Humaan FGF basiseiwit, Onderzoeksgraad

FGF basic (also known as FGF2 and HBGF-2) is an 18-34 kDa, heparin-binding member of the FGF superfamily of molecules (1-3) . Superfamily members are characterized by the presence of a centrally placed beta -trefoil structure. FGF acidic (FGF-1) and FGF basic (FGF2) were the first two identified FGFs, and the designations acidic and basic refer to their relative isoelectric points. Human FGF basic is 288 amino acids (aa) in length. There are multiple start sites, four of which utilize atypical CUG codons, and one that initiates at an AUG start site (4 - 6) . The four CUG start sites generate high molecular weight (HMW) FGF basic. There is a 34 kDa, 288 aa form, a 24 kDa, 210 aa form, a 22.5 kDa, 201 aa form, and a 22 kDa, 196 aa form. All are retained intracellularly, undergo extensive methylation, and possess one or more nuclear localization signals (NLS) (7-9) . The AUG initiating form is 18 kDa and 155 aa in length. There is no signal sequence (ss) . It is, however, secreted directly through the plasma membrane via a mechanism that appears to be dependent upon tertiary structure (10) . In place of a ss, there is purportedly a 9 aa N-terminal prosegment that precedes a 146 aa mature segment (11) . Early isolations of 18 kDa bovine FGF basic yielded 146 aa molecules, an effect attributed to the presence of acid proteases (12) . The molecule contains a heparin-binding site (aa residues 128-144), and undergoes phosphorylation at Ser117 (13) . There is also an ill-defined C-terminal NLS that may be more “functional” (or 3-dimensional) than structural (7) . Human 146 aa FGF basic is 97% aa identical to mouse FGF basic (14) .

FGF basic (also known as FGF2 and HBGF-2) is an 18-34 kDa, heparin-binding member of the FGF superfamily of molecules (1-3) . Superfamily members are characterized by the presence of a centrally placed beta -trefoil structure. FGF acidic (FGF-1) and FGF basic (FGF2) were the first two identified FGFs, and the designations acidic and basic refer to their relative isoelectric points. Human FGF basic is 288 amino acids (aa) in length. There are multiple start sites, four of which utilize atypical CUG codons, and one that initiates at an AUG start site (4 - 6) . The four CUG start sites generate high molecular weight (HMW) FGF basic. There is a 34 kDa, 288 aa form, a 24 kDa, 210 aa form, a 22.5 kDa, 201 aa form, and a 22 kDa, 196 aa form. All are retained intracellularly, undergo extensive methylation, and possess one or more nuclear localization signals (NLS) (7-9) . The AUG initiating form is 18 kDa and 155 aa in length. There is no signal sequence (ss) . It is, however, secreted directly through the plasma membrane via a mechanism that appears to be dependent upon tertiary structure (10) . In place of a ss, there is purportedly a 9 aa N-terminal prosegment that precedes a 146 aa mature segment (11) . Early isolations of 18 kDa bovine FGF basic yielded 146 aa molecules, an effect attributed to the presence of acid proteases (12) . The molecule contains a heparin-binding site (aa residues 128-144), and undergoes phosphorylation at Ser117 (13) . There is also an ill-defined C-terminal NLS that may be more “functional” (or 3-dimensional) than structural (7) . Human 146 aa FGF basic is 97% aa identical to mouse FGF basic (14) .

This protein carries no "tag". The protein has a calculated MW of 16.5 kDa. The protein migrates as 17 kDa±3 kDa when calibrated against Star Ribbon Pre-stained Protein Marker under reducing (R) condition (SDS-PAGE) .

Pro 143 - Ser 288

FGF basic

Unconjugated

Native

-20°C to -70°C for 24 months in lyophilized state; -70°C for 3 months under sterile conditions after reconstitution. For long term storage, the product should be stored at lyophilized state at -20°C or lower.

0.01 EU per μg

95%

Powder

PBS, pH7.4

16.5 kDa

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RT

-20°C

20ug*1

E. coli

Human

NP_001997

Trehalose