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Index > Protein center > GSN(Gene name) > Human
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  • GSN (Gene name),
  • Gelsolin (Protein name ),  GELS_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:
    GSN;
    Protein name:
    Gelsolin;
    Alternative:
    Actin-depolymerizing factor(ADF);AGEL;Brevin;
    Organism:
    Human (Homo sapiens). 
    General Annotation
    Sub Unit:
    Binds to actin and to fibronectin.
    Function:
    Calcium-regulated, actin-modulating protein that binds to the plus (or barbed) ends of actin monomers or filaments, preventing monomer exchange (end-blocking or capping). It can promote the assembly of monomers into filaments (nucleation) as well as sever filaments already formed. Plays a role in ciliogenesis.
    Subcellular Location:
    Isoform 1 Secreted
    Protein Attributes:
    Sequence length:
    782
    Sequence:
    50:
    MAPHRPAPAL | LCALSLALCA | LSLPVRAATA | SRGASQAGAP | QGRVPEARPN | 
    100:
    SMVVEHPEFL | KAGKEPGLQI | WRVEKFDLVP | VPTNLYGDFF | TGDAYVILKT | 
    150:
    VQLRNGNLQY | DLHYWLGNEC | SQDESGAAAI | FTVQLDDYLN | GRAVQHREVQ | 
    200:
    GFESATFLGY | FKSGLKYKKG | GVASGFKHVV | PNEVVVQRLF | QVKGRRVVRA | 
    250:
    TEVPVSWESF | NNGDCFILDL | GNNIHQWCGS | NSNRYERLKA | TQVSKGIRDN | 
    300:
    ERSGRARVHV | SEEGTEPEAM | LQVLGPKPAL | PAGTEDTAKE | DAANRKLAKL | 
    350:
    YKVSNGAGTM | SVSLVADENP | FAQGALKSED | CFILDHGKDG | KIFVWKGKQA | 
    400:
    NTEERKAALK | TASDFITKMD | YPKQTQVSVL | PEGGETPLFK | QFFKNWRDPD | 
    450:
    QTDGLGLSYL | SSHIANVERV | PFDAATLHTS | TAMAAQHGMD | DDGTGQKQIW | 
    500:
    RIEGSNKVPV | DPATYGQFYG | GDSYIILYNY | RHGGRQGQII | YNWQGAQSTQ | 
    550:
    DEVAASAILT | AQLDEELGGT | PVQSRVVQGK | EPAHLMSLFG | GKPMIIYKGG | 
    600:
    TSREGGQTAP | ASTRLFQVRA | NSAGATRAVE | VLPKAGALNS | NDAFVLKTPS | 
    650:
    AAYLWVGTGA | SEAEKTGAQE | LLRVLRAQPV | QVAEGSEPDG | FWEALGGKAA | 
    700:
    YRTSPRLKDK | KMDAHPPRLF | ACSNKIGRFV | IEEVPGELMQ | EDLATDDVML | 
    750:
    LDTWDQVFVW | VGKDSQEEEK | TEALTSAKRY | IETDPANRDR | RTPITVVKQG | 
    782:
    FEPPSFVGWF | LGWDDDYWSV | DPLDRAMAEL | AA
    3D Structure:
    N/A
    Predicted Eptitope:
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    EIAab Sequence  Vaild Sequence:
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    Related Databases
    KEGG:
    Pfam:
    UniGene:
    MIM:
    SMR:
    String:
    Uniprot:
     
    FOR
    ELISA Kit for Human Gelsolin
    Cat.:
    E0372h
    Price:
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    MSDS:
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    Packing:
    96T
    Range:
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    ELISA Kit for Human Gelsolin
    Cat.:
    E0372b
    Price:
    Please sign in first.
    MSDS:
    Please sign in first.
    Packing:
    96T
    Range:
    Please sign in first.
    ELISA Kit for Human Gelsolin
    Cat.:
    E0372r
    Price:
    Please sign in first.
    MSDS:
    Please sign in first.
    Packing:
    96T
    Range:
    Please sign in first.
    ELISA Kit for Human Gelsolin
    Cat.:
    E0372p
    Price:
    Please sign in first.
    MSDS:
    Please sign in first.
    Packing:
    96T
    Range:
    Please sign in first.
