.Secretory immunoglobulin A (SIgA) enhances host-microbiota symbiosis, whereas SIgM remains poorly understood. We found that gut IgMplasma cells (PCs) were more abundant in humans than mice and clonally related to a large repertoire of memory IgMB cells disseminated throughout the intestine but rare in systemic lymphoid organs. In addition to sharing a gut-specific gene signature with memory IgAB cells, memory IgMB cells were related to some IgAclonotypes and switched to IgA in response to T cell-independent or T cell-dependent signals. These signals induced abundant IgM which, together with SIgM from clonally affiliated PCs, recognized mucus-embedded commensals. Bacteria recognized by human SIgM were dually coated by SIgA and showed increased richness and diversity compared to IgA-only-coated or uncoated bacteria. Thus, SIgM may emerge from pre-existing memory rather than newly activated naive IgMB cells and could help SIgA to anchor highly diverse commensal communities to mucus.
1721 related Products with: Human Secretory IgM Emerges from Plasma Cells Clonally Related to Gut Memory B Cells and Targets Highly Diverse Commensals.Anti C Reactive Protein A anti CD38 Hematopoietic p Plasma Membrane GFP Tag H Human Brain Microvascular GFP Expressing Human Brai Human Tonsil Microvascula Human Bladder Microvascul Human Cord Blood CD34+ Ce Human Red Blood Cells Uni AccuPrep Genomic DNA Extr AccuzolTM Total RNA Extra Astra Blue 6GLL, Stain fo
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Myelin Basic Protein Citrullination, a Hallmark of Central Nervous System Demyelination, Assessed by Novel Monoclonal Antibodies in Prion Diseases.Myelin basic protein (MBP) citrullination by peptidylarginine deiminase (PAD) enzymes leads to incomplete protein-lipid bilayer interactions and vulnerability to proteolytic enzymes, resulting in disorganization of the myelin sheath in the central nervous system. Therefore, citrullinated MBP (citMBP) has been suggested as a hallmark of demyelination, but how citMBP is implicated in prion diseases remains unknown. For the first time, we developed mouse monoclonal anti-citMBP IgG1 (clones 1B8, 1H1, and 3C6) and IgM (clone 3G5) antibodies that recognize human citMBP at its R25, R122, and R130 residues and at its C-terminal region (or the corresponding sites in mouse MBP), respectively. Using a biochemical, immunohistochemical, and immunogold-silver staining for electron microscopy techniques, we found that MBP residue R23 (corresponding to human R25) was specifically citrullinated, was stained as intense punctae in the corpus callosum, the striatum, and the cerebellar white matter, and was predominantly localized in disorganized myelin in the brains of scrapie-infected mice. In the brains of Creutzfeldt-Jakob disease (CJD) patients, MBP residues R25, R122, and R130 were markedly citrullinated and were stained as fibrils and punctae. In particular, white matter regions, such as the midbrain and the medulla, exhibited high levels of citMBP compared to other regions. However, the high levels of citMBP were not correlated with PAD2 expression. The clone 3G5 recognized significantly increased expression of the 18.5 kDa and/or 21.5 kDa variants of MBP in prion disease. Our findings suggest that significantly increased levels of citMBP may reflect demyelinating neuropathology, and that these newly developed antibodies may be useful for identifying demyelination.
