重組人巨噬細(xì)胞遷移抑制因子，蛋白

Synonyms	GLF, L-dopachrome Isomerase, Phenylpyruvate Tautomerase
Species	Human
Source	Escherichia coli.
Molecular Weight	重組人巨噬細(xì)胞遷移抑制因子，蛋白Approximately 13.5 kDa, a single non-glycosylated polypeptide chain containing 117 amino acids, with 6 × His at the C-terminus.
Quantity	10μg/50μg/1000μg
AA Sequence	MPMFIVNTNV PRASVPDGFL SELTQQLAQA TGKPPQYIAV HVVPDQLMAF GGSSEPCALC SLHSIGKIGG AQNRSYSKLL CGLLAERLRI SPDRVYINYY DMNAANVGWN NSTFALEHHH HHH
Purity	重組人巨噬細(xì)胞遷移抑制因子，蛋白> 95 % by SDS-PAGE and HPLC analyses.
Biological Activity	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, His as determined by LAL method.
Reconstitution	重組人巨噬細(xì)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(xì)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.