FGF2 Protein (AA 143-288) (AVI tag,His tag,Biotin)
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- Target See all FGF2 Proteins
- FGF2 (Fibroblast Growth Factor 2 (Basic) (FGF2))
- Protein Type
- Recombinant
- Biological Activity
- Active
- Protein Characteristics
- AA 143-288
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Origin
- Human
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Source
- Escherichia coli (E. coli)
- Purification tag / Conjugate
- This FGF2 protein is labelled with AVI tag,His tag,Biotin.
- Purpose
- Biotinylated Human FGF basic Protein, Avitag™,His Tag (MALS verified)
- Specificity
- Biotinylation of this product is performed using Avitag™ technology. Briefly, the single lysine residue in the Avitag is enzymatically labeled with biotin.
- Purity
- >90 % as determined by SDS-PAGE.
- Endotoxin Level
- Less than 1.0 EU per μg by the LAL method.
- Top Product
- Discover our top product FGF2 Protein
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- Comment
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Ready-to-use Avitag™ biotinylated protein:
The product is exclusively produced using the Avitag™ technology. Briefly, a unique 15 amino acid peptide, the Avi tag, is introduced into the recombinant protein during expression vector construction. The single lysine residue in the Avi tag is enzymatically biotinylated by the E. Coli biotin ligase BirA.
This single-point enzymatic labeling technique brings many advantages for commonly used binding assays. The biotinylation happens on the lysine residue of Avi tag, and therefore does NOT interfere with the target protein's natural binding activities. In addition, when immobilized on an avidin-coated surface, the protein orientation is uniform because the position of the Avi tag in the protein is precisely controlled. - Restrictions
- For Research Use only
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- Format
- Lyophilized
- Buffer
- 50 mM Tris,150 mM NaCl, pH 7.5
- Storage
- -20 °C
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- Target
- FGF2 (Fibroblast Growth Factor 2 (Basic) (FGF2))
- Alternative Name
- FGF basic (FGF2 Products)
- 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.
- Molecular Weight
- 20.1 kDa
- NCBI Accession
- NP_001997
- Pathways
- RTK Signaling, Fc-epsilon Receptor Signaling Pathway, EGFR Signaling Pathway, Neurotrophin Signaling Pathway, C21-Steroid Hormone Metabolic Process, Inositol Metabolic Process, Glycosaminoglycan Metabolic Process, Protein targeting to Nucleus, S100 Proteins
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