نتایج جستجو برای: blots
تعداد نتایج: 5091 فیلتر نتایج به سال:
The core complex, formed by the SNARE proteins synaptobrevin 2, syntaxin 1 and SNAP-25, is an important component of the synaptic fusion machinery and shows remarkable in vitro stability, as exemplified by its SDS-resistance. In western blots, antibodies against one of these SNARE proteins reveal the existence of not only an SDS-resistant ternary complex but also as many as five bands between 6...
The Journal of Experimental Medicine regrets that due to a production error, the original version of this paper included incorrect labels to the right of the blots in Fig. 8 B. The legend remains correct, and the corrected figure appears below. The online HTML and PDF versions of this article have been corrected. The error only remains in the print version.
Rabbit antiserum was generated against the N-terminus of human GPR30 followed by peptide affinity purification. In this article, the methodology used and validation data are presented. The peptide affinity purified polyclonal antibody specifically detects human GPR30 in ELISA and on western blots of total protein prepared from human breast cancer cell lines.
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cDNA clones for rat muscle carbonic anhydrase III have been isolated from a lambda gt-11 library and sequenced. Comparison with human CAIII cDNA showed about 90% homology to rat. The rat clones were used to estimate mRNA from liver and muscle on Northern blots and showed that the sexual dimorphism of CAIII in rat liver relates to a difference in mRNA levels.
Ureaplasma urealyticum is an organism considered susceptible to tetracycline. Ten tetracycline-resistant (Tcr) clinical isolates and Tcr serotype 9 were examined. All contained DNA sequences homologous to the streptococcal determinant tetM. They differed from each other on sodium dodecyl sulfate-polyacrylamide gel electrophoresis, Southern blots, and immunoblots and appeared to represent differ...
A toxic shock syndrome toxin 1 (TSST-1) antibody-binding protein produced by an ovine-associated strain of Staphylococcus aureus was examined. The protein showed total identity to TSST-1 by immunodiffusion analysis. Western blots (immunoblots) of proteins separated by isoelectric focusing revealed that the TSST-1 antibody-binding protein had a pI of 8.6 rather than 7.0, the pI of standard TSST-1.
Polyclonal antibodies raised against 4-phosphothiophen-2-yl alanine 2a, a novel five-membered ring analogue of phosphotyrosine, showed high selectivity for phosphotyrosine and no cross-reactivity with other phosphorylated amino acids. Western blots showed that the polyclonal was similarly effective, but different in selectivity, to a commercially available monoclonal antibody.
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