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Immunoglobulin heavy constant gamma 1 (Ig gamma-1 chain C region) (Ig gamma-1 chain C region EU) (Ig gamma-1 chain C region KOL) (Ig gamma-1 chain C region NIE)

 IGHG1_HUMAN             Reviewed;         330 AA.
P01857;
21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
21-JUL-1986, sequence version 1.
27-SEP-2017, entry version 191.
RecName: Full=Immunoglobulin heavy constant gamma 1 {ECO:0000303|PubMed:11340299, ECO:0000303|Ref.11};
AltName: Full=Ig gamma-1 chain C region {ECO:0000305};
AltName: Full=Ig gamma-1 chain C region EU {ECO:0000305|PubMed:5489771, ECO:0000305|PubMed:5530842};
AltName: Full=Ig gamma-1 chain C region KOL {ECO:0000305|PubMed:6884994};
AltName: Full=Ig gamma-1 chain C region NIE {ECO:0000305|PubMed:826475};
Name=IGHG1 {ECO:0000303|PubMed:11340299, ECO:0000303|Ref.11};
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
PROTEIN SEQUENCE.
PubMed=826475;
Ponstingl H., Hilschmann N.;
"The rule of antibody structure. The primary structure of a monoclonal
IgG1 immunoglobulin (myeloma protein Nie). III. The chymotryptic
peptides of the H-chain, alignment of the tryptic peptides and
discussion of the complete structure.";
Hoppe-Seyler's Z. Physiol. Chem. 357:1571-1604(1976).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] (IMGT ALLELE IGHG1*01).
PubMed=6811139; DOI=10.1016/0092-8674(82)90183-0;
Takahashi N., Ueda S., Obata M., Nikaido T., Nakai S., Honjo T.;
"Structure of human immunoglobulin gamma genes: implications for
evolution of a gene family.";
Cell 29:671-679(1982).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=6287432; DOI=10.1093/nar/10.13.4071;
Ellison J.W., Berson B.J., Hood L.E.;
"The nucleotide sequence of a human immunoglobulin C gamma1 gene.";
Nucleic Acids Res. 10:4071-4079(1982).
[4]
PROTEIN SEQUENCE (IMGT ALLELE IGHG1*03), DISULFIDE BONDS, AND VARIANTS
ARG-97; GLU-239 AND MET-241.
PubMed=6884994;
Schmidt W.E., Jung H.-D., Palm W., Hilschmann N.;
"Three-dimensional structure determination of antibodies. Primary
structure of crystallized monoclonal immunoglobulin IgG1 KOL, I.";
Hoppe-Seyler's Z. Physiol. Chem. 364:713-747(1983).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] (IMGT ALLELE IGHG1*05).
PubMed=12508121; DOI=10.1038/nature01348;
Heilig R., Eckenberg R., Petit J.-L., Fonknechten N., Da Silva C.,
Cattolico L., Levy M., Barbe V., De Berardinis V., Ureta-Vidal A.,
Pelletier E., Vico V., Anthouard V., Rowen L., Madan A., Qin S.,
Sun H., Du H., Pepin K., Artiguenave F., Robert C., Cruaud C.,
Bruels T., Jaillon O., Friedlander L., Samson G., Brottier P.,
Cure S., Segurens B., Aniere F., Samain S., Crespeau H., Abbasi N.,
Aiach N., Boscus D., Dickhoff R., Dors M., Dubois I., Friedman C.,
Gouyvenoux M., James R., Madan A., Mairey-Estrada B., Mangenot S.,
Martins N., Menard M., Oztas S., Ratcliffe A., Shaffer T., Trask B.,
Vacherie B., Bellemere C., Belser C., Besnard-Gonnet M.,
Bartol-Mavel D., Boutard M., Briez-Silla S., Combette S.,
Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C., Muselet D.,
Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P., Trybou A.,
Vega-Czarny N., Bataille E., Bluet E., Bordelais I., Dubois M.,
Dumont C., Guerin T., Haffray S., Hammadi R., Muanga J., Pellouin V.,
Robert D., Wunderle E., Gauguet G., Roy A., Sainte-Marthe L.,
Verdier J., Verdier-Discala C., Hillier L.W., Fulton L., McPherson J.,
Matsuda F., Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W.,
Quetier F., Waterston R., Hood L., Weissenbach J.;
"The DNA sequence and analysis of human chromosome 14.";
Nature 421:601-607(2003).
