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  • 产品名称：FGFacidic(AA16-155)(Active)Protein

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  • 产品厂商：ACROBiosystems
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简单介绍：
FGFacidic(AA16-155)(Active)Protein
详情介绍：
Characteristics This protein carries no "tag". The protein has a calculated MW of 15.8 kDa. The protein migrates as 15.8 kDa under reducing (R) condition (SDS-PAGE).
Purity >98 % as determined by SDS-PAGE.
Sterility 0.22 μm filtered
Endotoxin Level Less than 1.0 EU per μg by the LAL method.
ProductDetails: Biological Activity Comment Biological Activity: The bioactivity of rh-aFGF protein was determined in a BALB/c 3T3 mouse fibroblasts cell proliferation assay. The ED50 of each lot is between 50-200 pg/mL.
Background Heparin-binding growth factor 1 is a protein that in humans is encoded by the FGF1 gene. The protein encoded by this gene is a member of the fibroblast growth factor (FGF) family. FGF acidic is a potent growth factor for fibroblasts and endothelial cells. FGF acidic is involved in wound repair, angiogenesis, and development. FGF acidic is secreted from cells via an endoplasmic reticulum/Golgi independent mechanism. The ability of FGF acidic to bind to heparin sulfate is required for its ability to interact with FGF receptors and induce signaling. There are four distinct FGF receptors and each has multiple splice variants. FGF acidic binds with high affinity to many, but not all, FGFRs. Signaling cascades activated through FGF basic binding to FGFR include the ras-raf-MAPK, PLCγ/PKC, and PI3K/Akt pathways.
Molecular Weight 15.8 kDa
NCBI Accession NP_000791
UniProt P05230
Restrictions For Research Use only
Format Lyophilized
Reconstitution Please see Certificate of Analysis for specific instructions. For best performance, we strongly recommend you to follow the reconstitution protocol provided in the CoA.
Buffer PBS, pH 7.4
Handling Advice Avoid repeated freeze-thaw cycles.
Storage -20 °C
Storage Comment No activity loss was observed after storage at: In lyophilized state for 1 year (4 °C-8 °C), After reconstitution under sterile conditions for 1 month (4 °C-8 °C) or 3 months (-20 °C to -70 °C).
Supplier Images
SDS-PAGE (SDS) image for FGF acidic (AA 16-155) (Active) Protein (ABIN2180569) Human FGF acidic, Tag Free on SDS-PAGE under reducing (R) condition. The gel was stai...
Background publications Powers, Zomorodi, Britz, Enterline, Miller, Smith: "Endovascular management of inadvertent brachiocephalic arterial catheterization." in: Journal of neurosurgery, Vol. 114, Issue 1, pp. 146-52, 2011 (PubMed).

Mohammadi, Olsen, Goetz: "A protein canyon in the FGF-FGF receptor dimer selects from an à la carte menu of heparan sulfate motifs." in: Current opinion in structural biology, Vol. 15, Issue 5, pp. 506-16, 2005 (PubMed).

Prudovsky, Mandinova, Soldi, Bagala, Graziani, Landriscina, Tarantini, Duarte, Bellum, Doherty, Maciag: "The non-classical export routes: FGF1 and IL-1alpha point the way." in: Journal of cell science, Vol. 116, Issue Pt 24, pp. 4871-81, 2003 (PubMed).

Ornitz, Itoh: "Fibroblast growth factors." in: Genome biology, Vol. 2, Issue 3, pp. REVIEWS3005, 2001 (PubMed).

Powers, McLeskey, Wellstein: "Fibroblast growth factors, their receptors and signaling." in: Endocrine-related cancer, Vol. 7, Issue 3, pp. 165-97, 2000 (PubMed).