EGF Protein (Monomer)

Catalog No. ABIN1589620

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

Quick Overview for EGF Protein (Monomer) (ABIN1589620)

Target: EGF (Epidermal Growth Factor (EGF))

Protein Type: Recombinant

Biological Activity: Active

Origin: Human

Source: Escherichia coli (E. coli)

Purity: > 95 % by SDS-PAGE

Product Details

Protein Characteristics: Monomer

Purpose: EGF

Sequence: MNSDSECPLS HDGYCLHDGV CMYIEALDKY ACNCVVGYIG ERCQYRDLKW WELR

Specificity: Chromosomal location:4q25

Cross-Reactivity: Mouse

Characteristics: Length (aa):54

Endotoxin Level: < 0.1 ng/μg of protein (<1EU/μg)

Application Details

Application Notes: The biological activity was determined by the ability to induce EGF receptor phosphorylation in the A431 tumor cell line [Soler et al, J Chromatography B, 788, 2003] and the induction of proliferation in NHDF cells (Normal Human Dermal Fibroblasts).

Comment:

Cytokines & Growth Factors

Restrictions: For Research Use only

Handling

Format: Lyophilized

Reconstitution: We recommend a quick spin followed by reconstitution in water to a concentration of 0.1-1.0 mg/mL.

Buffer: PBS

Handling Advice: Centrifuge vial prior to opening.

Storage: RT,-20 °C

Storage Comment: The lyophilized protein is stable for a few weeks at room temperature, but best stored at -20°C. Reconstituted EGF should be stored in working aliquots at -20°C.

Target Details

Target: EGF (Epidermal Growth Factor (EGF))

Alternative Name: EGF

Background: Epidermal growth factor (EGF) is the founding member of the EGF family that also includes TGFα, amphiregulin (AR), betacellulin (BTC), epiregulin (EPR), heparin-binding EGF-like growth factor (HBEGF), epigen, and the neuregulins (NRG) 1 through 6. Members of the EGF family share a structural motif, the EGF-like domain, which is characterized by three intra-molecular disulfide bonds that are formed by six similarly spaced conserved cysteine residues. All EGF family members are synthesized as type I transmembrane precursor proteins that may contain several EGF domains in the extracellular region. The mature proteins are released from the cell surface by regulated proteolysis. The 1207 amino acid (aa) human EGF precursor contains nine EGF domains and nine LDLR class B repeats. The mature protein consists of 53 aa and is generated by proteolytic excision of the EGF domain proximal to the transmembrane region. Mature human EGF shares 70 % aa sequence identity with mature mouse and rat EGF. EGF is present in various body fluids, including blood, milk, urine, saliva, seminal fluid, pancreatic juice, cerebrospinal fluid, and amniotic fluid. Four ErbB (HER) family receptor tyrosine kinases including EGFR/ErbB1, ErbB2, ErbB3 and ErbB4, mediate responses to EGF family members. EGF binds ErbB1 and depending on the context, induces the formation of homodimers or heterodimers containing ErbB2. Biological activities ascribed to EGF include epithelial development, angiogenesis, inhibition of gastric acid secretion, fibroblast proliferation, and colony formation of epidermal cells in culture.
Synonyms: EGF, URG, HOMG4, Urogastrone, Epidermal growth factor

Molecular Weight: 6.35 kDa

Gene ID: 1950

NCBI Accession: NM_1963, NP_001954

UniProt: P01133

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