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Recombinant Human Fibroblast Growth Factor 12
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| 性状 | Recombinant Human Fibroblast Growth Factor 12 是在 E. coli 中产生的成纤维细胞生长因子，分子量为 20.4kDa。FGF12 可通过质膜转运到细胞中而在组织中发挥作用。
Synonyms rHuFGF-12; FHF1; FGF12B Species Human Source E. coli Accession P61328 Gene ID 2257 Molecular Weight Approximately 20.4 kDa AA Sequence MESKEPQLKG IVTRLFSQQG YFLQMHPDGT IDGTKDENSD YTLFNLIPVG LRVVAIQGVK ASLYVAMNGE GYLYSSDVFT PECKFKESVF ENYYVIYSST LYRQQESGRA WFLGLNKEGQ IMKGNRVKKT KPSSHFVPKP IEVCMYREPS LHEIGEKQGR SRKSSGTPTM NGGKVVNQDS T Biological Activity The ED50 is <20 ng/mL as measured by TF-1 cells, corresponding to a specific activity of >5 × 104 units/mg. Appearance Lyophilized powder. Formulation Lyophilized after extensive dialysis against PBS. Endotoxin Level <0.2 EU/μg, determined by LAL method. Reconstitution Reconstitute the lyophilized recombinant Human Fibroblast Growth Factor 12 (rHuFGF-12) to 100 µg/mL using ddH2O or diluted with PBS. Storage & Stability Lyophilized recombinant Human Fibroblast Growth Factor 12 (rHuFGF-12) is stored at -20°C. After reconstitution, it is stable at 4°C for 2 weeks or -20°C for longer. It is recommended to freeze aliquots at -20°C or -80°C for extended storage. Shipping Room temperature in continental US; may vary elsewhere. Background Fibroblast growth factors (FGFs) play important roles in embryogenesis, angiogenesis, and wound repair, and the FGF family is currently composed of 22 members in humans. FGF12, initially designated as FGF homologous factor 1 (FHF1), is identified by its sequence homology to known FGFs, and it has a high degree of homology with FGF11 (FHF2), FGF12 (FHF3), and FGF14 (FHF4), with a 58–71% amino acid sequence identity with these FGF11 subfamily members. FGF12 has structural similarity with FGF1 and FGF2, in that it lacks a classical signal sequence and contains a nuclear localization signal (NLS), resulting in the accumulation of FGF12 in the nucleus without any release from cells. FGF12 has two forms, a long form (FGF12A) and a short form (FGF12B). FGF12B lacks the NLS because the N-terminal 66 amino acid residues of FGF12A are substituted by 4 amino acids by means of alternative splicing. FGF12 can play a role in tissues by translocating into cells through the plasma membrane, and the availability of this novel CPP provides a new tool for the intracellular delivery of bioactive molecules[1]. |
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