EGF Protein, Human, Recombinant

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EGF Protein, Human, Recombinant: 产品信息

纯度
> 92 % as determined by SDS-PAGE
内毒素
Please contact us for more information.
生物活性
Measured in a cell proliferation assay using Balb/C 3T3 mouse embryonic fibroblasts.
The ED50 for this effect is typically 0.15-0.75 ng/mL.
蛋白构建
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.
NP No.
表达宿主
E. coli
种属
Human
预测 N 端
Met 1
分子量
The recombinant human EGF consisting of 54 amino acids and has a calculated molecular mass of 6.3 kDa as estimated in SDS-PAGE under reducing conditions.
缓冲液
Lyophilized from sterile PBS, pH 7.4
1. Normally 5 % - 8 % trehalose, mannitol and 0.01% Tween80 are added as protectants before lyophilization. Specific concentrations are included in the hardcopy of COA.
2. Please contact us for any concerns or special requirements.
Please refer to the specific buffer information in the hard copy of CoA.
运输方式
In general, recombinant proteins are provided as lyophilized powder which are shipped at ambient temperature.
Bulk packages of recombinant proteins are provided as frozen liquid. They are shipped out with blue ice unless customers require otherwise.
稳定性 & 储存条件
Samples are stable for up to twelve months from date of receipt at -70℃
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.
复溶
A hardcopy of COA with reconstitution instruction is sent along with the products. Please refer to it for detailed information.

EGF Protein, Human, Recombinant: 图片

EGF Protein, Human, Recombinant: 别称

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 645-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.
全称
epidermal growth factor
参考文献
  • 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.
  • Prokaryotic expression and refolding of EGFR extracellular domain and generation of phage display human scFv against EGFR
    Author
    Zhou, Y;Zhang, J;Jin, H;Chen, Z;Wu, Q;Li, W;Yue, M;Luo, C;Wang, M;
    Year
    2013
    Journal
    Biomed. Pharmacother.
    Application
    ELISA
  • Plasma-Generated OH Radical Production for Analyzing Three-Dimensional Structure in Protein Therapeutics
    Author
    Minkoff, BB;Blatz, JM;Choudhury, FA;Benjamin, D;Shohet, JL;Sussman, MR;
    Year
    2017
    Journal
    Sci Rep
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