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  • 產品名稱:重組人巨噬細胞遷移抑制因子蛋白

  • 產品型號:rHuMIF
  • 產品廠商:KALANG
  • 產品文檔:
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簡單介紹:
重組人巨噬細胞遷移抑制因子蛋白與其它公司提供的重組蛋白不同,rHuMIF蛋白產品為采用CFS的無細胞麥胚蛋白合成系統表達出來的重組蛋白,可表達出對細胞有毒性、易被蛋白酶降解的蛋白;并獲得具有良好的可溶性,并有翻譯后修飾、從而部分具有功能的蛋白.同時獨有的全自動蛋白純化技術則簡便高效,將蛋白純化過程中對蛋白的損傷降低到*小程度.重組人巨噬細胞遷移抑制因子蛋白(全長序列)產品可用于Western Blot驗證、抗體制備、蛋白檢測、ELISA等試驗中.
詳情介紹:

重組人巨噬細胞遷移抑制因子蛋白

Synonyms GLF, L-dopachrome Isomerase, Phenylpyruvate Tautomerase
Species Human
Source Escherichia coli.
Molecular Weight Approximately 12.5 kDa, a single non-glycosylated polypeptide chain containing 115 amino acids.
Quantity 重組人巨噬細胞遷移抑制因子蛋白10μg/50μg/1000μg
AA Sequence MPMFIVNTNV PRASVPDGFL SELTQQLAQA TGKPPQYIAV HVVPDQLMAF GGSSEPCALC SLHSIGKIGG AQNRSYSKLL CGLLAERLRI SPDRVYINYY DMNAANVGWN NSTFA
Purity > 97 % by SDS-PAGE and HPLC analyses.
Biological Activity 重組人巨噬細胞遷移抑制因子蛋白Fully biologically active when compared to standard. The specific activity is determined by binding rhCD74 in a functional ELISA.
Physical Appearance Sterile Filtered White lyophilized (freeze-dried) powder.
Formulation Lyophilized from a 0.2 μm filtered concentrated solution in PBS, pH 7.4.
Endotoxin Less than 1 EU/μg of rHuMIF as determined by LAL method.
Reconstitution 重組人巨噬細胞遷移抑制因子蛋白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.
Storage 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.
重組人巨噬細胞遷移抑制因子蛋白
Reference 1. Edwards KM, Tomfohr LM, Mills PJ, et al. 2011. Sleep, 34: 161-3.
2. Delaloye J, De Bruin IJ, Darling KE, et al. 2012. Cytokine, 
3. Leu RW, Woodson PD, Whitley SB. 1977. J Reticuloendothel Soc, 22: 329-40.
4. Landolfo S. 1977. G Batteriol Virol Immunol, 70: 137-43.
5. Baugh JA, Chitnis S, Donnelly SC, et al. 2002. Genes Immun, 3: 170-6.
Background Migration Inhibitory Factor (MIF) is a secreted protein without a cleavable signal sequence and is secreted via a specialized, non-classical pathway. It is secreted by macrophages upon stimulation by bacterial lipopolysaccharide (LPS), or by M.tuberculosis antigens. MIF consists of two α-helices and six β-strands, four of which form a β-sheet. The two remaining β-strands interact with other MIF molecules, creating a trimer. Structure-function studies suggest MIF is bifunctional with segregated topology. The N- and C-termini mediate enzyme activity (in theory). Phenylpyruvate tautomerase activity (enol-to-keto) has been demonstrated and is dependent upon Pro at position 1. Amino acids 50-65(a.a.) have also been suggested to contain thiol-protein oxidoreductase activity. MIF has proinflammatory cytokine activity centered around (a.a.) 49 - 65. On fibroblasts, MIF induces, IL-1, IL-8 and MMP expression; on macrophages, MIF stimulates NO production and TNF-α release folllowing IFN-γ activation. MIF apparently acts through CD74 and CD44, likely in some form of trimeric interaction. Human MIF is active on mouse cells. Human MIF is 90 %, 94 %, 95 %, and 90 % aa identical to mouse, bovine, porcine and rat MIF, respectively.

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