Search results for: Rabbit Anti-phospho-cardiac Troponin I(Thr143) Polyclonal Antibody
#18402291 2008/04/11 Save this To Up
Native troponin-T of the American cockroach (CR), Periplaneta americana, binds to IgE in sera of CR allergic Thais.The American cockroach, Periplaneta americana, is the predominant cockroach (CR) species in Thailand and a major source of indoor allergens second only to the house dust mite. The incidence of CR allergy among allergic Thai patients is increasing but basic information on the allergenic components is scarce. In this study a recombinant troponin-T was produced by using cDNA prepared from RNA of the P. americana as a template and PCR primers designed from the P. americana troponin-T sequence deposited in the GenBank database. The recombinant protein (Mr approximately 50) did not bind to IgE in the sera of 18 skin prick test positive CR allergic patients. Rabbit polyclonal antiserum (PAb) against the recombinant troponin-T was produced and used in preparing an affinity column for the purification of native troponin-T from the crude P. americana extract (Mr approximately 47). IgE-immunoblotting revealed that the native protein bound to IgE in 3 of the 18 (16.7%) patients. Our results imply that native P. americana troponin-T, but not its recombinant counterpart, is a minor allergen among the CR allergic Thais.
2137 related Products with: Native troponin-T of the American cockroach (CR), Periplaneta americana, binds to IgE in sera of CR allergic Thais.Native Influenza HA (A To Native Influenza HA (A To Native Influenza HA (A To FDA Standard Frozen Tissu FDA Standard Frozen Tissu FDA Standard Frozen Tissu FDA Standard Frozen Tissu BIBW2992 (Tovok); Appeara BIBW2992 (Tovok); Appeara Recombinant Human Interfe Native Influenza HA (A Ta Native Influenza HA (A Ta
#15989792 2005/07/01 Save this To Up
[Prokaryotic expression of human cTnI and preparation of rabbit anti-hcTnI antibody].To construct the prokaryotic expression vector pET-21a(+)-hcTnI and prepare the rabbit anti-hcTnI antibody using hcTnI expressed in E.coli as immunogen.
2163 related Products with: [Prokaryotic expression of human cTnI and preparation of rabbit anti-hcTnI antibody].Rabbit Anti-Human Androge Rabbit Anti-Human Androge Anti RAGE (Receptor for A Anti RAGE (Receptor for A Anti RAGE (Receptor for A Anti Galectin(Gal-3) Huma Anti Galectin(Gal 3) Huma Anti Galectin(Gal 3) Huma Rabbit Anti-Melanoma Mela Rabbit Anti-Melanoma Mela Rabbit Anti-Melanoma Mela Rabbit Anti-Melanoma Mela
#15607674 2004/12/20 Save this To Up
Granulocyte-colony stimulating factor directly enhances proliferation of human troponin I-positive cells derived from idiopathic dilated cardiomyopathy through specific receptors.Our previous study showed that granulocyte-colony stimulating factor (G-CSF) enhanced bone-marrow-cell migration into the injured heart and that bone-marrow cells differentiated into cardiomyocytes. However, the number of bone-marrow-derived cardiomyocytes seems too small to have a direct, positive impact on pump function. Therefore, we hypothesized that G-CSF directly could affect the host myocardium through G-CSF receptors (G-CSFRs).
2554 related Products with: Granulocyte-colony stimulating factor directly enhances proliferation of human troponin I-positive cells derived from idiopathic dilated cardiomyopathy through specific receptors.Human Granulocyte Macroph Human Granulocyte Colony Macrophage Colony Stimula Macrophage Colony Stimula Epidermal Growth Factor ( Epidermal Growth Factor ( Human Macrophage Colony S Macrophage Colony Stimula Macrophage Colony Stimula Macrophage Colony Stimula Macrophage Colony Stimula Mouse Granulocyte Colony
#12215382 2002/09/06 Save this To Up
A skeletal muscle troponin T specific ELISA based on the use of an antibody against the soluble troponin T (16-31) fragment.Proteolytic degradation of muscle, which occurs post-mortem as part of the meat-ageing process, results in the production of protein fragments. In beef, degradation of skeletal muscle troponin T (TnT) results in the generation of a 16-residue long peptide (TnT (16-31)), identified in trichloroacetic acid (TCA) soluble extracts. We report the development of a competitive enzyme-linked immunosorbent assay (ELISA) for the quantification of TnT (16-31), using polyclonal antibodies raised against synthetic TnT (16-31). The ELISA procedure is based on inhibition of binding of the antibodies to immobilised TnT (16-31) by TnT (16-31) present in solution. Its useful range is 30 pmol to 2 nmol TnT (16-31)/ml. Quantification of TnT (16-31) in TCA muscle extracts showed that its concentration was enhanced with ageing. Moreover, a correlation between TnT (16-31) levels and meat tenderness was observed. The ELISA developed herein may prove advantageous for future use at the research and industrial level.
