FGF17 Human, His

Fibroblast Growth Factor 17 Human Recombinant, His Tag

FGF17 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 219 amino acids (23-216 a.a) and having a molecular mass of 25.2kDa.
FGF17 is fused to a 25 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT8728
Source
E.coli.
Appearance
Sterile Filtered colorless solution.

FGF-18 Rat

Fibroblast Growth Factor-18 Rat Recombinant

FGF18 Rat Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 180 amino acids and having a molecular mass of 21.0kDa.
The FGF 18 Rat is purified by proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT8796
Source
Escherichia Coli.
Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.

FGF19 Human, HEK

Fibroblast Growth Factor-19 Human Recombinant, HEK

FGF19 Mouse Recombinant produced in HEK293 cells is a single, glycosylated polypeptide chain (a.a 23-216) containing 205 amino acids and having a molecular mass of 23.0 kDa.
FGF19 is fused to a 6 amino acid His-tag at C-terminus & purified by proprietary chromatographic techniques.

Shipped with Ice Packs
Cat. No.
BT8864
Source

HEK293 cells.

Appearance
Sterile Filtered colorless solution.

FGF2 (147), Bovine

Fibroblast Growth Factor-basic (147 a.a.) Bovine Recombinant

Fibroblast Growth Factor-basic (147 a.a.) Bovine Recombinant produced in E.Coli is a non-glycosylated polypeptide chain containing 147 amino acid and having a molecular mass of approximately 16.5kDa.
FGF2 (147) is purified by proprietary chromatographic techniques.

Shipped with Ice Packs
Cat. No.
BT8953
Source

Escherichia Coli.

Appearance

Sterile Filtered White lyophilized (freeze-dried) powder.

FGF-2 Bovine

Fibroblast Growth Factor-Basic Bovine Recombinant

FGF-2 Bovine Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 155 amino acids and having a molecular mass of 17250 Dalton. The Fibroblast Growth Factor 2 is purified by proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT9012
Source
Escherichia Coli.
Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.

FGF20 Human

Fibroblast Growth Factor-20 Human Recombinant

FGF20 Human Recombinant (1-211) produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 217 amino acids and having a molecular mass of 24kDa.
The FGF-20 is fused to a 6 amino acid His tag [HHHHHH] at N-terminus and purified by proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT9095
Source
Escherichia Coli.
Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.

FGF23 Human

Fibroblast Growth Factor-23 Human Recombinant

Fibroblast Growth Factor-23 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing a total of 228 amino acids and having a molecular mass of 22.5kDa.
The FGF-23 is and purified by chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT9211
Source
Escherichia Coli.
Appearance
Sterile Filtered white lyophilized powder.

FGF23 Human, Sf9

Fibroblast Growth Factor-23 Human Recombinant, Sf9

FGF23 produced in Sf9 Insect cells is a single, glycosylated polypeptide chain containing 236 amino acids (25-251a.a.) and having a molecular mass of 26.4kDa (Molecular size on SDS-PAGE will appear at approximately 13.5-18kDa).
FGF23 is expressed with an 9 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

Shipped with Ice Packs
Cat. No.
BT9297
Source

Sf9, Insect cells.

Appearance

Sterile filtered colorless solution.

FGF4 Human

Fibroblast Growth Factor-4 Human Recombinant

FGF4 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 182 amino acids and having a molecular mass of 19.8kDa.

The FGF4 is purified by proprietary chromatographic techniques.

Shipped with Ice Packs
Cat. No.
BT9391
Source
Escherichia Coli.
Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.

FGF5 Human

Fibroblast Growth Factor-5 Human Recombinant

FGF5 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain having containing 252 amino acids and having a molecular mass of 27.7kDa.
The FGF-5 is purified by proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT9462
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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