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Recombinant Rat EGF Protein

Catalog #: 3214-EG
12 Citations Datasheet / COA / SDS

Carrier Free

Catalog # Availability Size / Price Qty
3214-EG-100/CF

With Carrier

Catalog # Availability Size / Price Qty
3214-EG-100
R&D Systems Recombinant Proteins and Enzymes
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Product Details
Citations (12)
FAQs
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Summary Product Datasheets Carrier Free Data Images Reconstitution Calculator Background Related Research Areas

Recombinant Rat EGF Protein Summary

Product Specifications

Purity
>97%, by SDS-PAGE under reducing conditions and visualized by silver stain.
Endotoxin Level
<0.10 EU per 1 μg of the protein by the LAL method.
Activity
Measured in a cell proliferation assay using Balb/3T3 mouse embryonic fibroblast cells. Rubin, J.S. et al. (1991) Proc. Natl. Acad. Sci. USA 88:415. The ED50 for this effect is 10-60 pg/mL.
Source
E. coli-derived rat EGF protein
Asn974-Arg1026, with an N-terminal Met
Accession #
P07522
N-terminal Sequence
Analysis
Met
Predicted Molecular Mass
6.3 kDa

Product Datasheets

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3214-EG (with carrier)

Product Datasheet
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3214-EG/CF (carrier free)

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COA
SDS

Carrier Free

What does CF mean?

CF stands for Carrier Free (CF). We typically add Bovine Serum Albumin (BSA) as a carrier protein to our recombinant proteins. Adding a carrier protein enhances protein stability, increases shelf-life, and allows the recombinant protein to be stored at a more dilute concentration. The carrier free version does not contain BSA.

What formulation is right for me?

In general, we advise purchasing the recombinant protein with BSA for use in cell or tissue culture, or as an ELISA standard. In contrast, the carrier free protein is recommended for applications, in which the presence of BSA could interfere.

3214-EG

Formulation Lyophilized from a 0.2 μm filtered solution in Acetonitrile and TFA with BSA as a carrier protein.
Reconstitution Reconstitute at 100 μg/mL in sterile 10 mM Acetic Acid containing at least 0.1% human or bovine serum albumin.
Shipping The product is shipped at ambient temperature. Upon receipt, store it immediately at the temperature recommended below.
Stability & Storage: Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
  • 12 months from date of receipt, -20 to -70 °C as supplied.
  • 1 month, 2 to 8 °C under sterile conditions after reconstitution.
  • 3 months, -20 to -70 °C under sterile conditions after reconstitution.

3214-EG/CF

Formulation Lyophilized from a 0.2 μm filtered solution in Acetonitrile and TFA.
Reconstitution Reconstitute at 100 μg/mL in sterile 10 mM Acetic Acid.
Shipping The product is shipped at ambient temperature. Upon receipt, store it immediately at the temperature recommended below.
Stability & Storage: Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
  • 12 months from date of receipt, -20 to -70 °C as supplied.
  • 1 month, 2 to 8 °C under sterile conditions after reconstitution.
  • 3 months, -20 to -70 °C under sterile conditions after reconstitution.
Reconstitution Calculator

Reconstitution Calculator

The reconstitution calculator allows you to quickly calculate the volume of a reagent to reconstitute your vial. Simply enter the mass of reagent and the target concentration and the calculator will determine the rest.

