Free Shipping on orders over 50$

British Pound Sterling - GBP Euro - EUR US Dollar - USD (EUR)

Welcom to Gentaur Biotech Products!

Guinea pig IgG, Clone MsGp3, Mab anti_; frozen, IH_ELISA

Be the first to review this product

Availability: In stock


Quick Overview

[#YSRTMCA561] Guinea pig IgG, Clone MsGp3, Mab anti_; frozen, IH_ELISA


YSRTMCA561 | Guinea pig IgG, Clone MsGp3, Mab anti_; frozen, IH_ELISA, 2 ml.
More informations about Guinea pig IgG, Clone MsGp3, Mab anti_; frozen, IH_ELISA in

Product Tags

Use spaces to separate tags. Use single quotes (') for phrases.

(1) High-throughput ClonePix FL analysis of mAb-expressing clones using the UCOE expression system.[TOP]

Pubmed ID :24518824
Publication Date : //
Therapeutic recombinant monoclonal antibodies (mAbs) are commonly produced by high-expressing, clonal, mammalian cells. Creation of these clones for manufacturing remains heavily reliant on stringent selection and gene amplification, which in turn can lead to genetic instability, variable expression, product heterogeneity and prolonged development timelines. Inclusion of cis-acting ubiquitous chromatin opening elements (UCOE™) in mammalian expression vectors has been shown to improve productivity and facilitate high-level gene expression irrespective of the chromosomal integration site without lengthy gene amplification protocols. In this study we have used high-throughput robotic clone selection in combination with UCOE™ containing expression vectors to develop a rapid, streamlined approach for early-stage cell line development and isolation of high-expressing clones for mAb production using Chinese hamster ovary (CHO) cells. Our results demonstrate that it is possible to go from transfection to stable clones in only 4 weeks, while achieving specific productivities exceeding 20 pg/cell/day. Furthermore, we have used this approach to quickly screen several process-crucial parameters including IgG subtype, enhancer-promoter combination and UCOE™ length. The use of UCOE™-containing vectors in combination with automated robotic selection provides a rapid method for the selection of stable, high-expressing clones.

Authors : Hou Jeff Jia Cheng, Hughes Ben S, Smede Matthew, Leung Kar Man, Levine Kara, Rigby Susan, Gray Peter P, Munro Trent P,

(2) Production and characterization of Monoclonal antibodies to bluetongue virus.[TOP]

Pubmed ID :21331886
Publication Date : //
In the present study, a total of 24 MAbs were produced against bluetongue virus (BTV) by polyethyleneglycol (PEG) mediated fusion method using sensitized lymphocytes and myeloma cells. All these clones were characterized for their reactivity to whole virus and recombinant BTV-VP7 protein, titres, isotypes and their reactivity with 24 BTV-serotype specific sera in cELISA. Out of 24 clones, a majority of them (n = 18) belong to various IgG subclasses and the remaining (n = 6) to the IgM class. A panel of eight clones reactive to both whole BTV and purified rVP7 protein were identified based on their reactivity in iELISA. For competitive ELISA, the clone designated as 4A10 showed better inhibition to hyperimmune serum of BTV serotype 23. However, this clone showed a variable percent of inhibition ranging from16.6% with BTV 12 serotype to 78.9% with BTV16 serotype using 24 serotype specific sera of BTV originating from guinea pig at their lowest dilutions. From the available panel of clones, only 4A10 was found to have a possible diagnostic application.

Authors : Bhanuprakash Veerakyathappa, Hosamani Madhusudhan, Balamurugan Vinayagamurthy, Gandhale Pradeep Narayan, Venkatesan Gnanavel, Singh Raj Kumar,

(3) Selective recognition and elimination of nicotinic acetylcholine receptor-reactive B cells by a recombinant fusion protein AChR-Fc in myasthenia gravis in vitro.[TOP]

Pubmed ID :20727598
Publication Date : //
AChR-reactive B cells play a key role in the pathogenesis of myasthenia gravis (MG) by producing autoantibodies. Selective elimination of AChR-reactive B cells will be a promising way to treat MG. Thus, we generated a fusion protein (referred to as AChR-Fc) composed of the human extracellular domain of AChR α1 subunit and the Fc domain of the human IgG1 heavy chain, which could bind both to AChR-reactive BCR and FcγRIIB on the surface of AChR-reactive B cells. Our results showed that AChR-Fc inhibited the proliferation of AChR-specific hybridoma cells, promoted their apoptosis, and mediated cytotoxicity by cross-linking effector cells and complement. Likewise, AChR-Fc significantly reduced the number of AChR-reactive B cells from spleen of Lewis rats immunized with AChR ex vivo.

