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Search results for: Anti-human Apolipoprotein Apolipoprotein-H (β2-Glycoprotein-I) Antibody

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#18494923   // To Up

Detection and quantification of apocrine secreted odor-binding protein on intact human axillary skin.

A proposed mechanism of axillary malodor formation is bacterial interaction with secreted odor carrier proteins leading to the release of volatile odor molecules. One primary volatile odor molecule, 3-methyl-2-hexenoic acid, is secreted into the apocrine glandular lumen bound to two carrier proteins known as apocrine secretion odor-binding proteins (ASOB1 and ASOB2). The objective of this study was to develop a biologic method to detect and quantify ASOB2 in vitro and on intact axillary skin. The proteins present in pure apocrine secretion were separated via SDS-polyacrylamide gel electrophoresis (PAGE), electro-blotted, and reacted with antibodies to detect ASOB2. The results of this study demonstrate that ASOB2 shares immunologically homologous epitopes with the human serum protein, apolipoprotein-D (apo-D). Axillary secretions and baseline microflora were collected from two groups of panelists 6 h after showering with a non-antibacterial soap. The extracts were fractionated by SDS-PAGE. ASOB2 was detected selectively by Western blot using a monoclonal mouse-antihuman apo-D antibody and quantified on human axillary skin using the presented methods. Axillary ASOB2 concentration varied among individuals (<0.1-4.1 microg cm(-2)) with significant differences (P < 0.05, anova) seen between those of Chinese descent and non-Chinese descent. Panelists of Chinese ancestry did not show significantly lower baseline microflora levels when compared to non-Chinese panelists.
R B Jacoby, J C Brahms, S A Ansari, J Mattai

1951 related Products with: Detection and quantification of apocrine secreted odor-binding protein on intact human axillary skin.

100 μg 100ul20 μg1000 TESTS/0.65ml0.1 mg0.1 mg1 mg200 100ul 100ul1 mg 100ul

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#11989785   // To Up

Apolipoprotein C polymorphism in sheep: allele frequencies and association with plasma lipid and lipoprotein levels.

The genetic polymorphism of apolipoprotein C in normal plasma of four European sheep breeds (Suffolk, Corriedale, Cheviot, and Finn) was first detected using one-dimensional polyacrylamide gel isoelectric focusing (pH 2.5-5.0) followed by immunoblotting with antihuman apolipoprotein CII antibody. Six phenotypes (1-1, 2-1, 2-2, 3-1, 3-2, and 3-3) were identified in the 4.3-4.8 pH range, consisting of the combination of three isoform groups. On the basis of family and population data, these phenotypes were controlled autosomally by three codominant alleles, designated APOC*1, APOC*2, and APOC*3, the first being the most common allele. The frequency distributions of these alleles were similar between the Suffolk and Corriedale sheep, and between the Cheviot and Finn sheep. The former breeds had a significantly lower APOC*2 frequency than the latter breeds (P < 0.001). The mean plasma total-, HDL- and LDL-cholesterol levels of type 3-1 animals were significantly higher compared to type 1-1 animals in the Suffolk sheep (P < or = 0.04). However these differences were not seen in the Corriedale sheep.
Kenji Tsunoda, Shohei Hamato, Shoei Kurosawa, Ayako Shirato, Yaetsu Kurosawa, Koichiro Fujimaki, Masahiro Muto, Keizo Sato

1852 related Products with: Apolipoprotein C polymorphism in sheep: allele frequencies and association with plasma lipid and lipoprotein levels.

10 mg100 mg100 mg2.5 mg25 mg10 mg100 µg25 mg100 mg

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#10936581   // To Up

Simple and practical sandwich-type enzyme immunoassay for human oxidatively modified low density lipoprotein using antioxidized phosphatidylcholine monoclonal antibody and antihuman apolipoprotein-B antibody.

To develop a simple and practical enzyme immunoassay (EIA) for oxidatively modified low density lipoprotein (Ox-LDL) in human blood, a biological marker of atherogenesis.
H Kohno, N Sueshige, K Oguri, H Izumidate, T Masunari, M Kawamura, H Itabe, T Takano, A Hasegawa, R Nagai

2791 related Products with: Simple and practical sandwich-type enzyme immunoassay for human oxidatively modified low density lipoprotein using antioxidized phosphatidylcholine monoclonal antibody and antihuman apolipoprotein-B antibody.

100 TESTS0.2 mg0.2 mg1 kit25 µg25 µg0.25 mg1 ml0.1mg 100ul 100ul

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#1356662   // To Up

A simple, sensitive technique for classification of apolipoprotein(a) isoforms by sodium dodecyl sulphate-polyacrylamide gel electrophoresis.