    ELISA Kit for Human Gelsolin
    Cat.:
    E0372m
    Price:
    Please sign in first.
    MSDS:
    Please sign in first.
    Packing:
    96T
    Range:
    Please sign in first.
    ELISA Kit for Human Gelsolin
    Cat.:
    E0372c
    Price:
    Please sign in first.
    MSDS:
    Please sign in first.
    Packing:
    96T
    CLIA Kit for Human Gelsolin
    Cat.:
    U0372m
    Price:
    Please sign in first.
    MSDS:
    Please sign in first.
    Packing:
    96T
    CLIA Kit for Human Gelsolin
    Cat.:
    U0372c
    Price:
    Please sign in first.
    MSDS:
    Please sign in first.
    Packing:
    96T
    CLIA Kit for Human Gelsolin
    Cat.:
    U0372p
    Price:
    Please sign in first.
    MSDS:
    Please sign in first.
    Packing:
    96T
    Range:
    Please sign in first.
    CLIA Kit for Human Gelsolin
    Cat.:
    U0372r
    Price:
    Please sign in first.
    MSDS:
    Please sign in first.
    Packing:
    96T
    Range:
    Please sign in first.
    CLIA Kit for Human Gelsolin
    Cat.:
    U0372b
    Price:
    Please sign in first.
    MSDS:
    Please sign in first.
    Packing:
    96T
    Range:
    Please sign in first.
    CLIA Kit for Human Gelsolin
    Cat.:
    U0372h
    Price:
    Please sign in first.
    MSDS:
    Please sign in first.
    Packing:
    96T
    Range:
    Please sign in first.
    Polyclonal Antibody for Human Gelsolin
    Cat.:
    P0372Rb-h
    Price:
    Please sign in first.
    Packing:
    40ug/0.2ml
    Polyclonal Antibody for Human Gelsolin
    Cat.:
    P0372Rb-m
    Price:
    Please sign in first.
    Packing:
    40ug/0.2ml
    Polyclonal Antibody for Human Gelsolin
    Polyclonal Antibody for Human Gelsolin
    Polyclonal Antibody for Human Gelsolin
    Polyclonal Antibody for Human Gelsolin
    Cat.:
    P0372Rb-r
    Price:
    Please sign in first.
    Packing:
    40ug/0.2ml
    Monoclonal Antibody for Human Gelsolin
    Monoclonal Antibody for Human Gelsolin
    Monoclonal Antibody for Human Gelsolin
    Monoclonal Antibody for Human Gelsolin
    Monoclonal Antibody for Human Gelsolin
    Monoclonal Antibody for Human Gelsolin
    Protein for Human Gelsolin
    Protein for Human Gelsolin
    Protein for Human Gelsolin
    Cat.:
    R0372h
    Price:
    Please sign in first.
    Packing:
    1mg
    Purity:
    >90%
    Protein for Human Gelsolin
    Protein for Human Gelsolin
    Protein for Human Gelsolin

    R&D Technical Data
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    Precision
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    Recovery
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    Linearity
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    References
    1. 1.
      "Plasma and cytoplasmic gelsolins are encoded by a single gene and contain a duplicated actin-binding domain."
      Kwiatkowski D.J. , Stossel T.P. , Orkin S.H. , Mole J.E. , Colten H.R. , Yin H.L.
      Nature323:455-458(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] (ISOFORMS 1 AND 2);ALTERNATIVE INITIATION
    2. 2.
      "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] (ISOFORMS 1; 2; 3 AND 4)
      tissue: Hippocampus.
      tissue: Testis.
      tissue: Tongue.
    3. 3.
      "DNA sequence and analysis of human chromosome 9."
      Humphray S.J. , Oliver K. , Hunt A.R. , Plumb R.W. , Loveland J.E. , Howe K.L. , Andrews T.D. , Searle S. , Hunt S.E. , Scott C.E. , Jones M.C. , Ainscough R. , Almeida J.P. , Ambrose K.D. , Ashwell R.I.S. , Babbage A.K. , Babbage S. , Bagguley C.L. , more...
      Nature429:369-374(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 GENOMIC DNA]
    4. 4.
      [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.
      tissue: Pancreas.
    6. 6.
      "Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides."
