EasySep™小鼠TIL（CD45）正选试剂盒
产品号 #01630_C
人促红细胞生成素的免疫检测与测定
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总览
糖蛋白EPO是红细胞形成的主要生理调节因子。EPO ELISA Kit是一种快速的3步酶联免疫吸附测定（ELISA），用于定量测定天然和重组人EPO。该检测使用了两种针对人尿促红细胞生成素的单克隆抗体。这些抗体结合EPO多肽上的两个不重叠的表位，对天然和重组EPO都表现出高亲和力结合。试剂盒的检测范围为1.6 ~ 100 mU/mL。EPO酶联免疫吸附测定试剂盒的测定时间约为3小时。
Subtype
Complete Kits
Cell Type
Other
Species
Human
Application
ELISA
Area of Interest
Drug Discovery and Toxicity Testing
CAS Number
108-32-7, 872-50-4, 111-46-6, 7664-93-9
产品说明书及文档
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应用领域
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相关材料与文献
技术资料 (3)
文献 (4)
The blood in systemic disorders. Lancet 2000 MAY
Abstract
* The high rate of proliferation required of the bone marrow renders it highly susceptible to the influence of external factors. * Anaemia is the most common haematological abnormality seen in systemic disorders. * In the anaemia of chronic disease, erythropoietin production is reduced and proliferation of erythroid progenitor cells is also impaired; this anaemia can generally be alleviated by correction of the underlying disease process. * The status of the endocrine system must always be considered in evaluation of a normocytic, normochromic anaemia. * Anaemia in infection can be due to host or parasite factors or to the treatment administered. * Anaemia due to malignant disease responds to erythropoietin therapy in many cases; failure to respond is a poor prognostic sign.
A specific in vitro bioassay for measuring erythropoietin levels in human serum and plasma. Blood 1990 OCT
Abstract
The accurate measurement of biologically active erythropoietin (Ep) in human serum and plasma using present in vivo and in vitro bioassays is difficult because of the presence of both inhibitors and non-Ep stimulators of erythropoiesis. We have developed a simple procedure to quantitatively purify Ep from serum and plasma for subsequent testing in the phenylhydrazine-treated mouse spleen cell assay. The method involves absorption of Ep to an immobilized high-affinity anti-Ep monoclonal antibody and acid elution of the antibody-bound material. After neutralization, the eluted EP is then tested directly in the in vitro bioassay without interference by other serum proteins. By using magnetic beads as a solid support for the antibody, washing and elution steps can be performed rapidly and efficiently. Recoveries of Ep after this procedure show very little sample-to-sample variation and are consistently between 45% and 55%, which is close to the maximum binding expected for the anti-Ep antibody. Coupled with the 7.4-fold concentration that this procedure affords, there is an overall increase in sensitivity of three- to fourfold, which makes this assay suitable for accurately measuring Ep levels in patients with below-average titers. Results with this magnetic bead assay indicate that accurate and reproducible estimates for Ep levels in the serum and plasma from healthy donors as well as from patients with hematologic disorders can be obtained. Titers of biologically active Ep in the sera from a group of patients with either leukemia or lymphoma were found to be elevated, and the values correlated well with titers of immunoreactive Ep measured in the Ep radioimmunoassay. Because of its specificity and high sensitivity, the magnetic bead assay is a valuable alternative to immunoassays for the measurement of elevated, normal, and even subnormal Ep levels in human serum and plasma.
Immunochemical analysis of monoclonal antibodies to human erythropoietin. Experimental hematology 1990 MAR
Abstract
We recently reported the development of three monoclonal antibodies (MoAbs) to biologically active human erythropoietin (Ep). In the present study, we investigated the epitope specificity of these three antibodies, as well as their reactivity with Eps derived from species other than man. All three antibodies reacted with the Ep polypeptide itself, rather than with its carbohydrate moieties. Moreover, all three antibodies recognized separate nonoverlapping epitopes. Further studies with reduced/alkylated Ep and with sodium dodecyl sulfate-denatured Ep suggested that two of the MoAbs, anti-Ep-2 and anti-Ep-16, were specific for conformational, nonlinear determinants on the Ep molecule, whereas the third MoAb, anti-Ep-26, appeared to recognize a linear epitope. However, anti-Ep-26 did not react with synthetic peptides representing the 26 amino-, the 99-129 mid-region, or the 10 carboxy-terminal residues of Ep, nor with trypsin-, chymotrypsin-, or V8 protease-digested fragments of Ep. When tested with Ep from different species, the neutralizing capabilities of the three MoAbs were clearly different. Comparing their effectiveness against baboon, ovine and murine Ep, antibody 2 was most effective at neutralizing baboon Ep, antibody 16 was most effective against murine Ep, and antibody 26 showed little reactivity with any of these nonhuman Eps. Because these various Eps readily stimulate across species barriers, it is likely that the receptor binding domain on Ep has remained relatively conserved during evolution. Our results therefore suggest that the neutralizing capacity of our three anti-Ep MoAbs is caused not by binding directly to the Ep receptor binding domain on Ep, but by binding to distant regions, causing conformational changes in Ep, or by binding to regions close to the binding site, steric hindrance.
更多信息
| 种属 | Human |
|---|---|
| Cas Number | 108-32-7, 872-50-4, 111-46-6, 7664-93-9 |
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