| Source: |
Escherichia coli |
| Molecular Weight: |
Approximately 20.5 kDa, a single non-glycosylated polypeptide chain containing 181 amino acids. |
| AA Sequence: |
MESKEPQLKG IVTRLFSQQG YFLQMHPDGT IDGTKDENSD YTLFNLIPVG LRVVAIQGVK ASLYVAMNGE GYLYSSDVFT PECKFKESVF ENYYVIYSST LYRQQESGRA WFLGLNKEGQ IMKGNRVKKT KPSSHFVPKP IEVCMYREQS LHEIGEKQGR SRKSSGTPTM NGGKVVNQDS T |
| Purity: |
> 98% by SDS-PAGE and HPLC analyses. |
| Biological Activity: |
The biological activity was determined by its binding ability in a functional ELISA. Immobilized rHuFGF R4/Fc Chimera at 5 µg/mL (100 µL/well) can bind rHuFGF-12 with a linear range of 1.6-100 ng/mL. |
| Physical Appearance: |
Sterile filtered white lyophilized (freeze-dried) powder. |
| Formulation: |
Lyophilized from a 0.2 µm filtered concentrated solution in PBS, pH7.4, with 1 mM DTT. |
| Endotoxin: |
Less than 0.1 EU/µg of rHuFGF-12 as determined by LAL method. |
| Background: |
Fibroblast growth factor-12 (FGF-12) belongs to the FGF superfamily, which includes at least 22 members. Human FGF-12 is synthesized as a 243 amino acid (aa) protein lacking a typical signal sequence, thus considered cytoplasmic. It features an N-terminal bipartite nuclear localization signal (NLS) spanning aa 11-18 and 28-38. Additionally, there exists an alternative splice variant, FGF-12B, comprising 181 aa. FGF-12B results from alternate splicing that deletes the N-terminal 66 aa of FGF-12 and replaces them with four different aa. Consequently, FGF-12B lacks the NLS present in the full-length form. Studies indicate that FGF-12B cannot bind common FGF receptors, consistent with its cytoplasmic localization. Instead, FGF-12B interacts with IB2 (islet brain-2), a cellular kinase scaffold protein, and voltage-gated sodium channels. This suggests that FGF-12B plays a critical role in intracellular signaling and ion exchange. Notably, mouse and human FGF-12B differ by only one amino acid. |
