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IgG (Fc), Goat anti_; ELISA

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[#YSRTSTAR157] IgG (Fc), Goat anti_; ELISA


YSRTSTAR157 | IgG (Fc), Goat anti_; ELISA, 0.5 mg.
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(1) Enzyme-assisted polymer film degradation-enabled biomolecule sensing with poly (N-isopropylacrylamide)-based optical devices.[TOP]

Pubmed ID :29254565
Publication Date : //
A biosensor for mouse Immunoglobulin G (IgG) was generated from responsive polymer-based interference filters (etalons). To accomplish this, an excess amount of alkaline phosphatase-modified goat anti-mouse IgG (AP-GAM, F(ab') fragment specific to mouse IgG) was added to mouse IgG, and allowed to react for some time. After a given reaction time, the bound AP-GAM could be isolated from the unbound, excess AP-GAM by addition of goat anti-mouse IgG (Fc fragment specific)-modified magnetic microspheres (GAM-M) that bind the mouse IgG bound to AP-GAM. After application of a magnetic field, the free, unbound AP-GAM was isolated from the mixture and exposed to an etalon that has its upper Au surface modified with phosphate-containing polymer that can be degraded by AP-GAM. By the phosphate-containing polymer being degraded by the excess AP-GAM, the cleaved phosphate groups can diffuse into the interference filter's active polymer layer that yields a change in the optical properties that can be related to the amount of IgG in the sample. This concept is extremely straightforward to implement, and can be modified to detect a variety of other analytes of interest.

Authors : Zhang Wei, Wei Menglian, Carvalho Wildemar S P, Serpe Michael J,

(2) SCM, the M Protein of Binds Immunoglobulin G.[TOP]

Pubmed ID :28401063
Publication Date : //
The M protein of (SCM) is a virulence factor and serves as a surface-associated receptor with a particular affinity for mini-plasminogen, a cleavage product of the broad-spectrum serine protease plasmin. Here, we report that SCM has an additional high-affinity immunoglobulin G (IgG) binding activity. The ability of a particular isolate to bind to IgG significantly correlates with a -positive phenotype, suggesting a dominant role of SCM as an IgG receptor. Subsequent heterologous expression of SCM in non-IgG binding and Western Blot analysis with purified recombinant SCM proteins confirmed its IgG receptor function. As expected for a zoonotic agent, the SCM-IgG interaction is species-unspecific, with a particular affinity of SCM for IgGs derived from human, cats, dogs, horses, mice, and rabbits, but not from cows and goats. Similar to other streptococcal IgG-binding proteins, the interaction between SCM and IgG occurs via the conserved Fc domain and is, therefore, non-opsonic. Interestingly, the interaction between SCM and IgG-Fc on the bacterial surface specifically prevents opsonization by C1q, which might constitute another anti-phagocytic mechanism of SCM. Extensive binding analyses with a variety of different truncated SCM fragments defined a region of 52 amino acids located in the central part of the mature SCM protein which is important for IgG binding. This binding region is highly conserved among SCM proteins derived from different isolates but differs significantly from IgG-Fc receptors of and sub. , respectively. In summary, we present an additional role of SCM in the pathogen-host interaction of . The detailed analysis of the SCM-IgG interaction should contribute to a better understanding of the complex roles of M proteins in streptococcal pathogenesis.

Authors : Bergmann Simone, Eichhorn Inga, Kohler Thomas P, Hammerschmidt Sven, Goldmann Oliver, Rohde Manfred, Fulde Marcus,

(3) Construction and measuring combination of KDR-targeted ultrasound contrast agent in vitro for evaluating endometrial receptivity.[TOP]

Pubmed ID :26524805
Publication Date : //
To investigate the preparation of a new kind of targeted lipid ultrasound contrast agent with anti-KDR antibody based on biotin-avidin bridge (MB-BAB-KDR) which could combine specifically with KDR that increases during the time of embryo implantation. Then its binding capability in vitro was evaluated.

