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Recombinant Human EGF Protein - Recombinant protein, ≥95% (SDS-PAGE), high purity, CAS No.62253-63-8

  • Animal Free
  • Bioactive
  • Carrier Free
  • GMP
  • High performance
  • Low Endotoxin
  • ≥98%(SDS-PAGE)
Features and benefits
  • Expression System: Pichia pastoris
  • Accession #: P01133
  • Protein Tag: No tag
  • Bioactivity: Measured in a cell proliferation assay using BALB/3T3 mouse embryo fibroblasts cell line. The ED₅₀ for this effect is typically <1 ng/mL.
  • Endotoxin Concentration: <1.0 EU/mg
Item Number
rp155969
Grouped product items
SKUSizeAvailabilityPrice Qty
rp155969-50μg
50μg
In stock
$119.90
rp155969-200μg
200μg
In stock
$329.90
rp155969-1mg
1mg
Available within 8-12 weeks(?)
Production requires sourcing of materials. We appreciate your patience and understanding.
$999.90

GMP, ≥98% (SDS-PAGE), Active, Pichia pastoris, No tag, 971-1023 aa

View related series
Accession#:P01133 EGF Gene ID:1950

Basic Description

Product NameRecombinant Human EGF Protein - Recombinant protein, ≥95% (SDS-PAGE), high purity, CAS No.62253-63-8
SynonymsNEPIDERMIN|62253-63-8|Human EGF|Nepidermin [INN]|Epidermal growth factor (human)|beta-Urogastrone (human)|UNII-TZK30RF92W|MG 111|Human epidermal growth factor|CCRIS 6735|TZK30RF92W|DTXSID80211314|AKOS040759488
GradeAnimal Free, Bioactive, Carrier Free, GMP, High performance, Low Endotoxin
Product Description

Purity
≥98% SDS-PAGE.
Endotoxin level
<1.0 EU/mg
Function
EGF stimulates the growth of various epidermal and epithelial tissues in vivo and in vitro and of some fibroblasts in cell culture. Magnesiotropic hormone that stimulates magnesium reabsorption in the renal distal convoluted tubule via engagement of EGFR and activation of the magnesium channel TRPM6. Can induce neurite outgrowth in motoneurons of the pond snail Lymnaea stagnalis in vitro (PubMed:10964941).

Specifications & PurityAnimal Free, Carrier Free, GMP, Low Endotoxin, High performance, Bioactive grade, ≥98%(SDS-PAGE)
Purity≥95% (SDS-PAGE)
BioactivityMeasured in a cell proliferation assay using BALB/3T3 mouse embryo fibroblasts cell line. The ED₅₀ for this effect is typically <1 ng/mL.
Endotoxin Concentration<1.0 EU/mg
Expression SystemPichia pastoris
SpeciesHuman
Amino Acids971-1023 aa
SequenceNSDSECPLSH DGYCLHDGVC MYIEALDKYA CNCVVGYIGE RCQYRDLKWW ELR
Protein TagNo tag
Protein LengthFull length protein
Accession #P01133
SourceRecombinant
Predicted molecular weight 6.5kD
SDS-PAGE7.1 kDa, under reducing conditions.

Images

Recombinant Human EGF Protein (rp155969)-Protein Bioactivity
Measured in a cell proliferation assay using BALB/3T3 mouse embryo fibroblasts cell line. The ED₅₀ for this effect is typically <1ng/mL.

Recombinant Human EGF Protein (rp155969)-SDS-PAGE
5μg/lane of Recombinant Human EGF was resolved with SDS-PAGE under reducing (R) and non-reducing (N) conditions and visualized by Coomassie® Blue staining, showing a single band at 7.1 kDa.

Product Specifications

FormLyophilized
ReconstitutionReconstitute in sterile water to a concentration of 100-200μg/ml, and further dilute it in other solvents. Upon reconstitution, the product could be stored at 4 ℃ for 2-7 days and used up as soon as possible. For future use, should be stored at -20 ℃.
Storage TempStore at -20°C,Avoid repeated freezing and thawing
Shipped InIce chest + Ice pads
Stability And StorageStore at -20℃ for 3 years. Upon delivery aliquot. Avoid freeze/thaw cycle.
CAS62253-63-8

Certificates

Certificate of Analysis(COA)

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8 results found

Lot NumberCertificate TypeDateItem
ZJ24F0607416Certificate of AnalysisJun 28, 2024 rp155969
ZJ24F0505983Certificate of AnalysisMay 23, 2024 rp155969
ZJ24F0505244Certificate of AnalysisMay 09, 2024 rp155969
ZJ24F0303826Certificate of AnalysisMar 29, 2024 rp155969
ZJ24F0303825Certificate of AnalysisMar 29, 2024 rp155969
ZJ23F0300039Certificate of AnalysisNov 10, 2023 rp155969
ZJ24F0505243Certificate of AnalysisNov 10, 2023 rp155969
ZJ23F0300040Certificate of AnalysisMar 13, 2023 rp155969

Safety and Hazards(GHS)

Pictogram(s) GHS07
Signal Warning
Hazard Statements

H315:Causes skin irritation

H319:Causes serious eye irritation

H335:May cause respiratory irritation

Precautionary Statements

P261:Avoid breathing dust/fume/gas/mist/vapors/spray.