1804 related Products with: A skeletal muscle troponin T specific ELISA based on the use of an antibody against the soluble troponin T (16-31) fragment.Troponin I antibody, Mono TCP-1 theta antibody Sour Beta Amyloid (40) ELISA K Beta Amyloid (1 42) ELISA Rabbit Anti-phospho-cardi Rabbit Anti-phospho-cardi Rabbit Anti-phospho-cardi Rabbit Anti-phospho-cardi Rabbit Anti-phospho-cardi Rabbit Anti-phospho-cardi Rabbit Anti-phospho-cardi Rabbit Anti-phospho-cardi
#9772180 1998/11/03 Save this To Up
Conformational modulation of troponin T by configuration of the NH2-terminal variable region and functional effects.Troponin T (TnT) is an essential element in the thin filament-based regulatory system of striated muscle. Alternative mRNA splicing generates multiple TnT isoforms with primary structural differences in the NH2-terminal region. The functional significance of this hypervariable NH2-terminal domain and the developmental or muscle type-specific TnT isoforms is not fully understood. We have analyzed chicken breast muscle TnT containing a metal-binding cluster [H(E/A)EAH]4-7 (Tx) in the NH2-terminal region to demonstrate potential effects of the NH2-terminal structure on the conformation of TnT [Ogut, O., and Jin, J.-P. (1996) Biochemistry 35, 16581-16590]. Using specific antibody epitope analysis on this metal-binding TnT model, this study revealed that the binding of Zn2+ to the NH2-terminal region of chicken breast muscle TnT induces extensive conformational changes in the whole protein as demonstrated by a significant decrease in binding avidity of a polyclonal anti-TnT serum which recognizes multiple epitopes on the TnT molecule. This NH2-terminal configuration-based effect is not restricted to the metal ion interaction, whereas the binding of anti-NH2 terminus monoclonal antibodies to TnT induced similar changes. Protein-binding assays have shown that the NH2-terminal variability-induced conformational changes can alter TnT's binding affinity for tropomyosin and troponin I. The results suggest a functional modulation of TnT through the configuration of the NH2-terminal domain, and this novel mechanism may mediate the physiological significance of the TnT isoform regulation.
2924 related Products with: Conformational modulation of troponin T by configuration of the NH2-terminal variable region and functional effects.Anti-Axin1 (C-terminal re Anti Axin1 (C terminal re BACTERIOLOGY BACTEROIDES Troponin I antibody, Mono Goat Anti- TRPM8, (intern Goat Anti- TFAP2D, (inter Goat Anti- T1R3, (interna Goat Anti-Human HMGB3 HMG Goat Anti-Human F2R PAR1, Goat Anti-Mouse APOBEC1, Rabbit Anti-Human Troponi Rabbit Anti-Human Troponi
#9316743 1997/11/06 Save this To Up
Analytical performance and clinical utility of a sensitive immunoassay for determination of human cardiac troponin I.To determine the serum and plasma level of human cardiac troponin I (cTnI) resulting from myocardial damage, we have developed a sensitive and specific one-step enzyme immunoassay to measure cardiac troponin I.