[6]
PROTEIN SEQUENCE OF 1-135 (IMGT ALLELE IGHG1*03), AND VARIANT ARG-97.
PubMed=5489771; DOI=10.1021/bi00818a008;
Cunningham B.A., Rutishauser U., Gall W.E., Gottlieb P.D.,
Waxdal M.J., Edelman G.M.;
"The covalent structure of a human gamma G-immunoglobulin. VII. Amino
acid sequence of heavy-chain cyanogen bromide fragments H1-H4.";
Biochemistry 9:3161-3170(1970).
[7]
PROTEIN SEQUENCE OF 136-329 (IMGT ALLELE IGHG1*03), AND VARIANTS
GLU-239 AND MET-241.
PubMed=5530842; DOI=10.1021/bi00818a009;
Rutishauser U., Cunningham B.A., Bennett C., Konigsberg W.H.,
Edelman G.M.;
"The covalent structure of a human gamma G-immunoglobulin. 8. Amino
acid sequence of heavy-chain cyanogen bromide fragments H5-H7.";
Biochemistry 9:3171-3181(1970).
[8]
DISULFIDE BONDS.
PubMed=4923144; DOI=10.1021/bi00818a011;
Gall W.E., Edelman G.M.;
"The covalent structure of a human gamma G-immunoglobulin. X.
Intrachain disulfide bonds.";
Biochemistry 9:3188-3196(1970).
[9]
DISULFIDE BONDS.
PubMed=1002129;
Dreker L., Schwarz J., Reichel W., Hilschmann N.;
"Rule of antibody structure. The primary structure of a monoclonal
IgG1 immunoglobulin (myeloma protein Nie), I: purification and
characterization of the protein, the L- and H-chains, the cyanogen
bromide cleavage products, and the disulfide bridges.";
Hoppe-Seyler's Z. Physiol. Chem. 357:1515-1540(1976).
[10]
NOMENCLATURE.
PubMed=11340299;
Lefranc M.P.;
"Nomenclature of the human immunoglobulin heavy (IGH) genes.";
Exp. Clin. Immunogenet. 18:100-116(2001).
[11]
NOMENCLATURE.
Lefranc M.P., Lefranc G.;
"The Immunoglobulin FactsBook.";
(In) Lefranc M.P., Lefranc G. (eds.);
The Immunoglobulin FactsBook., pp.1-458, Academic Press, London.
(2001).
[12]
REVIEW ON SOMATIC HYPERMUTATION.
PubMed=17576170; DOI=10.1146/annurev.genet.41.110306.130340;
Teng G., Papavasiliou F.N.;
"Immunoglobulin somatic hypermutation.";
Annu. Rev. Genet. 41:107-120(2007).
[13]
GLYCOSYLATION AT ASN-180.
PubMed=19358553; DOI=10.1021/ac900231w;
Thaysen-Andersen M., Mysling S., Hojrup P.;
"Site-specific glycoprofiling of N-linked glycopeptides using MALDI-
TOF MS: strong correlation between signal strength and glycoform
quantities.";
Anal. Chem. 81:3933-3943(2009).
[14]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-180.
TISSUE=Liver;
PubMed=19159218; DOI=10.1021/pr8008012;
Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
"Glycoproteomics analysis of human liver tissue by combination of
multiple enzyme digestion and hydrazide chemistry.";
J. Proteome Res. 8:651-661(2009).
[15]
GLYCOSYLATION AT ASN-180.
PubMed=19139490; DOI=10.1074/mcp.M800504-MCP200;
Jia W., Lu Z., Fu Y., Wang H.P., Wang L.H., Chi H., Yuan Z.F.,
Zheng Z.B., Song L.N., Han H.H., Liang Y.M., Wang J.L., Cai Y.,
Zhang Y.K., Deng Y.L., Ying W.T., He S.M., Qian X.H.;
"A strategy for precise and large scale identification of core
fucosylated glycoproteins.";
Mol. Cell. Proteomics 8:913-923(2009).
