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Synonyms
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GLF, L-dopachrome Isomerase, Phenylpyruvate Tautomerase
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Species
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Human
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Source
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Escherichia coli.
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Molecular Weight
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Approximately 12.5 kDa, a single non-glycosylated polypeptide chain containing 115 amino acids.
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Quantity
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重组人巨噬细胞迁移抑制因子蛋白10µg/50µg/1000µg
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AA Sequence
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MPMFIVNTNV PRASVPDGFL SELTQQLAQA TGKPPQYIAV HVVPDQLMAF GGSSEPCALC SLHSIGKIGG AQNRSYSKLL CGLLAERLRI SPDRVYINYY DMNAANVGWN NSTFA
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Purity
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> 97 % by SDS-PAGE and HPLC analyses.
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Biological Activity
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重组人巨噬细胞迁移抑制因子蛋白Fully biologically active when compared to standard. The specific activity is determined by binding rhCD74 in a functional ELISA.
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Physical Appearance
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Sterile Filtered White lyophilized (freeze-dried) powder.
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Formulation
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Lyophilized from a 0.2 µm filtered concentrated solution in PBS, pH 7.4.
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Endotoxin
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Less than 1 EU/µg of rHuMIF as determined by LAL method.
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Reconstitution
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重组人巨噬细胞迁移抑制因子蛋白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.
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Storage
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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.
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重组人巨噬细胞迁移抑制因子蛋白
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Reference
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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.
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Background
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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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