Recombinant Human FGF basic/FGF2/bFGF (146 aa) Protein, CF

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Recombinant Human FGF basic/FGF2/bFGF (146 aa) (Catalog # 233-FB/CF) stimulates cell proliferation of the NR6R‑3T3 mouse fibroblast cell line. The activity is approximately 3-fold greater than the top competitor's FGF ...read more
1 µg/lane of Recombinant Human FGF basic/FGF2/bFGF (146 aa) was resolved by SDS-PAGE with silver staining, under reducing (R) conditions, showing a band at 17 kDa.

Product Details

Summary
Reactivity HuSpecies Glossary
Applications Bioactivity
Format
Carrier-Free

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Recombinant Human FGF basic/FGF2/bFGF (146 aa) Protein, CF Summary

Additional Information
Newer 145 aa Version is Available!
Details of Functionality
Measured in a cell proliferation assay using NR6R‑3T3 mouse fibroblast cells. Raines, E.W. et al. (1985) Methods Enzymol. 109:749. The ED50 for this effect is 0.1-0.6 ng/mL.
The specific activity of Recombinant Human FGF basic/FGF2/bFGF  is approximately 2.6 x 106 IU/mg, which is calibrated against recombinant human FGF basic/FGF2/bFGF WHO International Standard (NIBSC code: 90/712).   Specific activity is for reference purposes only and is not routinely tested.  
Source
E. coli-derived human FGF basic/FGF2/bFGF protein
Pro143-Ser288, with an N-terminal Ala
Accession #
N-terminal Sequence
Ala-Pro143
Protein/Peptide Type
Recombinant Proteins
Gene
FGF2
Purity
>97%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.
Endotoxin Note
<0.10 EU per 1 μg of the protein by the LAL method.

Applications/Dilutions

Dilutions
  • Bioactivity
Theoretical MW
16.5 kDa.
Disclaimer note: The observed molecular weight of the protein may vary from the listed predicted molecular weight due to post translational modifications, post translation cleavages, relative charges, and other experimental factors.
SDS-PAGE
17 kDa, reducing conditions
Publications
Read Publications using
233-FB/CF in the following applications:

Packaging, Storage & Formulations

Storage
Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
  • 12 months from date of receipt, -20 to -70 °C as supplied.
  • 1 month, 2 to 8 °C under sterile conditions after reconstitution.
  • 3 months, -20 to -70 °C under sterile conditions after reconstitution.
Buffer
Lyophilized from a 0.2 μm filtered solution in Tris-HCl and NaCl.
Purity
>97%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.
Reconstitution Instructions
Reconstitute at 100-250 μg/mL in sterile PBS.

Notes

This product is produced by and ships from R&D Systems, Inc., a Bio-Techne brand.

Alternate Names for Recombinant Human FGF basic/FGF2/bFGF (146 aa) Protein, CF

  • basic fibroblast growth factor bFGF
  • Basic fibroblast growth factor
  • bFGF
  • FGF basic
  • FGF2
  • FGF-2
  • FGFBprostatropin
  • fibroblast growth factor 2 (basic)
  • HBGF-2
  • heparin-binding growth factor 2
  • Prostatropin

Background

FGF basic (also known as FGF-2 and HBGF-2) is a member of the FGF superfamily of mitogenic proteins which show 35-60% amino acid conservation. FGF acidic and basic are unique from other members of the family in that they lack classical secretory signal peptides. However, they are both readily secreted from cells by an alternative secretory pathway involving direct translocation and aided by several chaperones. FGF acidic (FGF-1) and FGF basic (FGF-2) were the first two identified FGFs, and the designations acidic and basic refer to their relative isoelectric points. The full length human FGF basic protein is 288 amino acids, but there are multiple start sites which produce various shorter forms. Further adding to the complexity, a variety of forms of FGF basic are produced as a result of N-terminal extensions. These extensions affect localization of FGF basic in cellular compartments but do not affect biological activity. FGF basic has been isolated from a number of sources, including neural tissue, adrenal cortex, pituitary gland, corpus luteum, and placenta. Binding of FGF to heparin or cell surface heparan sulfate proteoglycans is required for FGF binding with high affinity to FGF receptors. FGF basic stimulates proliferation of all cells of mesodermal origin as well as many cells of neuroectodermal, ectodermal, and endodermal origin. FGF basic also induces neuronal differentiation, survival, and regeneration, and modulates embryonic development and differentiation. These observed in vitro functions suggest FGF basic may play a role in vivo in the modulation of such normal processes as angiogenesis, wound healing and tissue repair, embryonic development and differentiation, and neuronal function and neural degeneration. Additionally, FGF basic may also participate in the development of several pathological conditions resulting from excessive cell proliferation and/or angiogenesis.