1828 related Products with: Analytical performance and clinical utility of a sensitive immunoassay for determination of human cardiac troponin I.Mouse Anti-Human Troponin Mouse Anti-Human Troponin Mouse Anti-Human Troponin Mouse Anti-Human Troponin Leptin ELISA Kit, Human A Mouse Anti-Human Troponin Mouse Anti-Human Troponin Mouse Anti-Human Troponin Mouse Anti-Human Troponin Mouse Anti-Human Troponin Mouse Anti-Human Troponin Mouse Anti-Human Troponin
#1862939 1991/08/30 Save this To Up
Monoclonal antibody to calmodulin: development, characterization, and comparison with polyclonal anti-calmodulin antibodies.Specific anti-calmodulin rabbit polyclonal and murine monoclonal antibodies have been produced with a thyroglobulin-linked peptide corresponding to amino acids 128-148 of bovine brain calmodulin. The monoclonal antibody is IgG-1 with kappa light chains. Both sets of antibodies recognize native vertebrate calmodulin, with the polyclonal antibody exhibiting an approximately fourfold higher sensitivity than the monoclonal antibody in a radioimmunoassay. The affinity of both polyclonal and monoclonal antibodies is approximately 2.5-fold higher for Ca(2+)-free calmodulin than for Ca(2+)-calmodulin. Other selected members of the calmodulin family (S100, troponin, and parvalbumin) do not exhibit significant cross-reactivity with the monoclonal antibody. Troponin and S100 beta displace some 125I-calmodulin from the polyclonal antibody, but require at least 900-fold excess concentration. The monoclonal antibody recognizes intact vertebrate calmodulin in solution and also on solid-phase. In addition, plant calmodulin and some forms of post-translationally modified calmodulin (phosphorylated or glycated) bind the monoclonal antibody. The affinity of the monoclonal antibody is approximately 5 x 10(8) liters/mol determined by displacement of 125I-calmodulin. On dot blotting the sensitivity for vertebrate calmodulin is 50 pg. The epitope for the monoclonal antibody is in the carboxyl terminal region (residues 107-148) of calmodulin. This highly specific anti-calmodulin monoclonal antibody should be a useful reagent in elucidating the mechanism by which calmodulin regulates intracellular metabolism.
2794 related Products with: Monoclonal antibody to calmodulin: development, characterization, and comparison with polyclonal anti-calmodulin antibodies.Anti AGO2 Human, Monoclon Anti AGO2 Mouse, Monoclon Anti AGO2 Human, Monoclon Anti Ago1, Monoclonal Ant Anti PIWIL1, Monoclonal A Anti AGO2 Mouse, Monoclon Anti Ago1, Monoclonal Ant Anti Human AGO3, Monoclon Signal Transduction Anti Signal Transduction Anti Shiga Toxin 1 antibody, M Shiga Toxin 2 antibody, M
#1692290 1990/06/12 Save this To Up
Competitive binding of the troponin T-specific pool of caldesmon antibodies and tropomyosin to skeletal troponin T and smooth muscle caldesmon.The fraction of polyclonal caldesmon antibodies cross-reacting with rabbit skeletal troponin T are shown to compete with smooth muscle tropomyosin for caldesmon and troponin T, as revealed by ELISA method. The epitope recognized by these antibodies was also found in Mr 77 kDa non-muscle caldesmon. These results provide functional confirmation for the suggestion that the regions of amino acid sequence homology in caldesmon isoforms and troponin T belong to the tropomyosin binding sites.
1154 related Products with: Competitive binding of the troponin T-specific pool of caldesmon antibodies and tropomyosin to skeletal troponin T and smooth muscle caldesmon.Rabbit Skeletal Muscle Tr Rabbit Skeletal Muscle Tr Rabbit Skeletal Muscle Tr Rabbit Anti-Rat Androgen Native Rat Troponin I (Sk Troponin I antibody, Mono Rabbit Anti-Human Troponi Rabbit Anti-Human Troponi Recombinant Human fast sk Recombinant Human fast sk Recombinant Human fast sk Mouse Anti-Human Troponin
#2318209 1990/05/08 Save this To Up
Fast and slow isoforms of troponin I and troponin C. Distribution in normal rabbit muscles and effects of chronic stimulation.Polyclonal antibodies were raised against troponin I (TnI) and troponin C (TnC) purified from fast-twitch and slow-twitch rabbit muscles. These antibodies were used to elucidate the distribution of fast and slow isoforms of TnI and TnC in normal and chronically stimulated rabbit hind limb muscles by immunoblots of one-dimensional and two-dimensional electrophoreses. In contrast to the multiplicity of fast and slow troponin T (TnT) isoforms, TnI and TnC were present as unique fast and slow isoforms. Whereas no charge variants were detected for slow TnI, fast TnI was present in at least three charge variants. As judged from the results of alkaline phosphatase digestion, these charge variants represent differently phosphorylated forms. Fast and slow TnC both exist as two charge variants which, however, were unaffected by alkaline phosphatase treatment. Chronic low-frequency stimulation of fast-twitch muscles induced progressive increases in the slow isoforms of TnC and TnI at the expense of their fast isoforms. The extent of the fast-to-slow transition was more pronounced in the case of TnC than in that of TnI. Long-term stimulated muscles with a complete fast-to-slow transition, at the level of the TnT isoforms, still contained fast and slow isoforms of both TnI and TnC. The coexistence of fast and slow isoforms of the three troponin subunits in the transforming muscle was interpreted as indicating the presence of hybrid troponin molecules composed of fast and slow isoforms. Studies at the mRNA level showed changes similar to those at the protein level. However, in long-term stimulated muscles, the fast-to-slow transition of TnI was more pronounced at the mRNA level than at the protein level.
