HGF B Human

Hepatocyte Growth Factor B Chain Human Recombinant

Recombinant Human HGF-B, produced in E. coli, is a single, non-glycosylated polypeptide chain. It consists of 234 amino acids (fragment 495-728) and has a molecular weight of 34kDa. The protein includes a 4.5kDa amino-terminal hexahistidine tag. HGF-B is purified using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT15683
Source
Escherichia Coli.
Appearance
Clear, sterile-filtered solution.

HGF Human

Hepatocyte Growth Factor Human Recombinant

Recombinant Human Hepatocyte Growth Factor, produced in Baculovirus, is a non-glycosylated polypeptide chain heterodimer consisting of 692 amino acids with a total molecular weight of 78.0 KDa. The purification process of HGF involves proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT15776
Source
Insect cells.
Appearance
Sterile, white, lyophilized powder.

HGF Human, CHO

Hepatocyte Growth Factor Human Recombinant, CHO

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.

Shipped with Ice Packs
Cat. No.
BT15869
Source
Chinese Hamster Ovarian Cells.
Appearance

The product appears as a sterile, filtered, white powder that has been lyophilized (freeze-dried).

HGF Human, HEK

Hepatocyte Growth Factor Human Recombinant, HEK

Recombinant human HGF, produced in HEK cells, is a glycosylated heterodimer with a disulfide bond. It comprises 697 amino acids (Gln-32 to Ser-728) and has a molecular weight of 80kDa.

The purification of HGF is achieved through specific chromatographic methods.

Shipped with Ice Packs
Cat. No.
BT15945
Source
HEK.
Appearance
The product appears as a sterile, filtered white powder that has been freeze-dried.

HGF Mouse

Hepatocyte Growth Factor Mouse Recombinant

Recombinant Mouse HGF, expressed in a Baculovirus system, is a single glycosylated polypeptide chain. This protein consists of 1146 amino acids (with a sequence spanning from amino acid 25 to 931) and exhibits a molecular weight of 127.8 kDa. For purification purposes, the HGF protein is engineered with a C-terminal fusion tag comprising a 239 amino acid sequence (hIgG-His-Tag). The recombinant HGF protein undergoes purification using proprietary chromatographic methods to ensure high purity.
Shipped with Ice Packs
Cat. No.
BT16021
Source

Sf9, Baculovirus cells.

Appearance
Sterile Filtered colorless solution.

pHGF Porcine

Hepatocyte promoting Growth Factor Porcine

Porcine Hepatocyte Growth Factor is derived from pig liver through specialized chromatographic purification techniques.
Shipped with Ice Packs
Cat. No.
BT16117
Source
Pig Liver.
Appearance
Presented as a sterile, white, lyophilized (freeze-dried) powder.

HGF (32-285) Human

Hepatoma-Derived Growth Factor (32-285 a.a) Human Recombinant

Recombinant human HGF, produced in E. coli, is a single, non-glycosylated polypeptide chain comprising 255 amino acids (specifically, amino acids 32 to 285) and possessing a molecular weight of 29.8 kDa. HGF is purified using specialized chromatographic methods.
Shipped with Ice Packs
Cat. No.
BT15613
Source
Escherichia Coli.
Appearance
A clear, sterile solution.
Definition and Classification

Hepatocyte Growth Factor (HGF) is a multifunctional protein that plays a critical role in various biological processes. It is classified as a growth factor and is also known as scatter factor (SF). HGF is a member of the plasminogen-related growth factor family and is primarily produced by mesenchymal cells.

Biological Properties

Key Biological Properties: HGF is a heterodimeric molecule composed of an alpha-chain and a beta-chain linked by a disulfide bond. It is secreted as an inactive precursor (pro-HGF) and is activated by proteolytic cleavage.

Expression Patterns: HGF is expressed in various tissues, including the liver, kidneys, lungs, and the nervous system. Its expression is regulated by various factors, including cytokines, growth factors, and hormones.

Tissue Distribution: HGF is widely distributed in the body, with high concentrations found in the liver, where it plays a crucial role in liver regeneration and repair. It is also present in other tissues such as the kidneys, lungs, and the nervous system.

Biological Functions

Primary Biological Functions: HGF is involved in a wide range of biological functions, including cell proliferation, differentiation, motility, and survival. It is essential for embryonic development, tissue regeneration, and wound healing.

Role in Immune Responses: HGF modulates immune responses by influencing the behavior of various immune cells, including macrophages, dendritic cells, and T cells. It has anti-inflammatory properties and can promote tissue repair and regeneration in response to injury.

Pathogen Recognition: HGF can enhance the ability of immune cells to recognize and respond to pathogens, thereby contributing to the body’s defense mechanisms.

Modes of Action

Mechanisms with Other Molecules and Cells: HGF exerts its effects by binding to its receptor, c-Met, a tyrosine kinase receptor. This binding triggers a cascade of downstream signaling events that mediate various cellular responses.

Binding Partners: HGF interacts with several binding partners, including heparan sulfate proteoglycans, which facilitate its binding to the c-Met receptor and enhance its biological activity.

Downstream Signaling Cascades: Upon binding to c-Met, HGF activates multiple signaling pathways, including the PI3K/Akt, MAPK/ERK, and STAT pathways. These pathways regulate various cellular processes, such as proliferation, survival, and migration.

Regulatory Mechanisms

Regulatory Mechanisms that Control Expression and Activity: The expression and activity of HGF are tightly regulated at multiple levels, including transcriptional, post-transcriptional, and post-translational mechanisms.

Transcriptional Regulation: HGF gene expression is regulated by various transcription factors, including NF-κB, AP-1, and STAT3. These factors can be activated by cytokines, growth factors, and other signaling molecules.

Post-Translational Modifications: HGF undergoes several post-translational modifications, including proteolytic cleavage, glycosylation, and phosphorylation. These modifications are essential for its activation, stability, and biological activity.

Applications

Biomedical Research: HGF is widely studied in biomedical research due to its diverse biological functions and therapeutic potential. It is used as a model to study cell signaling, tissue regeneration, and cancer biology.

Diagnostic Tools: HGF levels can serve as biomarkers for various diseases, including liver disease, kidney disease, and cancer. Measuring HGF levels in biological samples can aid in the diagnosis and prognosis of these conditions.

Therapeutic Strategies: HGF has therapeutic potential in regenerative medicine and tissue engineering. It is being explored as a treatment for liver cirrhosis, myocardial infarction, and chronic kidney disease. Additionally, HGF-based therapies are being developed for cancer treatment due to its ability to inhibit tumor growth and metastasis.

Role in the Life Cycle

Development: HGF plays a crucial role in embryonic development, particularly in the formation of the liver, kidneys, and nervous system. It regulates cell proliferation, differentiation, and migration during organogenesis.

Aging: HGF levels decline with age, which may contribute to the reduced regenerative capacity of tissues in older individuals. Enhancing HGF activity has been proposed as a potential strategy to promote healthy aging and tissue repair.

Disease: Dysregulation of HGF signaling is associated with various diseases, including cancer, fibrosis, and inflammatory conditions. Understanding the role of HGF in these diseases can provide insights into their pathogenesis and lead to the development of novel therapeutic approaches.

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