2431 related Products with: Myelin Basic Protein Citrullination, a Hallmark of Central Nervous System Demyelination, Assessed by Novel Monoclonal Antibodies in Prion Diseases.Goat Anti-Rat Myelin Prot Goat Anti-Human Prion Pro Anti Myelin Basic Protein Rat monoclonal anti mouse Rat monoclonal anti mouse Rat monoclonal anti mouse Rat monoclonal anti mouse Rat monoclonal anti mouse Mouse Anti-Myelin Basic P Anti VGLUT 1 Rat, polyclo Anti Rat VGLUT 2, Rabbit HIV1 integrase antibody,
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Senescent cells expose and secrete an oxidized form of membrane-bound vimentin as revealed by a natural polyreactive antibody.Studying the phenomenon of cellular senescence has been hindered by the lack of senescence-specific markers. As such, detection of proteins informally associated with senescence accompanies the use of senescence-associated β-galactosidase as a collection of semiselective markers to monitor the presence of senescent cells. To identify novel biomarkers of senescence, we immunized BALB/c mice with senescent mouse lung fibroblasts and screened for antibodies that recognized senescence-associated cell-surface antigens by FACS analysis and a newly developed cell-based ELISA. The majority of antibodies that we isolated, cloned, and sequenced belonged to the IgM isotype of the innate immune system. In-depth characterization of one of these monoclonal, polyreactive natural antibodies, the IgM clone 9H4, revealed its ability to recognize the intermediate filament vimentin. By using 9H4, we observed that senescent primary human fibroblasts express vimentin on their cell surface, and MS analysis revealed a posttranslational modification on cysteine 328 (C328) by the oxidative adduct malondialdehyde (MDA). Moreover, elevated levels of secreted MDA-modified vimentin were detected in the plasma of aged senescence-accelerated mouse prone 8 mice, which are known to have deregulated reactive oxygen species metabolism and accelerated aging. Based on these findings, we hypothesize that humoral innate immunity may recognize senescent cells by the presence of membrane-bound MDA-vimentin, presumably as part of a senescence eradication mechanism that may become impaired with age and result in senescent cell accumulation.
2245 related Products with: Senescent cells expose and secrete an oxidized form of membrane-bound vimentin as revealed by a natural polyreactive antibody.Anti C Reactive Protein A MOUSE ANTI BOVINE ROTAVIR anti CD16 monoclonal anti Astrovirus antibody, Mono Mouse anti-chick type I c Mouse anti-chick type I c Mouse anti-bovine type I Mouse anti-bovine type I Mouse anti-porcine type I Mouse anti-porcine type I Mouse anti-human type I c Mouse anti-mouse type I c
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-Lactoglobulin Influences Human Immunity and Promotes Cell Proliferation.-Lactoglobulin (LG) is suspected to enhance or modulate human immune responses. Moreover, LG is also hypothesized to increase human cell proliferation. However, these potential functions of LG have not been directly or thoroughly addressed. In this study, we demonstrated that LG is a potent stimulator of cell proliferation using a hybridoma cell (a splenocyte fused with a myeloma cell) model. LG's ability to promote cell proliferation was lost when the protein is denatured. To further investigate the influence of LG's conformation on cell proliferation, we chemically modified LG by either carboxymethylation (CM) or acetylation and observed significantly reduced cell proliferation when the protein structure was altered. Furthermore, we proved that LG enhances cell proliferation via receptor-mediated membrane IgM receptor. These data indicated that nondenatured LG is the major component in milk that modulates cell proliferation. Collectively, our study showed that LG plays a key role in enhancing immune responses by promoting cell proliferation through IgM receptor.
1970 related Products with: -Lactoglobulin Influences Human Immunity and Promotes Cell Proliferation.Epidermal Growth Factor ( Epidermal Growth Factor ( T-cell proliferation grad TCHI T cell proliferation TCHI T cell proliferation Macrophage Colony Stimula Macrophage Colony Stimula T-cell proliferation grad TCHII T cell proliferatio TCHII T cell proliferatio Anti C Reactive Protein A anti SLAM anti CDw150 IgG
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Epitope analysis of Japanese cedar pollen allergen Cry j2 with a human IgM class monoclonal antibody 404-117.Japanese cedar pollen allergen Cry j2 is a causal allergen of seasonal pollinosis in Japan. To analyze B cell epitopes of Cry j2, we established two human-mouse hybridomas secreting IgM class human monoclonal antibodies to Cry j2. A pin-peptide enzyme-linked immunosorbent assay with synthesized icosa peptides showed that 404-117 monoclonal antibody bound to peptides #11-13 with cry j2 amino acid sequence of 101F-L140. Detailed analysis with octa peptides and alanine substituted peptides indicated that an amino acid sequence of 118FKVD121 was an essential for antibody binding. When K119 (Asn) was substituted with alanine, 404-117 monoclonal antibody did not bind to the alanine substituted peptide. We concluded that the 118FKVD121 sequence might have a very important role in early recognition by Cry j2-specific B cells, which could act as antigen presenting cells.
