Search results for: Rabbit Anti-Human MIF Antibodies
#9576065 // To Up
Identification of macrophage migration inhibitory factor (MIF) in human vascular endothelial cells and its induction by lipopolysaccharide.
Cytokines play an important role in inflammation and immunity. In this study, the authors examined expression of macrophage migration inhibitory factor (MIF) in vascular endothelial cells, using human umbilical vein endothelial cells (HUVEC), by reverse transcription-polymerase chain reaction (RT-PCR)/Southern blot, Western blot analysis, and immunohistochemistry. The RT-PCR/Southern blot showed that MIF mRNA was exceedingly upregulated by the stimulation of lipopolysaccharide (LPS) and reached the maximum 12 h after the stimulation. At the range of 10 pg/ml to 10 ng/ml of LPS, the MIF mRNA expression was induced in a dose-dependent manner, but drastically decreased at doses of more than 100 ng/ml. Western blot analysis and immunohistochemistry using an anti-human MIF antibody revealed the presence of MIF protein in cytoplasm of the unstimulated cells. The precise pathophysiological role of MIF in HUVEC has not been fully understood; however, the upregulation of MIF mRNA expression in vascular endothelial cells by LPS stimulation suggests the possibility that the cytokine plays an important role in systemic inflammatory events such as endotoxaemia.J Nishihira, Y Koyama, Y Mizue
1292 related Products with: Identification of macrophage migration inhibitory factor (MIF) in human vascular endothelial cells and its induction by lipopolysaccharide.
5ug1 mg10 ug5 2ug x 202 1.00 flask1.00 flask5ug1.00 flask1.00 flask10Related Pathways
#7980871 // To Up
Migration inhibitory factor-binding sarcolectin from human placenta is indistinguishable from a subfraction of human serum albumin.
Human sarcolectin is known as growth promoter and interferon-alpha/beta antagonist. Besides N-acetylneuraminic acid-dependent cell agglutination it also binds to a macrophage migration inhibitory factor (MIF). Several types of negatively charged carbohydrates interfere with this binding, indicating importance of a negatively charged cluster. Since human serum albumin that has very similar properties in gel electrophoretic analysis can also bind to this factor with a comparatively reduced extent, sarcolectin and albumin are compared biochemically and immunologically. Their peptide maps, generated by cleavage with cyanogen bromide and N-chlorosuccinimide, reveal no differences. The N-terminal sequences are identical up to the fourteenth position that have unequivocally been determined. Reactivities to anti-human serum albumin antibody that inhibits binding of sarcolectin to MIF are similar. Fractionation of human albumin by chromatography on hydroxyapatite yields a subfraction with increased specific activity, measured by extent of inhibition of sarcolectin-MIF interaction. It exhibits the same inhibitory capacity as a similarly derived subfraction from sarcolectin. Interestingly, rabbit and pig serum albumins are as active as human albumin to inhibit binding of sarcolectin to MIF, whereas hamster, mouse, horse and bovine albumin preparations were ineffective up to 2.5 mg/ml. Thus, sarcolectin appears to be a subfraction of human serum albumin whose functionally relevant molecular peculiarities are presently unknown. Neither treatment with organic solvents nor with lipases, but exposure to trypsin, chymotrypsin and pronase can impair sarcolectin's ability to bind MIF.F Y Zeng, H Kratzin, H J Gabius
1188 related Products with: Migration inhibitory factor-binding sarcolectin from human placenta is indistinguishable from a subfraction of human serum albumin.
100 ug1 mg100 ul10gm5ug100 mg100 mg100ug Lyophilized50 mg50 mg100ug Lyophilized 100ulRelated Pathways
#6162242 // To Up
Characteristic and functional specificity of anti-human BAT (brain associated thymocyte antigen) serum.
A rabbit antiserum to human fetal brain after multiple absorption reacted with 100% of thymocytes, 55% of peripheral blood lymphocytes and 90% of enriched T lymphocytes, but not significantly with B lymphocytes. Spontaneous SRBC rosette formation was inhibited by anti-BAT pretreatment, but EAC-rosette formation remained unaffected. The antiserum was itself highly stimulatory. However, cells treated with the antiserum and complement exhibited marked inhibition of responsiveness to Con A, little effect with PHA and no alteration with PWM. The MLC reaction was inhibited only when the responder cells were treated with the antiserum and complement. Treatment of sensitized lymphocytes with the antiserum and complement caused a dose-dependent suppression of blastogenic response to both PPD and n-DNA. No effect, however, was noted in MIF producing cells. Con A induced suppressor function of lymphocytes was abolished by treatment with the antiserum and complement. These results indicate that the anti-BAT serum obtained by us can be utilized for the isolation of T lymphocyte subsets.C Morimoto, T Abe, T Toguchi, M Homma
2375 related Products with: Characteristic and functional specificity of anti-human BAT (brain associated thymocyte antigen) serum.
1 mg0.1 mg100 ug/vial1 ml.100 µg1 mg1 mg96T2 mL0.1ml (1mg/ml)100 ug/vialRelated Pathways
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