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Background: EGF

Epidermal growth factor (EGF) is a small, potent growth factor capable of inducing cell proliferation, differentiation, and survival. EGF is the founding member of the EGF family that also includes TGF-alpha, amphiregulin (AR), betacellulin (BTC), epiregulin (EPR), heparin‑binding EGF‑like growth factor (HB‑EGF), epigen, and the neuregulins (NRG)-1 through -6 (1). Members of The EGF family are characterized by a shared structural motif, the EGF‑like domain, which contains three intramolecular disulfide bonds that are formed by six similarly spaced, conserved cysteine residues (2). These disulfide bonds are essential for proper protein conformation and receptor binding. 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 (1). The full length EGF protein is 1207 amino acids (aa) (EGF precursor) containing nine EGF domains and nine LDLR class B repeats. However, the mature protein is much smaller, only 53 aa, and is generated by proteolytic cleavage of the EGF domain proximal to the transmembrane region (3). EGF is well conserved across mammals with mature human EGF 70% identical to mature mouse and rat EGF. Physiologically, EGF is found in various body fluids, including blood, milk, urine, saliva, seminal fluid, pancreatic juice, cerebrospinal fluid, and amniotic fluid (4). EGF is a high affinity ligand of the EGF receptor (ErbB). Four ErbB (HER) family receptor tyrosine kinases including EGFR/ErbB1, ErbB2, ErbB3 and ErbB4, mediate responses to EGF family members (5). EGF binding induces dimerization of the EGF receptor resulting in activation of the protein tyrosine kinase signaling pathway. These receptors undergo a complex pattern of ligand-induced homo- or hetero-dimerization to transduce EGF family signals (6, 7). EGF binds ErbB1 and depending on the context, induces the formation of homodimers or heterodimers containing ErbB2. Dimerization results in autophosphorylation of the receptor at specific tyrosine residues to create docking sites for a variety of signaling molecules (5, 8). Biological activities ascribed to EGF include epithelial development, angiogenesis, inhibition of gastric acid secretion, fibroblast proliferation, and colony formation of epidermal cells in culture.

References
  1. Harris, R.C. et al. (2003) Exp. Cell Res. 284:2.
  2. Carpenter, G. and Cohen, S. (1990) J. Biol. Chem. 265:7709.
  3. Saggi, S.J. et al. (1992) DNA Cell Biol. 11:481.
  4. Carpenter, G. and Zendegui, J.G. (1986) Exp. Cell Res. 164:1.
  5. Jorissen, R.N. et al. (2003) Exp. Cell Res. 284:31.
  6. Gamett, D.C. et al. (1997) J. Biol. Chem. 272:12052.
  7. Qian, X. et al. (1994) Proc. Natl. Acad. Sci. 91:1500.
  8. Qian, X. et al. (1999) J. Biol. Chem. 274:574.
Long Name
Epidermal Growth Factor
Entrez Gene IDs
1950 (Human); 13645 (Mouse); 25313 (Rat)
Alternate Names
beta-urogastrone; EGF; epidermal growth factor (beta-urogastrone); epidermal growth factor; hEGF; HOMG4; pro-epidermal growth factor; URG; Urogastrone

Citations for Recombinant Rat EGF Protein

R&D Systems personnel manually curate a database that contains references using R&D Systems products. The data collected includes not only links to publications in PubMed, but also provides information about sample types, species, and experimental conditions.

