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Перевод: antiserum
иммунная сыворотка
Тезаурус:
- Addition of anti-peptide A, but not the preimmune serum, causes either a supershift and concomitant reduction in DRTF1a, b and c (Fig. 2 b , antiserum 3; compare tracks 1 and 2) or abolishes all DRTF1 complexes (Fig. 2 b , antiserum 4; compare tracks 5 and 6).
- Immunoblotting affinity-purified DRTF1/E2F with anti-peptide 15 revealed two polypeptides with apparent M r s 46K and 55K (Fig. 2 a , track 2) that were recognized by the antiserum (Fig. 2 a ; compare tracks 5 and 6).
- Immunohistochemical staining using antiserum reacting against complement factor C3d was used to visualize neuritic plaques.
- Therefore we used anti-peptide 18 (Fig. 2 e ; antiserum 11), representing sequence from the DNA-binding domain of DP-1, which specifically inhibits the DNA-binding activity of affinity-purified DRTF1/E2F (Fig. 2 c ; compare tracks 11, 12).
- The foal is given a health check and normally given a routine antibiotic and tetanus antiserum as well as an enema to aid the passing of meconium.
- Similar results were obtained when a rabbit anti-ribophorin I antiserum or immunoadsorbant-purified rat IgG2a monoclonal antibodies against the KDEL tetra- peptide were used to label the ER in double-labelling experiments with anti-Bcl-2 antibody (not shown).
- When anti-peptide A was incubated with affinity-purified DRTF1/E2F, a supershift was apparent (Fig. 2 c ; compare tracks 1, 2 and 5, 6; clearest for antiserum 3).
- The sections were then overlaid with peroxidase-conjugated swine anti-rabbit antiserum (Dakopatts) at a dilution of 1 in 100 in Tris buffer for 1h at room temperature, washed three times with Tris buffer and the bound antibody complex visualized using diaminobenzidine (Sigma; 60mg per 100ml in Tris containing 40l 30% v/v H 2 O 2 ).
- Brain sections were incubated for 1h with rabbit polyclonal C3d antiserum (Dakopatts) at a dilution of 1 in 100 in 50mM Tris-HCl, pH7.4, containing 200mM NaCl in a closed chamber at room temperature, followed by three 5-min washes in the same Tris buffer.
- ER proteins were labelled with a rabbit polyclonal antiserum against rough ER proteins (diluted 1:100).
- When, however, the cells were double-labelled with the anti-Bcl-2 antibody and either human autoantibodies against a set of mitochondrial proteins or a rabbit antiserum against ER proteins, it could be seen that Bcl-2 was present in the mitochondria (Fig. 3e, f), as well as in the nuclear envelope and ER (Fig. 3c, d).
- Antisera recognizing rat TAP1 (ref. 5) and a new, previously undescribed antiserum raised against the rat TAP2 C-terminal sequence EQDVYAHLVQQRLEA were used at a 1/1,000 dilution.
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