[16]
REVIEW ON IMMUNOGLOBULINS.
PubMed=20176268; DOI=10.1016/j.jaci.2009.09.046;
Schroeder H.W. Jr., Cavacini L.;
"Structure and function of immunoglobulins.";
J. Allergy Clin. Immunol. 125:S41-S52(2010).
[17]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[18]
REVIEW ON FUNCTION.
PubMed=22158414; DOI=10.1038/nri3128;
McHeyzer-Williams M., Okitsu S., Wang N., McHeyzer-Williams L.;
"Molecular programming of B cell memory.";
Nat. Rev. Immunol. 12:24-34(2012).
[19]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[20]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25944712; DOI=10.1002/pmic.201400617;
Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M.,
Ayoub D., Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
"N-terminome analysis of the human mitochondrial proteome.";
Proteomics 15:2519-2524(2015).
[21]
X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS).
PubMed=7236608; DOI=10.1021/bi00512a001;
Deisenhofer J.;
"Crystallographic refinement and atomic models of a human Fc fragment
and its complex with fragment B of protein A from Staphylococcus
aureus at 2.9- and 2.8-A resolution.";
Biochemistry 20:2361-2370(1981).
[22]
INVOLVEMENT IN MULTIPLE MYELOMA.
PubMed=8943038; DOI=10.1073/pnas.93.24.13931;
Bergsagel P.L., Chesi M., Nardini E., Brents L.A., Kirby S.L.,
Kuehl W.M.;
"Promiscuous translocations into immunoglobulin heavy chain switch
regions in multiple myeloma.";
Proc. Natl. Acad. Sci. U.S.A. 93:13931-13936(1996).
[23]
INVOLVEMENT IN MULTIPLE MYELOMA.
PubMed=11972529; DOI=10.1046/j.1365-2141.2002.03438.x;
Harrison C.J., Mazzullo H., Ross F.M., Cheung K.L., Gerrard G.,
Harewood L., Mehta A., Lachmann H.J., Hawkins P.N., Orchard K.H.;
"Translocations of 14q32 and deletions of 13q14 are common chromosomal
abnormalities in systemic amyloidosis.";
Br. J. Haematol. 117:427-435(2002).
-!- FUNCTION: Constant region of immunoglobulin heavy chains.
Immunoglobulins, also known as antibodies, are membrane-bound or
secreted glycoproteins produced by B lymphocytes. In the
recognition phase of humoral immunity, the membrane-bound
immunoglobulins serve as receptors which, upon binding of a
specific antigen, trigger the clonal expansion and differentiation
of B lymphocytes into immunoglobulins-secreting plasma cells.
Secreted immunoglobulins mediate the effector phase of humoral
immunity, which results in the elimination of bound antigens
(PubMed:22158414, PubMed:20176268). The antigen binding site is
formed by the variable domain of one heavy chain, together with
that of its associated light chain. Thus, each immunoglobulin has
two antigen binding sites with remarkable affinity for a
particular antigen. The variable domains are assembled by a
process called V-(D)-J rearrangement and can then be subjected to
somatic hypermutations which, after exposure to antigen and
selection, allow affinity maturation for a particular antigen
(PubMed:17576170, PubMed:20176268). {ECO:0000303|PubMed:17576170,
ECO:0000303|PubMed:20176268, ECO:0000303|PubMed:22158414}.
-!- SUBUNIT: Immunoglobulins are composed of two identical heavy
chains and two identical light chains; disulfide-linked.
{ECO:0000303|PubMed:20176268}.
-!- INTERACTION:
P31994:FCGR2B; NbExp=31; IntAct=EBI-356114, EBI-724784;
P01834:IGKC; NbExp=3; IntAct=EBI-356114, EBI-1054530;
P0CG04:IGLC1; NbExp=2; IntAct=EBI-356114, EBI-1221063;
P38507:spa (xeno); NbExp=2; IntAct=EBI-356114, EBI-7840885;
-!- SUBCELLULAR LOCATION: Secreted {ECO:0000303|PubMed:20176268,
ECO:0000303|PubMed:22158414}. Cell membrane
{ECO:0000303|PubMed:20176268, ECO:0000303|PubMed:22158414}.
