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Gibco™ Human FGF-basic (FGF-2/bFGF) Recombinant Protein

Catalog No. 13256029
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13-256-029 10 μg
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Catalog No. 13-256-029 Supplier Gibco™ Supplier No. 13256029
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Recombinant Protein

Carrier-Free Reconstitution: Reconstitute in 100 μL of 10 mM Tris, pH 7.6, to yield a stock solution of 0.1 mg/mL of bFGF. To avoid loss due to adsorption, prepare dilute solutions in appropriate assay buffer containing at least 0.1% BSA just prior to use. Do not store in dilute solution. For longer term storage, aliquot into buffer containing 0.1% BSA and store in polypropylene vials at -20°C. Avoid repeated freezing and thawing. In applications requiring long-term use of this growth factor in cell cultures, refilter material after dilution in BSA-containing buffer, through a 0.22 micron low protein-binding filter Storage: Six months at -20°C as received. Up to six months at -20°C when aliquoted into solution containing carrier protein (see Reconstitution Recommendation). NOTE: Do not store in dilute aqueous solution. Avoid repeated freeze/thaw.

FGF2 (FGFb, fibroblast growth factor basic) belongs to the fibroblast growth factor (FGF) family, and interacts with high-affinity transmembrane receptors to influence cell proliferation and tissue neovascularization. FGF2 exists as five isoforms with distinct intracellular localizations and functions. The 18 kDa isoform is predominantly cytosolic and acts through cell surface receptors, whereas the 22, 22.5, 24 and 34 kDa isoforms are nuclear and may signal independent of transmembrane receptor pathways. In humans, the gene is located on the q arm of chromosome 4. FGF2 has been implicated in diverse biological processes, such as limb and nervous system development, wound healing, and tumor growth. The mRNA for FGF2 contains multiple polyadenylation sites, and is alternatively translated from non-AUG and AUG initiation codons, resulting in five different isoforms with distinct properties. The CUG-initiated isoforms are localized in the nucleus and are responsible for the intracrine effect, whereas, the AUG-initiated form is mostly cytosolic and is responsible for the paracrine and autocrine effects of this FGF. Diseases associated with FGF2 dysfunction include Kaposi Sarcoma and corneal neovascularization.
TRUSTED_SUSTAINABILITY

Specifications

Accession Number P09038
For Use With (Application) Bioactivity
Formulation Protein with no preservative
Gene ID (Entrez) 2247
Name Human FGF-basic (FGF-2/bFGF)
Purification Method Purified
Quantity 10 μg
Storage Requirements -20°C
Regulatory Status RUO
Endotoxin Concentration ≤0.1 ng/μg
Gene Alias Basic fibroblast growth factor; basic fibroblast growth factor bFGF; bFGF; FGF; fgf basic; Fgf2; Fgf-2; Fgfb; FGF-b; Fibroblast growth factor; fibroblast growth factor 2; fibroblast growth factor 2 (basic); Fibroblast growth factor basic; HBGF-2; Heparin-binding growth factor 2; H-FGF-b-147; H-FGF-b-154; M-FGF-b; Prostatic growth factor; prostatropin
Common Name FGF2
Gene Symbol FGF2
Biological Activity ED50 < 1.0 ng/mL; determined by the dose-dependent stimulation of BALB/3T3 cells.
Product Type Protein
Conjugate Unconjugated
Species Human
Recombinant Recombinant
Content And Storage -20°C
Classification Carrier-Free
Activity ED50 < 1.0 ng/mL; determined by the dose-dependent stimulation of BALB/3T3 cells.
Endotoxin Level <0.1 ng/μg
Shipping Condition Dry Ice
Expression System E. coli
Protein Family Growth Factors & Receptors
Protein Form Full Length, Recombinant, Ligand
Form Lyophilized
Protein Subtype FGFs (Fibroblast Growth Factors)
Research Category Neurobiology, Oncology, Stem Cell Research, Microbiology, Differentiation, Angiogenesis
Purity or Quality Grade ≥95% by SDS-PAGE
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Can I reconstitute bFGF Recombinant Human Protein (Cat. No. 13256029) in distilled water?

As bFGF Recombinant Human Protein can lose some activity in purely aqueous solutions, we recommend resuspending the product in 10 mM Tris, pH 7.6 as recommended in the product sheet.

It looks like the recombinant protein vial I received from you is empty. Is this normal?

Gibco recombinant proteins are frequently formulated without carrier proteins or additives (e.g., BSA, HSA, sucrose, etc.) and no Gibco PeproTech recombinant protein contains a carrier protein. As a result, during lyophilization, the protein product may be deposited on the vial as a thin, and sometimes invisible, film instead of a pellet. The size of the pellet, if any, is not directly related to the quantity of the recombinant protein in the vial. Our quality control procedures assure that each vial contains the correct amount of product.

To ensure complete recovery of protein product, before opening a vial of lyophilized recombinant protein, we recommend centrifuging it in a microcentrifuge for 20-30 seconds to drive any protein that may be lodged in the cap or on the side to the bottom of the vial. After reconstitution, you can confirm the presence of product protein by running a small amount on SDS-PAGE. In general, a protein band with expected size should be visible with as little as 10 ng of protein loaded on an acrylamide gel.

Why does my recombinant protein not show activity in my own experiment?

Assay time is critical. Each assay needs to beoptimized and performed at the peak response time. Different cells may respond differently to a growth factor or cytokine. We suggest repeating our QC assay using same indicator cells as suggested in the manual to see if you can obtain a similar response. In addition, serum may be masking the response. Serum starvation might be needed for certain types of assays.

How should I store the reconstituted recombinant proteins?

Protein solutions are generally not very stable when frozen at low concentration. Upon freeze and thaw, some proteins in the solution may stick to the wall of the container, which results in significant reduction of protein concentration if the starting concentration was low. Therefore, carrier proteins are used to reduce such loss. The most commonly used carrier proteins include bovine serum albumin (BSA), human serum albumin (HSA), or fetal bovine serum (FBS). These carrier proteins are generally used at 0.1% concentration. As a rule of thumb, if the concentration of the recombinant protein is less than 0.5 mg/mL, it is a good idea to add some carrier protein

How do I store my lyophilized recombinant protein?

Lyophilized proteins can typically be stored at 2 to 8 degrees C for several weeks, or stored dessicated at -20 degrees C for long-term storage.

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