產(chǎn)品詳情
簡單介紹：
重組人巨噬細(xì)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(chǎn)品為采用CFS的無細(xì)胞麥胚蛋白合成系統(tǒng)表達(dá)出來的重組蛋白，可表達(dá)出對細(xì)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(dú)有的全自動蛋白純化技術(shù)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(xì)胞遷移抑制因子蛋白（全長序列）產(chǎn)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(xì)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(xì)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(xì)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(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. |
