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

Features and benefits

Specifications & Purity: Animal Free, Carrier Free, GMP, Low Endotoxin, High performance, Bioactive grade, ≥98%(SDS-PAGE)
Biological Activity: Measured in a cell proliferation assay using BALB/3T3 mouse embryo fibroblasts cell line. The ED₅₀ for this effect is typically <1 ng/mL.
Protein Tag: No tag

Item Number

rp155969

Grouped product items
SKU	Size	Availability	Price
rp155969-50μg (Trial Size) Apply for free trial size（?） Every year, as a valued customer, you have the exclusive opportunity to explore and enjoy three different trial products of your choice, absolutely free!	50μg	Available within 8-12 weeks(?) Production requires sourcing of materials. We appreciate your patience and understanding.	$113.90
rp155969-200μg	200μg	Available within 4-8 weeks(?) Items will be manufactured post-order and can take 4-8 weeks. Thank you for your patience!	$333.90
rp155969-1mg	1mg	Available within 8-12 weeks(?) Production requires sourcing of materials. We appreciate your patience and understanding.	$1,233.90

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

View related series

Accession#:P01133 EGF Gene ID:1950

Basic Description

Product Name	Recombinant Human EGF Protein - Recombinant protein, ≥95% (SDS-PAGE), high purity, CAS No.62253-63-8
Synonyms	NEPIDERMIN\|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
Specifications & Purity	Animal Free, Carrier Free, GMP, Low Endotoxin, High performance, Bioactive grade, ≥98%(SDS-PAGE)
Purity	≥95% (SDS-PAGE)
Biological Activity	Measured in a cell proliferation assay using BALB/3T3 mouse embryo fibroblasts cell line. The ED₅₀ for this effect is typically <1 ng/mL.
Species	Human
Amino Acids	971-1023 aa
Sequence	NSDSECPLSH DGYCLHDGVC MYIEALDKYA CNCVVGYIGE RCQYRDLKWW ELR
Protein Tag	No tag
Protein Length	Full length protein
Accession #	P01133
Source	Recombinant
Predicted molecular weight	6.5kD
SDS-PAGE	7.1 kDa, under reducing conditions.
Grade	Animal Free, Bioactive, Carrier Free, GMP, High performance, Low Endotoxin

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

Form	Lyophilized
Reconstitution	Reconstitute 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 Temp	Store at -20°C,Avoid repeated freezing and thawing
Shipped In	Dry ice
Stability And Storage	Store at -20℃ for 3 years. Upon delivery aliquot. Avoid freeze/thaw cycle.
CAS	62253-63-8

Certificates

Certificate of Analysis(COA)

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To view the certificate results,please click on a Lot number.For Lot numbers from past orders,please use our order status section

7 results found

Lot Number	Certificate Type	Date	Item
ZJ24F0505983	Certificate of Analysis	May 23, 2024	rp155969
ZJ24F0505244	Certificate of Analysis	May 09, 2024	rp155969
ZJ24F0303826	Certificate of Analysis	Mar 29, 2024	rp155969
ZJ24F0303825	Certificate of Analysis	Mar 29, 2024	rp155969
ZJ23F0300039	Certificate of Analysis	Nov 10, 2023	rp155969
ZJ24F0505243	Certificate of Analysis	Nov 10, 2023	rp155969
ZJ23F0300040	Certificate of Analysis	Mar 13, 2023	rp155969

Pictogram(s)

GHS07

Signal

Warning

Hazard Statements

H315,H319,H335

Precautionary Statements

P261,P305+P351+P338,P280,P302+P352,P321,P405,P501,P264,P271,P304+P340,P403+P233,P362+P364,P264+P265,P337+P317,P332+P317,P319

WGK Germany

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]

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

Basic Description

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