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Index > Protein center > EGF(Gene name) > Human
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  • EGF (Gene name),
  • Pro-epidermal growth factor (Protein name ),  EGF_HUMAN from NCBI database.
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  • General Annotation
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  • Antigen Annotation
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  • 3D
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  • Predicted Eptitope
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  • Vaild Sequence
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  • Related Databases
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  • Gene name:
    EGF;
    Protein name:
    Pro-epidermal growth factor(EGF);
    Alternative:

    Organism:
    Human (Homo sapiens). 
    General Annotation
    Sub Unit:
    Interacts with EGFR and promotes EGFR dimerization. Interacts with RHBDF2 (By similarity). Interacts with RHBDF1; may retain EGF in the endoplasmic reticulum and regulates its degradation through the endoplasmic reticulum-associated degradation (ERAD).
    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.
    Subcellular Location:
    Membrane Single-pass type I membrane protein
    Protein Attributes:
    Sequence length:
    1207
    Sequence:
    50:
    MLLTLIILLP | VVSKFSFVSL | SAPQHWSCPE | GTLAGNGNST | CVGPAPFLIF | 
    100:
    SHGNSIFRID | TEGTNYEQLV | VDAGVSVIMD | FHYNEKRIYW | VDLERQLLQR | 
    150:
    VFLNGSRQER | VCNIEKNVSG | MAINWINEEV | IWSNQQEGII | TVTDMKGNNS | 
    200:
    HILLSALKYP | ANVAVDPVER | FIFWSSEVAG | SLYRADLDGV | GVKALLETSE | 
    250:
    KITAVSLDVL | DKRLFWIQYN | REGSNSLICS | CDYDGGSVHI | SKHPTQHNLF | 
    300:
    AMSLFGDRIF | YSTWKMKTIW | IANKHTGKDM | VRINLHSSFV | PLGELKVVHP | 
    350:
    LAQPKAEDDT | WEPEQKLCKL | RKGNCSSTVC | GQDLQSHLCM | CAEGYALSRD | 
    400:
    RKYCEDVNEC | AFWNHGCTLG | CKNTPGSYYC | TCPVGFVLLP | DGKRCHQLVS | 
    450:
    CPRNVSECSH | DCVLTSEGPL | CFCPEGSVLE | RDGKTCSGCS | SPDNGGCSQL | 
    500:
    CVPLSPVSWE | CDCFPGYDLQ | LDEKSCAASG | PQPFLLFANS | QDIRHMHFDG | 
    550:
    TDYGTLLSQQ | MGMVYALDHD | PVENKIYFAH | TALKWIERAN | MDGSQRERLI | 
    600:
    EEGVDVPEGL | AVDWIGRRFY | WTDRGKSLIG | RSDLNGKRSK | IITKENISQP | 
    650:
    RGIAVHPMAK | RLFWTDTGIN | PRIESSSLQG | LGRLVIASSD | LIWPSGITID | 
    700:
    FLTDKLYWCD | AKQSVIEMAN | LDGSKRRRLT | QNDVGHPFAV | AVFEDYVWFS | 
    750:
    DWAMPSVMRV | NKRTGKDRVR | LQGSMLKPSS | LVVVHPLAKP | GADPCLYQNG | 
    800:
    GCEHICKKRL | GTAWCSCREG | FMKASDGKTC | LALDGHQLLA | GGEVDLKNQV | 
    850:
    TPLDILSKTR | VSEDNITESQ | HMLVAEIMVS | DQDDCAPVGC | SMYARCISEG | 
    900:
    EDATCQCLKG | FAGDGKLCSD | IDECEMGVPV | CPPASSKCIN | TEGGYVCRCS | 
    950:
    EGYQGDGIHC | LDIDECQLGE | HSCGENASCT | NTEGGYTCMC | AGRLSEPGLI | 
    1000:
    CPDSTPPPHL | REDDHHYSVR | NSDSECPLSH | DGYCLHDGVC | MYIEALDKYA | 
    1050:
    CNCVVGYIGE | RCQYRDLKWW | ELRHAGHGQQ | QKVIVVAVCV | VVLVMLLLLS | 
    1100:
    LWGAHYYRTQ | KLLSKNPKNP | YEESSRDVRS | RRPADTEDGM | SSCPQPWFVV | 
    1150:
    IKEHQDLKNG | GQPVAGEDGQ | AADGSMQPTS | WRQEPQLCGM | GTEQGCWIPV | 
    1200:
    SSDKGSCPQV | MERSFHMPSY | GTQTLEGGVE | KPHSLLSANP | LWQQRALDPP | 
    1207:
    HQMELTQ
    3D Structure:
    N/A
    Predicted Eptitope:
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    EIAab Sequence  Vaild Sequence:
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    Related Databases
    String:
    Pfam:
    MIM:
    UniGene:
    SMR:
    KEGG:
    Uniprot:
     
