Scatter Factor (SF), Hepatopoietin (HPTA), HGF.
Sterile Filtered White lyophilized (freeze-dried) powder.
Greater than 97.0% as determined by SDS-PAGE.
Hepatocyte Growth Factor Human Recombinant produced in CHO is a heterodimer, non-glycosylated, polypeptide chain consisting an a-chain of 463 amino acids and b-chain of 234 having a total molecular mass of approximately 75kDa.
The HGF is purified by proprietary chromatographic techniques.
Hepatocyte Growth Factor (HGF) is a versatile growth factor that plays a crucial role in regulating both cell growth and movement. It exhibits a significant growth-promoting effect on hepatocytes, which are the primary cells of the liver, as well as on epithelial cells. HGF acts in synergy with Interleukin-3 (IL-3) and Granulocyte-Macrophage Colony-Stimulating Factor (GM-CSF) to enhance the formation of colonies by hematopoietic progenitor cells in laboratory settings. This suggests that HGF may also have a regulatory role in hematopoiesis, the process of blood cell formation.
Recombinant Human Hepatocyte Growth Factor, produced in Chinese Hamster Ovary (CHO) cells, is a heterodimeric, non-glycosylated polypeptide. It comprises an alpha-chain of 463 amino acids and a beta-chain of 234 amino acids, resulting in a total molecular mass of approximately 75 kDa. The purification of HGF is achieved through proprietary chromatographic methods.
The product appears as a sterile, filtered, white powder that has been lyophilized (freeze-dried).
The protein was subjected to lyophilization from a concentrated solution (1.4 mg/ml) prepared in Phosphate-Buffered Saline (PBS) containing 0.02% Tween 80, at a pH of 7.4.
To reconstitute the lyophilized Hepatocyte Growth Factor, it is recommended to dissolve it in sterile 18 megaohm-centimeter (MΩ·cm) H2O to a concentration of at least 100 micrograms per milliliter (µg/ml). This reconstituted solution can then be further diluted into other aqueous solutions as needed.
Lyophilized Hepatocyte Growth Factor demonstrates stability at room temperature for a period of 3 weeks. However, for long-term storage, it is recommended to store the lyophilized product in a desiccated state at a temperature below -18 degrees Celsius (-0.4 degrees Fahrenheit). Once reconstituted, HGF should be stored at 4 degrees Celsius (39.2 degrees Fahrenheit) for a period of 2 to 7 days. For extended storage after reconstitution, it is advisable to store the solution at -18 degrees Celsius (-0.4 degrees Fahrenheit).
To further enhance long-term stability during storage, it is recommended to add a carrier protein such as 0.1% Human Serum Albumin (HSA) or Bovine Serum Albumin (BSA) to the solution.
Repeated cycles of freezing and thawing should be avoided to maintain product integrity.
The purity of the Hepatocyte Growth Factor is determined to be greater than 97.0% using Sodium Dodecyl Sulfate-Polyacrylamide Gel Electrophoresis (SDS-PAGE).
The ED50 value, which represents the effective dose at which 50% of the maximum response is observed, was determined by assessing the dose-dependent proliferation of monkey 4MBr-5 indicator cells. The ED50 for this product was found to be in the range of 20 to 40 nanograms per milliliter (ng/ml).
Scatter Factor (SF), Hepatopoietin (HPTA), HGF.
Agrees with the sequence of native human HGF.
Hepatocyte Growth Factor (HGF), also known as scatter factor, is a multifunctional growth factor that plays a crucial role in various biological processes, including cell proliferation, motility, survival, and differentiation. HGF is produced by cells of mesenchymal origin and exerts its effects by binding to the c-MET receptor, a receptor tyrosine kinase, which triggers a cascade of intracellular signaling pathways .
HGF is initially synthesized as an inactive polypeptide chain known as pre-pro-HGF. This precursor consists of a signal sequence, a heavy α-chain, and a light β-chain. The signal sequence is cleaved to produce pro-HGF, which is further processed by the protease HGF activator (HGF-A) to release the α and β chains. These chains form an active heterodimer via disulfide bonding, which then binds to the c-MET receptor .
The binding of HGF to the c-MET receptor induces dimerization and activation of the receptor, leading to the stimulation of various signaling pathways, including PI3K/AKT, FAK, JNK, and ERK1/2. These pathways are involved in regulating cell growth, motility, and survival .
HGF has a wide range of biological activities, including:
Recombinant HGF is produced using Chinese Hamster Ovary (CHO) cells, which are widely used in biotechnology for the production of therapeutic proteins. The recombinant HGF produced in CHO cells is a heterodimer consisting of an α-chain and a β-chain, with a total molecular mass of approximately 80 kDa .
The recombinant HGF is purified to a high degree of purity (≥ 95%) and is biologically active, capable of promoting cell proliferation and other biological activities similar to the native HGF .
Recombinant HGF has several applications in research and therapeutic settings, including: