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                Recombinant Human EPOα-Fc

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                • 產(chǎn)品型號:abs00841
                • 廠商性質(zhì):生產(chǎn)廠家
                • 更新時間:2025-03-24
                • 訪  問  量:1649

                詳細(xì)介紹

                品牌absin貨號abs00841
                規(guī)格2ug供貨周期一周
                概述
                形態(tài)Lyophilized from a 0.2 μm filtered concentrated solution in PBS, pH 7.4.
                來源CHO
                內(nèi)毒素水平Less than 1 EU/μg of Recombinant HumanEPO-Fc a as determined by LAL method.
                活性Fully biologically active when compared to standard. The Specific Activity was measured by the stimulation of reticulocyte production in normocyth-aemic mice and is no less than 5.0 × 105 IU/mg.
                預(yù)期分子量Recombinant Human EPO/Fc produced in CHO is a dimeric, glycosylated, polypeptide chain consisting of two mature human EPO molecules linked to the Fc portion of human IgG1. The Fc component contains the CH2 domain, the CH3 domain and hinge region, but not the CH1 domain of IgG1. As a result of glycosylation, the recombinant protein migrates with an apparent molecular mass of 140 kDa in non-reducing SDS-PAGE.
                性能
                溶解方法We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Reconstitute in sterile distilled water or aqueous buffer containing 0.1 % BSA to a concentration of 0.1-1.0 mg/mL. Stock solutions should be apportioned into working aliquots and stored at ≤ -20 °C. Further dilutions should be made in appropriate buffered solutions.
                保存方法This lyophilized preparation is stable at 2-8 °C, but should be kept at -20 °C for long term storage, preferably desiccated. Upon reconstitution, the preparation is stable for up to one week at 2-8 °C. For maximal stability, apportion the reconstituted preparation into working aliquots and store at -20 °C to -70 °C. Avoid repeated freeze/thaw cycles.
                純度> 98 % by SDS-PAGE and HPLC analyses.
                參考文獻
                1. Hanicki Z. 1988. Pol Arch Med Wewn, 80: 290-3.<br/>2. Haniu M, Narhi LO, Arakawa T, et al. 1993. Protein Sci, 2: 1441-51.<br/>3. Baranowska-Daca EandKsiazek A. 1994. Ann Univ Mariae Curie Sklodowska Med, 48 Suppl 3: 51-60.<br/>4. Chow KM, Szeto CC, Li PK. 2003. Am J Kidney Dis, 41: 266-7; author reply 7.<br/>5. Maurer MH, Schabitz WR, Schneider A. 2008. Curr Med Chem, 15: 1407-11.

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