2989 related Products with: Fast and slow isoforms of troponin I and troponin C. Distribution in normal rabbit muscles and effects of chronic stimulation.Androgen Receptor (Phosph Androgen Receptor (Phosph Rabbit Anti-Human Androge Rabbit Anti-Human Androge Androgen Receptor (Ab 650 Rabbit Anti-phospho-cardi Rabbit Anti-phospho-cardi Rabbit Anti-phospho-cardi Rabbit Anti-phospho-cardi Rabbit Anti-phospho-cardi Rabbit Anti-phospho-cardi Rabbit Anti-phospho-cardi
#2553122 1989/11/30 Save this To Up
Chicken skeletal muscle has three Ca2+-dependent proteinases.Chicken breast muscle has three Ca2+-dependent proteinases, two requiring millimolar Ca2+ (m-calpain and high m-calpain) and one requiring micromolar Ca2+ (mu-calpain). High m-calpain co-purifies with mu-calpain through successive DEAE-cellulose (steep gradient), phenyl-Sepharose, octylamine agarose, and Sephacryl S-300 columns, but elutes after mu-calpain when using a shallow KCl gradient to elute a DEAE-cellulose column. The mu- and m-calpains have 80 and 28 kDa polypeptides and are analogous to the mu- and m-calpains that have been purified from bovine, porcine and rabbit skeletal muscle. High m-calpain, which seems to be a new Ca2+-dependent proteinase, is still heterogeneous after the DEAE-cellulose column eluted with a shallow KCl gradient. Additional purification through two successive HPLC-DEAE columns and one HPLC-SW-4000 gel permeation column produces a fraction having six major polypeptides and 6-8 minor polypeptides on SDS-PAGE. A 74-76 kDa polypeptide in this fraction reacts in Western blots with monospecific, polyclonal anti-calpain antibodies that react with both the 80 kDa and the 28 kDa polypeptides of mu- or m-calpain. High m-calpain also is related to mu- and m-calpain in that it causes the same limited digestion of skeletal muscle myofibrils, has a similar pH optimum near pH 7.9-8.4, requires Ca2+ for activity, and reacts with the calpain inhibitor, calpastatin, and a variety of serine and cysteine proteinase inhibitors in a manner identical to mu- and m-calpain. High m-calpain differs from mu- and m-calpain in its elution off DEAE-cellulose columns and its requirement of 3800 microM Ca2+ for one-half maximal activity compared with 5.35 microM Ca2+ for mu-calpain and 420 microM Ca2+ for m-calpain. The physiological significance of high m-calpain in unclear. The presence of mu-calpain in chicken breast muscle suggests that all skeletal muscles contain both mu- and m-calpain, although the relative proportions of these two proteinases may vary in different species.
Rabbit Skeletal Muscle Tr Rabbit Skeletal Muscle Tr Rabbit Skeletal Muscle Tr Actin, Skeletal Muscle Ab Actin, Skeletal Muscle Ab Actin, Skeletal Muscle Ab Actin, Skeletal Muscle Ab Actin, Muscle Specific; Actin, Muscle Specific; Actin, Alpha-Smooth Musc Actin, Alpha-Smooth Musc Actin, Muscle Specific;
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