1565 related Products with: Epitope analysis of Japanese cedar pollen allergen Cry j2 with a human IgM class monoclonal antibody 404-117.Human IgM antibody, Monoc MOUSE ANTI HUMAN CD15, Pr MOUSE ANTI HUMAN CD15, Pr Anti C Reactive Protein A Anti AGO2 Human, Monoclon Anti AGO2 Human, Monoclon Anti AGO2 Human, Monoclon Anti AGO2 Human, Monoclon Anti AGO2 Human, Monoclon Anti AGO2 Human, Monoclon Anti Human AGO3, Monoclon anti FAS IgM (monoclonal)
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Specificity and biologic activities of novel anti-membrane IgM antibodies.The concept that the B-cell Receptor (BCR) initiates a driver pathway in lymphoma-leukemia has been clinically validated. Previously described unique BCR Ig-class-specific sequences (proximal domains (PDs)), are not expressed in serum Ig (sIg). As a consequence of sequence and structural differences in the membrane IgM (mIgM) µ-Constant Domain 4, additional epitopes distinguish mIgM from sIgM. mAbs generated to linear and conformational epitopes, restricted to mIgM and not reacting with sIgM, were generated despite the relative hydrophobicity of the PDm sequence. Anti-PD mAbs (mAb1, mAb2, and mAb3) internalize mIgM. Anti-mIgM mAb4, which recognizes a distinct non-ligand binding site epitope, mediates mIgM internalization, and in low-density cultures, growth inhibition, anti-clonogenic activity, and apoptosis. We show that mAb-mediated mIgM internalization generally does not interrupt BCR-directed cell growth, however, mAb4 binding to a non-ligand binding site in the mIgM PDm-μC4 domain induces both mIgM internalization and anti-tumor effects. BCR micro-clustering in many B-cell leukemia and lymphoma lines is demonstrated by SEM micrographs using these new mAb reagents. mAb4 is a clinical candidate as a mediator of inhibition of the BCR signaling pathway. As these agents do not bind to non-mIgM B-cells, nor cross-react to non-lymphatic tissues, they may spare B-cell/normal tissue destruction as mAb-drug conjugates.
2500 related Products with: Specificity and biologic activities of novel anti-membrane IgM antibodies.Mouse anti IgA1 antibody, Mouse anti Human IgM anti Mouse anti Human IgM anti Blood Group Antibodies a Rabbit anti Mouse IgM, Un anti-5-Methylcytosine (an Mouse Anti-Human IgM Anti Mouse Anti-Human IgM [+FI Mouse Anti-Human IgM [+RP N A Anti-Mouse IgM kappa Mouse Anti-IgM neg. contr Rat Anti-Human IgM mu Cha
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Generation and characterization of monoclonal antibodies specific for 18 kDa antigen from Taenia solium cysticerci.The gene encoding a mature 18 kDa glycoprotein of Taenia solium cysticerci (Ts18) was cloned and bacterially expressed with a His-tagged fusion protein. Monoclonal antibodies (MAbs) against the recombinant Ts18 antigen were generated in vitro by routine murine hybridoma technique of fusing splenocytes, from BALB/c mice immunized with the vesicular fluid of T. solium cysticerci (TsVF), with mouse myeloma cells (SP2/0). The reactivity and specificity of these MAbs were evaluated by indirect ELISA and immunoblotting techniques. Three stable hybridoma clones, namely 3B11, 6C5, and 6G4, were screened using His-Ts18-based ELISA, and these showed two IgG1 isotypes and one IgM isotype. All MAbs reacted with His-Ts18 at molecular weight (MW) 12.8 kDa and the native antigen at MW 18 kDa in TsVF and whole larval extracts (WLE). In a dot blotting test, MAbs 6C5 and 6G4 showed no obvious cross-reactivity with heterologous vesicular fluids from other taeniid species, including Taenia saginata (TsaVF), Taenia pisiformis (TpVF), Taenia hydatigena (ThVF), Taenia multiceps (TmVF), and Echinococcus granulosus (EgVF). Immunofluorescent assays showed that MAb 6C5 specifically reacted with the Ts18 expressed from pEGFP-N1-Ts18-transfected HeLa cells. Immunolocalization analysis, using MAb 6C5 as a probe, indicated that Ts18 was present at high concentrations in the region of the larval sucker and spiral canal. The results indicate that the Ts18 protein is an abundantly secreted parasite protein and MAbs against it might provide a step forward for improving the diagnosis of porcine cysticercosis.