    FOR
    ELISA Kit for Human EGF
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    E0560h
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    ELISA Kit for Human EGF
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    E0560d
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    ELISA Kit for Human EGF
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    ELISA Kit for Human EGF
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    E0560r
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    ELISA Kit for Human EGF
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    E0560p
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    96T
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    CLIA Kit for Human EGF
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    U0560p
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    Please sign in first.
    Packing:
    96T
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    CLIA Kit for Human EGF
    Cat.:
    U0560r
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    MSDS:
    Please sign in first.
    Packing:
    96T
    Range:
    Please sign in first.
    CLIA Kit for Human EGF
    Cat.:
    U0560m
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    Please sign in first.
    MSDS:
    Please sign in first.
    Packing:
    96T
    Range:
    Please sign in first.
    CLIA Kit for Human EGF
    Cat.:
    U0560d
    Price:
    Please sign in first.
    MSDS:
    Please sign in first.
    Packing:
    96T
    Range:
    Please sign in first.
    CLIA Kit for Human EGF
    Cat.:
    U0560h
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    Please sign in first.
    MSDS:
    Please sign in first.
    Packing:
    96T
    Range:
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    Polyclonal Antibody for Human EGF
    Polyclonal Antibody for Human EGF
    Cat.:
    P0560Rb-h
    Price:
    Please sign in first.
    Packing:
    40ug/0.2ml
    Polyclonal Antibody for Human EGF
    Polyclonal Antibody for Human EGF
    Cat.:
    P0560Rb-m
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    Please sign in first.
    Packing:
    40ug/0.2ml
    Polyclonal Antibody for Human EGF
    Cat.:
    P0560Rb-r
    Price:
    Please sign in first.
    Packing:
    40ug/0.2ml
    Monoclonal Antibody for Human EGF
    Monoclonal Antibody for Human EGF
    Monoclonal Antibody for Human EGF
    Monoclonal Antibody for Human EGF
    Monoclonal Antibody for Human EGF
    Protein for Human EGF
    Protein for Human EGF
    Protein for Human EGF
    Protein for Human EGF
    Protein for Human EGF

    R&D Technical Data
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    Precision

    Intra-Assay CV: ≤4.3

    Inter-Assay CV: ≤7.5

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    Recovery
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    Linearity
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    References
    1. 1.
      "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) [PubMed] [Europe PMC] [Abstract]
      [15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s) Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1)
      tissue: Kidney.
    2. 2.
      NIEHS SNPs program
      Submitted (2003-12) to the EMBL/GenBank/DDBJ databases
      [15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s) Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA];VARIANTS ARG-16; HIS-257; LYS-431; ARG-638; ILE-708; VAL-784; THR-842; VAL-920; GLU-981; PHE-1043 AND GLY-1084
    3. 3.
      "Complete 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. , more...
      Nat. Genet.36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      [15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s) Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2);VARIANT VAL-920
      tissue: Teratocarcinoma.
    4. 4.
      "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. , more...
      Nature434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
      [15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s) Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]
    5. 5.
      "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res.14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      [15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s) Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1)
      tissue: Colon.
    6. 6.
      [15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s) Cited for: PROTEIN SEQUENCE OF 971-1023
    7. 7.
      "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) [PubMed] [Europe PMC] [Abstract]
      [15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s) Cited for: PROTEIN SEQUENCE OF 971-1023
    8. 8.
      "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. Proteomics0:0-0(2011) [PubMed] [Europe PMC] [Abstract]
      [15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s) Cited for: GLYCOSYLATION AT SER-954 AND THR-955;STRUCTURE OF CARBOHYDRATES;IDENTIFICATION BY MASS SPECTROMETRY
    9. 9.
      "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) [PubMed] [Europe PMC] [Abstract]
      [15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s) Cited for: STRUCTURE BY NMR OF EGF
    10. 10.
      [15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s) Cited for: FUNCTION;TISSUE SPECIFICITY;VARIANT HOMG4 LEU-1070;CHARACTERIZATION OF VARIANT HOMG4 LEU-1070
    11. 11.
      "Rhomboid family pseudoproteases use the ER quality control machinery to regulate intercellular signaling."
      Zettl M. , Adrain C. , Strisovsky K. , Lastun V. , Freeman M.
      Cell145:79-91(2011) [PubMed] [Europe PMC] [Abstract]
      [15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s) Cited for: INTERACTION WITH RHBDF1
    12. 12.
      "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) [PubMed] [Europe PMC] [Abstract]
      [15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s) Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 971-1021;DISULFIDE BONDS
    13. 13.
      "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.
      Cell110:775-787(2002) [PubMed] [Europe PMC] [Abstract]
      [15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s) Cited for: X-RAY CRYSTALLOGRAPHY (3.3 ANGSTROMS) OF 971-1023 IN COMPLEX WITH EGFR;DISULFIDE BONDS
    14. 14.
      "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. Cell11:507-517(2003) [PubMed] [Europe PMC] [Abstract]
      [15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s) Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 971-1023 IN COMPLEX WITH EGFR;DISULFIDE BONDS
    15. 15.
      "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) [PubMed] [Europe PMC] [Abstract]
      [15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s) Cited for: STRUCTURE BY NMR OF 971-1023 IN COMPLEX WITH SURAMIN
    16. 16.
      "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) [PubMed] [Europe PMC] [Abstract]
      [15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s) Cited for: X-RAY CRYSTALLOGRAPHY (3.3 ANGSTROMS) OF 975-1021 IN COMPLEX WITH EGFR;DISULFIDE BONDS
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