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IgG1, Bovine; ELISA

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[#YSRTPBP003] IgG1, Bovine; ELISA

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(1) A Single-Step Gold Nanoparticle-Blood Serum Interaction Assay Reveals Humoral Immunity Development and Immune Status of Animals from Neonates to Adults.[TOP]

Pubmed ID :30521752
Publication Date : //
A well-developed, functional immune system is paramount to combat harmful attack from pathogenic organisms and prevent infectious diseases. Newborn animals and humans have only limited immunity upon birth, but their immune functions are expected to develop within weeks to months and eventually to reach a maturity that will provide full protection. Despite the importance of immune activity in animal and human health management, there is no convenient test available that allows for rapid assessment of the state of immune function in non-laboratory settings. Here we report an extremely simple and rapid blood test that may be used in point-of-care clinics or field settings to evaluate the humoral immune status of animals. The test detects a cooperative interaction between a gold nanoparticle and arguably the three most important proteins involved in the immune system: immunoglobulin M (IgM), immunoglobulin G (IgG) and at least one complement protein, C3, in the blood serum. Such interactions cause the gold nanoparticles to form clusters and aggregates. The average particle size of the gold nanoparticle-serum mixture, measured by dynamic light scattering, corresponds positively to the immune status and activity of the subject. Our study demonstrates that the test may be used not only for monitoring the immune function development from neonates to adults, but also for detecting active immune responses during infection. Although data reported here are largely based on murine and bovine models, it is likely that this test will be applicable to humans as well.

Authors : Zheng Tianyu, Crews John, McGill Jodi, Dhume Kunal, Finn Caroline, Strutt Tara, McKinstry Karl K, Huo Qun,



(2) Cytometric Micro-Bead Magnetic Suspension Array for High-Throughput Ultra-Sensitive Detection of Aflatoxin B1.[TOP]

Pubmed ID :30520622
Publication Date : //
High-throughput and low-cost detection of mycotoxins in complex matrices is becoming increasingly urgent but still challenged for ultra-sensitive analyses. Here we reported a green and practical cytometric micro-bead magnetic suspension array (CBMSA) strategy for rapid and economical detection of aflatoxin B1 (AFB1) in multiple batches of lotus seeds samples. The protocol included the fabrication of the suspension array chips by immobilizing the biotin-modified bovine serum albumin-AFB1 (antigen) onto the surface of streptavidin-coated magnetic micro-beads in a multi-wells array, the indirect immuno-competition of antigen and target of AFB1 in lotus seed samples with the specific antibodies, the rapid magnetic separation regardless complex pretreatment steps, and the ultra-sensitive fluorescence detection of fluorescein isothiocyanate labeled goat anti-mouse immunoglobulin G (FITC-IgG) probes. After systematical optimization regarding some crucial parameters, the developed CBMSA assay allowed for ultra-sensitive detection of AFB1 with limit of detection as low as 7.8125 pg kg-1. For high-throughput analysis, the CBMSA technique was capable of on-site coinstantaneous detection of 50-100 samples in one operation within 30 s only needing a small amount (50 μL) of solution, which is much cheaper, greener and more user-friendly than conventional techniques. Moreover, CBMSA with magnetic separation are free of multi-times' centrifugation and clean-up steps to avoid unpredictable loss of targets. Since various capture and fluorescent probes can be randomly constructed and bound onto the surface of magnetic micro-beads to establish the ultra-sensitive detection system, the CBMSA technique is very promising for more trace-analytes in complex matrices and for broad point-of-need applications, such as drug screening and real-time high-throughput analysis.

Authors : Liu Xiaofei, Liao Xiaofang, Sun Chaonan, Ying Guangyao, Wei Fang, Xing Xiaoyan, Shi Linchun, Sun Yifan, Zhou Lidong, Kong Weijun,



(3) Thermal effects on IgM-milk fat globule-mediated agglutination.[TOP]

Pubmed ID :30520391
Publication Date : //
The process of agglutination causes firm cream layers in bovine milk, and a functioning agglutination mechanism is paramount to the quality of non-homogenized milks. The phenomenon is not well-described, but it is believed to occur due to interactions between immunoglobulins (Ig) and milk fat globules. For the first time, this paper demonstrates how the process of agglutination can be visualized using confocal laser scanning microscopy, rhodamine red and a fluoresceinisothiocynat-conjugated immunoglobulin M antibody. The method was used to illustrate the effect on agglutination of storage temperature and pasteurization temperature. Storage at 5 °C resulted in clearly visible agglutination which, however, was markedly reduced at 15 °C. Increasing storage temperature to 20 or 37 °C cancelled any detectable interaction between IgM and milk fat globules, whereby the occurrence of cold agglutination was documented. Increasing 20 s pasteurization temperatures from 69 °C to 71 °C and further to 73 °C lead to progressively higher inactivation of IgM and, hence, reduction of agglutination. Furthermore, 2-dimensional sodium dodecyl sulfate polyacrylamide gel electrophoresis showed that changes in storage temperature caused a redistribution of Ig-related proteins in milk fat globule membrane isolates. Poly-immunoglobulin G receptor was present in milk fat globule preparations stored at cold (4 °C) conditions, but absent at storage at higher temperature (25 °C). The findings provide valuable knowledge to dairy producers of non-homogenized milk in deciding the right pasteurization temperature to retain the crucial agglutination mechanism.

