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> Chemicals & Drugs > Amino Acid > Fibroblast Growth Factor

Fibroblast Growth Factor

Fibroblast Growth Factors (FGFs) are a family of proteins involved in a variety of biological processes, including cell proliferation, differentiation, and angiogenesis.
These growth factors play a crucial role in tissue development, repair, and regeneration.
FGFs bind to specific cell surface receptors, triggering signaling cascades that regulate gene expression and cellular functions.
Reserach on FGFs has implications for understanding and treating a range of medical conditions, from wound healing to cancer.
Pubcompare.AI's AI-driven platform can help optimize your FGF research by locating the best protocols and products from literature, preprints, and patents, streamlining your workflow and experiecning the power of AI-driven research optimization.

Most cited protocols related to «Fibroblast Growth Factor»

1
Mitochondrial DNA Copy Number Quantification
Cited 12 times
We used EDTA tubes to collect 7 ml whole blood that was promptly centrifuged on site at 2500 rpm for 15 minutes. The buffy coat (400 μl) was transferred in a cryovial, immediately frozen in vapour phase of liquid nitrogen, and shipped in nitrogen dry shippers to the laboratory. DNA was extracted using the Wizard Genomic DNA purification kit (Promega, Madison, WI) following the manufacturer's instructions. The samples collected in the 1st and 4th day were processed using the same exact protocols.
Relative MtDNAcn (RMtDNAcn) was measured in buffy coat DNA by a quantitative real time polymerase chain reaction (PCR) assay that measure relative mitochondrial copy number by determining the ratio of mitochondrial (Mt) copy number to single copy gene (S) copy number in experimental samples relative to a reference [28 (link)]. This method is based on quantification of Mt and S quantities expressed as Cts derived from a standard curve obtained from serial dilutions of a reference DNA. The reference single copy gene used in this study was human [beta] globin (hbg). The Mt PCR mix was: iQ SYBR Green Supermix (Bio-Rad) 1×, MtF3212 500 nM, MtR3319 500 nM, EDTA 1×. The S (hbg) PCR mix was: iQ SYBR Green Supermix (Bio-Rad) 1×, hbgF 500 nM, hbgR 500 nM, EDTA 1×. 9 ng DNA was loaded in a 20 μl PCR reaction. We used pooled DNA from 20 participants randomly selected from this same study (500 ng for each sample) to create in every Mt and S PCR run a fresh standard curve, which ranged from 20 ng/μl to 0.25 ng/μl. The primers for RT Q-PCR analysis of MtDNA were: MtF3212 5'CAC CCA AGA ACA GGG TTT GT3', and MtR3319 5'TGG CCA TGG GTA TGT TGT TA3'. The primers for RT Q-PCR analysis of hbg were: hbgF 5'GCT TCT GAC ACA ACT GTG TTC ACT AGC3', and hbgR 5'CAC CAA CTT CAT CCA CGT TCA CC3'. All PCRs were performed on a DNA Engine thermal cycler Chromo4 (Bio-Rad, Hercules, California, USA). The thermal cycling conditions for MtDNA PCR were: initial 2 minutes at 50°C, and 3 minutes at 95°C to activate the hot-start iTaq DNA polymerase, followed by 40 cycles comprised of 15 s denaturation at 95°C and 49 s anneal/extend at 60°C. The thermal cycling conditions for the hbg PCR were 3 minutes at 95°C to activate the hot-start iTaq DNA polymerase, followed by 40 cycles comprised of 15 s denaturation at 95°C and 49 s anneal/extend at 58°C. Each run was completed by melting curve analysis to confirm the amplification specificity and absence of primer dimers.
All samples were run in triplicates. The average of the three Mt measurements was divided by the average of the three S measurements to calculate the Mt/S ratio for each sample. For quality control purposes, 10 blind duplicate samples were interdispersed among the test samples. The coefficient of variation for the Mt/S ratio in duplicate samples was 3.2%.