-!- POLYMORPHISM: There are several alleles. The sequence shown is
that of IMGT allele IGHG1*05. {ECO:0000305}.
-!- DISEASE: Multiple myeloma (MM) [MIM:254500]: A malignant tumor of
plasma cells usually arising in the bone marrow and characterized
by diffuse involvement of the skeletal system, hyperglobulinemia,
Bence-Jones proteinuria and anemia. Complications of multiple
myeloma are bone pain, hypercalcemia, renal failure and spinal
cord compression. The aberrant antibodies that are produced lead
to impaired humoral immunity and patients have a high prevalence
of infection. Amyloidosis may develop in some patients. Multiple
myeloma is part of a spectrum of diseases ranging from monoclonal
gammopathy of unknown significance (MGUS) to plasma cell leukemia.
{ECO:0000269|PubMed:11972529, ECO:0000269|PubMed:8943038}.
Note=The disease is caused by mutations affecting the gene
represented in this entry. A chromosomal aberration involving
IGHG1 is found in multiple myeloma. Translocation
t(11;14)(q13;q32) with the IgH locus. Translocation
t(11;14)(q13;q32) with CCND1; translocation t(4;14)(p16.3;q32.3)
with FGFR3; translocation t(6;14)(p25;q32) with IRF4.
-!- CAUTION: For an example of a full-length immunoglobulin gamma
heavy chain see AC P0DOX5. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAC82527.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
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EMBL; J00228; AAC82527.1; ALT_INIT; Genomic_DNA.
EMBL; AL122127; -; NOT_ANNOTATED_CDS; Genomic_DNA.
PIR; A93433; GHHU.
UniGene; Hs.510635; -.
PDB; 1AJ7; X-ray; 2.10 A; H=1-103.
PDB; 1AQK; X-ray; 1.84 A; H=21-245.
PDB; 1AXS; X-ray; 2.60 A; B/H=1-101.
PDB; 1BEY; X-ray; 3.25 A; H=1-98.
PDB; 1D5B; X-ray; 2.80 A; B/H=1-101.
PDB; 1D5I; X-ray; 2.00 A; H=1-101.
PDB; 1D6V; X-ray; 2.00 A; H=1-101.
PDB; 1DFB; X-ray; 2.70 A; H=1-103.
PDB; 1DN2; X-ray; 2.70 A; A/B=120-326.
PDB; 1E4K; X-ray; 3.20 A; A/B=106-330.
PDB; 1FC1; X-ray; 2.90 A; A/B=106-329.
PDB; 1FC2; X-ray; 2.80 A; D=106-329.
PDB; 1FCC; X-ray; 3.20 A; A/B=121-326.
PDB; 1GAF; X-ray; 1.95 A; H=1-103.
PDB; 1H3T; X-ray; 2.40 A; A/B=108-330.
PDB; 1H3U; X-ray; 2.40 A; A/B=108-330.
PDB; 1H3V; X-ray; 3.10 A; A/B=108-330.
PDB; 1H3W; X-ray; 2.85 A; M=108-330.
PDB; 1H3X; X-ray; 2.44 A; A/B=108-330.
PDB; 1H3Y; X-ray; 4.10 A; A/B=108-330.
PDB; 1HKL; X-ray; 2.68 A; H=1-103.
PDB; 1HZH; X-ray; 2.70 A; H/K=1-330.
PDB; 1I7Z; X-ray; 2.30 A; B/D=1-103.
PDB; 1L6X; X-ray; 1.65 A; A=120-326.
PDB; 1N7M; X-ray; 1.80 A; L=2-102.
PDB; 1OP3; X-ray; 1.75 A; H/M=1-102.
PDB; 1OQO; X-ray; 2.30 A; A/B=119-330.