Authors : Hansen Steffen F, Larsen Lotte B, Wiking Lars,



(4) Mining Milk for Factors which Increase the Adherence of subsp. to Intestinal Cells.[TOP]

Pubmed ID :30513877
Publication Date : //
Bifidobacteria play a vital role in human nutrition and health by shaping and maintaining the gut ecosystem. In order to exert a beneficial effect, a sufficient population of bifidobacteria must colonise the host. In this study, we developed a miniaturised high-throughput in vitro assay for assessing the colonising ability of bacterial strains in human cells. We also investigated a variety of components isolated from different milk sources for their ability to increase the adherence of subsp. ATCC 15697, a common member of the gastrointestinal microbiota of breastfed infants, to HT-29 cells. Both conventional and miniaturised colonisation assays were employed to examine the effect of 13 different milk-derived powders on bacterial adherence, including positive controls which had previously resulted in increased bifidobacterial adherence (human milk oligosaccharides and a combination of 3'- and 6'-sialylactose) to intestinal cells. Immunoglobulin G enriched from bovine whey and goat milk oligosaccharides resulted in increased adhesion (3.3- and 8.3-fold, respectively) of to the intestinal cells and the miniaturised and conventional assays were found to yield comparable and reproducible results. This study highlights the potential of certain milk components to favourably modulate adhesion of bifidobacteria to human intestinal cells.

Authors : Quinn Erinn M, Slattery Helen, Thompson Aoife P, Kilcoyne Michelle, Joshi Lokesh, Hickey Rita M,



(5) Anti-Bovine Podoplanin Monoclonal Antibody PMab-44 Detects Goat Podoplanin in Immunohistochemistry.[TOP]

Pubmed ID :30457925
Publication Date : //
Podoplanin (PDPN) is expressed in type I alveolar cells, kidney podocytes, and lymphatic endothelial cells. We have characterized the PDPNs of various animal species using specific anti-PDPN monoclonal antibodies (mAbs). In this study, we investigated whether these anti-PDPN mAbs cross-react with goat PDPN (gPDPN). Flow cytometry demonstrated that the anti-bovine PDPN mAb PMab-44 (IgG, kappa) reacts with gPDPN, which is overexpressed in CHO-K1 cells. Using immunohistochemical analysis, type I alveolar cells of goat lung were strongly detected by PMab-44. These results indicate that PMab-44 is useful for investigating gPDPN.

Authors : Yamada Shinji, Kaneko Mika K, Furusawa Yoshikazu, Itai Shunsuke, Sano Masato, Nakamura Takuro, Yanaka Miyuki, Handa Saori, Hisamatsu Kayo, Nakamura Yoshimi, Koyanagi Masanori, Fukui Masato, Harada Hiroyuki, Kato Yukinari,



(6) Epidemiological surveillance of bovine viral diarrhea and rift valley fever infections in camel.[TOP]

Pubmed ID :30410242
Publication Date : //
This study was designed to investigate the current epidemiological situation of bovine viral diarrhea virus (BVDV) and rift valley fever virus (RVFV) infection of camels originating from Sudan "smuggler" and Egypt as part of our future plan for a national surveillance program in Egyptian provinces, which will aid in establishment of control strategy for animal diseases.

Authors : El Bahgy Halla E K, Abdelmegeed Hala K, Marawan Marawan A,



(7) Perinatal immuno/inflammatory responses in the presence or absence of bovine fetal infection.[TOP]

Pubmed ID :30382887
Publication Date : //
It is known that the bovine fetus can mount an immune and inflammatory reaction to infection, but it is not known whether there is a contemporaneous maternal response. Nor is it known whether the response of calves which die perinatally, with or without infection, differs from that of live perinates. Hence, the objective of this study was to determine if acute phase reactant and immunoglobulin concentrations differed between calves (and their dams) in three groups: live calves (CC; n = 21) and dead calves with (PM INF+; n = 22) or without (PM INF-; n = 89) in utero infection. In calf plasma, serum amyloid A, haptoglobin, immunoglobulins M, G and G and interleukin-6 were measured. In dam serum, SAA and Hp was measured and in amniotic and abomasal fluid, IL-6 was measured.

