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FGF2 Protein

Recombinant FGF2 protein expressed in Escherichia coli (E. coli).
Catalog No. ABIN7539324

Quick Overview for FGF2 Protein (ABIN7539324)

Target

See all FGF2 Proteins
FGF2 (Fibroblast Growth Factor 2 (Basic) (FGF2))

Protein Type

Recombinant

Biological Activity

Active

Origin

  • 30
  • 12
  • 11
  • 6
  • 3
  • 3
  • 2
  • 1
  • 1
  • 1
  • 1
  • 1
Pig

Source

  • 54
  • 9
  • 2
  • 1
  • 1
  • 1
Escherichia coli (E. coli)

Purity

> 98 % by SDS-PAGE
  • Purpose

    FGF-2 (basic)

    Sequence

    AAGSITTLPA LPEDGGSGAF PPGHFKDPKR LYCKNGGFFL RIHPDGRVDG VREKSDPHIK LQLQAEERGV VSIKGVCANR YLAMKEDGRL LASKCVTDEC FFFERLESNN YNTYRSRKYS SWYVALKRTG QYKLGPKTGP GQKAILFLPM SAKS

    Characteristics

    Length (aa):145

    Endotoxin Level

    < 0.1 ng per μg of porcine FGF-2
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  • Application Notes

    The ED50 for stimulation of cell proliferation in human umbilical vein endothelial cells (HUVEC) by porcine FGF-2 has been determined to be in the range of 0.1-2 ng/mL.

    Restrictions

    For Research Use only
  • Format

    Lyophilized

    Reconstitution

    The porcine FGF-2 is supplied in lyophilized form and can be reconstituted with ddH2O at 50 μg/mL. This solution can be diluted into other buffered solutions or stored frozen for future use. For long term storage we would recommend to add at least 0.1 % human or bovine serum albumin.

    Buffer

    0.5X PBS

    Storage

    RT,-20 °C,-80 °C

    Storage Comment

    The lyophilized porcine FGF-2, though stable at room temperature, is best stored in working aliquots at -20°C to -70°C
  • Target

    FGF2 (Fibroblast Growth Factor 2 (Basic) (FGF2))

    Alternative Name

    FGF-2

    Background

    Fgf2, bFGF, Fgf-2,FGF2 (basic) is one of at least 23 mitogenic proteins of the FGF family, which show 35-60 % amino acid conservation. Unlike other FGFs, FGF acidic and basic lack signal peptides and are secreted by an alternate pathway. Storage pools within the cell or on cell surface heparan sulfate proteoglycans (HSPG) are likely. FGF2 has been isolated from a number of sources, including neural tissue, pituitary, adrenal cortex, corpus luteum and placenta. This factor contains four cysteine residues but reduced FGF2 retains full biological activity, indicating that disulfide bonds are not required for this activity. Several reports indicate that a variety of forms of FGF2 are produced as a result of N-terminal extensions. These extensions apparently affect localization of FGF2 in cellular compartments but do not affect biological activity. Studies indicate that binding of FGF to heparin or cell surface heparan sulfate proteoglycans is necessary for binding of FGF to high affinity FGF receptors. FGF acidic and basic appear to bind to the same high affinity receptors and show a similar range of biological activities. FGF2 stimulates the proliferation of all cells of mesodermal origin, and many cells of neuroectodermal, ectodermal and endodermal origin. The cells include fibroblasts, endothelial cells, astrocytes, oligodendrocytes, neuroblasts, keratinocytes, osteoblasts, smooth muscle cells, and melanocytes. FGF2 is chemotactic and mitogenic for endothelial cells in vitro. FGF2 induces neuron differentiation, survival and regeneration. The 17 kDa porcine sequence has 95 % aa identity with human and sheep FGF basic.

    Molecular Weight

    16.34 kDa

    NCBI Accession

    NM_174056, NP_776481

    UniProt

    P13109

    Pathways

    RTK Signaling, Fc-epsilon Receptor Signaling Pathway, EGFR Signaling Pathway, Neurotrophin Signaling Pathway, C21-Steroid Hormone Metabolic Process, Inositol Metabolic Process, Glycosaminoglycan Metabolic Process, Protein targeting to Nucleus, S100 Proteins
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