FGF4 Human

Fibroblast Growth Factor-4 Human Recombinant

Recombinant human FGF4 is a single, non-glycosylated polypeptide chain containing 182 amino acids with a molecular mass of 19.8 kDa. The protein is produced in E. coli and purified using proprietary chromatographic techniques.

Shipped with Ice Packs
Cat. No.
BT9391
Source
Escherichia Coli.
Appearance

The appearance of this product is a sterile, filtered, white, lyophilized (freeze-dried) powder.

FGF5 Human

Fibroblast Growth Factor-5 Human Recombinant

Recombinant Human FGF5, produced in E. coli, is a single, non-glycosylated polypeptide chain with a molecular weight of 27.7 kDa. It comprises 252 amino acids. The purification of FGF-5 is carried out using proprietary chromatographic methods.
Shipped with Ice Packs
Cat. No.
BT9462
Source
Escherichia Coli.
Appearance
White, lyophilized powder, sterile-filtered.

FGFBP Human

Fibroblast Growth Factor Binding Protein 1 Human Recombinant

Recombinant human FGFBP is a single, non-glycosylated polypeptide chain produced in E. coli. It consists of 234 amino acids (residues 24-234) and has a molecular weight of 26.2 kDa. The protein contains a 23-amino acid His-tag at the N-terminus to facilitate purification, which is carried out using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT9682
Source
Escherichia Coli.
Appearance
Clear, colorless, and sterile-filtered solution.

FIBP Human

FGF-1 Intracellular-Binding Protein Human Recombinant

Recombinant human FIBP, produced in E. coli, is a single, non-glycosylated polypeptide chain comprising 387 amino acids (1-364) with a molecular weight of 44.3 kDa. A 23 amino acid His-Tag is fused to the N-terminus of FIBP. The protein undergoes purification using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT9795
Source
E.coli.
Appearance
A sterile, colorless solution that has been filtered for sterility.

FGF 18 Mouse

Fibroblast Growth Factor-18 Mouse Recombinant

Recombinant Mouse FGF-18, produced in E. coli, is a single, non-glycosylated polypeptide chain with 180 amino acids and a molecular weight of 21 kDa. It undergoes purification using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT6170
Source
Escherichia Coli.
Appearance
White, sterile-filtered lyophilized powder.

FGF 19 Human

Fibroblast Growth Factor-19 Human Recombinant

Recombinant Human FGF19, produced in E. coli, is a single, non-glycosylated polypeptide chain comprising 195 amino acids with a molecular weight of 21.8 kDa.
The purification process for FGF-19 involves proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT6263
Source
Escherichia Coli.
Appearance
White lyophilized powder after filtration.

FGF 21 Rat

Fibroblast Growth Factor-21 Rat Recombinant

Recombinant Rat FGF 21, produced in E. coli, is a single, non-glycosylated polypeptide chain composed of 180 amino acids, with a molecular weight of 19.7 kDa. The purification process involves proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT7361
Source
Escherichia Coli.
Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.

FGF 22 Human

Fibroblast Growth Factor-22 Human Recombinant

Recombinant human fibroblast growth factor 22 (FGF-22) is produced in E. coli and is a non-glycosylated polypeptide chain consisting of 149 amino acids. It has a molecular weight of 17.3 kDa. This protein is purified using chromatographic methods.
Shipped with Ice Packs
Cat. No.
BT7442
Source
Escherichia Coli.
Appearance
White, lyophilized powder that is sterile and filtered.

FGF 23 Human, His

Fibroblast Growth Factor-23 Human Recombinant, His Tag

Recombinant Human Fibroblast Growth Factor-23, expressed in E. coli, is a single, non-glycosylated polypeptide chain with a -6xHis tag. It consists of 257 amino acids (251 a.a. FGF23 + 6 a.a. His tag) and has a molecular weight of 28629.5 Daltons. The protein is purified using chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT7561
Source
Escherichia Coli.
Appearance
White, sterile-filtered lyophilized powder.

FGF 8 Human

Fibroblast Growth Factor-8 Human Recombinant

Recombinant Human FGF 8, produced in E. coli, is a non-glycosylated polypeptide chain consisting of 194 amino acids. It has a molecular weight of 22.5 kDa.
Shipped with Ice Packs
Cat. No.
BT7644
Source
Escherichia Coli.
Appearance
The product appears as a sterile, white powder obtained by lyophilization (freeze-drying).
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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