EGF Protein (AA 971-1023, N-Term)

Catalog No. ABIN2666929

This Recombinant EGF protein is expressed in Escherichia coli (E. coli).

Quick Overview for EGF Protein (AA 971-1023, N-Term) (ABIN2666929)

Target: EGF (Epidermal Growth Factor (EGF))

Protein Type: Recombinant

Biological Activity: Active

Origin: Human

Source: Escherichia coli (E. coli)

Application: ELISA, Flow Cytometry (FACS)

Purity: > 98 % , as determined by Coomassie stained SDS-PAGE.

Product Details

Protein Characteristics: AA 971-1023, N-Term

Sterility: 0.22 μm filtered

Endotoxin Level:

Less than 0.01 ng per μg cytokine as determined by the LAL method.

Application Details

Application Notes: Optimal working dilution should be determined by the investigator.

Comment:

Biological activity: The ED50 is 1-2 ng/ml, corresponding to a specific activity 5x105 - 1x106 units/mg, as determined by a dose-dependent inhibition on A431 cells proliferation.

Restrictions: For Research Use only

Handling

Format: Liquid

Reconstitution: For maximum results, quick spin vial prior to opening. Stock solutions should be prepared at no less than 10 μg/mL in sterile buffer (PBS, HPBS, DPBS, and EBSS) containing carrier protein such as 1 % BSA or HSA. After dilution, the cytokine can be stored between 2 °C and 8 °C for one month or from -20 °C to -70 °C for up to 3 months.

Buffer: 0.22 μm filtered protein solution is in PBS.

Handling Advice: Avoid repeated freeze/thaw cycles.

Storage: -20 °C

Storage Comment: Unopened vial can be stored between 2°C and 8°C for three months, at -20°C for six months, or at -70°C for one year.

Target Details

Target: EGF (Epidermal Growth Factor (EGF))

Alternative Name: EGF

Background: Epidermal growth factor (EGF) is a small 6 kD polypeptide and has six conserved cysteine residues that form three intramolecular disulfide bonds. Human and mouse EGF share 70 % homology in amino acid structure. Human EGF is synthesized as a transmembrane precursor protein (1207 amino acids) which is proteolytically cleaved to generate the 54 amino acid mature EGF. Many different cells including mammary gland cells, macrophages, gut epithelial cells, and cells in the nervous system and the kidney can produce EGF. EGF plays important roles in the regulation of cell survival, proliferation, and differentiation by binding to its receptor EGFR. For example, EGF can stimulate the proliferation of mouse embryonic stem cells or induce the terminal differentiation/growth inhibition of A431 cells. The binding of EGF to EGFR will induce receptor dimerization, which is required for activating the tyrosine kinase in the receptor cytoplasmic domain. In addition, the binding of EGF to its receptor triggers several signal transduction pathways including JAK/STAT, Ras/ERK and PI3K/AKT pathways. Blocking of the EGF/EGFR pathway can suppress some tumor cell's proliferation. Other members of the EGF family (including transforming growth factor-α (TGF-α), heparin-binding EGF-like growth factor (HB-EGF), amphiregulin (AR), betacellulin (BTC), epiregulin (EPR), and epigen) also bind to EGFR.

Molecular Weight: The 54 amino acid recombinant protein has a predicted molecular mass of approximately 6 kDa. The DTT-reduced protein migrates at approximately 6 kDa and non-reduced protein migrates at approximately 13 kDa by SDS-PAGE. The N-terminal amino acid is Methion

Pathways: NF-kappaB Signaling, RTK Signaling, Fc-epsilon Receptor Signaling Pathway, EGFR Signaling Pathway, Neurotrophin Signaling Pathway, Regulation of Carbohydrate Metabolic Process, Hepatitis C, Protein targeting to Nucleus, Interaction of EGFR with phospholipase C-gamma, Thromboxane A2 Receptor Signaling, EGFR Downregulation