PDB; 1OQX; X-ray; 2.60 A; A/B=119-330.
PDB; 1PG7; X-ray; 2.50 A; H/I=1-100.
PDB; 1T83; X-ray; 3.00 A; A/B=107-330.
PDB; 1T89; X-ray; 3.50 A; A/B=107-330.
PDB; 1VGE; X-ray; 2.00 A; H=1-103.
PDB; 2DTS; X-ray; 2.20 A; A/B=108-330.
PDB; 2GJ7; X-ray; 5.00 A; A/B=106-330.
PDB; 2I5Y; X-ray; 2.20 A; H=1-101.
PDB; 2IWG; X-ray; 2.35 A; A/D=120-326.
PDB; 2J6E; X-ray; 3.00 A; A/B=99-330.
PDB; 2JB5; X-ray; 2.80 A; H=1-102.
PDB; 2JB6; X-ray; 2.85 A; B/H=1-102.
PDB; 2O5X; X-ray; 2.05 A; H=1-108.
PDB; 2O5Y; X-ray; 2.85 A; H=1-108.
PDB; 2O5Z; X-ray; 2.40 A; H=1-108.
PDB; 2OSL; X-ray; 2.60 A; A/H=1-103.
PDB; 2QAD; X-ray; 3.30 A; D/H=1-101.
PDB; 2QL1; X-ray; 2.53 A; A=106-330.
PDB; 2QQK; X-ray; 2.75 A; H=1-107.
PDB; 2QQL; X-ray; 3.10 A; H=1-107.
PDB; 2QQN; X-ray; 2.20 A; H=1-107.
PDB; 2QR0; X-ray; 3.50 A; B/F/H/L/N/R/T/X=1-103.
PDB; 2R56; X-ray; 2.80 A; H/I=1-100.
PDB; 2RCJ; X-ray; -; C/D/G/H/K/L/O/P/S/T=1-326.
PDB; 2RCS; X-ray; 2.10 A; H=1-103.
PDB; 2VXQ; X-ray; 1.90 A; H=1-100.
PDB; 2WAH; X-ray; 2.51 A; A/B=120-328.
PDB; 3AGV; X-ray; 2.15 A; A/B=120-330.
PDB; 3AVE; X-ray; 2.00 A; A/B=108-330.
PDB; 3AY4; X-ray; 2.20 A; A/B=108-330.
PDB; 3B2U; X-ray; 2.58 A; C/F/H/J/N/Q/T/W=1-102.
PDB; 3B2V; X-ray; 3.30 A; H=1-102.
PDB; 3BDY; X-ray; 2.60 A; H=1-107.
PDB; 3BE1; X-ray; 2.90 A; H=1-107.
PDB; 3BKY; X-ray; 2.61 A; H=1-104.
PDB; 3BN9; X-ray; 2.17 A; D/F=1-107.
PDB; 3BQU; X-ray; 3.00 A; B=2-103.
PDB; 3C08; X-ray; 2.15 A; H=1-102.
PDB; 3C09; X-ray; 3.20 A; C/H=1-102.
PDB; 3C2S; X-ray; 2.30 A; A=106-330.
PDB; 3CFJ; X-ray; 2.60 A; B/D/F/H=1-104.
PDB; 3CFK; X-ray; 2.60 A; B/D/F/H/I/K/N/P=1-104.
PDB; 3CSY; X-ray; 3.40 A; A/C/E/G=1-101.
PDB; 3D0L; X-ray; 2.35 A; B=2-105.
PDB; 3D0V; X-ray; 2.05 A; B=2-105.
PDB; 3D6G; X-ray; 2.30 A; A/B=119-328.
PDB; 3D85; X-ray; 1.90 A; B=1-108.
PDB; 3DJ9; X-ray; 1.75 A; A=119-225.
PDB; 3DNK; X-ray; 2.84 A; A/B=119-330.
PDB; 3DO3; X-ray; 2.50 A; A/B=119-330.
PDB; 3DRO; X-ray; 3.90 A; B=2-103.
PDB; 3DRQ; X-ray; 2.00 A; B=2-103.
