FGF 21 Mouse

Fibroblast Growth Factor-21 Mouse Recombinant

Fibroblast Growth Factor -21 Mouse Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 183 amino acids including N-terminal Methionin and having a molecular mass of 20.1 kDa.
The FGF-21 is purified by proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT7133
Source
Escherichia Coli.
Appearance
Filtered white lyophilized powder.

FGF 21 Mouse, His

Fibroblast Growth Factor-21 Mouse Recombinant, His Tag

Fibroblast Growth Factor -21 Mouse Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 192 amino acids and having a molecular mass of 21.2 kDa. The amino acid sequence of the recombinant human FGF21 is 100% homologous to the amino acid sequence of the Mouse FGF21 without signal sequence and contains 10 a.a. His tag at N-terminal.
The FGF-21 is purified by proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT7204
Source
Escherichia Coli.
Appearance
Filtered white lyophilized powder.

FGF 21 Mouse, Sf9

Fibroblast Growth Factor-21 Mouse Recombinant, Sf9

FGF-21 produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 190 amino acids (29-210a.a.) and having a molecular mass of 21.0kDa (Molecular size on SDS-PAGE will appear at approximately 18-28kDa).
FGF21 is expressed with an 8 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT7299
Source
Sf9, Baculovirus cells.
Appearance
Sterile Filtered colorless clear solution.

FGF 21 Rat

Fibroblast Growth Factor-21 Rat Recombinant

FGF 21 Rat Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 180 amino acids and having a molecular mass of 19.7kDa.
The FGF 21 is purified by 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

Fibroblast Growth Factor-22 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 149 amino acids and having a molecular mass of 17.3 kDa.
The FGF-22 is purified by chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT7442
Source
Escherichia Coli.
Appearance
Sterile Filtered white lyophilized powder.

FGF 23 Human, His

Fibroblast Growth Factor-23 Human Recombinant, His Tag

Fibroblast Growth Factor-23 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain expressed with a -6xHis tag containing a total of 257 amino acids (251 a.a. FGF23+ 6 a.a. His tag) and having a molecular mass of 28629.5 Dalton.
The FGF-23 is and purified by chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT7561
Source
Escherichia Coli.
Appearance
Sterile Filtered white lyophilized powder.

FGF 8 Human

Fibroblast Growth Factor-8 Human Recombinant

FGF 8 Human Recombinant produced in E.Coli is a non-glycosylated polypeptide chain containing 194 amino acids and having a total molecular mass of 22.5kDa. 
Shipped with Ice Packs
Cat. No.
BT7644
Source
Escherichia Coli.
Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.

FGF 8 Mouse

Fibroblast Growth Factor-8 Mouse Recombinant

FGF-8 Mouse Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 246 amino acids and having a molecular mass of 28.1kDa.
The FGF-8 is purified by proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT7715
Source
Escherichia Coli.
Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.

FGF 8 Mouse, 194 a.a.

Fibroblast Growth Factor-8 Mouse Recombinant, 194 a.a.

FGF 8 Mouse Recombinant produced in E.Coli is a non-glycosylated polypeptide chain containing 194 amino acids and having a total molecular mass of 22.5kDa. 
Shipped with Ice Packs
Cat. No.
BT7779
Source
Escherichia Coli.
Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.

FGF 9 Human

Fibroblast Growth Factor-9 Human Recombinant

Fibroblast Growth Factor-9 Human Recombinant produced in E.coli is a single, non-glycosylated, polypeptide chain containing 207 amino acids and having a molecular mass of 23.4 kDa. The FGF-9 is purified by proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT7842
Source
Escherichia coli.
Appearance
Sterile Filtered white lyophilized 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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