Hou L., Zhu Z.Z., Zhang X., Nordio F., Bonzini M., Schwartz J., Hoxha M., Dioni L., Marinelli B., Pegoraro V., Apostoli P., Bertazzi P.A, & Baccarelli A. (2010). Airborne particulate matter and mitochondrial damage: a cross-sectional study. Environmental Health, 9, 48.
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Publication 2010
beta-Globins Biological Assay BLOOD DNA, Mitochondrial DNA-Directed DNA Polymerase Edetic Acid Fibroblast Growth Factor Freezing Genes Genome Homo sapiens Mitochondria Nitrogen Oligonucleotide Primers Polymerase Chain Reaction Promega Real-Time Polymerase Chain Reaction SYBR Green I Technique, Dilution Visually Impaired Persons
2
Jawbone NICO Tissue Analysis
Cited 10 times
We collected JC tissue samples from 31 patients. Inclusion criteria of the studied population were patients with systemic immunological or neurodegenerative diseases and local diagnosis of NICO in the jawbone. Patients taking any medications due to systemic complaints were not excluded from the study. We analyzed regulated upon activation, normal T-cell expressed, and secreted (RANTES)/C-C motif chemokine 5 (CCL5) (hereafter referred to as RANTES) and fibroblast growth factor (FGF)-2 expression in NICO in these 31 patients, and in serum (n = 14). The following symptoms were present in the 31 patients (multiple counts are due to overlapping symptoms): seven patients with nonspecific facial pain/trigeminal neuralgia; seven patients with joint aches or rheumatoid arthritis (RA); four patients with chronic fatigue syndrome; five patients with breast cancer (BC); three patients with autoimmune disease of the thyroid gland (Hashimoto’s thyroiditis); two patients with multiple sclerosis (MS); one patient with Parkinson’s disease; one patient with asthma; one patient with leukemia (cured); one patient with allergy/intolerance; and one patient with amyotrophic lateral sclerosis (ALS).
Inclusion criteria for the JC group were the medical indication for NICO surgery in these patients based on orthopantomogram X-rays (two-dimensional) and an additional cone beam X-ray (three-dimensional), and multiple and irregular remnants of lamina dura present in a subtle radiolucent background, leading to the suspicion of the presence of JC. The definite indication for NICO surgery is from the complementary evaluation of additional measurement of bone density by TAU. Demographic data of the 31 cases in the NICO cohort were average age (57.1 years, range 36–86 years) and sex (female:male 21:10).
Additionally, we collected tissue samples from the normal jawbones of three patients who gave their consent for bone specimen collection during implantation and analysis. Inclusion criteria for this cohort were no radiographic evidence of NICO and inconspicuous measurement of bone density by TAU. Patients showed no systemic health risks.
Lechner J, & von Baehr V. (2013). RANTES and fibroblast growth factor 2 in jawbone cavitations: triggers for systemic disease?. International Journal of General Medicine, 6, 277-290.
Publication 2013
Amyotrophic Lateral Sclerosis Arthralgia Asthma Bone Density Bones CCL5 protein, human Cells Chronic Fatigue Syndrome Diagnosis Dura Mater Face Fibroblast Growth Factor Fibroblast Growth Factor 2 Hashimoto Disease Hypersensitivity Jaw Leukemia Males Malignant Neoplasm of Breast Multiple Sclerosis Neurodegenerative Disorders Operative Surgical Procedures Ovum Implantation Pain Panoramic Radiography Parkinson Disease Patients Pharmaceutical Preparations Radiography Retinal Cone Rheumatoid Arthritis Serum Specimen Collection Thyroid Diseases Tissues Trigeminal Neuralgia Woman X-Rays, Diagnostic
3
Immunohistochemistry of Tendon Pathology
Cited 10 times