  1. Coulier, F. et al. (1997) J. Mol. Evol. 44:43.
  2. Chen, C.H. et al. (2004) Curr. Vasc. Pharmacol. 2:33.
  3. Mohammadi, M. et al. (2005) Curr. Opin. Struct. Biol. 15:506.
  4. Fernig, D. et al. (1994) Prog. Growth Factor Res. 5:353.

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Publications for FGF basic/FGF2/bFGF (233-FB/CF)(409)

We have publications tested in 14 confirmed species: Human, Mouse, Rat, Bovine, Canine, Chicken, Hamster, Humane, N/A, Porcine, Primate - Callitrix jacchus (Common Marmoset), Squirrel, Xenograft, Zebrafish.

We have publications tested in 9 applications: Binding Assay, Bioassay, Cell Culture, Differentiation, Dififerentiation, ELISA (Standard), In Vivo, Tissue Culture, neural differentiation.


Filter By Application
Binding Assay
(1)
Bioassay
(360)
Cell Culture
(28)
Differentiation
(2)
Dififerentiation
(1)
ELISA (Standard)
(1)
In Vivo
(9)
Tissue Culture
(1)
neural differentiation
(1)
All Applications
Filter By Species
Human
(318)
Mouse
(47)
Rat
(12)
Bovine
(5)
Canine
(3)
Chicken
(6)
Hamster
(1)
Humane
(1)
N/A
(1)
Porcine
(6)
Primate - Callitrix jacchus (Common Marmoset)
(1)
Squirrel
(1)
Xenograft
(1)
Zebrafish
(2)
All Species
Showing Publications 1 - 10 of 409. Show All 409 Publications.
Publications using 233-FB/CF Applications Species
Q Heydt, C Xintaropou, A Clear, M Austin, I Pislariu, F Miraki-Mou, P Cutillas, K Korfi, M Calaminici, W Cawthorn, K Suchacki, A Nagano, JG Gribben, M Smith, JD Cavenagh, H Oakervee, A Castleton, D Taussig, B Peck, A Wilczynska, L McNaughton, D Bonnet, F Mardakheh, B Patel Adipocytes disrupt the translational programme of acute lymphoblastic leukaemia to favour tumour survival and persistence Nature Communications, 2021;12(1):5507. 2021 [PMID: 34535653] (Cell Culture, Human) Cell Culture Human
T Jia, T Jacquet, F Dalonneau, P Coudert, E Vaganay, C Exbrayat-H, J Vollaire, V Josserand, F Ruggiero, JL Coll, B Eymin FGF-2 promotes angiogenesis through a SRSF1/SRSF3/SRPK1-dependent axis that controls VEGFR1 splicing in endothelial cells Bmc Biology, 2021;19(1):173. 2021 [PMID: 34433435] (Bioassay, Human) Bioassay Human
AV Parent, G Faleo, J Chavez, M Saxton, DI Berrios, NR Kerper, Q Tang, M Hebrok Selective deletion of human leukocyte antigens protects stem cell-derived islets from immune rejection Cell Reports, 2021;36(7):109538. 2021 [PMID: 34407395] (Bioassay, Human) Bioassay Human
D Boso, E Carraro, E Maghin, S Todros, A Dedja, M Giomo, N Elvassore, P De Coppi, PG Pavan, M Piccoli Porcine Decellularized Diaphragm Hydrogel: A New Option for Skeletal Muscle Malformations Biomedicines, 2021;9(7):. 2021 [PMID: 34206569] (Bioassay, Human) Bioassay Human
J Dong, J Li, Y Li, Z Ma, Y Yu, CY Wang Transcriptional super-enhancers control cancer stemness and metastasis genes in squamous cell carcinoma Nature Communications, 2021;12(1):3974. 2021 [PMID: 34172737] (Bioassay, Human) Bioassay Human
S Dvir, A Argoetti, C Lesnik, M Roytblat, K Shriki, M Amit, T Hashimshon, Y Mandel-Gut Uncovering the RNA-binding protein landscape in the pluripotency network of human embryonic stem cells Cell Reports, 2021;35(9):109198. 2021 [PMID: 34077720] (Bioassay, Human) Bioassay Human
T Distler, I Lauria, R Detsch, CM Sauter, F Bendt, J Kapr, S Rütten, AR Boccaccini, E Fritsche Neuronal Differentiation from Induced Pluripotent Stem Cell-Derived Neurospheres by the Application of Oxidized Alginate-Gelatin-Laminin Hydrogels Biomedicines, 2021;9(3):. 2021 [PMID: 33808044] (Bioassay, Human) Bioassay Human
RM Agoglia, D Sun, F Birey, SJ Yoon, Y Miura, K Sabatini, SP Pa?ca, HB Fraser Primate cell fusion disentangles gene regulatory divergence in neurodevelopment Nature, 2021;0(0):. 2021 [PMID: 33731928] (Bioassay, Human) Bioassay Human
CV Latchouman, MI Betancur, GA Simchick, MK Sun, R Forghani, CE Lenear, A Ahmed, R Mohankumar, N Balaji, HD Mason, SA Archer-Har, P Azadi, PV Holmes, Q Zhao, RV Bellamkond, L Karumbaiah Engineered glycomaterial implants orchestrate large-scale functional repair of brain tissue chronically after severe traumatic brain injury Science Advances, 2021;7(10):. 2021 [PMID: 33674306] (Bioassay, Rat) Bioassay Rat
X Dong, L Yang, K Liu, X Ji, C Tang, W Li, L Ma, Y Mei, T Peng, B Feng, Z Wu, Q Tang, Y Gao, K Yan, W Zhou, M Xiong Transcriptional networks identify synaptotagmin-like 3 as a regulator of cortical neuronal migration during early neurodevelopment Cell Reports, 2021;34(9):108802. 2021 [PMID: 33657377] (Bioassay, Human) Bioassay Human
Show All 409 Publications.