2319 related Products with: Generation and characterization of monoclonal antibodies specific for 18 kDa antigen from Taenia solium cysticerci.MOUSE ANTI BORRELIA BURGD HBV core recombinant anti MOUSE ANTI BOVINE ROTAVIR MONOBODIES (Monoclonal An Viral antibodies: anti-H Proteins and Antibodies H Proteins and Antibodies H Proteins and Antibodies H Rat monoclonal anti mouse Rat monoclonal anti mouse Rat monoclonal anti mouse MOUSE ANTI CANINE DISTEMP
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A potent neutralizing IgM mAb targeting the N218 epitope on E2 protein protects against Chikungunya virus pathogenesis.Chikungunya virus (CHIKV) is a medically important human viral pathogen that causes Chikungunya fever accompanied with debilitating and persistent joint pain. Host-elicited or passively-transferred monoclonal antibodies (mAb) are essential mediators of CHIKV clearance. Therefore, this study aimed to generate and characterize a panel of mAbs for their neutralization efficacy against CHIKV infection in a cell-based and murine model. To evaluate their antigenicity and neutralization profile, indirect enzyme-linked immunosorbent assay (ELISA), an immunofluorescence assay (IFA) and a plaque reduction neutralization test were performed on mAbs of IgM isotype. CHIKV escape mutants against mAb 3E7b neutralization were generated, and reverse genetics techniques were then used to create an infectious CHIKV clone with a single mutation. 3E7b was also administered to neonate mice prior or after CHIKV infection. The survival rate, CHIKV burden in tissues and histopathology of the limb muscles were evaluated. Both IgM 3E7b and 8A2c bind strongly to native CHIKV surface and potently neutralize CHIKV replication. Further analyses of 3E7b binding and neutralization of CHIKV single-mutant clones revealed that N218 of CHIKV E2 protein is a potent neutralizing epitope. In a pre-binding neutralization assay, 3E7b blocks CHIKV attachment to permissive cells, possibly by binding to the surface-accessible E2-N218 residue. Prophylactic administration of 3E7b to neonate mice markedly reduced viremia and protected against CHIKV pathogenesis in various mice tissues. Given therapeutically at 4 h post-infection, 3E7b conferred 100% survival rate and similarly reduced CHIKV load in most mice tissues except the limb muscles. Collectively, these findings highlight the usefulness of 3E7b for future prophylactic or epitope-based vaccine design.
2706 related Products with: A potent neutralizing IgM mAb targeting the N218 epitope on E2 protein protects against Chikungunya virus pathogenesis.Rubella virus E2 recombin Rabbit Anti-SARS Virus Nu Recombinant Dengue Virus Recombinant Measles Virus Recombinant Measles Virus Recombinant Measles Virus Recombinant Measles Virus Recombinant Measles Virus Recombinant Measles Virus Recombinant SARS Virus Nu Recombinant SARS Virus Nu Recombinant SARS Virus Nu
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Anti-NeuGcGM3 reactivity: a possible role of natural antibodies and B-1 cells in tumor immunosurveillance.While not naturally expressed in normal human tissues, N-glycolylated (NeuGc) gangliosides are overexpressed in several tumors and have immunosuppressive capacity, which contributes to cancer progression. Naturally occurring antibodies against NeuGcGM3 exist in healthy donors that specifically recognize and kill tumor cells expressing the antigen by complement-dependent and -independent mechanisms, the latter resembling an oncotic necrosis-type of cell death. Both the levels of anti-NeuGcGM3 antibodies in the sera of healthy donors and the percentage of donors with these natural antibodies decrease with age. Our work has shown that anti-NeuGcGM3 antibodies are not detected in the sera of non-small cell lung cancer (NSCLC) patients, compared to age- and sex-matched healthy donors, which have anti-NeuGcGM3. Interestingly, the level of serum total IgM, but not IgG, was significantly lower in cancer patients than in healthy donors. Screening of immortalized mouse splenic and peritoneal-derived hybridomas showed that peritoneal B-1 cells secrete anti-NeuGcGM3 with tumor cytotoxic capacity. Defects in the natural surveillance against tumor antigens could increase the risk of elderly donors developing cancer and affect the capacity of cancer patients to effectively fight against tumor cells.
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