PDB; 3DVG; X-ray; 2.60 A; B=1-107.
PDB; 3DVN; X-ray; 2.70 A; B/H=1-107.
PDB; 3EYF; X-ray; 2.30 A; B/D=1-108.
PDB; 3EYO; X-ray; 2.50 A; B/D=1-108.
PDB; 3EYQ; X-ray; 2.40 A; D=1-108.
PDB; 3FJT; X-ray; 2.50 A; A/B=119-327.
PDB; 3MCL; X-ray; 1.70 A; H=1-107.
PDB; 3O11; X-ray; 2.80 A; B/H=1-103.
PDB; 3RY6; X-ray; 3.80 A; A/B=114-327.
PDB; 3S7G; X-ray; 3.13 A; A/B/C/D=104-330.
PDB; 3SGJ; X-ray; 2.20 A; A/B=106-330.
PDB; 3SGK; X-ray; 2.40 A; A/B=106-330.
PDB; 3TV3; X-ray; 1.29 A; H=1-104.
PDB; 3TWC; X-ray; 1.65 A; H=1-104.
PDB; 3TYG; X-ray; 3.25 A; H=1-104.
PDB; 3U0W; X-ray; 2.00 A; H=1-103.
PDB; 3U7W; X-ray; 2.60 A; H=1-104.
PDB; 3U7Y; X-ray; 2.45 A; H=1-104.
PDB; 3V7M; X-ray; 2.02 A; A=119-327.
PDB; 3V8C; X-ray; 2.77 A; A/B=119-330.
PDB; 3V95; X-ray; 2.70 A; A/B=119-330.
PDB; 3WJJ; X-ray; 2.60 A; A/B=99-328.
PDB; 3WJL; X-ray; 2.86 A; A/B=99-328.
PDB; 3WKN; X-ray; 2.90 A; A/B/C/D/I/J/M/N=119-330.
PDB; 3WN5; X-ray; 2.78 A; A/B/D/E=99-328.
PDB; 4ACP; X-ray; 2.49 A; A/B=101-329.
PDB; 4B7I; X-ray; 2.36 A; A/B=120-329.
PDB; 4BM7; X-ray; 1.95 A; A/B=106-329.
PDB; 4BSV; X-ray; 1.75 A; A/B=106-330.
PDB; 4BSW; X-ray; 2.15 A; A/B=106-330.
PDB; 4BYH; X-ray; 2.30 A; A/B=106-329.
PDB; 4CDH; X-ray; 2.30 A; A/B=101-330.
PDB; 4D9Q; X-ray; 2.28 A; E/H=2-102.
PDB; 4D9R; X-ray; 2.42 A; E/H=2-103.
PDB; 4DAG; X-ray; 3.39 A; H=2-98.
PDB; 4DZ8; X-ray; 1.91 A; A/B=108-330.
PDB; 4EOW; X-ray; 1.97 A; H=1-101.
PDB; 4HIX; X-ray; 2.20 A; H=1-107.
PDB; 4J12; X-ray; 1.90 A; A=119-327.
PDB; 4KU1; X-ray; 1.90 A; A/B=120-327.
PDB; 4LLD; X-ray; 1.19 A; A=1-103.
PDB; 4LLM; X-ray; 1.75 A; A=1-103.
PDB; 4LLQ; X-ray; 1.42 A; A=1-103.
PDB; 4N0U; X-ray; 3.80 A; E=119-327.
PDB; 4NQS; X-ray; 2.64 A; A/B/G/H=118-330.
PDB; 4NQT; X-ray; 2.10 A; A=118-330.
PDB; 4NQU; X-ray; 2.50 A; A=118-330.
PDB; 4NWT; X-ray; 1.75 A; H=6-95.
PDB; 4NWU; X-ray; 1.60 A; H=6-105.
PDB; 4O4Y; X-ray; 1.85 A; A=106-119.
PDB; 4O51; X-ray; 2.20 A; M/N/O/P=106-119.
PDB; 4Q6Y; X-ray; 3.00 A; A/B/C/D=109-329.
PDB; 4Q74; X-ray; 2.19 A; A/B=108-329.