      Gevaert K. , Goethals M. , Martens L. , Van Damme J. , Staes A. , Thomas G.R. , Vandekerckhove J.
      Nat. Biotechnol.21:566-569(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: PROTEIN SEQUENCE OF 53-72 (ISOFORM 2)
      tissue: Platelet.
    7. 7.
      "Human plasma gelsolin binds to fibronectin."
      Lind S.E. , Janmey P.A.
      J. Biol. Chem.259:13262-13266(1984) [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 FIBRONECTIN
    8. 8.
      "Amyloid protein in familial amyloidosis (Finnish type) is homologous to gelsolin, an actin-binding protein."
      Haltia M. , Prelli F. , Ghiso J. , Kiuru S. , Sommer H. , Palo J. , Frangione B.
      Biochem. Biophys. Res. Commun.167:927-932(1990) [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: IDENTITY OF AMYL5 AMYLOID PROTEIN WITH GELSOLIN
    9. 9.
      "Finnish hereditary amyloidosis. Amino acid sequence homology between the amyloid fibril protein and human plasma gelsoline."
      Maury C.P.J. , Alli K. , Baumann M.
      FEBS Lett.260:85-87(1990) [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: IDENTITY OF AMYL5 AMYLOID PROTEIN WITH GELSOLIN
    10. 10.
      "The plasma and cytoplasmic forms of human gelsolin differ in disulfide structure."
      Wen D. , Corina K. , Chow E.P. , Miller S. , Janmey P.A. , Pepinsky R.B.
      Biochemistry35:9700-9709(1996) [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: DISULFIDE BOND
    11. 11.
      "Functional consequences of disulfide bond formation in gelsolin."
      Allen P.G.
      FEBS Lett.401:89-94(1997) [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: DISULFIDE BOND
    12. 12.
      "Identification of Tyr438 as the major in vitro c-Src phosphorylation site in human gelsolin: a mass spectrometric approach."
      De Corte V. , Demol H. , Goethals M. , Van Damme J. , Gettemans J. , Vandekerckhove J.
      Protein Sci.8:234-241(1999) [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: PHOSPHORYLATION AT TYR-86; TYR-409; TYR-465; TYR-603 AND TYR-651
    13. 13.
      "Functional genomic screen for modulators of ciliogenesis and cilium length."
      Kim J. , Lee J.E. , Heynen-Genel S. , Suyama E. , Ono K. , Lee K. , Ideker T. , Aza-Blanc P. , Gleeson J.G.
      Nature464:1048-1051(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: FUNCTION
    14. 14.
      [15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s) Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]
    15. 15.
      "Structure of gelsolin segment 1-actin complex and the mechanism of filament severing."
      McLaughlin P.J. , Gooch J.T. , Mannherz H.-G. , Weeds A.G.
      Nature364:685-692(1993) [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 (2.5 ANGSTROMS) OF 28-503
    16. 16.
      "Spectroscopic studies of a phosphoinositide-binding peptide from gelsolin: behavior in solutions of mixed solvent and anionic micelles."
      Xian W. , Vegners R. , Janmey P.A. , Braunlin W.H.
      Biophys. J.69:2695-2702(1995) [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 177-196
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      [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 (1.55 ANGSTROMS) OF 439-782;CALCIUM-BINDING SITES
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      "Structural states and dynamics of the D-loop in actin."
      Durer Z.A. , Kudryashov D.S. , Sawaya M.R. , Altenbach C. , Hubbell W. , Reisler E.
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      [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 53-174 IN COMPLEX WITH ACTA1; COBL AND TMSB4X;SUBUNIT
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      "Gelsolin variant (Asn-187) in familial amyloidosis, Finnish type."
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      [15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s) Cited for: VARIANT AMYL5 ASN-214
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      "Gelsolin-derived familial amyloidosis caused by asparagine or tyrosine substitution for aspartic acid at residue 187."
      de la Chapelle A. , Tolvanen R. , Boysen G. , Santavy J. , Bleeker-Wagemakers L. , Maury C.P.J. , Kere J.
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      [15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s) Cited for: VARIANTS AMYL5 ASN-214 AND TYR-214
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      [15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s) Cited for: VARIANTS [LARGE SCALE ANALYSIS] LEU-22; ILE-201 AND ASN-611
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