Authors : Han X, Chen Y, Yang L, He Y, Chen M, Liu H,

(4) Detection of leukemia markers using long-range surface plasmon waveguides functionalized with Protein G.[TOP]

Pubmed ID :26374150
Publication Date : //
A novel optical biosensor based on long-range surface plasmon-polariton (LRSPP) waveguides is demonstrated for the detection of leukemia markers in patient serum using a functionalization strategy based on Protein G. The sensor consists of thin straight Au waveguides (5 μm × 35 nm × 3.2 mm) embedded in fluoropolymer CYTOP™ with a fluidic channel etched into the top cladding. B-cell leukemia is characterized by a high B-cell count and abnormal distribution of immunoglobulin G kappa (IgGκ) and lambda (IgGλ) light chains in serum. The detection of leukemic abnormalities in serum was performed based on determining IgGκ-to-IgGλ ratios (κ : λ). Three patient sera were tested: high kappa (HKS, κ : λ ~12.7 : 1), high lambda (HLS, λ : κ ~6.9 : 1) and normal (control) sera (NS, κ : λ ~1.7 : 1). Au waveguides were functionalized with Protein G and two complementary immobilization approaches were investigated: a) the reverse approach, where the Protein G surface is functionalized with patient serum and then tested against goat anti-human IgG light chains in buffer, and b) the direct approach, where the Protein G surface is functionalized with goat anti-human IgGs first and then tested against patient serum. The reverse approach was found to be more effective and robust because Protein G-functionalized surface performs as an "immunological filter" by capturing primarily IgGs out of the pool of serum proteins. For the reverse approach, the ratios measured were 3.7 : 1(κ : λ), 9.7 : 1(λ : κ) and 1.9 : 1(κ : λ) for HKS, HLS and NS, respectively, which compare favorably with corresponding protein densitometry measurements. The respective ratios for the direct approach were 2.6 : 1(κ : λ), 2.6 : 1(λ : κ) and 1.7 : 1(κ : λ). The binding strength and cross-reactivity of goat anti-human IgGs light chains were also determined using pure solutions. The LRSPP biosensor along with the innovative "reverse approach" can provide a low-cost and compact solution to B-cell leukemia screening.

Authors : Krupin O, Wang C, Berini P,

(5) Application of bispecific antibody against antigen and hapten for immunodetection and immunopurification.[TOP]

Pubmed ID :24071736
Publication Date : //
We present a bispecific antibody that recognizes an antigen and a hapten and can be applied to various biological assays, including immunoblotting and immunoprecipitation. In immunoblot analysis of serum, an anti-C5 × anti-cotinine bispecific tandem single-chain variable fragment (scFv)-Fc fusion protein and cotinine-conjugated horseradish peroxidase (HRP) generated a clean signal without the high background that was observed in a parallel experiment using HRP-conjugated goat anti-rabbit immunoglobulin G (Fc-specific) antibody. In immunoprecipitation analysis of serum, use of the bispecific tandem scFv-Fc fusion protein and cotinine-crosslinked magnetic beads significantly reduced the amount of protein contaminants compared with a parallel experiment done with protein A agarose beads. In subsequent immunoblot analysis, use of cotinine-HRP as the secondary probe instead of HRP-conjugated goat anti-rabbit IgG (Fc-specific) antibody successfully eliminated the band corresponding to the bispecific tandem scFv-Fc fusion protein.

