Human FGF-8b Protein, Research Grade

Research use only
This product is designed for academic and scientific research institutions.
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FGB-H5116-20ug
$150.00
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FGB-H5116-100ug
$460.00
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FGB-H5116-1mg (200ug X 5)
$2,230.00
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FGB-H5116
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  • Product Details
  • Performance Data
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  • Important Statement
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Features and Advantages
  • Native Conformation: Native sequences, tag-free and natural function.
  • Reliable Activity: Biological activity calibrated against WHO/NIBSC standards.
  • Stringent Quality Control: Protein content, purity, and cell-based bioactivity testing for each batch.
  • Lowest Endotoxin level (<0.01 EU/ug).
  • Safety Assurance: Sterile filtration through 0.2 μm membrane.
  • AOF: Animal origin-free raw materials throughout the production process.
Synonyms

FGF8, Fibroblast growth factor 8, FGF-8,Androgen-induced growth factor,Heparin-binding growth factor 8 , AIGF

Source

Human FGF-8b Protein, Research Grade (FGB-H5116) is expressed from E. coli cells. It contains AA Gln 23 - Arg 215 (Accession # P55075-3).

Predicted N-terminus: Met

Molecular Characterization

This protein carries no "tag".

The protein has a calculated MW of 22.5 kDa. The protein migrates as 25 kDa±3 kDa when calibrated against Star Ribbon Pre-stained Protein Marker under reducing (R) condition (SDS-PAGE).

Endotoxin

Less than 0.01 EU per μg by the LAL method / rFC method.

Purity

>95% as determined by SDS-PAGE.

Formulation

Lyophilized from 0.22 μm filtered solution in PBS, pH7.4 with trehalose as protectant.

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.

Shipping and Storage

This product is shipped at ambient temperature.

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

Please avoid repeated freeze-thaw cycles.

This product is stable after storage at:
  • -20°C to -70°C for 24 months in lyophilized state;
  • -70°C for 3 months under sterile conditions after reconstitution.
Quality Description

ACRO's Research-grade products are suitable for a wide range of cell culture applications, particularly for research use in academic institutions. These products are sterilized by filtration, followed by lyophilization where applicable. Typical specifications include endotoxin levels of <0.01 EU/μg and purities >95%. Biological activity is calibrated against WHO/NIBSC standards when available.
ACRO's Premium-grade (Pre-GMP) products are characterized by their high quality and enhanced safety profiles, making them ideal for early-stage discovery and manufacturing processes in cell therapy companies. A key advantage is their seamless transition to corresponding GMP-grade versions. Biological activity is calibrated against WHO/NIBSC standards when available. Typical specifications include endotoxin levels of <0.01 EU/μg and purities >95%. In addition, rigorous testing is conducted to ensure the absence of mycoplasma, HCD, and HCP, thereby guaranteeing product safety.

Background

FGF-8 is a member of the fibroblast growth factor family that was originally discovered as a growth factor essential for the androgen-dependent growth of mouse mammary carcinoma cells (1-3). Alternate splicing of mouse FGF-8 mR generates eight secreted isoforms, designated a-h, but only FGF-8a, b, e and f exist in humans (4). FGF-8 contains a 22 amino acid (aa) signal sequence, an N‑terminal domain that varies according to the isoform (30 aa for FGF-8b; 20 aa for the shortest, FGF-8a), a 125 aa FGF domain and a 37 aa proline‑rich C‑terminal sequence. The FGF domain of FGF-8 shares the most aa identity with FGF17 (75%) and FGF-18 (67%), and the three form an FGF subfamily (2). Mouse FGF-8b shares 100% aa identity with human FGF-8b. FGF-8 is widely expressed during embryogenesis, and mediates epithelial-mesenchymal transitions. It plays an organizing and inducing role during gastrulation, and regulates patterning of the midbrain/hindbrain, eye, ear, limbs and heart in the embryo (2, 5 - 8). The isoforms may play different roles in development. FGF-8b shows the strongest receptor affinity and oncogenic transforming capacity although FGF-8a and FGF-8e are also transforming and have been found in human prostate, breast or ovarian tumors (1, 5, 9-12). FGF-8 shows limited expression in the normal adult, but low levels are found in the reproductive and genitourinary tract, peripheral leukocytes and bone marrow hematopoietic cells (3, 9, 13).