Reviews for FGF basic/FGF2/bFGF (233-FB/CF) (0)

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FAQs for FGF basic/FGF2/bFGF (233-FB/CF). (Showing 1 - 1 of 1 FAQs).

  1. I am looking for an ovine antibody for bFGF and PDGF-AB and ELISA Kits for both. It is for a research work on meniscus healing in sheep. Do you have anything suitable? How is the homology with sheep? Is it ever tested and/or published in papers?
    • Unfortunately, most of the products you are interested in have not yet been tested in sheep, but this should not be a problem, due to sequence homology, and our Innovators Reward Program. In terms of an antibody for bFGF, also called FGF-2, we have two antibodies that are validated to detect the bovine protein, which is almost identical to that from sheep (99% homology). Here is a link to those FGF-2 antibodies. We only have FGF2 ELISA kits that have been tested with human or mouse. Mouse FGF-2 has 94% homology with sheep; human has 98% homology for most of its sequence, but also has an additional stretch of amino acids that is not present in the sheep protein. I therefore think that the mouse kit would be most suitable, just in case the human kit targets the region of the human protein not present in mouse. We sell antibodies to PDGF-A or PDGF-B rather than PDGF-AB. We don't have any PDGF-A antibodies that have been tested in sheep but there are several options you may find of interest. There isn't a sheep PDGFA sequence in UniProt, so I can't comment on how similar it is to the PDGFA from other species. Nevertheless, our NBP1-52533 PDGFB antibody has been shown to work in sheep. We sell two PDGF-AB ELISA kits , but these are for human and rat. I'm not sure how well these would work with sheep. Note that if you test a product with a species (or application) that it has not yet been validated in, you are eligible for our Innovator's Reward: Novus would provide you a 50% refund on the purchased product as well as a 50% discount on a future product of equal or lesser value. You would email innovators@novusbio.com to apply for your award, and we

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Bioinformatics

Gene Symbol FGF2
Uniprot