Recombinant FGF-12, Human
Catalogue Numbers: -10, -50
Sizes: 10μg, 50μg
Source: Escherichia coli
Molecular Weight: 20.4 kDa, observed by reducing SDS-PAGE.
Purity: > 95% as analyzed by SDS-PAGE and HPLC.
Biological Activity: ED50 < 20 ng/ml, measured by its binding ability in a functional ELISA with immobilized rhFGF R4/Fc Chimera, corresponding to a specific activity of > 5×10ˆ4 units/mg.
Physical Appearance: Sterile Filtered White lyophilized (freeze-dried) powder.
Formulation: Lyophilized after extensive dialysis against PBS.
AA Sequence: MESKEPQLK GIVTRLFSQQ GYFLQMHPDG TIDGTKDENS DYTLFNLIPV GLRVVAIQGV KASLYVAMNG EGYLYSSDVF TPECKFKESV FENYYVIYSS
TLYRQQESGR AWFLGLNKEG QIMKGNRVKK TKPSSHFVPK PIEVCMYREP SLHEIGEKQG RSRKSSGTPT MNGGKVVNQD ST
Endotoxin: < 0.2 EU/μg, determined by LAL method.
Reconstitution: Reconstituted in ddH2O or PBS at 100 μg/ml.
Storage: Lyophilized recombinant human Fibroblast Growth Factor-12 (rhFGF-12) remains stable up to 6 months at -80°C from date of receipt. Upon reconstitution, rhFGF-12 remains stable up to 2 weeks at 4°C or up to 3 months at -20°C.
Usage: This material is offered by USA Bioworld biotech for research, laboratory or further evaluation purposes. For research use only.
Description: Fibroblast Growth Factor-12(FGF-12) is a heparin binding cytokine belonging to the FGF family. FGF-12 along with FGF-11, -13, and -14, form a sublineage within the FGF family: in contrast to the other members, they are all intracellular signaling proteins lacking signal peptides and containing a flanking domain beside the family conserved β-trefoil domain. FGF-12 is expressed in the cartilaginous skeleton and heart, suggesting a role in the development of connective tissue and heart. In vivo, FGF-12 binds to Islet Brain-2 and Voltage-Gated Sodium Channels (VGSC), and plays a critical role in the membrane targeting and function of VGSC. FGF-12 has been implicated in heart diseases such as cardiac arrhythmias.Recombinant human Fibroblast Growth Factor-12 (rhFGF-12) produced in E.coli is a single non-glycosylated polypeptide chain containing 181 amino acids. A fully biologically active molecule, rhFGF-12 has a molecular mass of 20.4 kDa analyzed by reducing SDS-PAGE and is obtained by proprietary chromatographic techniques at GenScript.