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Growth Factors

Fibroblast Growth Factor

CSF

Prolactin PRL

RANK Ligand

Retinol Binding Protein

Stem Cell Factor

CTGF

Transforming Growth Factor

EGF

Epigen

Erythropoietin

VEGF Protein

Other Growth Factors

Galectin

Growth Hormone

HDGF

Hepatocyte Growth Factor

IGFBP

Insulin-Like Growth Factor

Insulin

Keratinocyte Growth Factor

Leptin

Macrophage Migration Inhibitory Factor

Melanoma Inhibitory Activity

Myostatin

Noggin

NOV

Omentin

Oncostatin-M

Osteopontin

Osteoprotegerin

PDGF

Periostin

Placental Growth Factor

Placental Lactogen

Product List

FGF 21 Mouse, His

Fibroblast Growth Factor-21 Mouse Recombinant, His Tag

Recombinant Mouse Fibroblast Growth Factor -21, produced in E. coli, is a single, non-glycosylated polypeptide chain consisting of 192 amino acids with a molecular weight of 21.2 kDa. The amino acid sequence of the recombinant human FGF21 exhibits 100% homology to the amino acid sequence of Mouse FGF21 without the signal sequence and incorporates a 10 amino acid His tag at the N-terminus. The purification of FGF-21 is achieved through proprietary chromatographic techniques.

Shipped with Ice Packs

Cat. No.

BT7204

Source

Escherichia Coli.

Appearance

White lyophilized powder after filtration.

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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 21.0 kDa. Molecular size on SDS-PAGE will appear at approximately 18-28 kDa. FGF21 is expressed with an 8 amino acid His tag at the 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.

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FGF14 Human

Fibroblast Growth Factor 14 Human Recombinant

Recombinant Human FGF14, expressed in E. coli, is a single, non-glycosylated polypeptide chain. It encompasses 271 amino acids, including amino acids 1-247 of the FGF14 sequence, and has a molecular weight of 30 kDa. A 24 amino acid His-tag is fused to the N-terminus of the FGF14 protein. Purification is achieved through proprietary chromatographic techniques.

Shipped with Ice Packs

Cat. No.

BT8441

Source

E.coli.

Appearance

A clear, colorless solution, sterile-filtered.

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FGF16 Human

Fibroblast Growth Factor 16 Human Recombinant

Recombinant human FGF16, produced in E. coli, is a single, non-glycosylated polypeptide chain consisting of 206 amino acids, with a molecular weight of 23.6 kDa. This FGF-16 variant is purified using proprietary chromatographic techniques.

Shipped with Ice Packs

Cat. No.

BT8528

Source

Escherichia Coli.

Appearance

A clear, colorless solution that has been sterilized by filtration.

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FGF16 Mouse

Fibroblast Growth Factor 16 Mouse Recombinant

Recombinant Mouse FGF16, produced in E. coli, is a single, non-glycosylated polypeptide chain comprising 207 amino acids. With a molecular weight of 23.8 kDa, this FGF-16 protein is purified using proprietary chromatographic techniques.

Shipped with Ice Packs

Cat. No.

BT8600

Source

Escherichia Coli.

Appearance

Clear, colorless, and sterile-filtered solution.

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FGF17 Human

Fibroblast Growth Factor 17 Human Recombinant

Recombinant Human FGF17, produced in E. coli, is a single, non-glycosylated polypeptide chain with a molecular weight of 22.6kDa. It consists of 195 amino acids.

Shipped with Ice Packs

Cat. No.

BT8657

Source

Escherichia Coli.

Appearance

Sterile Filtered White lyophilized (freeze-dried) powder.

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FGF17 Human, His

Fibroblast Growth Factor 17 Human Recombinant, His Tag

Recombinant Human FGF17, expressed in E. coli, is a single, non-glycosylated polypeptide chain. It comprises 219 amino acids (spanning from amino acid 23 to 216), resulting in a molecular weight of 25.2 kDa. For purification purposes, FGF17 is tagged with a 25 amino acid His-tag at its N-terminus and subsequently purified using proprietary chromatographic techniques.

Shipped with Ice Packs

Cat. No.

BT8728

Source

E.coli.

Appearance

The product appears as a clear, colorless solution that has been sterilized by filtration.

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IFNAR1 Human

Interferon Alpha and Beta Receptor Subunit 1 Human Recombinant

IFNAR1, produced in Sf9 Insect cells, is a single, glycosylated polypeptide chain consisting of 415 amino acids (28-436a.a.) with a molecular weight of 47.9kDa. This protein is expressed with a C-terminal 6-amino acid His tag and purified using proprietary chromatographic techniques.

Shipped with Ice Packs

Cat. No.

BT9900

Source

Sf9, Insect cells.

Appearance

A colorless solution that has been sterilized by filtration.

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aFGF Bovine

Fibroblast Growth Factor Acidic Bovine

FGF-1 (Fibroblast Growth Factor-acidic Bovine), purified from Bovine Brain, consists of a 17 kDa and a 20 kDa polypeptide chain. Derived from the 20 kDa peptide through restricted proteolysis (see Jaye et al.), the acidic FGF is purified using proprietary chromatographic techniques.

Shipped with Ice Packs

Cat. No.

BT5655

Source

Bovine Brain.

Appearance

White, sterile-filtered powder in lyophilized (freeze-dried) form.

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FGF 1 Human

Fibroblast Growth Factor-Acidic Human Recombinant

Recombinant Human Fibroblast Growth Factor-acidic (FGF-1) is produced in E. coli. This non-glycosylated polypeptide chain consists of 140 amino acids, resulting in a molecular weight of approximately 15.8 kDa. The purification process involves proprietary chromatographic techniques.

Shipped with Ice Packs

Cat. No.

BT5730

Source

Escherichia Coli.

Appearance

White, sterile-filtered lyophilized powder.

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Showing 11 to 20 of 55 results

Introduction

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.