Authors : Kim Hyori, Park Sunyoung, Lee Hwa Kyoung, Chung Junho,

(6) Development of a biosensor-based immunogenicity assay capable of blocking soluble drug target interference.[TOP]

Pubmed ID :23933325
Publication Date : //
As with other protein therapeutics, trebananib (AMG 386), an investigational peptide Fc-fusion protein ("peptibody") that inhibits angiogenesis by neutralizing the interaction of angiopoietin-1 (Ang1) and angiopoietin-2 (Ang2) with the Tie2 receptor, has the potential to trigger an immune response in cancer patients treated with the therapeutic. An electrochemiluminescence bridging anti-drug antibody (ADA) assay that was utilized to support early-phase clinical trials in the development of trebananib was found to lack adequate sensitivity and drug tolerance in later-phase clinical studies when higher doses of trebananib were administered. Therefore, we developed a surface plasmon resonance (SPR) immunoassay method utilizing a secondary confirmatory detector antibody (goat anti-human IgG F[ab']2) known to cross-react with human IgG and IgM to better assess the potential impact of immunogenicity on the pharmacokinetics, pharmacodynamics, and toxicity of trebananib. The SPR method was more sensitive than the electrochemiluminescence bridging assay because of signal amplification from the confirmatory binding of the detector antibody; drug tolerance was improved since antibody binding avidity does not affect detection on this platform. Despite the inability of the confirmatory detector antibody to bind angiopoietins in protein-free buffer, false-positive ADA results were generated from patient serum samples containing Ang1 and Ang2 through an apparently specific binding between the angiopoietins and the confirmatory detector antibody, likely mediated by the interaction of the angiopoietins with serum immunoglobulins. Addition to the sample diluent of a human antibody that specifically binds to Ang1 and Ang2 with high affinity resulted in a complete block of angiopoietin interference without affecting ADA detection. This biosensor-based assay provides a reliable method for assessing immunogenicity in phase 3 clinical trials.

Authors : Weeraratne Dohan K, Lofgren James, Dinnogen Steve, Swanson Steven J, Zhong Zhandong Don,

(7) Well-oriented ZZ-PS-tag with high Fc-binding onto polystyrene surface for controlled immobilization of capture antibodies.[TOP]

Pubmed ID :23601284
Publication Date : //
The site specificity and bioactivity retention of antibodies immobilized on a solid substrate are crucial requirements for solid phase immunoassays. A fusion protein between an immunoglobulin G (IgG)-binding protein (ZZ protein) and a polystyrene-binding peptide (PS-tag) was constructed, and then used to develop a simple method for the oriented immobilization of the ZZ protein onto a PS support by the specific attachment of the PS-tag onto a hydrophilic PS. The orientation of intact IgG was achieved via the interaction of the ZZ protein and the constant fragment (Fc), thereby displayed the Fab fragment for binding antigen. The interaction between rabbit IgG anti-horseradish peroxidase (anti-HRP) and its binding partner HRP was analyzed. Results showed that the oriented ZZ-PS-tag yielded an IgG-binding activity that is fivefold higher than that produced by the passive immobilization of the ZZ protein. The advantage of the proposed immunoassay strategy was demonstrated through an enzyme-linked immunosorbent assay, in which monoclonal mouse anti-goat IgG and HRP-conjugated rabbit F(ab')2 anti-goat IgG were used to detect goat IgG. The ZZ-PS-tag presented a tenfold higher sensitivity and a wider linear range than did the passively immobilized ZZ protein. The proposed approach may be an attractive strategy for a broad range of applications involving the oriented immobilization of intact IgGs onto PS supports, in which only one type of phi-PS (ZZ-PS-tag) surface is used.

Authors : Tang Jin-Bao, Sun Xi-Feng, Yang Hong-Ming, Zhang Bao-Gang, Li Zhi-Jian, Lin Zhi-Juan, Gao Zhi-Qin,

(8) Measurement of the localised plasmon penetration depth for gold nanoparticles using a non-invasive bio-stacking method.[TOP]

Pubmed ID :23503322
Publication Date : //
We have used the formation of a bio-probe stack with up to 24 steps on gold nanoparticle and continuous gold surfaces to characterize the penetration depth of the plasmon field in a non-invasive manner by only involving biomolecules from standard bio-assays. An alternating anti-goat rabbit IgG and anti-rabbit IgG bio-probe stack is polymerized on protein A/G functionalized gold surfaces. The change in plasmon excitation angle or light scattering decreases exponentially with each stacking step although the bio-integrity of the antibody epitope is maintained. The exponential decay in the derived kinetic parameters is attributed to the change in the penetration depth and the step size is calibrated using a commercial continuous gold surface plasmon resonance surface to be 17.5 ± 0.8 nm, consistent with the expected dimension of the antibody. The penetration depth of the gold spherical nanoparticles of diameter 90 ± 13 nm is determined to be 93 ± 10 nm.