Immunohistochemical analysis was performed on flexor digitorum tendons collected from normal controls (n=12), trained controls (n = 9), and rats that had performed either the HRHF task for 3 (n = 4), 6 (n=4) or 12 weeks (n=4), or the LRNF task for 3 (n=3), 6 (n=4) or 12 weeks (n = 3). Animals were euthanized, perfused transcardially with 4% paraformaldehyde in PO4 buffer, and forearm musculotendinous tissues were dissected as a mass off the forearm bones as shown in Figure 3K,L, and sectioned longitudinally as a soft tissue mass (en bloc) as described previously (19 (link), 23 (link)). Sections, on slides, were incubated in 3% H2O2 in methanol (4°C) for 30 min, washed, incubated in 4% dried milk in PBS (Blotto) for 20 min, and then overnight at rm temp with a Substance P antibody (# MAB1566, Chemicon, Temecula, CA; 1:500 dilution with 4% carnation milk in PBS). After washing, sections were incubated for 2 hrs at rm temp with goat anti-mouse peroxidase-conjugated (HRP) secondary antibody (Jackson ImmunoResearch, West Grove, PA) diluted 1:100 with PBS. HRP was visualized as a black immunoreactive stain using diaminobenzidene (DAB) with cobalt (Sigma-Aldrich, St. Louis, MO). For IL-1β and periostin like factor (PLF; labels activated fibroblasts producing this matricellular protein), sections were immunolabeled and detected with HRP-DAB as previously described (21 (link),24 (link)). Eosin and/or nuclear red were used as counterstains. A series of adjacent sections were also stained with hematoxylin and eosin (H&E) only. Sections were dehydrated and coverslipped with DPX mounting medium. For connective tissue growth factor (CTGF; a fibroblast growth factor that induces collagen production and an activated fibroblast marker), sections were immunolabeled and detected with Cy3 (red fluorescence), and coverslipped with 80% glycerol in PBS, as previously described (22 (link)). Negative control slides included omission of either the primary antibody or the secondary antibody.
Selected sections were double-labeled after Substance P immunolabeling with either anti-ED1 (detects a 90 kDa lysosomal membrane protein in monocytes/macrophages) or anti-PGP9.5 (a pan neuronal marker). After Substance P immunolabeling with secondary antibody conjugated to Cy2 (green tag; Jackson, diluted 1:100 in PBS for 2 hrs), tissue sections were washed, digested with 0.5% pepsin in 0.01 N HCl for 20 min at rm temp, and then incubated with goat serum (4%) in PBS for 30 min at rm temp. Sections were then incubated with either anti-ED1 (MAB1435, Chemicon, Temecula, CA, 1:250 dilution in 4% goat serum in PBS) or anti-PGP9.5 (ab8189, Abcam, Cambridge, MA, 1:50 dilution in 10% goat serum in PBS) overnight at rm temp. Sections were incubated with appropriate secondary antibodies conjugated to Cy3 (red tag; Jackson). Slides were coverslipped with 80% glycerol in PBS. Selected sections were also double-labeled with CTGF and collagen type I antibodies as described previously (22 (link)).
Fedorczyk J.M., Barr A.E., Rani S., Gao H., Amin M., Amin S., Litvin J, & Barbe M.F. (2010). Exposure dependent increases in IL-1beta, Substance P, CTGF and tendinosis in flexor digitorum tendons with upper extremity repetitive strain injury. Journal of orthopaedic research : official publication of the Orthopaedic Research Society, 28(3), 298-307.
Publication 2009
Animals Antibodies Buffers Carnation Cobalt Collagen Collagen Type I Connective Tissue Growth Factor Eosin Fibroblast Growth Factor Fibroblasts Fluorescence Forearm Glycerin Goat Immunoglobulins Interleukin-1 beta Lysosome-Associated Membrane Glycoproteins Macrophage Methanol Milk, Cow's Monocytes Mus Neurons paraform Pepsin A Peroxidase Peroxide, Hydrogen POSTN protein, human Proteins Rattus Serum Stains Substance P Technique, Dilution Tendons Tissues UCHL1 protein, human Ulna
4
Fatty Acid Oxidation in Neural Stem Cells
Cited 9 times

