Home / FGF acidic/FGF1 / Recombinant Human FGF acidic/FGF1 (aa 16-155) Protein

Recombinant Human FGF acidic/FGF1 (aa 16-155) Protein

Catalog #: 232-FA
22 Citations 1 Review Datasheet / COA / SDS

Carrier Free

Catalog # Availability Size / Price Qty
232-FA-025/CF

With Carrier

Catalog # Availability Size / Price Qty
232-FA-025
Best Seller
R&D Systems Recombinant Proteins and Enzymes
1 Image
Product Details
Citations (22)
FAQs
Supplemental Products
Reviews (1)
Summary Product Datasheets Carrier Free Data Images Reconstitution Calculator Background Related Research Areas

Recombinant Human FGF acidic/FGF1 (aa 16-155) Protein Summary

Product Specifications

Purity
>97%, by SDS-PAGE under reducing conditions and visualized by silver stain.
Endotoxin Level
<0.01 EU per 1 μg of the protein by the LAL method.
Activity
Measured in a cell proliferation assay using NR6R‑3T3 mouse fibroblast cells. Rizzino, A. et al. (1988) Cancer Res. 48:4266; Thomas, K. et al. (1987) Methods Enzymol. 147:120. The ED50 for this effect is 0.015-0.15 ng/mL in the presence of 10 µg/mL of heparin.
Source
E. coli-derived human FGF acidic/FGF1 protein
Phe16-Asp155, with an N-terminal Met
Accession #
NP_000791
N-terminal Sequence
Analysis
Met
Predicted Molecular Mass
15.5 kDa

Product Datasheets

You must select a language.

x

232-FA (with carrier)

Product Datasheet
COA
SDS

You must select a language.

x

232-FA/CF (carrier free)

Product Datasheet
COA
SDS

Carrier Free

What does CF mean?

CF stands for Carrier Free (CF). We typically add Bovine Serum Albumin (BSA) as a carrier protein to our recombinant proteins. Adding a carrier protein enhances protein stability, increases shelf-life, and allows the recombinant protein to be stored at a more dilute concentration. The carrier free version does not contain BSA.

What formulation is right for me?

In general, we advise purchasing the recombinant protein with BSA for use in cell or tissue culture, or as an ELISA standard. In contrast, the carrier free protein is recommended for applications, in which the presence of BSA could interfere.

232-FA

Formulation Lyophilized from a 0.2 μm filtered solution in MOPS, Na2SO4 and EDTA with BSA as a carrier protein.
Reconstitution Reconstitute at 100 μg/mL in sterile PBS containing at least 0.1% human or bovine serum albumin.
Shipping The product is shipped at ambient temperature. Upon receipt, store it immediately at the temperature recommended below.
Stability & 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 °C under sterile conditions after reconstitution.

232-FA/CF

Formulation Lyophilized from a 0.2 μm filtered solution in MOPS, Na2SO4 and EDTA.
Reconstitution Reconstitute at 100 μg/mL in sterile PBS.
Shipping The product is shipped at ambient temperature. Upon receipt, store it immediately at the temperature recommended below.
Stability & 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 °C under sterile conditions after reconstitution.
Reconstitution Calculator

Reconstitution Calculator

The reconstitution calculator allows you to quickly calculate the volume of a reagent to reconstitute your vial. Simply enter the mass of reagent and the target concentration and the calculator will determine the rest.

=
÷

Background: FGF acidic/FGF1

FGF acidic, also known as FGF1, ECGF, and HBGF-1, is a 17 kDa nonglycosylated member of the FGF family of mitogenic peptides. FGF acidic, which is produced by multiple cell types, stimulates the proliferation of all cells of mesodermal origin and many cells of neuroectodermal, ectodermal, and endodermal origin. It plays a number of roles in development, regeneration, and angiogenesis (1-3). Human FGF acidic shares 54% amino acid sequence identity with FGF basic and 17%‑33% with other human FGFs. It shares 92%, 96%, 96%, and 96% aa sequence identity with bovine, mouse, porcine, and rat FGF acidic, respectively, and exhibits considerable species crossreactivity. Alternate splicing generates a truncated isoform of human FGF acidic that consists of the N-terminal 40% of the molecule and functions as a receptor antagonist (4). During its nonclassical secretion, FGF acidic associates with S100A13, copper ions, and the C2A domain of synaptotagmin 1 (5). It is released extracellularly as a disulfide-linked homodimer and is stored in complex with extracellular heparan sulfate (6). The ability of heparan sulfate to bind FGF acidic is determined by its pattern of sulfation, and alterations in this pattern during embryogenesis thereby regulate FGF acidic bioactivity (7). The association of FGF acidic with heparan sulfate is a prerequisite for its subsequent interaction with FGF receptors (8, 9). Ligation triggers receptor dimerization, transphosphorylation, and internalization of receptor/FGF complexes (10). Internalized FGF acidic can translocate to the cytosol with the assistance of Hsp90 and then migrate to the nucleus by means of its two nuclear localization signals (11-13). The phosphorylation of FGF acidic by nuclear PKC delta triggers its active export to the cytosol where it is dephosphorylated and degraded (14, 15). Intracellular FGF acidic functions as a survival factor by inhibiting p53 activity and proapoptotic signaling (16).

