KGF Human

Keratinocyte Growth Factor Human Recombinant
Cat. No.
BT19743
Source
Escherichia Coli.
Synonyms
HBGF-7, FGF7, FGF-7, KGF.
Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Purity
Greater than 96.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.
Usage
THE BioTek's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
Shipped with Ice Packs
In Stock

Description

Keratinocyte Growth Factor-1 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 164 amino acids and having a molecular mass of 18995 Dalton.
The FGF-7 is purified by proprietary chromatographic techniques.

Product Specs

Introduction
Keratinocyte growth factor (KGF), also known as fibroblast growth factor 7 (FGF7), is a protein that belongs to the fibroblast growth factor (FGF) family. These growth factors are involved in various cellular processes, including cell growth, survival, and differentiation. KGF plays a crucial role in the development and repair of epithelial tissues, such as the skin and lining of the lungs. It specifically stimulates the growth and proliferation of keratinocytes, which are the major cell type found in the outermost layer of the skin.
Description
Recombinant human keratinocyte growth factor-1 (KGF-1) is a single, non-glycosylated polypeptide chain consisting of 164 amino acids. Produced in E. coli, it has a molecular mass of 18995 Daltons. This purified form of FGF-7 is obtained through proprietary chromatographic techniques, ensuring its high quality and purity.
Physical Appearance
White, lyophilized (freeze-dried) powder, sterile filtered.
Formulation
The product is lyophilized from a 0.2µm filtered solution containing 20mM PB (phosphate buffer), pH 8.0, and 1M NaCl (sodium chloride).
Solubility
To reconstitute the lyophilized Keratinocyte Growth Factor, it is recommended to dissolve it in sterile 18MΩ-cm H2O (water) at a concentration of at least 100µg/ml. This solution can then be further diluted as needed using other aqueous solutions.
Stability
Lyophilized Keratinocyte Growth Factor1 is stable at room temperature for up to 3 weeks. However, for long-term storage, it is recommended to store it desiccated below -18°C. After reconstitution, the FGF7 solution should be stored at 4°C and used within 2-7 days. For extended storage, adding a carrier protein like HSA (human serum albumin) or BSA (bovine serum albumin) at a concentration of 0.1% is advisable. Avoid repeated freeze-thaw cycles to preserve protein integrity.
Purity
The purity of this product is greater than 96.0%, as determined by two methods: (a) Analysis using RP-HPLC (Reverse Phase High-Performance Liquid Chromatography), and (b) Analysis using SDS-PAGE (Sodium Dodecyl Sulfate Polyacrylamide Gel Electrophoresis).
Biological Activity
The biological activity of KGF is measured by its ability to stimulate thymidine uptake in BaF3 cells expressing KGF receptors. This assay demonstrated an ED50 (half-maximal effective dose) of less than 10ng/ml, corresponding to a specific activity of 1.0×105 IU/mg.
Protein Content
The protein content is quantified using two independent methods: 1. UV spectroscopy at 280 nm, utilizing an absorbency value of 0.9 as the extinction coefficient for a 0.1% (1mg/ml) solution. This value is determined using the PC GENE computer analysis program for protein sequences (IntelliGenetics). 2. Analysis by RP-HPLC, employing a calibrated solution of KGF as a reference standard.
Synonyms
HBGF-7, FGF7, FGF-7, KGF.
Source
Escherichia Coli.
Amino Acid Sequence
MCNDMTPEQM ATNVNCSSPE RHTRSYDYME GGDIRVRRLF CRTQWYLRID KRGKVKGTQE MKNNYNIMEI RTVAVGIVAI KGVESEFYLA MNKEGKLYAK KECNEDCNFK ELILENHYNT YASAKWTHNG GEMFVALNQK GIPVRGKKTK KEQKTAHFLP MAIT.

Product Science Overview

Introduction

Keratinocyte Growth Factor (KGF), also known as Fibroblast Growth Factor 7 (FGF7), is a potent mitogen specifically for epithelial cells. It plays a crucial role in the proliferation, differentiation, and migration of these cells, as well as in protecting them from various insults under stress conditions . The recombinant form of KGF, known as human recombinant KGF (rhKGF), has been developed for therapeutic purposes.

Discovery and Structure

KGF was originally isolated from human embryonic lung fibroblast-conditioned medium. It belongs to the fibroblast growth factor (FGF) family, which comprises 23 members classified into six subfamilies in mammals . The original KGF-1 cDNA, encoding 194 residues, was isolated from a human embryonic lung fibroblast cell line. It contains 31 residues of signal peptide and five N- and O-glycosylation sites .

Production

The production of recombinant human KGF involves expressing the protein in a suitable host, such as Escherichia coli. In one study, an amino-terminally truncated KGF-1 variant with 135 residues was produced and purified in E. coli. This variant demonstrated biological activity similar to the full-length KGF-1 . The recombinant form, known as palifermin (trade name Kepivance®), is used to prevent and treat oral mucositis following radiation or chemotherapy .

Biological Activity

KGF interacts with the FGF receptor 2 (FGFR2-IIIb), which is specifically expressed in stromal fibroblasts from epithelial tissues . This interaction promotes the growth of epithelial cells and plays an important role in repairing the epithelium in various tissues and organs during the early stages of wound healing . Additionally, KGF has been shown to stimulate the growth of hair follicles and repress hair growth during the telogen phase .

Therapeutic Applications

Recombinant human KGF has been developed for several therapeutic applications. One of the most notable uses is in the treatment of oral mucositis, a common side effect of radiation and chemotherapy. Palifermin has been shown to reduce the incidence and duration of severe oral mucositis in patients undergoing these treatments . Additionally, KGF has been investigated for its potential in treating other conditions, such as hemorrhagic cystitis, where it has shown promising results in promoting the proliferation of urothelial cells and reducing bleeding .

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