Recombinant Human FGF-4, Animal-Free Protein Summary
Learn more about Animal-Free Recombinant ProteinsAnimal Free Proteins
Animal-free proteins are particularly important for researchers concerned with experimental variables caused by trace animal components or mammalian pathogens. Our products generated under animal-free conditions share the same biological activities as those produced using our standard laboratory techniques.
Product Specifications
Ser54-Leu206
Produced using non-animal reagents in an animal-free laboratory.
Analysis
Complete Your Research
Complete Your Experiment
Product Datasheets
Carrier Free
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.
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.
AFL235
Formulation | Lyophilized from a 0.2 μm filtered solution in PBS. |
Reconstitution | Reconstitute at 0.2 mg/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.
|
Animal Free Proteins
Animal-free proteins are particularly important for researchers concerned with experimental variables caused by trace animal components or mammalian pathogens. Our products generated under animal-free conditions share the same biological activities as those produced using our standard laboratory techniques.
Reconstitution Calculator
Background: FGF-4
FGF-4 (fibroblast growth factor-4), also known as FGF-K or K-FGF (Kaposi’s sarcoma-associated FGF), is a 25 kDa secreted, heparin-binding member of the FGF family (1, 2). The human FGF-4 cDNA encodes 206 amino acids (aa) with a 33 aa signal sequence and a 173 aa mature protein with an FGF homology domain that contains a heparin binding region near the C-terminus (2). Mature human FGF-4 (aa 71-206) shares 91%, 82%, 94% and 91% aa identity with mouse, rat, canine and bovine FGF-4, respectively. Human FGF-4 has been shown to exhibit cross species activity. Expression of FGF-4 and its receptors, FGF R1c, 2c, 3c and 4, is spatially and temporally regulated during embryonic development (1, 3). Its expression in the mouse trophoblast inner cell mass promotes expression of FGF R2, and is required for maintenance of the trophectoderm and primitive endoderm (3-5). Later in mouse development, FGF-4 works together with FGF-8 to mediate the activities of the apical ectodermal ridge, which direct the outgrowth and patterning of vertebrate limbs (3, 6-9). FGF-4 is proposed to play a physiologically relevant role in human embryonic stem cell self-renewal. It promotes stem cell proliferation, but may also aid differentiation depending on context and concentration, and is often included in embryonic stem cell media in vitro (10-12). A C-terminally truncated 15 kDa isoform that opposes full-length FGF-4 and promotes differentiation is endogenously expressed in human embryonic stem cells. FGF-4 is mitogenic for fibroblasts and endothelial cells in vitro and has autocrine transforming potential (13). It is a potent angiogenesis promoter in vivo and has been investigated as therapy for coronary artery disease (14).
- Reuss, B. and O. von Bohlen und Halbach (2003) Cell Tiss. Res. 313:139.
- Hebert, J.M. et al. (1990) Dev. Biol. 138:454.
- Niswander, L. and G.R. Martin (1992) Development 114:755.
- Feldman, B. et al. (1995) Science 267:246.
- Goldin, S.N. and V.E. Papaioannou (2003) Genesis 36:40.
- Sun, X. et al. (2002) Nature 418:501.
- Boulet, A.M. et al. (2004) Dev. Biol. 273:361.
- Yu, K and D.M. Ornitz (2008) Development 135:483.
- Mariani, F.V. et al. (2008) Nature 453:401.
- Johannesson, M. et al. (2009) PLoS ONE 4:e4794.
- Kunath, T. et al. (2007) Development 134:2895.
- Mayshar, Y. et al. (2008) Stem Cells 26:767.
- Hajitou, A. et al. (1998) Oncogene 17:2059.
- Flynn, A. and T. O’Brien (2008) IDrugs 11:283.
Manufacturing Specifications
Animal-Free Manufacturing ConditionsOur dedicated controlled-access animal-free laboratories ensure that at no point in production are the products exposed to potential contamination by animal components or byproducts. Every stage of manufacturing is conducted in compliance with R&D Systems' stringent Standard Operating Procedures (SOPs). Production and purification procedures use equipment and media that are confirmed animal-free.
Production
- All molecular biology procedures use animal-free media and dedicated labware.
- Dedicated fermentors are utilized in committed animal-free areas.
Purification
- Protein purification columns are animal-free.
- Bulk proteins are filtered using animal-free filters.
- Purified proteins are stored in animal-free containers in a dedicated cold storage room.
- Low Endotoxin Level.
- No impairment of biological activity.
- High quality product obtained under stringent conditions.
- For ex vivo research or bioproduction, additional documentation can be provided.
FAQs
No product specific FAQs exist for this product, however you may
View all Proteins and Enzyme FAQsReviews for Recombinant Human FGF-4, Animal-Free Protein
There are currently no reviews for this product. Be the first to review Recombinant Human FGF-4, Animal-Free Protein and earn rewards!
Have you used Recombinant Human FGF-4, Animal-Free 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