PDB; 4Q7D; X-ray; 2.35 A; A/B=109-329.
PDB; 4W4N; X-ray; 1.80 A; A/B=107-329.
PDB; 4W4O; X-ray; 1.80 A; A/B=107-330.
PDB; 4WI2; X-ray; 1.90 A; A/B=120-327.
PDB; 4WI3; X-ray; 2.70 A; A/B=120-327.
PDB; 4WI4; X-ray; 2.80 A; A/B=121-327.
PDB; 4WI5; X-ray; 2.80 A; A/B=120-327.
PDB; 4WI6; X-ray; 2.20 A; A/B=120-327.
PDB; 4WI7; X-ray; 1.90 A; A/B=120-327.
PDB; 4WI8; X-ray; 2.80 A; A/B=120-327.
PDB; 4WI9; X-ray; 2.65 A; A/B=120-327.
PDB; 4X4M; X-ray; 3.48 A; A/B/C/D=112-330.
PDB; 4X98; X-ray; 2.50 A; A=108-327, B=121-327.
PDB; 4X99; X-ray; 2.50 A; A/B=108-330.
PDB; 4XMP; X-ray; 1.78 A; H=1-103.
PDB; 4XNY; X-ray; 2.30 A; H=1-103.
PDB; 4XNZ; X-ray; 3.39 A; B/E/H=1-103.
PDB; 4XXD; X-ray; 2.41 A; B/E=1-107.
PDB; 4ZNE; X-ray; 2.42 A; E/J=104-330.
PDB; 5BW7; X-ray; 3.00 A; A/B=108-330.
PDB; 5D4Q; X-ray; 2.39 A; A/B=109-329.
PDB; 5D6D; X-ray; 3.13 A; A/B=108-329.
PDB; 5DI8; X-ray; 1.90 A; A/B=104-330.
PDB; 5DJ0; X-ray; 2.28 A; A/B=104-330.
PDB; 5DJ2; X-ray; 2.56 A; A/B=104-330.
PDB; 5DJ6; X-ray; 2.00 A; A/B=104-330.
PDB; 5DJ8; X-ray; 2.40 A; A/B=104-330.
PDB; 5DJA; X-ray; 2.90 A; A/B=104-330.
PDB; 5DJC; X-ray; 2.10 A; A/B/D/E=104-330.
PDB; 5DJD; X-ray; 2.30 A; A/B=104-330.
PDB; 5DJX; X-ray; 2.25 A; A/B/D/E=104-330.
PDB; 5DJY; X-ray; 2.15 A; A/B=104-330.
PDB; 5DJZ; X-ray; 1.90 A; A/B=104-330.
PDB; 5DK0; X-ray; 2.30 A; A/B=104-330.
PDB; 5DK2; X-ray; 2.60 A; A/B/D/E=104-330.
PDB; 5DVK; X-ray; 2.60 A; A=104-330.
PDB; 5DVL; X-ray; 1.90 A; A=104-330.
PDB; 5DVM; X-ray; 2.95 A; A=104-330.
PDB; 5DVN; X-ray; 2.50 A; A=104-330.
PDB; 5DVO; X-ray; 2.50 A; A/B=104-330.
PDB; 5HSF; X-ray; 1.52 A; A/B=221-330.
PDB; 5HY9; X-ray; 2.70 A; A/B=104-330.
PDB; 5HYE; X-ray; 1.89 A; A/C=104-330.
PDB; 5HYF; X-ray; 1.80 A; A=104-330.
PDB; 5HYI; X-ray; 2.90 A; A/B/C/D=104-330.
PDB; 5IQ7; X-ray; 3.29 A; H=1-102.
PDB; 5IQ9; X-ray; 2.40 A; A/H=1-101.
PDB; 5IW3; X-ray; 2.05 A; A=119-326.
PDB; 5IW6; X-ray; 2.34 A; A=119-327, B=122-326.
PDB; 5JIH; X-ray; 1.66 A; A/B=108-329.
PDB; 5JII; X-ray; 1.79 A; A/B=108-329.