References
  1. Jaye, M. et al. (1986) Science 233:541.
  2. Galzie, Z. et al. (1997) Biochem. Cell Biol. 75:669.
  3. Presta, M. et al. (2005) Cytokine Growth Factor Rev. 16:159.
  4. Yu, Y.L. et al. (1992) J. Exp. Med. 175:1073.
  5. Rajalingam, D. et al. (2007) Biochemistry 46:9225.
  6. Guerrini, M. et al. (2007) Curr. Pharm. Des. 13:2045.
  7. Allen, B.L. and A.C. Rapraeger (2003) J. Cell Biol. 163:637.
  8. Robinson, C.J. et al. (2005) J. Biol. Chem. 280:42274.
  9. Mohammadi, M. et al. (2005) Cytokine Growth Factor Rev. 16:107.
  10. Wiedlocha, A. and V. Sorensen (2004) Curr. Top. Microbiol. Immunol. 286:45.
  11. Wesche, J. et al. (2006) J. Biol. Chem. 281:11405.
  12. Imamura, T. et al. (1990) Science 249:1567.
  13. Wesche, J. et al. (2005) Biochemistry 44:6071.
  14. Wiedlocha, A. et al. (2005) Mol. Biol. Cell 16:794.
  15. Nilsen, T. et al. (2007) J. Biol. Chem. 282:26245.
  16. Bouleau, S. et al. (2005) Oncogene 24:7839.
Long Name
Fibroblast Growth Factor acidic
Entrez Gene IDs
2246 (Human); 14164 (Mouse); 25317 (Rat); 281160 (Bovine)
Alternate Names
AFGF; alpha; alpha-ECGF; beta-ECGF; ECGF; ECGFB; ECGF-betaAcidic fibroblast growth factor; endothelial cell growth factor, beta; FGF acidic; FGF-1; FGFABeta-endothelial cell growth factor; FGF-alpha; fibroblast growth factor 1 (acidic); GLIO703; HBGF1; HBGF-1; heparin-binding growth factor 1

Citations for Recombinant Human FGF acidic/FGF1 (aa 16-155) Protein

R&D Systems personnel manually curate a database that contains references using R&D Systems products. The data collected includes not only links to publications in PubMed, but also provides information about sample types, species, and experimental conditions.

22 Citations: Showing 1 - 10
Filter your results:

Filter by:

  1. Estrogen regulation and functional role of FGFR4 in estrogen receptor positive breast cancer
    Authors: Ding, K;Chen, L;Levine, K;Sikora, M;Tasdemir, N;Dabbs, D;Jankowitz, R;Hazan, R;Shah, OS;Atkinson, JM;Lee, AV;Oesterreich, S;
    bioRxiv : the preprint server for biology
    Species: Human
    Sample Types: Whole Cells
    Applications: Bioassay
  2. Beneficial Effects of Fibroblast Growth Factor-1 on Retinal Pigment Epithelial Cells Exposed to High Glucose-Induced Damage: Alleviation of Oxidative Stress, Endoplasmic Reticulum Stress, and Enhancement of Autophagy
    Authors: Huang, HW;Yang, CM;Yang, CH;
    International journal of molecular sciences
    Species: Human
    Sample Types: Whole Cells
    Applications: Bioassay
  3. Localized astrogenesis regulates gyrification of the cerebral cortex
    Authors: Y Shinmyo, K Saito, T Hamabe-Hor, N Kameya, A Ando, K Kawasaki, TAD Duong, M Sakashita, J Roboon, T Hattori, T Kannon, K Hosomichi, M Slezak, MG Holt, A Tajima, O Hori, H Kawasaki
    Science Advances, 2022-03-11;8(10):eabi5209.
    Species: Mouse
    Sample Types: Whole Cells
    Applications: Bioassay
  4. Fibroblast Growth Factor Type 1 Ameliorates High-Glucose-Induced Oxidative Stress and Neuroinflammation in Retinal Pigment Epithelial Cells and a Streptozotocin-Induced Diabetic Rat Model
    Authors: HW Huang, CM Yang, CH Yang
    International Journal of Molecular Sciences, 2021-07-05;22(13):.
    Species: Human
    Sample Types: Whole Cells
    Applications: Bioassay
  5. FGF signal is not required for hepatoblast differentiation of human iPS cells
    Authors: Y Toba, A Kiso, S Nakamae, F Sakurai, K Takayama, H Mizuguchi
    Sci Rep, 2019-03-06;9(1):3713.
    Species: Human
    Sample Types: Whole Cells
    Applications: Bioassay
  6. Higher-Order Kidney Organogenesis from Pluripotent Stem Cells
    Authors: A Taguchi, R Nishinakam
    Cell Stem Cell, 2017-11-09;0(0):.
    Species: Human
    Sample Types: Whole Cells
    Applications: Bioassay
  7. Reciprocal cellular cross-talk within the tumor microenvironment promotes oncolytic virus activity.
    Authors: Ilkow C, Marguerie M, Batenchuk C, Mayer J, Ben Neriah D, Cousineau S, Falls T, Jennings V, Boileau M, Bellamy D, Bastin D, de Souza C, Alkayyal A, Zhang J, Le Boeuf F, Arulanandam R, Stubbert L, Sampath P, Thorne S, Paramanthan P, Chatterjee A, Strieter R, Burdick M, Addison C, Stojdl D, Atkins H, Auer R, Diallo J, Lichty B, Bell J
    Nat Med, 2015-04-20;21(5):530-6.
    Species: Human
    Sample Types: Whole Cells
    Applications: Bioassay
  8. Patient-specific iPSC-derived photoreceptor precursor cells as a means to investigate retinitis pigmentosa.
    Authors: Tucker, Budd A, Mullins, Robert F, Streb, Luan M, Anfinson, Kristin, Eyestone, Mari E, Kaalberg, Emily, Riker, Megan J, Drack, Arlene V, Braun, Terry A, Stone, Edwin M
    Elife, 2013-08-27;2(0):e00824.
    Species: Human
    Sample Types: Whole Cells
    Applications: Bioassay
  9. Use of a synthetic xeno-free culture substrate for induced pluripotent stem cell induction and retinal differentiation.
    Authors: Tucker B, Anfinson K, Mullins R, Stone E, Young M
    Stem Cells Transl Med, 2012-12-27;2(1):16-24.
    Species: Human
    Sample Types: Whole Cells
    Applications: Bioassay
  10. Identification of BMP and activin membrane-bound inhibitor (BAMBI) as a potent negative regulator of adipogenesis and modulator of autocrine/paracrine adipogenic factors.
    Authors: Luo X, Hutley LJ, Webster JA, Kim YH, Liu DF, Newell FS, Widberg CH, Bachmann A, Turner N, Schmitz-Peiffer C, Prins JB, Yang GS, Whitehead JP
    Diabetes, 2012-01-01;61(1):124-36.
    Species: Human
    Sample Types: Whole Cells
    Applications: Bioassay
  11. Human embryonic and rat adult stem cells with primitive endoderm-like phenotype can be fated to definitive endoderm, and finally hepatocyte-like cells.
    Authors: Roelandt P, Pauwelyn KA, Sancho-Bru P
    PLoS ONE, 2010-08-11;5(8):e12101.
    Species: Human
    Sample Types: Whole Cells
    Applications: Cell Culture
  12. Similar expression to FGF (Sef) inhibits fibroblast growth factor-induced tumourigenic behaviour in prostate cancer cells and is downregulated in aggressive clinical disease.
    Authors: Darby S, Murphy T, Thomas H, Robson CN, Leung HY, Mathers ME, Gnanapragasam VJ
