Pro-epidermal growth factor Recombinant Protein | EGF recombinant protein

Recombinant Human Pro-epidermal growth factor

Cat. Num. AAA719371

• Gene Names: EGF; URG; HOMG4
• Purity: Greater or equal to 85% purity as determined by SDS-PAGE.
• Synonyms: Pro-epidermal growth factor; Recombinant Human Pro-epidermal growth factor; Urogastrone; EGF recombinant protein

• Host: E Coli
• Purity/Purification: Greater or equal to 85% purity as determined by SDS-PAGE.
• Form/Format: Liquid containing glycerol
• Sequence Positions: 977-1023. Partial
• Sequence: PLSHDGYCLHDGVCMYIEALDKYACNCVVGYIGERCQYRDLKWWELR

• Preparation and Storage: Store at -20 degree C, for extended storage, conserve at -20 degree C or -80 degree C.

SDS-PAGE

Related Product Information for EGF recombinant protein

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 engagent of EGFR and activation of the magnesium channel TRPM6. Can induce neurite outgrowth in motoneurons of the pond snail Lymnaea stagnalis in vitro.

Product Categories/Family for EGF recombinant protein

Signal Transduction

References

Human epidermal growth factor precursor cDNA sequence, expression in vitro and gene organization.Bell G.I., Fong N.M., Stempien M.M., Wormsted M.A., Caput D., Ku L., Urdea M.S., Rall L.B., Sanchez-Pescador R.Nucleic Acids Res. 14:8427-8446(1986) NIEHS SNPs programComplete sequencing and characterization of 21,243 full-length human cDNAs.Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.Nat. Genet. 36:40-45(2004) Generation and annotation of the DNA sequences of human chromosomes 2 and 4.Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.Nature 434:724-731(2005) The primary structure of human urogastrone.Gregory H., Preston B.M.Int. J. Pept. Protein Res. 9:107-118(1977) The primary structure of human EGF produced by genetic engineering, studied by high-performance tandem mass spectrometry.Furuya M., Akashi S., Hirayama K.Biochem. Biophys. Res. Commun. 163:1100-1106(1989) Human urinary glycoproteomics; attachment site specific analysis of N-and O-linked glycosylations by CID and ECD.Halim A., Nilsson J., Ruetschi U., Hesse C., Larson G.Mol. Cell. Proteomics 0:0-0(2011) Human epidermal growth factor. High resolution solution structure and comparison with human transforming growth factor alpha.Hommel U., Harvey T.S., Driscoll P.C., Campbell I.D.J. Mol. Biol. 227:271-282(1992) Neurotrophic actions of a novel molluscan epidermal growth factor.Hermann P.M., van Kesteren R.E., Wildering W.C., Painter S.D., Reno J.M., Smith J.S., Kumar S.B., Geraerts W.P., Ericsson L.H., Smit A.B., Bulloch A.G., Nagle G.T.J. Neurosci. 20:6355-6364(2000) Impaired basolateral sorting of pro-EGF causes isolated recessive renal hypomagnesemia.Groenestege W.M.T., Thebault S., van der Wijst J., van den Berg D., Janssen R., Tejpar S., van den Heuvel L.P., van Cutsem E., Hoenderop J.G., Knoers N.V., Bindels R.J.J. Clin. Invest. 117:2260-2267(2007) Rhomboid family pseudoproteases use the ER quality control machinery to regulate intercellular signaling.Zettl M., Adrain C., Strisovsky K., Lastun V., Freeman M.Cell 145:79-91(2011) Crystal structure of human epidermal growth factor and its dimerization.Lu H.S., Chai J.J., Li M., Huang B.R., He C.H., Bi R.C.J. Biol. Chem. 276:34913-34917(2001) Crystal structure of the complex of human epidermal growth factor and receptor extracellular domains.Ogiso H., Ishitani R., Nureki O., Fukai S., Yamanaka M., Kim J.H., Saito K., Sakamoto A., Inoue M., Shirouzu M., Yokoyama S.Cell 110:775-787(2002) EGF activates its receptor by removing interactions that autoinhibit ectodomain dimerization.Ferguson K.M., Berger M.B., Mendrola J.M., Cho H.S., Leahy D.J., Lemmon M.A.Mol. Cell 11:507-517(2003) The NMR solution structure of human epidermal growth factor (hEGF) at physiological pH and its interactions with suramin.Huang H.W., Mohan S.K., Yu C.Biochem. Biophys. Res. Commun. 402:705-710(2010) Structural evidence for loose linkage between ligand binding and kinase activation in the epidermal growth factor receptor.Lu C., Mi L.Z., Grey M.J., Zhu J., Graef E., Yokoyama S., Springer T.A.Mol. Cell. Biol. 30:5432-5443(2010)

NCBI and Uniprot Product Information

• NCBI GI #: 296011013
• NCBI GeneID: 1950
• NCBI Accession #: NP_001171601.1
• NCBI GenBank Nucleotide #: NM_001178130.2
• UniProt Accession #: P01133; Q52LZ6; B4DRK7; E7EVD2; E9PBF0
• Molecular Weight: 32.6 kDa
• NCBI Official Full Name: pro-epidermal growth factor isoform 2
• NCBI Official Synonym Full Names: epidermal growth factor
• NCBI Official Symbol: EGF
• NCBI Official Synonym Symbols: URG; HOMG4
• NCBI Protein Information: pro-epidermal growth factor
• UniProt Protein Name: Pro-epidermal growth factor
• Protein Family: Pro-epidermal growth factor
• UniProt Gene Name: EGF
• UniProt Synonym Gene Names: EGF
• UniProt Entry Name: EGF_HUMAN

NCBI Description

This gene encodes a member of the epidermal growth factor superfamily. The encoded preproprotein is proteolytically processed to generate the 53-amino acid epidermal growth factor peptide. This protein acts a potent mitogenic factor that plays an important role in the growth, proliferation and differentiation of numerous cell types. This protein acts by binding with high affinity to the cell surface receptor, epidermal growth factor receptor. Defects in this gene are the cause of hypomagnesemia type 4. Dysregulation of this gene has been associated with the growth and progression of certain cancers. Alternative splicing results in multiple transcript variants, at least one of which encodes a preproprotein that is proteolytically processed. [provided by RefSeq, Jan 2016]

Uniprot Description

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).