Search results for: Rat monoclonal anti mouse EGF (Epidermal Growth Factor) Anti-Mouse antibodies
#17112414 // To Up
CCR3 monoclonal antibody inhibits airway eosinophilic inflammation and mucus overproduction in a mouse model of asthma.
To explore the effect of a rat anti-mouse CC-chemokine receptor-3 (CCR3) monoclonal antibody (CCR3 mAb) on airway eosinophilia and mucus overproduction in asthmatic mice.Hua-hao Shen, Feng Xu, Gen-sheng Zhang, Shao-bin Wang, Wei-hua Xu
2474 related Products with: CCR3 monoclonal antibody inhibits airway eosinophilic inflammation and mucus overproduction in a mouse model of asthma.
100ug8 Sample Kit100ug50 ul100ug Lyophilized100ug Lyophilized100ug100ug100ug4 Sample Kit32-50 Sample Kit100ugRelated Pathways
#9592680 // To Up
Magnetic cell separation for purification of human oral keratinocytes: an effective method for functional studies without prior cell subcultivation.
In studying human oral keratinocytes, it would be very helpful to obtain a pure population of cells without prior in vitro expansion. An immunomagnetic separation technique, or magnetic cell separation (MACS), was modified for efficient purification of human oral keratinocytes. Subsequent to two-step enzymatic digestion, the cell suspension was labelled with a mouse anti-CD45 (pan-leukocyte) monoclonal antibody (MoAb) to stain mononuclear cells. In a second step a rat anti-mouse antibody conjugated with colloidal superparamagnetic particles was used. Labelled cells were retained in the magnetic field of a permanent magnet on columns containing a ferromagnetic matrix. The unlabelled, unretained cells were further examined by flow cytometry analysis, enzyme-linked immunosorbent assay and polymerase chain reaction. After the MACS procedure, unretained cells showed a strong positivity for the lu-5 MoAb (as a marker for pan-cytokeratin) and were negative for anti-vimentin (to mark mesenchymal cells), for anti-CD45 MoAb and for melanocyte-detecting antibodies, thus representing pure keratinocytes (> 98%). Purified keratinocytes maintained full viability (> 91%) and functional capacities. [3H]thymidine uptake and epidermal growth factor (EGF) receptor expression were unaltered when compared with the non-separated cell population. Furthermore, interleukin-1 alpha was detected at the protein and RNA levels in keratinocytes immediately after MACS enrichment. Our findings show that MACS appears to be a useful tool for purification of oral keratinocytes and allows for further functional studies without prior subcultivation of cells.M Formanek, A Temmel, B Knerer, M Willheim, W Millesi, J Kornfehl
1409 related Products with: Magnetic cell separation for purification of human oral keratinocytes: an effective method for functional studies without prior cell subcultivation.
0.1ml (1mg/ml)0.5 ml100ug Lyophilized25 0.2 mL1 mg0.1 mg 5 lt 100ul200 100ug LyophilizedRelated Pathways
#3633949 // To Up
Characterization of monoclonal antibodies against rat glandular kallikrein.
Monoclonal antibodies can be produced in large amounts, are homogenous and can be highly purified. A specific monoclonal antibody against glandular kallikrein could be very useful in studies of the kallikrein-kinin system, both in vivo and in vitro. Two monoclonal antibodies against rat glandular kallikrein (rgKK) were produced by immunized mouse spleen and lymph node fusion with myeloma Ag8.653. Both antibodies, named 2E9.8 and 2E9.9, bound active 125I-kallikrein and phenylmethylsulfonyl fluoride (PMSF)-inactivated 125I-kallikrein. A radioimmunoassay (RIA) was developed with each of the antibodies using rabbit anti-mouse gamma globulin to separate bound from free 125I-rgKK. The standard curve (range 10-1000 ng/tube) was curved even when subjected to logit-log transformation. Using 3% polyethylene glycol (PEG) to assist separation of bound from free, the standard curve became straight for 2E9.8 and the RIA was more sensitive, with a binding range of 0.35-2.4 ng/tube. Both antibodies were specific for rgKK since they had negligible cross-reaction with purified proteases from the submandibular gland of the rat (tonin, esterases B and E). They did not cross-react with mouse nerve growth factor, epidermal growth factor, nor with pig pancreatic kallikrein. Antibody 2E9.9 did appear to bind some human kallikrein when tested with high concentrations of this enzyme, while 2E9.8 did not. When preincubated with purified rgKK, both antibodies prevented the enzyme from releasing kinins from semi-purified dog kininogen and from cleaving [3H]-L-arginine methyl ester (3H-TAME). These results suggested that both antibodies bind an epitope near to, and maybe including, the active site of the enzyme. Monoclonal antibody 2E9.8 appears to be specific for rgKK, can be used in a sensitive RIA, and is capable of inhibiting the enzymatic activity of kallikrein. It should prove to be useful in vivo for examining the role of kallikrein in physiological processes.R T Savoy-Moore, M Khullar, K Swartz, A G Scicli, O A Carretero
1374 related Products with: Characterization of monoclonal antibodies against rat glandular kallikrein.
250 ug100.00 ug1 mg1 mg1 mg100.00 ug100.00 ug100 ul1100 ug1 mg100.00 ugRelated Pathways
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