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Human FGF basic Protein, Tag Free  pdf  pdf  pdf


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Synonym

FGF2,BFGF,FGFB,FGF basic,HBGF-2

Source

Human FGF basic, Tag Free (BFF-H4117) is expressed from E.coli cells. It contains AA Pro 143 - Ser 288 (Accession # NP_001997).

Predicted N-terminus: Met

Molecular Characterization

FGF basic(Pro 143 - Ser 288)NP_001997

This protein carries no "tag".

The protein has a calculated MW of 16.5 kDa. The protein migrates as 17 kDa on a SDS-PAGE gel under reducing (R) condition.

Endotoxin

Less than 1.0 EU per μg by the LAL method.

 

Purity

>98% as determined by SDS-PAGE.

Formulation

Lyophilized from 0.22 μm filtered solution in PBS, pH7.4. Normally trehalose is added as protectant before lyophilization.

Contact us for customized product form or formulation.

Reconstitution

Please see Certificate of Analysis for specific instructions.

For best performance, we strongly recommend you to follow the reconstitution protocol provided in the CoA.

Storage

For long term storage, the product should be stored at lyophilized state at -20°C or lower.

Please avoid repeated freeze-thaw cycles.

No activity loss is observed after storage at:

  1. 4-8°C for 12 months in lyophilized state;
  2. -70°C for 3 months under sterile conditions after reconstitution.
 

SDS-PAGE

Human FGF basic, Tag Free (Catalog # BFF-H4117) SDS-PAGE gel

Human FGF basic, Tag Free on SDS-PAGE under reducing (R) condition. The gel was stained overnight with Coomassie Blue. The purity of the protein is greater than 98%.

Bioactivity

Human FGF basic, Tag Free (Catalog # BFF-H4117) ELISA bioactivity

Immobilized Human FGF basic, Tag Free (Catalog # BFF-H4117) at 2μg/mL (100 μL/well) can bind Human Glypican 3, Fc Tag (Catalog # GP3-H5258) with a linear range of 0.48-7.8 ng/mL.

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Citations

Background

FGF basic is a member of the FGF family of at least 23 related mitogenic proteins which show 35-60% amino acid conservation. FGF acidic and basic, unlike the other members of the family, lack signal peptides and are apparently secreted by mechanisms other than the classical protein secretion pathway. FGF basic has been isolated from a number of sources, including neural tissue, pituitary, adrenal cortex, corpus luteum, and placenta. This factor contains four cysteine residues, but reduced FGF basic retains full biological activity, indicating that disulfide bonds are not required for this activity. bFGF is a critical component of human embryonic stem cell culture medium; the growth factor is necessary for the cells to remain in an undifferentiated state, although the mechanisms by which it does this are poorly defined. It has been demonstrated to induce gremlin expression which in turn is known to inhibit the induction of differentiation by bone morphogenetic proteins. It is necessary in mouse-feeder cell dependent culture systems, as well as in feeder and serum-free culture systems.

References

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