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Publication 2017
Adult Bone Morphogenetic Protein 4 Brain carnitine palmitoyltransferase 1A, human Cell Extracts Dietary Supplements Electroporation Embryo Epidermal growth factor etomoxir Fibroblast Growth Factor Gas Chromatography-Mass Spectrometry Heparin Injections, Intraperitoneal isolation Liquid Chromatography Malonyl Coenzyme A Mass Spectrometry Mus neuro-oncological ventral antigen 2, human Palmitic Acid Plasmids Proteins Psychological Inhibition Radioactivity Recombination, Genetic Short Hairpin RNA Strains Tamoxifen Tandem Mass Spectrometry Tissues Uterus Virus
5
Derivation and Culture of Human Glioblastoma Neurosphere Lines
Cited 9 times
The human glioblastoma neurosphere lines HSR-GBM1A (20913) and HSR-GBM 1B (10627) were originally derived by Vescovi and colleagues and maintained in serum-free medium supplemented with epidermal growth factor and fibroblast growth factor (Vescovi et al., 1999 (link); Galli et al., 2004 (link); Bar et al., 2007 (link); Sun et al., 2009 (link)). Cells were incubated in a humidified incubator containing 5% CO2/95% air at 37 °C, and passaged every 4–5 days. The GBM-DM140207 and GBM-KK190156 neurosphere lines were derived from glioblastomas at the University of Freiburg and kindly provided by Dr Jaroslaw Maciaczy. The primary neurospheres JHH551 was derived from a malignant glioma at Johns Hopkins using the same methods and culture conditions as described in Galli et al. (2004) (link). JHH551 neurospheres were used at passage ≤10. All human materials were obtained and used in compliance with the Johns Hopkins IRB.
Ying M., Wang S., Sang Y., Sun P., Lal B., Goodwin C., Guerrero-Cazares H., Quinones-Hinojosa A., Laterra J, & Xia S. (2011). Regulation of glioblastoma stem cells by retinoic acid: role for Notch pathway inhibition. Oncogene, 30(31), 3454-3467.
Publication 2011
Cells Epidermal growth factor Fibroblast Growth Factor Glioblastoma Homo sapiens Malignant Glioma Serum