12 Citations: Showing 1 - 10
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  1. Decellularized Pancreatic Tail as Matrix for Pancreatic Islet Transplantation into the Greater Omentum in Rats
    Authors: Z Berkova, K Zacharovov, A Patikova, I Leontovyc, Z Hladikova, D Cerveny, E Tihlarikov, V Nedela, P Girman, D Jirak, F Saudek
    Journal of functional biomaterials, 2022-09-30;13(4):.
    Species: Rat
    Sample Types: Whole Cell
    Applications: Cell Culture
  2. Sox9 is involved in the thyroid differentiation program and is regulated by crosstalk between TSH, TGFbeta and thyroid transcription factors
    Authors: A López-Márq, C Carrasco-L, A Martínez-C, P Lemoine, CE Pierreux, P Santisteba
    Scientific Reports, 2022-02-09;12(1):2144.
    Species: Rat
    Sample Types: Whole Cells
    Applications: Bioassay
  3. Let-7, Lin28 and Hmga2 Expression in Ciliary Epithelium and Retinal Progenitor Cells
    Authors: LT Frasson, B Dalmaso, PS Akamine, ET Kimura, DE Hamassaki, CB Del Debbio
    Investigative Ophthalmology & Visual Science, 2021-03-01;62(3):31.
    Species: Rat
    Sample Types: Whole Cells
    Applications: Bioassay
  4. Long noncoding RNA mediates stroke-induced neurogenesis
    Authors: B Fan, W Pan, X Wang, M Wei, A He, A Zhao, M Chopp, ZG Zhang, XS Liu
    Stem Cells, 2020-05-02;0(0):.
    Species: Rat
    Sample Types: Whole Cells
    Applications: Bioassay
  5. Canine mesenchymal stromal cell-conditioned medium promotes survival and neurite outgrowth of neural stem cells
    Authors: M Nakamura, H Nishida, K Yoshizaki, H Akiyoshi, S Hatoya, K Sugiura, T Inaba
    J. Vet. Med. Sci., 2020-04-06;0(0):.
    Species: Rat
    Sample Types: Cells
    Applications: Cell Culture
  6. Implantation of engineered conduction tissue in the rat heart
    Authors: W Zhang, X Li, S Sun, X Zhang
    Mol Med Rep, 2019-02-05;0(0):.
    Species: Rat
    Sample Types: Whole Cells
    Applications: Bioassay
  7. Non-Canonical Activation of the Epidermal Growth Factor Receptor by Carbon Nanoparticles
    Authors: D Stöckmann, T Spannbruck, N Ale-Agha, P Jakobs, C Goy, N Dyballa-Ru, T Hornstein, A Kümper, A Kraegeloh, J Haendeler, K Unfried
    Nanomaterials (Basel), 2018-04-23;8(4):.
    Species: Rat
    Sample Types: Whole Cells
    Applications: Bioassay
  8. Comparative Analysis of the Cell Fates of Induced Schwann Cells from Subcutaneous Fat Tissue and Na�ve Schwann Cells in the Sciatic Nerve Injury Model
    Authors: M Zhang, MH Jiang, DW Kim, W Ahn, E Chung, Y Son, G Chi
    Biomed Res Int, 2017-06-20;2017(0):1252851.
    Species: Rat
    Sample Types: Tissue Homogenates
    Applications: Bioassay
  9. Wound healing protects against chemotherapy-induced alopecia in young rats via up-regulating interleukin-1?-mediated signaling
    Authors: O Stojadinov, TC Wikramanay, AC Villasante, NC Yin, L Liang, E Hinde, J Escandon, M Tomic-Cani, DM Ansell, R Paus, JJ Jimenez
    Heliyon, 2017-05-30;3(5):e00309.
    Species: Rat
    Sample Types: In Vivo
    Applications: In Vivo
  10. TGF-beta signalling in the adult neurogenic niche promotes stem cell quiescence as well as generation of new neurons.
    Authors: Kandasamy M, Lehner B, Kraus S, Sander P, Marschallinger J, Rivera F, Trumbach D, Ueberham U, Reitsamer H, Strauss O, Bogdahn U, Couillard-Despres S, Aigner L
    J Cell Mol Med, 2014-04-30;18(7):1444-59.
    Species: Rat
    Sample Types: Whole Cells
    Applications: Bioassay
  11. A combination of Wnt and growth factor signaling induces Arl4c expression to form epithelial tubular structures.
    Authors: Matsumoto, Shinji, Fujii, Shinsuke, Sato, Akira, Ibuka, Souji, Kagawa, Yoshinor, Ishii, Masaru, Kikuchi, Akira
    EMBO J, 2014-02-20;33(7):702-18.
    Species: Rat
    Sample Types: Whole Cells
    Applications: Bioassay
  12. Histone deacetylase inhibition attenuates diabetes-associated kidney growth: potential role for epigenetic modification of the epidermal growth factor receptor.
    Authors: Gilbert RE, Huang Q, Thai K, Advani SL, Lee K, Yuen DA, Connelly KA, Advani A
    Kidney Int., 2011-03-09;79(12):1312-21.
    Species: Rat
    Sample Types: Whole Cells
    Applications: Bioassay

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