FGF 9 Mouse

Fibroblast Growth Factor-9 Mouse Recombinant

Fibroblast Growth Factor-9 Mouse Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 205 amino acids and having a molecular mass of 23308 Dalton.
The FGF-9 Mouse Recombinant is purified by proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT8002
Source
Escherichia Coli.
Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.

FGF 9 Rat

Fibroblast Growth Factor-9 Rat Recombinant

Rat FGF9 Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 207 amino acids and having a molecular mass of 23.3kDa.
The FGF-9 Mouse Recombinant is purified by proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT8075
Source
Escherichia Coli.
Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.

FGF1 Human, 154 a.a.

Fibroblast Growth Factor-acidic (154 a.a.) Human Recombinant

Fibroblast Growth Factor-acidic Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 154 amino acids and having a molecular mass of 17.3kDa. The FGF1 is purified by proprietary chromatographic techniques.

Shipped with Ice Packs
Cat. No.
BT8149
Source

Escherichia Coli.

Appearance

Sterile Filtered White lyophilized (freeze-dried) powder.

FGF12 Human

Fibroblast Growth Factor 12 Human Recombinant

Fibroblast Growth Factor 12 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 181 amino acids and having a molecular mass of 20.5kDa. The FGF12 is purified by proprietary chromatographic techniques. 

Shipped with Ice Packs
Cat. No.
BT8204
Source

Escherichia Coli. 

Appearance

Sterile Filtered White lyophilized (freeze-dried) powder.

FGF12 Human, His

Recombinant Human Fibroblast Growth Factor 12, His Tag

The FGF-12 Human recombinant protein is a single, non-glycosylated polypeptide chain produced in E. coli, having a molecular weight of 22.6kDa and containing 201 amino acids (1-181). The FGF12 is fused to a 20 amino acid His tag at the N-terminus.
Shipped with Ice Packs
Cat. No.
BT8265
Source
Escherichia Coli.
Appearance
Sterile liquid colorless solution.

FGF13 Human

Fibroblast Growth Factor 13 Human Recombinant

FGF13 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 245 amino acids and having a molecular mass of 27.6kDa.
The FGF-13 is purified by proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT8361
Source
Escherichia Coli.
Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.

FGF14 Human

Fibroblast Growth Factor 14 Human Recombinant

FGF14 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 271 amino acids (1-247 a.a) and having a molecular mass of 30kDa.
FGF14 is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT8441
Source
E.coli.
Appearance
Sterile Filtered colorless solution.

FGF16 Human

Fibroblast Growth Factor 16 Human Recombinant

FGF16 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 206 amino acids and having a molecular mass of 23.6kDa.
The FGF-16 is purified by proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT8528
Source
Escherichia Coli.
Appearance
Sterile Filtered colorless clear solution.

FGF16 Mouse

Fibroblast Growth Factor 16 Mouse Recombinant

FGF16 Mouse Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 207 amino acids and having a molecular mass of 23.8kDa.
The FGF-16 is purified by proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT8600
Source
Escherichia Coli.
Appearance
Sterile Filtered colorless clear solution.

FGF17 Human

Fibroblast Growth Factor 17 Human Recombinant

FGF17 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 195 amino acids and having a molecular mass of 22.6kDa. 
Shipped with Ice Packs
Cat. No.
BT8657
Source
Escherichia Coli.
Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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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