Most recents protocols related to «Fibroblast Growth Factor»

1
Chemotherapeutics Affect Pancreatic Cancer Spheres
MiaPaCa-2 and Panc-1 cells (1,000 cells/well) were plated in 96-well extremely low attachment plates (Corning, Inc.) and treated with oxaliplatin (5 µM)/cisplatin (5 µM)/carboplatin (4 µM) at 37°C for 48 h. Fibroblast growth factor (20 ng/ml), human recombinant epidermal growth factor (20 ng/ml) and serum substitute B27 (1X) were mixed into serum-free DMEM/F-12 and were added to each well (all from Invitrogen; Thermo Fisher Scientific, Inc.). The number of spheres >50 mm in diameter was counted under a light microscope after 2 weeks of incubation at 37°C and 5% CO2.
Xia R., Hu C., Ye Y., Zhang X., Li T., He R., Zheng S., Wen X, & Chen R. (2023). HNF1A regulates oxaliplatin resistance in pancreatic cancer by targeting 53BP1. International Journal of Oncology, 62(4), 45.
Publication 2023
Carboplatin Cells Cisplatin Epidermal growth factor Fibroblast Growth Factor Homo sapiens Light Microscopy Oxaliplatin Serum
2
Cell Culture in Serum-Supplemented DMEM/F12
Cells were cultured in DMEM/F12 Ham (Sigma, D6421) with 10% (v/v) foetal calf serum (Labtech), 100 U.mL−1penicillin/ 100 µg.mLstreptomycin (Invitrogen), 2 mM L-glutamine (Invitrogen) and 0.25 ng/ml fibroblast growth factor (R&D Systems).
Gamwell J.M., Paphiti K., Hodson L., Karpe F., Pinnick K.E, & Todorčević M. (2023). An optimised protocol for the investigation of insulin signalling in a human cell culture model of adipogenesis. Adipocyte, 12(1), 2179339.
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Publication 2023
Cells Fetal Bovine Serum Fibroblast Growth Factor Glutamine
3
Cell Culture of Human Lung Fibroblasts and Breast Cancer Cell Lines
All cell culture supplies were purchased from Thermo Fisher Scientific (Waltham, MA, USA) unless otherwise noted. Human lung fibroblast (HLF) cells were purchased from American Type Culture Collection (ATCC) (Manassas, VA, USA) and cultured in Fibroblast basal medium (FBM) (Lonza, Quakertown, PA, USA) supplemented with 2% fetal bovine serum (FBS), 0.1% insulin, 0.1% r-human fibroblast growth factor (rhFGF) and 0.1% Gentamicin sulfate amphotericin-B (GA-1000) (Lonza, Quakertown, PA, USA). HLFs were used from passages 1 to 10. Human breast cancer cell line MDA-MB-231 was provided by Dr. Shannon Hughes. Lung tropic MDA-MB-231 LM2 and MDA-MB-231 cell lines were cultured in Dulbecco’s modified eagle’s medium (DMEM), supplemented with 1% penicillin-streptomycin, and 10% FBS. BT474 cell line was cultured in Roswell Park Memorial Institute (RPMI) 1640 medium, supplemented with 1% penicillin-streptomycin, and 10% FBS.
Kundu A.N., Dougan C.E., Mahmoud S., Kilic A., Panagiotou A., Irakoze N., Richbourg N, & Peyton S.R. (2023). Tenascin-C activation of lung fibroblasts in a 3D synthetic lung extracellular matrix mimic. bioRxiv.
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Publication Preprint 2023
Amphotericin B Cell Culture Techniques Cell Lines Culture Media Eagle endothelial PAS domain protein 1, human Fetal Bovine Serum Fibroblast Growth Factor Fibroblasts Homo sapiens Insulin Lung MCF-7 Cells MDA-MB-231 Cells Penicillins Streptomycin Sulfate, Gentamicin
4
Analyzing Gene Expression and Phenolics
Gene expression and phenolic compound data were analyzed using a two-way ANOVA with phenotype and time as fixed factors and replicate as the random factor. The PROC GLIMMIX procedure of SAS (version 9.4, SAS Institute, Inc., Cary, NC) was used for the analysis. The least significant difference (LSD) test was used for multiple means separation at α = 0.05.
Abbey J., Jose S., Percival D., Jaakola L, & Asiedu S.K. (2023). Modulation of defense genes and phenolic compounds in wild blueberry in response to Botrytis cinerea under field conditions. BMC Plant Biology, 23, 117.
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Publication 2023
Fibroblast Growth Factor Gene Expression neuro-oncological ventral antigen 2, human Phenotype
5
Culturing Peritoneal Tissue Samples
Fresh peritoneal tissue was obtained directly from the operating room, with informed consent from the patients, and transferred immediately to the laboratory in E199 medium (Biochrom AG, Berlin, Germany). The tissue samples were then incubated for 15 min in phosphate-buffered saline (PBS) containing penicillin/streptomycin and amphotericin B (Sigma-Aldrich Chemie, St. Louis, MO, USA). Extraperitoneal fat was removed, and 7 × 7 mm tissue pieces were inserted between two stainless steel rings, which are available in various sizes, and thus enable large variations in the setting of these experiments. Moreover, stainless steel rings are more stable than plastic rings. In this setup, the ring system allows for tissue orientation with the mesothelial cells pointing upwards, thereby better reflecting the peritoneal cavity in the in vivo setting. The peritoneum was cultured in E199 medium containing penicillin/streptomycin, L-glutamine (Biochrom AG), FCS (Thermo Fisher Scientific), hydrocortisone (Sigma-Aldrich Chemie), fibroblast growth factor (PeproTech GmbH, Hamburg, Germany), and heparin (Biochrom AG), as described previously [12 (link)].
Koch J., Beil J., Berchtold S., Mönch D., Maaß A., Smirnow I., Schenk A., Carter M.E., Kloker L.D., Leibold T., Renner P., Dahlke M.H, & Lauer U.M. (2023). Establishing a New Platform to Investigate the Efficacy of Oncolytic Virotherapy in a Human Ex Vivo Peritoneal Carcinomatosis Model. Viruses, 15(2), 363.
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Publication 2023
Amphotericin B Cells Culture Media Fibroblast Growth Factor Glutamine Heparin Hydrocortisone Mesothelium Patients Penicillins Peritoneal Cavity Peritoneum Phosphates Retroperitoneal Fat Saline Solution Stainless Steel Streptomycin Tissues

Top products related to «Fibroblast Growth Factor»