Authors : Read Thomas, Olkhov Rouslan V, Shaw Andrew M,

(9) [Optimal expression and activity detection of recombinant, chimeric and genetically engineered tetravalent anti-human CD22 antibodies in P.pastoris].[TOP]

Pubmed ID :22691356
Publication Date : //
To express the recombinant, chimeric and genetically engineered tetravalent anti-human CD22 antibodies (cRFB4FC and cRFB4CH3) using yeast cells secreting type carrier pPIC9K, and screen for optimal conditions of engineered yeast cells expressing cRFB4FC and cRFB4CH3.

Authors : Shi Sheng, Zhong Hua, Ma Ling, Nong Jiang, Bai An-bin, Chen Feng-lian, Wu Jian-min,

(10) A novel hypothesis for the etiology of Graves' disease: TSAb may be thyroid stimulating animal IgG-like hormone and TBAb may be the precursor of TSAb.[TOP]

Pubmed ID :22472575
Publication Date : //
There are doubtful points about the theory that autoimmunity with auto-antibody (Ab) to TSH receptor (R) causes hyperthyroidism in Graves' disease (GD). A main doubtful point is no curative effect of corticosteroid on Graves' hyperthyroidism in spite of curative effect of corticosteroid for all autoimmune diseases. Recently we demonstrated the immunological similarity of TSAb and TBAb-IgG to animal IgGs, except for human (h)IgG, by neutralization and purification of TSAb and TBAb-IgG using (1) heterophilic Ab to animal IgG in GD sera and (2) experimentally generated anti-animal IgG Abs [such as dog (d), bovine (b), porcine (p), and rabbit (rb)]. Furthermore, greater immunological similarity of Fab- and F(ab')(2)-portion of TSAb- and TBAb-IgG to bovine Fab, compared to hFab, was demonstrated using goat anti-bovine F(ab')(2) Ab. Existence of b and p TSH-like portions in the LATS-IgG molecule (probably Fab portion) was suggested by a previous report of neutralization of LATS activity by anti-b- or anti-p-TSH Ab. We suggested the existence of a mammalian animal-TSH-like structure, excepting hTSH, in the TSAb-IgG molecule (probably Fab portion), by discovery of anti-mammalian TSH Ab (such as d, b, p, guinea-pig, rat, whale, except h) in sera of GD. Lately, similar TSHR binding of H- and L-chain of human stimulating monoclonal TSHR Ab (M22)-Fab with TSH-α and-β subunit was reported. This evidence suggests that Fab portion of TSAb has a structure like mammalian TSH, but not hTSH. IgG-λ type of d, horse, b, p, goat, ovine is 95% and IgG-κ type is 5%, while human κ and λ chain is 60:40. Previous report that LATS (TSAb)-IgG composed of predominant λ type is supporting evidence that TRAb-IgG has immunological similarity with these animal IgGs compared to hIgG. We speculate that TSAb-IgG may be referred as a mermaid consisted in face (Fab) and trunk-leg (Fc). Face may be a kind of hormone with animal TSH-like structure and trunk-leg has animal IgG-like structure (in spite of no antibody function). There are many reports for co-existence of TSAb and TBAb-IgG in sera of GD. We reported conversion from TBAb (non-thyroid stimulating type IgG) to TSAb by co-incubation of anti-hIgG Ab (containing anti-animal IgG Ab as a cross-reaction) with TBAb-bound porcine thyroid cells. Thus, we suggest that TBAb may be the precursor form of TSAb.

Authors : Ochi Yukio, Kajita Yoshihiro, Hachiya Takashi, Hamaoki Masaru,