|Applications||ELISA, IHC, WB|
|Product Name||Anti-FGF2 Antibody|
|Storage & Handling||At -20°C for one year. After reconstitution, at 4°C for one month. It can also be aliquotted and stored frozen at -20°C for a longer time.Avoid repeated freezing and thawing.|
|Description||Rabbit IgG polyclonal antibody for Fibroblast growth factor 2(FGF2) detection. Tested with WB, IHC-P, ELISA in Human.|
|Cite This Product||Anti-FGF2 Antibody (Boster Biological Technology, Pleasanton CA, USA, Catalog # RP1006)|
|Contents/Buffer||Each vial contains 0.9mg NaCl, 0.2mg Na2HPO4, 0.05mg NaN3. Carrier free (No BSA) form available in stock. If you want this antibody carrier free please specify "Carrier Free" or "No BSA" in your order note.|
|Immunogen||E.coli-derived human FGF2 recombinant protein(Position: P143-S288).|
Assay Dilutions Overview
Immunohistochemistry(Paraffin-embedded Section), 0.5-1μg/ml, Human, By Heat
ELISA , 0.1-0.5μg/ml, Human, -
Western blot, 0.1-0.5μg/ml, Human
Boster's Secondary Antibodies And IHC, WB Kits
The following reagents are used to generate the images below.Boster recommends Enhanced Chemiluminescent Kit with anti-Rabbit IgG (EK1002) for Western blot, and HRP Conjugated anti-Rabbit IgG Super Vision Assay Kit (SV0002-1) for IHC(P).
Images And Assay Conditions
Anti- FGF2 antibody, RP1006, Western blotting
All lanes: Anti FGF2(RP1006) at 0.5ug/ml
Lane 1: Recombinant Human FGF2 Protein 10ng
Lane 2: Recombinant Human FGF2 Protein 5ng
Lane 3: Recombinant Human FGF2 Protein 2.5ng
Predicted bind size: 17KD
Observed bind size: 17KD
Protein Target Info (Source: Uniprot.org)
|Protein Name||Fibroblast growth factor 2|
|Tissue Specificity||Expressed in granulosa and cumulus cells. Expressed in hepatocellular carcinoma cells, but not in non- cancerous liver tissue. .|
|Alternative Names||Fibroblast growth factor 2;FGF-2;Basic fibroblast growth factor;bFGF;Heparin-binding growth factor 2;HBGF-2;FGF2;FGFB;|
|Subcellular Localization||Secreted. Nucleus. Exported from cells by an endoplasmic reticulum (ER)/Golgi-independent mechanism. Unconventional secretion of FGF2 occurs by direct translocation across the plasma membrane. Binding of exogenous FGF2 to FGFR facilitates endocytosis followed by translocation of FGF2 across endosomal membrane into the cytosol. Nuclear import from the cytosol requires the classical nuclear import machinery, involving proteins KPNA1 and KPNB1, as well as CEP57.|
|Molecular Weight||30770 MW|
*if product is indicated to react with multiple species, protein info is based on the human gene.
|Protein Function||Plays an important role in the regulation of cell survival, cell division, angiogenesis, cell differentiation and cell migration. Functions as potent mitogen in vitro. .|
|Research Areas||Angiogenesis, Cancer, Cardiovascular, Developmental Biology, Growth Factors, Growth Factors/Hormones, Invasion/Microenvironment, Neural Stem Cells, Neurogenesis, Neurology Process, Neuroscience, Organogenesis, Signal Transduction, Stem Cells
*You can search these to find other products in these research areas.
|Background||FGF2 has been implicated in a multitude of physiologic and pathologic processes, including limb development, angiogenesis, wound healing, and tumor growth. Human FGF2 shares 96% and 97% amino acid sequence homology with mouse and rat respectively. FGF2 belongs to the fibroblast growth factor(FGF) family. Fibroblast growth factors(FGFs) exhibit widespread mitogenic and neurotrophic activities. Nine members of the family are currently known, and FGF-1 and FGF-2 are present in relatively high levels in CNS. FGF-2 is expressed by at low levels in many tissues and cell types and reaches high concentrations in brain and pituitary.|
Other Recommended Resources
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1. Post-translational modification:phosphorylation, methylation, glycosylation etc. These modifications prevent SDS molecules from binding to the target protein and thus make the band size appear larger than expected
2. Post-translational cleavage: this can cause smaller bands and or multiple bands
3. Alternative splicing: the same gene can have alternative splicing patterns generating different size proteins, all with reactivities to the antibody.
4. Amino Acid R chain charge: SDS binds to positive charges. The different size and charge of the Amino Acid side chains can affect the amount of SDS binding and thus affect the observed band size.
5. Multimers: Multimers are usually broken up in reducing conditions. However if the interactions between the multimers are strong, the band may appear higher.,