Authors : Jawor Paulina, Mee John F, Stefaniak Tadeusz,



(8) Immune responses in bovines to recombinant glycoprotein D of bovine herpesvirus type 5 as vaccine antigen.[TOP]

Pubmed ID :30381153
Publication Date : //
Bovine herpesvirus 5 (BoHV-5) is responsible for outbreaks of meningoencephalitis that cause important economic losses in young cattle. BoHV-5 glycoprotein D (gD5) is essential for attachment and penetration into permissive cells and targeting of host immune systems, inducing strong humoral and cellular immune responses. The aim of this study was to evaluate the vaccinal immune response of vaccines formulated with the recombinant BoHV-5 gD (rgD5) in bovines. For the experiment, 72 heifers were randomly allotted into 6 different groups with 12 animals each. Group 1: vaccine formulated using inactivated BoHV-5 (iBoHV-5) adjuvanted with ISA50V2; Group 2: iBoHV-5 associated with 100 µg of rgD5 adjuvanted with ISA50V2; Group 3: 100 µg of rgD5 adjuvanted with ISA50V2; Group 4: 100 µg of rgD5 adjuvanted with Al(OH); Group 5: commercial vaccine; and Group 6: control group. Two doses were administered in a 26-day interval and the third after 357 days from primo vaccination. Cattle vaccinated with the vaccines formulated with iBoHV-5 plus rgD5 showed a significant (p < 0.01) five-fold increase in total immunoglobulin G (IgG) for BoHV-5, BoHV-1, and rgD5 as compared with the commercial and control groups. Also, a significant (p < 0.05) increase in IgG1 and IgG2a levels was induced in serum for rgD5. In addition, these same vaccines showed significant (p < 0.01) four-fold higher titers of BoHV-1 and -5 neutralizing antibodies. The results demonstrated that the rgD5 conserved important epitopes that were able to stimulate bovine humoral immunity response capable of viral neutralization of BoHV-1 and -5, suggesting it as a promising vaccine antigen to be used in vaccine for BoHV-1 and -5 endemic areas.

Authors : Araujo Itauá Leston, Dummer Luana Alves, Rodrigues Paulo Ricardo Centeno, Dos Santos Alceu Gonçalves, Fischer Geferson, Cunha Rodrigo Casquero, Leite Fábio Pereira Leivas,



(9) Data concerning the chromatographic isolation of bovine IgG from milk- and colostral whey.[TOP]

Pubmed ID :30370323
Publication Date : //
Data included are related to the research article "Isolation of biofunctional bovine immunoglobulin G from milk- and colostral whey with mixed-mode chromatography at lab and pilot scale" (Heidebrecht et al., 2018) [1]. Data show individual bovine whey proteins in flow-through and elution fractions using different chromatographic resins as well as different binding and elution conditions. The relevant analytical methods for individual protein detection were SDS-PAGE and reversed phase- high performance liquid chromatography. The focus of the data is on the two mixed mode materials MEP HyperCel and Capto-multimodal chromatography. Resins were used individually, in series and at different scale. Data provide information at which binding and elution conditions it is possible to isolate bovine IgG from milk and colostral whey and at which purity.

Authors : Heidebrecht Hans-Jürgen, Kainz Bernadette, Schopf Roland, Godl Klaus, Karcier Züleyha, Kulozik Ulrich, Förster Beatrix,



(10) Establishment of Monoclonal Antibody PMab-202 Against Horse Podoplanin.[TOP]

Pubmed ID :30362932
Publication Date : //
Podoplanin (PDPN), a type I transmembrane glycoprotein, is expressed in several body tissues, including podocytes of renal glomerulus, type I alveolar cells of lung, and lymphatic endothelial cells. PDPN activates platelet aggregation by binding to C-type lectin-like receptor-2 (CLEC-2) presented on platelets. Monoclonal antibodies (mAbs) against human-, mouse-, rat-, rabbit-, dog-, bovine-, and cat-PDPN have already been established. However, anti-horse PDPN mAbs have not yet been developed. In this study, we immunized mice with synthetic horse PDPN peptides and developed anti-horse PDPN mAbs. One of the established mAbs, PMab-202 (IgG, kappa), was specifically able to detect horse PDPN in Chinese hamster ovary/horse PDPN (CHO/horPDPN) cells in flow cytometry experiments. PMab-202 was also able to detect endogenous horse PDPN expressed in and a horse kidney cell line, FHK-Tcl3.1, in flow cytometry and Western blot analyses. PMab-202 is expected to prove useful in investigating the function of horse PDPN.

Authors : Furusawa Yoshikazu, Yamada Shinji, Itai Shunsuke, Sano Masato, Nakamura Takuro, Yanaka Miyuki, Handa Saori, Mizuno Takuya, Maeda Ken, Fukui Masato, Harada Hiroyuki, Kaneko Mika K, Kato Yukinari,