P305+P351+P338:IF IN EYES: Rinse cautiously with water for several minutes. Remove contact lenses if present and easy to do - continue rinsing.

P280:Wear protective gloves/protective clothing/eye protection/face protection.

P302+P352:IF ON SKIN: wash with plenty of water.

P321:Specific treatment (see ... on this label).

P405:Store locked up.

P501:Dispose of contents/container to ...

P264:Wash hands [and …] thoroughly after handling.

P271:Use only outdoors or in a well-ventilated area.

P304+P340:IF INHALED: Remove person to fresh air and keep comfortable for breathing.

P403+P233:Store in a well-ventilated place. Keep container tightly closed.

P362+P364:Take off contaminated clothing and wash it before reuse.

P264+P265:Wash hands [and …] thoroughly after handling. Do not touch eyes.

P337+P317:If eye irritation persists: Get medical help.

P332+P317:If skin irritation occurs: Get medical help.

P319:Get medical help if you feel unwell.

WGK Germany 3

Related Documents

References

1. Ogiso H, Ishitani R, Nureki O, Fukai S, Yamanaka M, Kim JH, Saito K, Sakamoto A, Inoue M, Shirouzu M et al..  (2002)  Crystal structure of the complex of human epidermal growth factor and receptor extracellular domains..  Cell,  110  (6): (775-87).  [PMID:12297050]
2. Feng Y, Yin Y, Weiser A, Griffin E, Cameron MD, Lin L, Ruiz C, Schürer SC, Inoue T, Rao PV, Schröter T, Lograsso P..  (2008)  Discovery of substituted 4-(pyrazol-4-yl)-phenylbenzodioxane-2-carboxamides as potent and highly selective Rho kinase (ROCK-II) inhibitors..  J Med Chem,  51  (21): (6642-6645).  [PMID:18834107]
3. Lesuisse D, Mauger J, Nemecek C, Maignan S, Boiziau J, Harlow G, Hittinger A, Ruf S, Strobel H, Nair A, Ritter K, Malleron JL, Dagallier A, El-Ahmad Y, Guilloteau JP, Guizani H, Bouchard H, Venot C..  (2011)  Discovery of the first non-ATP competitive IGF-1R kinase inhibitors: advantages in comparison with competitive inhibitors..  Bioorg Med Chem Lett,  21  (8): (2224-2228).  [PMID:21441024]
4. Gregory, H H and Preston, B M BM..  (1977)  The primary structure of human urogastrone..  International journal of peptide and protein research,      [PMID:300079]
5. Hommel, U U, Harvey, T S TS, Driscoll, P C PC and Campbell, I D ID..  (1992)  Human epidermal growth factor. High resolution solution structure and comparison with human transforming growth factor alpha..  Journal of molecular biology,    (5):   [PMID:1522591]
6. Furuya, M M, Akashi, S S and Hirayama, K K..  (1989)  The primary structure of human EGF produced by genetic engineering, studied by high-performance tandem mass spectrometry..  Biochemical and biophysical research communications,    (15):   [PMID:2789514]
7. Bell, G I GI and 8 more authors..  (1986)  Human epidermal growth factor precursor: cDNA sequence, expression in vitro and gene organization..  Nucleic acids research,    (11):   [PMID:3491360]
8. Lu, H S HS and 5 more authors..  (2001)  Crystal structure of human epidermal growth factor and its dimerization..  The Journal of biological chemistry,    (14):   [PMID:11438527]
9. Ferguson, Kathryn M KM and 5 more authors..  (2003)  EGF activates its receptor by removing interactions that autoinhibit ectodomain dimerization..  Molecular cell,      [PMID:12620237]
10. Hillier, Ladeana W LW and 121 more authors..  (2005)  Generation and annotation of the DNA sequences of human chromosomes 2 and 4..  Nature,    (7):   [PMID:15815621]
11. Groenestege, Wouter M Tiel WM and 10 more authors..  (2007)  Impaired basolateral sorting of pro-EGF causes isolated recessive renal hypomagnesemia..  The Journal of clinical investigation,      [PMID:17671655]
12. Lu, Chafen C and 6 more authors..  (2010)  Structural evidence for loose linkage between ligand binding and kinase activation in the epidermal growth factor receptor..  Molecular and cellular biology,      [PMID:20837704]
13. Huang, Hsiao-Wen HW, Mohan, Sepuru K SK and Yu, C C..  (2010)  The NMR solution structure of human epidermal growth factor (hEGF) at physiological pH and its interactions with suramin..  Biochemical and biophysical research communications,    (26):   [PMID:21029725]
14. Zettl, Markus M, Adrain, Colin C, Strisovsky, Kvido K, Lastun, Viorica V and Freeman, Matthew M..  (2011)  Rhomboid family pseudoproteases use the ER quality control machinery to regulate intercellular signaling..  Cell,    (1):   [PMID:21439629]

Solution Calculators