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FGF-1-Acidic (AA 16-155), (N-Term) (Active) Protein

This Recombinant FGF-1-Acidic protein is produced in Escherichia coli (E. coli).
Catalog No. ABIN2667397
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Quick Overview for FGF-1-Acidic (AA 16-155), (N-Term) (Active) Protein (ABIN2667397)

Target

FGF-1-Acidic

Protein Type

Recombinant

Biological Activity

Active

Origin

Human

Source

Escherichia coli (E. coli)

Application

Intracellular Flow Cytometry (ICFC)

Purity

>97 % , as determined by Coomassie stained SDS-PAGE.
  • Protein Characteristics

    AA 16-155, N-Term

    Sterility

    0.22 μm filtered

    Endotoxin Level

    Less than 0.01 ng per μg cytokine as determined by the LAL method.

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  • Application Notes

    Optimal working dilution should be determined by the investigator.

    Comment

    Biological activity: The ED50 is 0.2 - 1.0 ng/ml, corresponding to a specific activity 1.0 - 5.0 x 106 units/mg, as determined by a dose-dependent stimulation of NIH3T3 cell proliferation in the presence of 10 μg/ml heparin.

    Restrictions

    For Research Use only
  • Format

    Liquid

    Reconstitution

    For maximum results, quick spin vial prior to opening. Stock solutions should be prepared at no less than 10 μg/mL in sterile buffer (PBS, HPBS, DPBS, and EBSS) containing carrier protein such as 1 % BSA or HSA.

    Buffer

    0.22 μm filtered protein solution is in 20 mM MOPS, 100 mM NaCl, pH 7.0.

    Handling Advice

    Avoid repeated freeze/thaw cycles.

    Storage

    -20 °C

    Storage Comment

    Unopened vial can be stored at -20°C for three months or at -70°C for 6 months.
  • Target

    FGF-1-Acidic

    Background

    FGF-1, one of the most studied members of the fibroblast growth factor family, is a powerful mitogen exhibiting strong action on many different cell types. FGF-1 activity can be mediated not only by autocrine/paracrine pathways but also by an intracrine pathway. FGF-1 lacks a secretion signal peptide and is exported through a non-classical pathway. Endogenous FGF-1 is found in the nucleus of most cell types. Nuclear localization is required for FGF-1 mitogenic activity. FGF-1 promotes tumor development by promoting cancer cell proliferation and survival. Increased FGF-1 expression in early stages of many different cancers has been reported. MCF-7 breast cancer cell line overexpressing FGF-1 can form vascularized, metastatic tumors when injected into ovariectomized or tamoxifen-treated nude mice. FGF-1 also induces angiogenesis in vitro and in vivo. Thus, FGF-1 is an attractive candidate for cancer immunotargeting. FGF-1 is also involved in neuronal cell differentiation and survival. FGF-1 is highly expressed in motor neurons. In response to damage, motor neurons can release FGF-1 which results in astrocyte activation. Under oxidative stress, astrocytes can also release FGF-1 which stimulates ApoE/HDL generation in an autocrine manner for protection of the brain against oxidative stress. Involvement of FGF-1 in inflammation, cardioprotection, wound healing, adipocyte remodeling, and restenosis is also reported.

    Molecular Weight

    The 140 amino acid recombinant protein has a predicted molecular mass of approximately 16 kDa. The DTT-reduced and non-reduced protein migrates at approximately 17 kDa by SDS-PAGE. The predicted N-terminal amino acid is Met.
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