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Canine EGF / Epidermal Growth Factor (aa 973-1024) Protein (Native)

Sino Biological Inc. liefert Canine EGF / Epidermal Growth Factor (aa 973-1024) Protein (Native) mit höherer Qualität und günstiger Kosten im Vergleich mit anderen globalen Lieferanten.

Weitere Informationen über Canine EGF / Epidermal Growth Factor (aa 973-1024) Protein (Native) lesen Sie bitte: http://www.sinobiological.com/EGF-Epidermal-Growth-Factor-Protein-g-9999.html

Produkt-Information von EGF / Epidermal Growth Factor Protein

Synonym EGF
Protein Construction

A DNA sequence encoding the canine EGF (Q9BEA0)(Asn973-Arg1024)was expressed , with a N-terminal Met.

Source Canine
Expression Host E.coli

QC Testing von EGF / Epidermal Growth Factor Protein

Purity > 95% as determined by SDS-PAGE SDS-PAGE:
SDS-PAGE

EGF protein

Endotoxin Please contact us for more information.
Stability Samples are stable for up to twelve months from date of receipt at -70℃
Predicted N terminal Met
Molecular Mass

The recombinant canine EGF comprises 53 amino acids and has a predicted molecular mass of 6.3 kDa. The apparent molecular mass of the protein is approximately 7 kDa in SDS-PAGE under reducing conditions due to glycosylation.

Formulation Lyophilized from sterile PBS.
  1. Normally 5 % - 8 % trehalose and mannitol are added as protectants before lyophilization. Specific concentrations are included in the hardcopy of COA.

Usage Guide von EGF / Epidermal Growth Factor Protein

Storage Store it under sterile conditions at -70℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
Reconstitution A hardcopy of COA with reconstitution instruction is sent along with the products. Please refer to it for detailed information.

Verwandte Produkte & Themen von EGF / Epidermal Growth Factor Protein

Related Areas:

Cancer>>Cancer Biomarkers>>EGF

Cancer>>Growth Factor & Receptor>>EGF Family & Receptor>>EGF

Proteins:
Molecule Species Description //For Detailed Info. and Price------CLICK! Cat. No
EGF Human EGF/Fc Protein, Recombinant 10605-H01H
EGF Human EGF Protein, Recombinant 10605-HNAE
EGF Mouse EGF Protein, Recombinant 50482-M01H
EGF Canine EGF / Epidermal Growth Factor Protein, Recombinant 70013-D07E
EGF Canine EGF / Epidermal Growth Factor (aa 973-1024) Protein, Recombinant, with Native 70013-DNAE
Antibodies:
Molecule Application Description //For Detailed Info. and Price------CLICK! Cat. No
Human
EGF
WB, ELISA EGF Antibody, Rabbit MAb 10605-R008

Beschreibung von EGF / Epidermal Growth Factor Protein

Epidermal growth factor (EGF), also known as urogastrone (URG) since it was isolated from urine based on its inhibitory effect on gastric secretion, is the founding member of the EGF-family of growth factors. All the members of this protein family have highly similar structural and functional characteristics. EGF is initially synthesized as a 130 kDa single-pass transmembrane protein containing 9 EGF-like units and 9 LDL-receptor class B repeats. The mature soluble EGF is a 6 kDa peptide corresponding to the EGF unit located proximal to the transmembrane domain. EGF is expressed in kidney, salivary gland, cerebrum and prostate, and plays an important role in the regulation of cell growth, proliferation, and differentiation by binding to its receptor EGFR. As a potent mitogen, EGF stimulates the growth of various epidermal and epithelial tissues both in vivo and in vitro. Furthermore, EGF is also identified as a magnesiotropic hormone that stimulates magnesium reabsorption in the renal distal convoluted tubule via engagement of EGFR and activation of the magnesium channel TRPM6. Defects in EGF are the cause of hypomagnesemia type 4 (HOMG4), a disorder characterized by massive renal hypomagnesemia and normal levels of serum calcium and calcium excretion.

References

  1. Ciardiello F. et al., 1991, Proc Natl Acad Sci. 88: 7792-6.
  2. Gout I. et al., 1992, Biochem J. 288: 395-405.
  3. Harris RC. et al., 2003, Exp Cell Res. 284: 2-13.
  4. Dreux AC. et al., 2006, Atherosclerosis. 186: 38-53.
  5. Groenestege WMT. et al., 2007, J Clin Invest. 117: 2260-7.
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