1
Fetal bovine serum (fbs) by Thermo Fisher Scientific
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Fetal Bovine Serum (FBS) is a cell culture supplement derived from the blood of bovine fetuses. FBS provides a source of proteins, growth factors, and other components that support the growth and maintenance of various cell types in in vitro cell culture applications.
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Penicillin streptomycin by Thermo Fisher Scientific
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Penicillin/streptomycin is a commonly used antibiotic solution for cell culture applications. It contains a combination of penicillin and streptomycin, which are broad-spectrum antibiotics that inhibit the growth of both Gram-positive and Gram-negative bacteria.
3
Epidermal growth factor (egf) by Thermo Fisher Scientific
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EGF is a lab equipment product from Thermo Fisher Scientific. It is a recombinant human Epidermal Growth Factor (EGF) protein. EGF is a growth factor that plays a role in cell proliferation and differentiation.
4
Fibroblast growth factor (fgf) by Thermo Fisher Scientific
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The FGF is a laboratory equipment product from Thermo Fisher Scientific. It is designed for the measurement and analysis of fibroblast growth factors. The core function of the FGF is to provide accurate and reliable data for researchers and scientists working in the field of cellular biology and biochemistry.
5
Heparin by Merck Group
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Heparin is a pharmaceutical product manufactured by Merck Group. It is a naturally occurring anticoagulant, primarily used as a laboratory reagent to prevent the clotting of blood samples.
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B27 supplement by Thermo Fisher Scientific
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B27 supplement is a serum-free and animal component-free cell culture supplement developed by Thermo Fisher Scientific. It is designed to promote the growth and survival of diverse cell types, including neurons, embryonic stem cells, and other sensitive cell lines. The core function of B27 supplement is to provide a defined, optimized combination of vitamins, antioxidants, and other essential components to support cell culture applications.
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DMEM/F12 is a cell culture medium developed by Thermo Fisher Scientific. It is a balanced salt solution that provides nutrients and growth factors essential for the cultivation of a variety of cell types, including adherent and suspension cells. The medium is formulated to support the proliferation and maintenance of cells in vitro.
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Epidermal growth factor (egf) by Merck Group
Sourced in United States, Germany, United Kingdom, China, Italy, Canada, Japan, Spain, France, Macao, Israel, Australia, Denmark, Sao Tome and Principe, Morocco, Austria, Portugal, Belgium, Poland, Switzerland
EGF is a laboratory equipment product manufactured by Merck Group. It is a protein that plays a key role in cell growth and differentiation processes. EGF primarily functions as a growth factor, stimulating cell division and proliferation in various cell types.
9
Streptomycin by Thermo Fisher Scientific
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Streptomycin is a broad-spectrum antibiotic used in laboratory settings. It functions as a protein synthesis inhibitor, targeting the 30S subunit of bacterial ribosomes, which plays a crucial role in the translation of genetic information into proteins. Streptomycin is commonly used in microbiological research and applications that require selective inhibition of bacterial growth.
10
Penicillin by Thermo Fisher Scientific
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Penicillin is a type of antibiotic used in laboratory settings. It is a broad-spectrum antimicrobial agent effective against a variety of bacteria. Penicillin functions by disrupting the bacterial cell wall, leading to cell death.

More about "Fibroblast Growth Factor"

Fibroblast Growth Factors (FGFs) are a family of proteins that play a crucial role in a variety of biological processes, including cell proliferation, differentiation, and angiogenesis.
These growth factors, also known as FGF proteins or FGF ligands, are essential for tissue development, repair, and regeneration.
FGFs bind to specific cell surface receptors, triggering signaling cascades that regulate gene expression and cellular functions.
This receptor-ligand interaction is facilitated by heparin, a sulfated polysaccharide, which helps stabilize the FGF-receptor complex.
Research on FGFs has implications for understanding and treating a range of medical conditions, from wound healing to cancer.
FGFs are often used in cell culture media, such as Dulbecco's Modified Eagle Medium (DMEM) and DMEM/F12, to support the growth and differentiation of various cell types, including fibroblasts, epithelial cells, and stem cells.
In addition to FGFs, other growth factors like Epidermal Growth Factor (EGF) and supplements like B27 are commonly used in cell culture to optimize the growth and development of cells.
Antibiotics like penicillin and streptomycin are also frequently included to prevent bacterial contamination.
By leveraging the power of AI-driven research optimization platforms like Pubcompare.AI, researchers can efficiently locate the best protocols and products related to Fibroblast Growth Factors, streamlining their workflow and maximizing the impact of their FGF-related studies.