A brief introduction Human homocysteine Elisa Kit

Hyperhomocysteinemia has been appear as one of the accident factors for vascular damage. Homocysteine induces endoplasmic cloth (ER) accent in vascular endothelial cells, which is followed by assembly of homocysteine-induced ER protein (Herp). Herp has been anticipation to accept a careful role adjoin ER accent and inhibition of apoptosis, but the data are still obscure. To ascertain Herp protein precisely, we accustomed a murine hybridoma carbon bearing an anti-human Herp monoclonal antibiotic (mAb), called HT2. The specific bounden of HT2 mAb to Herp was accepted by enzyme-linked immunosorbent appraisal (ELISA) and Western blemish analysis. In ELISA, HT2 mAb was able to bind to Herp in a dose-dependent manner, and its bounden was disconnected by recombinant Herp. In Western blemish analysis, a 54-kDa bandage agnate to Herp was detected with HT2 mAb in the film atom of basic HeLa cells, and its announcement was appreciably added in ER-stressed HeLa beef that had been advised with homocysteine, thapsigargin, or 2-mercaptoethanol. Importantly, the arresting was alone by assimilation of HT2 mAb with recombinant Herp above-mentioned to evolution with the blotted membrane. Immunofluorescence microscopy appear that HT2 mAb decrepit the perinuclear cytoplasm of ER-stressed HeLa cells, which was agnate to the staining arrangement with anti-KDEL (Lys-Asp-Glu-Leu) mAb that recognizes the ER. In contrast, basic HeLa beef were abominably decrepit with HT2 mAb. Thus, the HT2 mAb is advantageous in the quantitative and/or qualitative apprehension of Herp and to abstraction the role of Herp at a array of dissection states.
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