Authors : Chang Ting, Lin Hong, Gao Jie, Li Wei, Xu Jiang, Sun Chen Jing, Li Hang, Li Fan Fan, Song Yue, Ye Jing, Li Zhu Yi,

(4) Establishment of a swine monocyte cell line.[TOP]

Pubmed ID :11497081
Publication Date : //
A swine monocyte cell line was established from peripheral blood sample collected from a healthy adult male pig. The cloned cells grow actively in forming monolayers in both glass and plastic cell culture flasks with the growth medium reported previously (Kadoi, 2000) at 36.5 degrees C incubation. The plating efficiency is more than 95%. Densely grown cells in flasks show an epithelioid morphology. The fundamental properties of the cells were examined for cytological definition as monocytes. A positive property detected was guinea pig complement receptor, porcine IgG receptor, non-specific esterase, and acid phosphatase. A significant phagocytic activity proved by the inoculation of Saccharomyces cerevisiae is also one of the characteristics observed in the LPS-activated cells.

Authors : Kadoi K, Tsukise A, Shiba H, Ikeda K, Seki T, Ariga T,

(5) Molecular parameters in melittin immunogenicity.[TOP]

Pubmed ID :9262645
Publication Date : //
Based on immunogenicity studies, two T-cell epitopes in melittin were found to be functional in guinea pigs, one being centrally located, the other one residing in the C-terminal chain. In Balb/c mice only the central epitope was found to be active. A human T-cell clone was found by T-cell proliferation studies to employ strictly the C-terminal chain. Truncation of melittin peptides at the N-terminus did not markedly affect the capacity of guinea pigs to develop anti-IgG responses towards peptidic epitopes and towards a C-terminally attached haptenic group. Attachment of various substituents inside and outside the T-cell epitopic areas had no marked effect on antibody responses. In contrast, the substituents positioned within a T-cell epitope abolished T-cell proliferation. This difference between whole animal data and cellular in vitro responses is presently not understood.

Authors : Curcio-Vonlanthen V, Schneider C H, Frutig K, Blaser K, Kalbacher H,

(6) Molecular cloning and characterization of guinea pig Fc gamma RIII: expression but not function is independent of the gamma chain of Fc epsilon RI.[TOP]

Pubmed ID :8921410
Publication Date : //
We have isolated two cDNA clones encoding the guinea pig receptor for the Fc portion of IgG2 (Fc gamma 2R) from a guinea pig peritoneal macrophage cDNA library. Analysis of the predicted amino acid sequence of the one cDNA clone indicated that the guinea pig Fc gamma 2R is a type I transmembrane protein and has approximately 72% DNA sequence homology and approximately 57% protein sequence homology with the human Fc gamma RIII. Therefore, we propose that the guinea pig Fc gamma 2R is referred to as guinea pig Fc gamma RIII. The most important finding in this report is that the obtained cDNA directed the cell surface expression of the Fc gamma 2R on COS-7 cells without association with the gamma chain of the high-affinity IgE receptor (Fc epsilon RI gamma) which is required for human and mouse Fc gamma RIII to be expressed on the cell surface. Furthermore, we demonstrated that the endocytosis activity of Fc gamma RIII is dependent upon the association with Fc epsilon RI gamma, suggesting that Fc epsilon RI gamma is involved in the functions of guinea pig Fc gamma RIII. The other clone was found to lack the sequence encoding transmembrane and cytoplasmic domains, suggesting the presence of a soluble form of guinea pig Fc gamma RIII. Northern blot analysis and RT-PCR showed that a transmembrane form of guinea pig Fc gamma RIII was expressed in peritoneal macrophages, but not in neutrophils in spite of the fact that they express Fc gamma 2R, indicating that the Fc gamma 2R on neutrophils is a product of a distinct gene.

Authors : Isashi Y, Yamashita T, Nagasawa S, Murakami M, Uede T,

(7) The rat neutrophil low-affinity Fc receptor for IgG: molecular cloning and functional characterization.[TOP]

Pubmed ID :7590913
Publication Date : //
A complementary DNA (cDNA) clone encoding rat Fc gamma receptor II (Fc gamma RII) was isolated from rat neutrophils and characterized. The cDNA encodes a type I transmembrane protein with 285 amino acids having an extracellular domain consisting of two immunoglobulin-like domains (179 amino acids), a transmembrane domain (26 amino acids), and a cytoplasmic domain (47 amino acids). The nucleotide sequences are identical to that of recently cloned Fc gamma RII from rat mast cells. This protein was expressed on FcR-negative Chinese hamster ovary (CHO) cells. The characterization of cDNA-transfected CHO cells clearly indicated that the protein encoded by the cDNA clone binds guinea-pig IgG1 and IgG2 complexes and unexpectedly binds monomeric rat IgG1, but not IgG2. Furthermore, the affinity for immune complexes was significantly augmented by protease treatment of transfectants. In addition, endocytosis of immune complex was noted in transfectants.

