Featured Products
- HCC-78
- HDLM-2
- DOHH-2
- L-540
- MX-1
- NALM-6
- NB-4
- CAL-51
- SNB-19
- KYSE-520
- MKN-45
- BA/F3
- MS-5
- HCEC-B4G12
- NK-92
- PA-TU-8988S
- MONO-MAC-1
- PA-TU-8902
- Human Microglia
- Human Hepatic Stellate Cells
- Human Skeletal Muscle Cells (DMD)
- Human Schwann Cells
- Human Oral Keratinocytes (HOK)
- Human Cardiomyocytes
- Human Small Intestinal Epithelial Cells
- Human Colonic Epithelial Cells
- Human Intestinal Fibroblasts
- Primary Human Large Intestine Microvascular Endothelial Cells
- Human Small Intestinal Microvascular Endothelial Cells
- Human Retinal Pigment Epithelial Cells
- Human Hepatocytes
- Cynomolgus Monkey Lung Microvascular Endothelial Cells
- Cynomolgus Monkey Vein Endothelial Cells
- C57BL/6 Mouse Primary Mammary Epithelial Cells
- C57BL/6 Mouse Vein Endothelial Cells
- Rat Primary Kidney Epithelial Cells
- Rat Gingival Epithelial Cells
- Rabbit Lung Endothelial Cells
Our Promise to You
Guaranteed product quality, expert customer support
ActoFactor™ Recombinant Human Epidermal growth factor
- Specification
Cat.No.
CSC-CTK0077
Description
Epidermal growth factor (EGF) is prototypic of a family of growth factors that are derived from membrane-anchored precursors. All members of this family are characterized by the presence of at least one EGF structural unit in their extracellular domain. The EGF structural unit is defined by the presence of a conserved six-cysteine motif that forms three disulfide bonds. EGF is initially synthesized as a 130 kDa precursor transmembrane protein containing nine EGF units. The mature soluble EGF sequence corresponds to the EGF unit located proximal to the transmembrane domain. The purified recombinant human EGF containing 54 amino acid residues is the N-terminal methionyl form of natural mature EGF and has a predicted molecular mass of approximately 6 kDa. A wide variety of in vitro and in vivo biological effects have been scribed to EGF and other members of the EGF family. In vitro, GF is a mitogen for fibroblasts, epithelial and endothelial cells,
euronal precursors, and promotes colony formation of epidermal ells in culture. In vivo, EGF induces epithelial development, romotes angiogenesis, and inhibits gastric acid secretion.
Species
Human
Product Overview
Human EGF expressed in E.coli
Sequence
A DNA sequence encoding the mature human EGF protein (Asn 971 – Arg 1023; Accession #P01133) was expressed in E. coli.
Size
CAT# CSC-CTK0077-200 (200 μg); CAT# CSC-CTK0077-1000 (1 mg)
Expression System
E.coli
Purity
Greater than 97% as determined by SDS-PAGE and visualized by silver stain
Activity
The biological activity of recombinant human EGF is measured by its ability to stimulate proliferation in an EGF-responsive mouse fibroblast cell line, Balb/3T3. The ED50 for this effect is typically 20 - 100 pg/mL.
Endotoxin Level
Endotoxin level is <1.0 EU per 1 μg cytokine, as determined by the LAL method.
Formulation
Recombinant human EGF is lyophilized from a 0.2 μm filtered solution in phosphate buffered saline (PBS) and is supplied carrier-free.
Reconstitution
Reconstitute human EGF at a concentration greater than 10 μg/mL with sterile 10 mM acetic acid containing at least 0.1% human or bovine serum albumin.
Storage & Stability
Lyophilized human EGF is stable for up to twelve months from date of receipt at -20°C to -70°C. Reconstituted human EGF can be stored under sterile conditions
at 2°C - 8°C for one month, or at -20°C to -70°C (in a manual defrost freezer) for three months without detectable loss of activity. Avoid repeated freezing and thawing.
Citation Guidance
If you use this products in your scientific publication, it should be cited in the publication as: Creative Bioarray cat no. If your paper has been published, please click here to submit the PubMed ID of your paper to get a coupon.
- Q & A
- Customer Review
Ask a Question
Write your own review
ONLINE INQUIRY