FGF 1 Human, Sf9

Fibroblast Growth Factor-Acidic Human Recombinant, Sf9

Recombinant Human Fibroblast Growth Factor-1 (FGF-1) is produced in Sf9 insect cells. It is a single glycosylated polypeptide chain with 140 amino acids and a molecular weight of 15.8 kDa. The protein is purified using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT5800
Source
Baculovirus.
Appearance
Sterile, clear and colorless solution.

FGF 1 Mouse

Fibroblast Growth Factor-Acidic Mouse Recombinant

Recombinant Mouse Fibroblast Growth Factor-acidic (FGF-1), expressed in E. coli, is a single, non-glycosylated polypeptide chain comprising 141 amino acids. This protein has a molecular weight of 15.9 kDa.

FGF-acidic is purified using specialized chromatographic techniques.

Shipped with Ice Packs
Cat. No.
BT5837
Source
Escherichia Coli.
Appearance
Sterile Filtered White lyophilized powder.

FGF 1 Mouse, His

Fibroblast Growth Factor-acidic Mouse Recombinant, His Tag

Recombinant Mouse FGF-1, produced in E. coli, is a single, non-glycosylated polypeptide chain. It comprises 161 amino acids (specifically, residues 16-155) and has a molecular weight of 18 kDa. However, its apparent molecular weight on SDS-PAGE might be higher. The protein is engineered with a 21 amino acid His-tag at the N-terminus and purified using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT5909
Source
Escherichia Coli.
Appearance
The product is a clear, colorless solution that has been sterilized by filtration.

FGF 1 Rat

Fibroblast Growth Factor-Acidic Rat Recombinant

Fibroblast Growth Factor-acidic Rat Recombinant (FGF-1), produced in E. coli, is a single, non-glycosylated polypeptide chain comprising 141 amino acids. It has a molecular mass of 15.9 kDa. The purification process for FGF acidic involves proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT5982
Source
Escherichia Coli.
Appearance
Sterile Filtered White lyophilized powder

FGF 18 Human

Fibroblast Growth Factor-18 Human Recombinant

A single, non-glycosylated polypeptide chain containing 181 amino acids makes up recombinant human FGF-18 generated in E.coli, which has a molecular weight of 21.1 kDa. Using specialized chromatographic methods, the FGF-18 is purified.

Shipped with Ice Packs
Cat. No.
BT6029
Source
Escherichia Coli.
Appearance
It is a white powder that has been sterile filtered and lyophilized (freeze-dried).

FGF 18 Human, His

Fibroblast Growth Factor-18 Human Recombinant, His Tag

Recombinant Human FGF18, produced in E. coli, is a single, non-glycosylated polypeptide chain encompassing amino acids Glu28 to Ala207 (total 190 amino acids). It includes a 10 amino acid His-tag located at the N-terminus. The calculated molecular mass is 22.3 kDa.
Shipped with Ice Packs
Cat. No.
BT6100
Source
Escherichia Coli.
Appearance
White lyophilized powder, filtered for sterility.

FGF 19 Human, His

Fibroblast Growth Factor-19 Human Recombinant, His Tag

Recombinant Human Fibroblast Growth Factor-19, produced in E. coli, is a single, non-glycosylated polypeptide chain containing 206 amino acids. It has a molecular mass of 23 kDa. The amino acid sequence of this recombinant human FGF19 is 100% homologous to the human FGF19 sequence without the signal sequence and includes an N-terminal His tag. Purification is achieved using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT6332
Source
Escherichia Coli.
Appearance
White lyophilized powder after filtration.

FGF 21 Human

Fibroblast Growth Factor-21 Human Recombinant

Recombinant Human Fibroblast Growth Factor -21, produced in E. coli, is a single, non-glycosylated polypeptide chain comprising 181 amino acids with a molecular weight of 19.4 kDa.

Purification of FGF-21 is achieved using proprietary chromatographic methods.

Shipped with Ice Packs
Cat. No.
BT6998
Source
Escherichia Coli.
Appearance
Sterile Filtered white lyophilized powder.

FGF 21 Human, His

Fibroblast Growth Factor-21 Human Recombinant, His Tag

Recombinant Human Fibroblast Growth Factor-21, produced in E. coli, is a single, non-glycosylated polypeptide chain containing 202 amino acids (29-209). It has a molecular mass of 21.6 kDa (SDS-PAGE analysis may show higher molecular weight due to the His tag). This FGF-21 protein is fused to a 20 amino acid His Tag at the N-terminus and is purified using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT7080
Source
Escherichia Coli.
Appearance
A clear, colorless solution that has been sterilized by filtration.

FGF 21 Mouse

Fibroblast Growth Factor-21 Mouse Recombinant

Recombinant Mouse Fibroblast Growth Factor-21, produced in E. coli, is a single, non-glycosylated polypeptide chain containing 183 amino acids. This includes an N-terminal Methionine and has a molecular weight of 20.1 kDa. The purification process of FGF-21 is carried out using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT7133
Source
Escherichia Coli.
Appearance
White lyophilized powder that has been filtered.
Definition and Classification

Fibroblast Growth Factors (FGFs) are a family of cell signaling proteins produced by macrophages. They play crucial roles in various biological processes, including embryonic development, tissue homeostasis, wound repair, and cancer . FGFs are typically classified into three main groups based on their mechanisms of action: intracrine FGFs, paracrine FGFs, and endocrine FGFs . In humans, there are 23 identified members of the FGF family, each with distinct functions and binding specificities .

Biological Properties

FGFs exhibit a wide range of biological properties. They are involved in the regulation of cell proliferation, migration, and differentiation in various tissues, including connective tissues, nerves, epithelial tissue, and bone . FGFs are expressed in different patterns and are distributed across various tissues. For example, FGF1 (acidic FGF) and FGF2 (basic FGF) are widely expressed in many tissues, while others like FGF18 are specifically involved in cartilage development .

Biological Functions

The primary biological functions of FGFs include promoting cell growth, differentiation, and survival. They play a significant role in immune responses and pathogen recognition by influencing the behavior of immune cells . FGFs are also involved in the repair and regeneration of tissues, making them key players in wound healing and tissue homeostasis .

Modes of Action

FGFs exert their effects by binding to specific fibroblast growth factor receptors (FGFRs) on the cell surface. This binding activates various downstream signaling cascades, including the RAS/MAPK pathway, PI3K/AKT pathway, and PLC-γ pathway . These signaling pathways regulate diverse cellular functions, such as proliferation, differentiation, and migration .

Regulatory Mechanisms

The expression and activity of FGFs are tightly regulated through multiple mechanisms. Transcriptional regulation involves various transcription factors that control the expression of FGF genes . Post-translational modifications, such as phosphorylation and glycosylation, also play a crucial role in modulating the activity and stability of FGFs .

Applications

FGFs have numerous applications in biomedical research, diagnostic tools, and therapeutic strategies. They are used in tissue engineering and regenerative medicine to promote the repair and regeneration of damaged tissues . FGFs are also employed in cancer therapy, as they can influence tumor growth and angiogenesis .

Role in the Life Cycle

Throughout the life cycle, FGFs play essential roles from development to aging and disease. During embryonic development, FGFs are involved in the formation of body axes, morphogenesis, and organogenesis . In adults, they contribute to tissue homeostasis and repair. Dysregulation of FGF signaling is associated with various diseases, including cancer, metabolic disorders, and neurodegenerative diseases .

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