Lipoprotein(a) (Lp(a)) is a lipoprotein containing a unique glycoprotein, apolipoprotein(a) (apo(a)), which shows considerable heterogeneity of apparent molecular mass on sodium dodecyl sulphate-polyacrylamide gel electrophoresis (SDS-PAGE). A unifying classification of isoform has been lacking. A simple sensitive procedure for classifying apo(a) isoforms was developed in which the relative mobility of apo(a) on SDS-PAGE was related to that of apolipoprotein (apo) B-100 (Rf vs B). After Western blotting apo(a) bands were visualised by a sensitive double antibody technique employing commercial polyclonal antibodies (sheep antihuman Lp(a) antibody, alkaline phosphatase-linked donkey antisheep antibody). The technique was sensitive (lower limit of detection 0.02 micrograms apo(a)) and had good reproducibility (coefficient of variation 0.9-6.4%). Ten isoform mobilities are described (less than 0.35, 0.40, 0.50, 0.60, 0.70, 0.80, 1.0, 1.10, greater than 1.15). Individuals may have single or double band phenotypes. This classification is compatible with those previously described and the method is suitable for many laboratories, as it employs standard equipment and commercially available materials.
M Farrer, F L Game, P C Adams, M F Laker, K G Alberti

2137 related Products with: A simple, sensitive technique for classification of apolipoprotein(a) isoforms by sodium dodecyl sulphate-polyacrylamide gel electrophoresis.

100ug1mg10 mg 25 G1 mg1 ml250 ml1 g100ug20 ug100μg0.5mg

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#2082049   // To Up

[Glomerular apolipoprotein B deposition in glomerular diseases].

In an attempt to elucidate the relationship between the progress of glomerular injury and abnormalities of lipid metabolism, we investigated glomerular deposition of apolipoprotein B (apo B) in renal biopsy specimens from 60 patients with glomerular diseases by indirect immunofluorescence using antihuman apo B-100 monoclonal antibody in comparison with clinical and histopathological findings. The patients were divided into 2 groups according to the intensity in staining of apo B in glomerulus (group A: negative or weakly positive; and group B: definitely positive). Staining of apo B in glomerulus was found in 37 patients (62%). The levels of serum total cholesterol, phospholipids, low density lipoprotein cholesterol and apo B in group B were significantly higher than in group A. The urinary protein excretion in group B was greater than that in group A. Group B was also shown to have a significantly decrease in renal function. Light microscopy revealed severe mesangial proliferation in patients with IgA nephropathy of group B. These findings suggested that glomerular apo B containing-lipoprotein deposition may play an important role in the progression of glomerular injury.
H Ohtani, K Matoba, Y Saika, R Tanaka, Y Yamada, K Bando, T Takahashi, M Mune, S Yukawa, H Nomoto

2786 related Products with: [Glomerular apolipoprotein B deposition in glomerular diseases].

50 UG100 mg100ug100 ml

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#3780392   // To Up

[The preparation of antihuman apolipoprotein B antisera and its clinical application].


X Zhou, H Z Zhang, Y L Yin

2535 related Products with: [The preparation of antihuman apolipoprotein B antisera and its clinical application].

0.1mg0.1ml (1mg/ml) 100ul 100ul 100ul100ug Lyophilized100ug Lyophilized0.1ml 100ul100 100ug Lyophilized

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#6208304   // To Up

Evolution of low density lipoprotein structure probed with monoclonal antibodies.

To assess the relationship of apoB structures in different species of animals, the expressions of apoB epitopes in the sera or plasmas of 23 different mammalian species and one marsupial, and on the low density lipoprotein (LDL) from three species of apes, six species of monkeys, and eight non-primates were measured in competitive radioimmunoassays. The abilities of the sera or LDL to compete with 125I-labeled human LDL for binding to seven monoclonal antihuman LDL antibodies immobilized on microtiter plates were determined. LDL of apes bound to most antibodies, while monkey LDL bound to two or three antibodies. Other mammalian LDL bound only weakly to two of the antibodies or to none. The two monoclonal antibodies binding the LDL of more species were those antibodies which also inhibited the binding to and degradation of LDL by human fibroblasts. The rank order of binding of the LDL of a given species to the antibodies correlated with the rank order inhibition of binding and degradation of 125I-labeled human LDL in the human fibroblast system. This suggests that epitopes spatially located near the recognition site of apoB for cellular receptors have a greater tendency to be conserved.
C A Nelson, M A Tasch, M Tikkanen, R Dargar, G Schonfeld

1118 related Products with: Evolution of low density lipoprotein structure probed with monoclonal antibodies.

50 1ml100.00 ug100.00 ug100 ul Product tipe: Anti200 ug1 mg100 ug1 mg200 ug100.00 ug100.00 ug

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