Authors : Isashi Y, Tamakoshi M, Nagai Y, Sudo T, Murakami M, Uede T,

(8) Indigenous anti-hepatitis A virus IgM capture ELISA for the diagnosis of hepatitis A.[TOP]

Pubmed ID :8088883
Publication Date : //
Anti-hepatitis A virus IgM capture ELISA was developed by using the reagents produced in the NIV laboratory. The major reagents of the assay were anti-human IgM antibody, hepatitis A virus (HAV) and anti-HAV IgG-horse radish peroxidase (HRP) conjugate. Of these, anti-human IgM antibodies were generated in rabbit against IgM secreted by human hybridoma clone(G3). HAV was derived from buffalo green money kidney cell line infected with HM-175 strain. Virus purified from the cell lysates was used for immunization of rabbits and guinea-pigs. There was very low anti-HAV response. A seropositive rhesus monkey was inoculated with monkey adapted strain of HAV to boost the anti-HAV antibody titre. Anti-HAV IgGs derived from hyperimmune sera of monkey and hepatitis A patient were conjugated with HRP. The preparations of conjugate--particularly human antibody--HRP conjugate yielded highly satisfactory results in anti-HAV capture ELISA. The assay appears to be specific, sensitive and quick and is useful in differentiating acute HAV infection from other acute infections caused by B, E and non-A non-B hepatitis viruses.

Authors : Chitambar S D, Murthy-Grewal S, Bokil M, Arankalle V A, Gore M M, Banerjee K,

(9) Expression cloning of complementary DNA encoding three distinct isoforms of guinea pig Fc receptor for IgG1 and IgG2.[TOP]

Pubmed ID :8345193
Publication Date : //
Three cDNA clones encoding the guinea pig Fc receptor for IgG1 and IgG2 (Fc gamma 1/gamma 2 R) have been isolated by an expression cloning strategy using mAb directed against the receptor. When transfected into COS-7 cells, these cDNA induced cell surface expression of the receptor that bound IgG1 and IgG2 antibodies complexed with the Ag. The ligand-binding affinities of these receptors were indistinguishable. Nucleotide sequencing has indicated that one of these clones, Fc gamma 1/gamma 2R-B1, is identical to the previously isolated cDNA clone homologous to the b2 isoform of human Fc gamma RIIB and that of murine Fc gamma RII, encoding a transmembrane glycoprotein containing two Ig-like extracellular domains. Two other clones, Fc gamma 1/gamma 2R-B2 and -B3, are identical to Fc gamma 1/gamma 2R-B1 except for an inframe insertion in the cytoplasmic region. The 48-nucleotide insertion found in Fc gamma 1/gamma 2R-B2 is identical to the first 48 nucleotides of the B3 insert that comprises 132 bp. Based on the size and homology of the inserted sequence, Fc gamma 1/gamma 2R-B2 and -B3 are identified as the homologues of the b1 isoform of human Fc gamma RIIB and that of murine Fc gamma RII, respectively. Reverse transcription and polymerase chain reaction of RNA revealed that macrophages and polymorphonuclear leukocytes expressed preferentially Fc gamma 1/gamma 2R-B1. On the other hand, B lymphocytes expressed all three forms, among which Fc gamma 1/gamma 2R-B2 and -B3 were selectively expressed in LPS-activated B lymphocytes that showed a dramatic increase in the levels of cell surface expression of Fc gamma 1/gamma 2R. These results suggest that the inserted sequences of Fc gamma 1/gamma 2R-B2 and -B3 are important to generate responses specific for B lymphocytes, which may include regulation of cell activation.

Authors : Yamashita T, Shinohara K, Yamashita Y,

(10) Neutralizing human monoclonal antibodies against Puumala virus, causative agent of nephropathia epidemica: a novel method using antigen-coated magnetic beads for specific B cell isolation.[TOP]

Pubmed ID :7687648
Publication Date : //
Human monoclonal antibodies (MAbs) against Puumala (PUU) virus were generated and characterized. Human spleen B lymphocytes were preselected for specific surface immunoglobulin (Ig) using magnetic beads coated with the viral glycoproteins, and subsequently immortalized by Epstein-Barr virus transformation. Four IgG-positive monoclonal lymphoblastoid cell lines (LCLs) were established and have remained stable MAb secretors for over 12 months. Analyses of the antigen and epitope specificities recognized by the MAbs showed overlapping binding patterns of four anti-glycoprotein 2-specific clones. Identical isotypes (IgGl lambda) and isoelectric points (9.2) of the four MAbs suggested that they were derived from the same original clone. The MAbs reacted with eight PUU virus-like strains, but were negative for Hantaan, Seoul, and Prospect Hill viruses in an immunofluorescence assay, indicating binding to a conserved epitope unique for strains associated with the European form of haemorrhagic fever with renal syndrome, nephropathia epidemica. The MAbs neutralized all investigated PUU virus-like strains in a focus reduction neutralization test. The MAb neutralizing activity was significantly enhanced in the presence of human or guinea-pig complement. To stabilize and increase antibody secretion and to reduce the demand for culture medium supplements (e.g. fetal calf serum), three of the monoclonal LCLs were fused with the non-secreting human x mouse partner SPAM-8. Several of the established human x (human x mouse) monoclonal triomas grew faster and produced larger amounts of MAbs when compared with the original LCLs.

Authors : Lundkvist A, Hörling J, Athlin L, Rosén A, Niklasson B,