    Br. J. Cancer, 2009-11-03;101(11):1891-9.
    Species: Human
    Sample Types: Whole Cells
    Applications: Bioassay
  13. The lineage-c-Kit+Sca-1+ cell response to Escherichia coli bacteremia in Balb/c mice.
    Authors: Zhang P, Nelson S, Bagby GJ, Siggins R, Shellito JE, Welsh DA
    Stem Cells, 2008-05-15;26(7):1778-86.
    Species: Mouse
    Sample Types: Whole Cells
    Applications: Bioassay
  14. Specific heparan sulfate structures modulate FGF10-mediated submandibular gland epithelial morphogenesis and differentiation.
    Authors: Patel VN, Likar KM, Zisman-Rozen S, Cowherd SN, Lassiter KS, Sher I, Yates EA, Turnbull JE, Ron D, Hoffman MP
    J. Biol. Chem., 2008-01-28;283(14):9308-17.
    Species: Mouse
    Sample Types: Whole Cells
    Applications: Bioassay
  15. Heparanase cleavage of perlecan heparan sulfate modulates FGF10 activity during ex vivo submandibular gland branching morphogenesis.
    Authors: Patel VN, Knox SM, Likar KM, Lathrop CA, Hossain R, Eftekhari S, Whitelock JM, Elkin M, Vlodavsky I, Hoffman MP
    Development, 2007-10-24;134(23):4177-86.
    Species: Mouse
    Sample Types: Whole Cells
    Applications: Bioassay
  16. Liver-specific activities of FGF19 require Klotho beta.
    Authors: Lin BC, Wang M, Blackmore C, Desnoyers LR
    J. Biol. Chem., 2007-07-11;282(37):27277-84.
    Species: Human
    Sample Types: Whole Cells
    Applications: Bioassay
  17. MIP-1alpha (CCL3) is a downstream target of FGFR3 and RAS-MAPK signaling in multiple myeloma.
    Authors: Masih-Khan E, Trudel S, Heise C, Li Z, Paterson J, Nadeem V, Wei E, Roodman D, Claudio JO, Bergsagel PL, Stewart AK
    Blood, 2006-07-18;108(10):3465-71.
    Species: Human
    Sample Types: Whole Cells
    Applications: Bioassay
  18. Differentiation of human embryonic stem cells into hepatocytes in 2D and 3D culture systems in vitro.
    Authors: Baharvand H, Hashemi SM, Kazemi Ashtiani S, Farrokhi A
    Int. J. Dev. Biol., 2006-01-01;50(7):645-52.
    Species: Human
    Sample Types: Whole Cells
    Applications: Bioassay
  19. Prox1 promotes lineage-specific expression of fibroblast growth factor (FGF) receptor-3 in lymphatic endothelium: a role for FGF signaling in lymphangiogenesis.
    Authors: Shin JW, Min M, Larrieu-Lahargue F, Canron X, Kunstfeld R, Nguyen L, Henderson JE, Bikfalvi A, Detmar M, Hong YK
    Mol. Biol. Cell, 2005-11-16;17(2):576-84.
    Species: Human
    Sample Types: Whole Cells
    Applications: Bioassay
  20. FGFR2b signaling regulates ex vivo submandibular gland epithelial cell proliferation and branching morphogenesis.
    Authors: Steinberg Z, Myers C, Heim VM, Lathrop CA, Rebustini IT, Stewart JS, Larsen M, Hoffman MP
    Development, 2005-02-16;132(6):1223-34.
    Species: Mouse
    Sample Types: Whole Cells
    Applications: Bioassay
  21. Liver tissue engineering at extrahepatic sites in mice as a potential new therapy for genetic liver diseases.
    Authors: Ohashi K, Waugh JM, Dake MD, Yokoyama T, Kuge H, Nakajima Y, Yamanouchi M, Naka H, Yoshioka A, Kay MA
    Hepatology, 2005-01-01;41(1):132-40.
    Species: Mouse
    Sample Types: In Vivo
    Applications: In Vivo
  22. A stepwise method for the isolation of endothelial cells and smooth muscle cells from individual canine coronary arteries.
    Authors: Dame MK, Yu X, Garrido R, Bobrowski W, McDuffie JE, Murphy HS, Albassam M, Varani J
    In Vitro Cell. Dev. Biol. Anim., 2003-11-01;39(10):402-6.
    Species: Canine
    Sample Types: Whole Cells
    Applications: Bioassay

FAQs

No product specific FAQs exist for this product, however you may

View all Proteins and Enzyme FAQs
Loading...

Reviews for Recombinant Human FGF acidic/FGF1 (aa 16-155) Protein

Average Rating: 4 (Based on 1 Review)

5 Star
0%
4 Star
100%
3 Star
0%
2 Star
0%
1 Star
0%

Have you used Recombinant Human FGF acidic/FGF1 (aa 16-155) Protein?

Submit a review and receive an Amazon gift card.

$25/€18/£15/$25CAN/¥75 Yuan/¥1250 Yen for a review with an image

$10/€7/£6/$10 CAD/¥70 Yuan/¥1110 Yen for a review without an image

Submit a Review

Filter by:


Recombinant Human FGF acidic (aa 16-155) Protein
By Anonymous on 09/22/2018
Application: In vitro bioactivity in cell culture
In vitro bioactivity in cell culture Recombinant Human FGF acidic (aa 16-155) Protein 232-FA