Allergen Rat n 1; Alpha (2) euglobulin; Alpha 2u globulin; Alpha2mu globulin; Alpha2u; Major urinary protein; MUP; PGCL1; Rat n1
Product Background
Antigen Description
Alpha 2-microglobulin (α2μ-globulin) is a member of the lipocalin super family and is quantitatively the major protein in urine of fertile male rats. Alpha 2-microglobulin is also known as MUP (major urinary protein) and is a very important allergen because it constitutes approximately 30% of the total protein content excreted in the urine. Rats are the most frequently used laboratory animals and allergy to them constitutes an occupational disease. Approximately 20 % of the personnel engaged in work with laboratory animals have acquired symptoms of allergy.
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References
ANTIBODY-BINDING TO ALPHA(2)-MACROGLOBULIN FACILITATES DIRECT QUANTITATION OF ELASTASE-ALPHA(2)-MACROGLOBULIN COMPLEXES BY A SIMPLE ELISA TECHNIQUE
In order to investigate the effect which the binding of anti-alpha2-macroglobulin (anti-A2M) antibody has on subsequent antigen-antibody reaction between the complexed elastase and the solid phase anti-elastase antibody, elastase alpha2-macroglobulin complex (EMC) was incubated with anti-A2M antibody and then extracted by a solid-phase bound rabbit anti-elastase antibody. A doubling dilution series of EMC generated dose related absorbance values. The critical factor permitting the immunological detection of A2M-bound elastase is the pre-incubation of anti-A2M antibody with EMC in solution. The assay exhibited a lower detection limit of 0.5 ng bound elastase per ml and EMC levels in serum samples from ten volunteers were significantly higher than in plasma (28 vs. 21 ng/ml, p < 0.05, Student's t test for paired samples). The EMC levels measured with this assay were essentially identical to those obtained when phenyl methyl sulfonyl fluoride (PMSF) was added to the assay buffer solution.
Selenium is critical for cancer-signaling gene expression but not cell proliferation in human colon Caco-2 cells
Selenium (Se) is a potential anticarcinogenic nutrient, and the essential role of Se in cell growth is well recognized but certain cancer cells appear to have acquired a survival advantage under conditions of Se-deficiency. To understand the molecular basis of Se-anticancer effects at nutritional doses (nmol/L) for cultured cells, we generated Se-deficient colon Caco-2 cells by gradually reducing serum in media because serum contains a trace amount of Se. The glutathione peroxidase (GPx) activity of Se-deficient Caco-2 cells was 10.8 mU/mg protein compared to 133.6 similar to 146.3 mU/mg protein in Caco-2 cells supplemented with 500 nmol/L selenite, SeMSC or SeMet (three tested Se-chemical forms) after 7-d culture in serum free media. Interestingly, there were no detectable differences in cell growth, cell cycle progression between Se-deficient cells and cells supplemented with 500 nmol/L Se. To examine differential cancer signaling-gene expression between Se-deficient and Se-supplemented cells, we employed a cancer signal pathway-specific array assay coupled with the real time PCR analysis. Our data demonstrate that although Caco-2 cells are resistant to Se deprivation, Se may exert its anticancer property through increasing the expression of humoral defense gene (A2M) and tumor suppressor-related genes (IGFBP3, HHIP) while decreasing pro-inflammatory gene (CXC L9, HSPB2) expression.
COA
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