Name :
Recombinant Human EGF Protein (ECD), GMP grade, HPLC-verified
Biological Activity :
Background :
EGF is the founding member of the EGF-family of proteins. Members of this protein family have highly similar structural and functional characteristics. EGF contains 9 EGF-like domains and 9 LDL-receptor class B repeats. Human EGF is a 6045-Da protein with 53 amino acid residues and three intramolecular disulfide bonds. As a low-molecular-weight polypeptide, EGF was first purified from the mouse submandibular gland, but since then it was found in many human tissues including submandibular gland, parotid gland. It can also be found in human platelets, macrophages, urine, saliva, milk, and plasma. EGF is a growth factor that stimulates the growth of various epidermal and epithelial tissues in vivo and in vitro and of some fibroblasts in cell culture. It results in cellular proliferation, differentiation, and survival. Salivary EGF, which seems also regulated by dietary inorganic iodine, also plays an important physiological role in the maintenance of oro-esophageal and gastric tissue integrity. EGF acts by binding with high affinity to epidermal growth factor receptor on the cell surface and stimulating the intrinsic protein-tyrosine kinase activity of the receptor. The tyrosine kinase activity, in turn, initiates a signal transduction cascade that results in a variety of biochemical changes within the cell – a rise in intracellular calcium levels, increased glycolysis and protein synthesis, and increases in the expression of certain genes including the gene for EGFR – that ultimately lead to DNA synthesis and cell proliferation.
Biological Activity :
Measured in a cell proliferation assay using Balb/3T3 mouse embryonic fibroblast cells. The specific activity of Recombinant Human EGF is >1,000 IU/μg, which is calibrated against the human EGF WHO International Standard (NIBSC code: 91/530).
Expression Host :
Human
Source :
E. coli
Tag :
Protein Accession No. :
NP_001954.2
NCBI Gene ID :
Synonyms :
Synonyms :
epidermal growth factor
Amino Acid Sequence :
Molecular Weight :
The recombinant human EGF consists of 54 amino acids and has a calculated molecular mass of 6.35 kDa.
Purity :
≥ 95 % as determined by SDS-PAGE. ≥ 95 % as determined by SEC-HPLC.
State of Matter :
Product Concentration :
Storage and Stability :
Samples are stable for up to twelve months from date of receipt at -20℃ to -80℃. Store it under sterile conditions at -20℃ to -80℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
Endotoxin Level :
< 5 EU per mg of the protein.
Protein Construction :
A DNA sequence encoding the mature form of human EGF (NP_001954.2) (Asn 971-Arg 1023) was expressed and purified with an initial Met at the N-terminus.
Buffer Solution :
Supplied as sterile PBS, pH 7.4Please contact us for any concerns or special requirements.Please refer to the specific buffer information in the hardcopy of datasheet.
Shipping :
Liquid. It is shipped out with blue ice.
Redissolution :
A hardcopy of COA with reconstitution instruction is sent along with the products. Please refer to it for detailed information.
Synonyms :
Epidermal Growth Factor Protein, Human; HOMG4 Protein, Human; URG Protein, Human EGF 背景信息 EGF is the founding member of the EGF-family of proteins. Members of this protein family have highly similar structural and functional characteristics. EGF contains 9 EGF-like domains and 9 LDL-receptor class B repeats. Human EGF is a 6045-Da protein with 53 amino acid residues and three intramolecular disulfide bonds. As a low-molecular-weight polypeptide, EGF was first purified from the mouse submandibular gland, but since then it was found in many human tissues including submandibular gland, parotid gland. It can also be found in human platelets, macrophages, urine, saliva, milk, and plasma. EGF is a growth factor that stimulates the growth of various epidermal and epithelial tissues in vivo and in vitro and of some fibroblasts in cell culture. It results in cellular proliferation, differentiation, and survival. Salivary EGF, which seems also regulated by dietary inorganic iodine, also plays an important physiological role in the maintenance of oro-esophageal and gastric tissue integrity. EGF acts by binding with high affinity to epidermal growth factor receptor on the cell surface and stimulating the intrinsic protein-tyrosine kinase activity of the receptor. The tyrosine kinase activity, in turn, initiates a signal transduction cascade that results in a variety of biochemical changes within the cell – a rise in intracellular calcium levels, increased glycolysis and protein synthesis, and increases in the expression of certain genes including the gene for EGFR – that ultimately lead to DNA synthesis and cell proliferation.
References & Citations :
Chen JX, et al. (2011) Involvement of c-Src/STAT3 signal in EGF-induced proliferation of rat spermatogonial stem cells. Mol Cell Biochem. 358(1-2):67-73.Guo Y, et al. (2012) Correlations among ERCC1, XPB, UBE2I, EGF, TAL2 and ILF3 revealed by gene signatures of histological subtypes of patients with epithelial ovarian cancer. Oncol Rep. 27(1):286-92.Kim S, et al. (2012) Smad7 acts as a negative regulator of the epidermal growth factor (EGF) signaling pathway in breast cancer cells. Cancer Lett. 314(2):147-54.Chatterton RT Jr, et al. (2010) Breast ductal lavage for assessment of breast cancer biomarkers. Horm Cancer. 1(4):197-204.
MedChemExpress (MCE) recombinant proteins include: cytokines, enzymes, growth factors, hormones, receptors, transcription factors, antibody fragments, etc. They are often essential for supporting cell growth, stimulating cell signaling pathways, triggering or inhibiting cell differentiation; and are useful tools for elucidating protein structure and function, understanding disease onset and progression, and validating pharmaceutical targets. At MedChemExpress (MCE), we strive to provide products with only the highest quality. Protein identity, purity and biological activity are assured by our robust quality control and assurance procedures.
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