EGF Protein, Mouse, Recombinant

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EGF Protein, Mouse, Recombinant: 製品情報

純度
> 95 % as determined by SDS-PAGE
内毒素
Please contact us for more information.
活性
Measured in a cell proliferation assay using Balb/c 3T3 mouse embryonic fibroblast cells. The ED50 for this effect is typically 30-180 pg/mL.
タンパク質の構築
A DNA sequence encoding the mouse EGF (P01132) (Asn977-Arg1029) was expressed and purified.
NCBI Reference No.
発現ホスト
Yeast
Mouse
予測N末端
Asn 977
分子量
The recombinant mouse EGF consists of 53 amino acids and predicts a molecular mass of 6 KDa. It migrates as an approximately 6 KDa band in SDS-PAGE under reducing conditions.
バッファー
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.
配送
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.
安定性 & 保存条件
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.
再構成
A hardcopy of COA with reconstitution instruction is sent along with the products. Please refer to it for detailed information.

EGF Protein, Mouse, Recombinant: 画像

EGF Protein, Mouse, Recombinant: 別名

AI790464 Protein, Mouse

EGF 背景情報

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.
完全な名称
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.
  • Androgen Promotes Differentiation of PLZF+ Spermatogonia pool via Indirect Regulatory Pattern
    Author
    Wang, J;Li, J;Gu, Y;Xia, Q;Song, W;Zhang, X;Yang, Y;Wang, W;Li, H;Zou, K;
    Year
    2018
    Journal
    bioRxiv
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