PDB; 5JIK; X-ray; 1.82 A; A/B=108-329.
PDB; 5K33; X-ray; 3.30 A; A=108-329.
PDB; 5K8D; X-ray; 4.19 A; B=104-329.
PDB; 5KWG; X-ray; 4.30 A; A=108-330.
PDB; 5M3V; X-ray; 1.97 A; A/B=104-330.
PDB; 5U52; X-ray; 1.94 A; A/B=119-326.
PDB; 5U66; X-ray; 1.70 A; A=120-326.
PDB; 5V43; X-ray; 2.32 A; A/B=104-329.
PDB; 5V4E; X-ray; 3.22 A; A/B/C/D/E/F/G/H=104-329.
PDBsum; 1AJ7; -.
PDBsum; 1AQK; -.
PDBsum; 1AXS; -.
PDBsum; 1BEY; -.
PDBsum; 1D5B; -.
PDBsum; 1D5I; -.
PDBsum; 1D6V; -.
PDBsum; 1DFB; -.
PDBsum; 1DN2; -.
PDBsum; 1E4K; -.
PDBsum; 1FC1; -.
PDBsum; 1FC2; -.
PDBsum; 1FCC; -.
PDBsum; 1GAF; -.
PDBsum; 1H3T; -.
PDBsum; 1H3U; -.
PDBsum; 1H3V; -.
PDBsum; 1H3W; -.
PDBsum; 1H3X; -.
PDBsum; 1H3Y; -.
PDBsum; 1HKL; -.
PDBsum; 1HZH; -.
PDBsum; 1I7Z; -.
PDBsum; 1L6X; -.
PDBsum; 1N7M; -.
PDBsum; 1OP3; -.
PDBsum; 1OQO; -.
PDBsum; 1OQX; -.
PDBsum; 1PG7; -.
PDBsum; 1T83; -.
PDBsum; 1T89; -.
PDBsum; 1VGE; -.
PDBsum; 2DTS; -.
PDBsum; 2GJ7; -.
PDBsum; 2I5Y; -.
PDBsum; 2IWG; -.
PDBsum; 2J6E; -.
PDBsum; 2JB5; -.
PDBsum; 2JB6; -.
PDBsum; 2O5X; -.
PDBsum; 2O5Y; -.
PDBsum; 2O5Z; -.
PDBsum; 2OSL; -.
PDBsum; 2QAD; -.
PDBsum; 2QL1; -.
PDBsum; 2QQK; -.
PDBsum; 2QQL; -.
PDBsum; 2QQN; -.
PDBsum; 2QR0; -.
PDBsum; 2R56; -.
PDBsum; 2RCJ; -.
PDBsum; 2RCS; -.
PDBsum; 2VXQ; -.
PDBsum; 2WAH; -.
PDBsum; 3AGV; -.
PDBsum; 3AVE; -.
PDBsum; 3AY4; -.
PDBsum; 3B2U; -.
PDBsum; 3B2V; -.
PDBsum; 3BDY; -.
PDBsum; 3BE1; -.
PDBsum; 3BKY; -.
PDBsum; 3BN9; -.
PDBsum; 3BQU; -.
PDBsum; 3C08; -.
PDBsum; 3C09; -.
PDBsum; 3C2S; -.
PDBsum; 3CFJ; -.
PDBsum; 3CFK; -.
PDBsum; 3CSY; -.
PDBsum; 3D0L; -.
PDBsum; 3D0V; -.
PDBsum; 3D6G; -.
PDBsum; 3D85; -.
PDBsum; 3DJ9; -.
PDBsum; 3DNK; -.
PDBsum; 3DO3; -.
PDBsum; 3DRO; -.
PDBsum; 3DRQ; -.
PDBsum; 3DVG; -.
PDBsum; 3DVN; -.
PDBsum; 3EYF; -.
PDBsum; 3EYO; -.
PDBsum; 3EYQ; -.
PDBsum; 3FJT; -.
PDBsum; 3MCL; -.
PDBsum; 3O11; -.
PDBsum; 3RY6; -.
PDBsum; 3S7G; -.
PDBsum; 3SGJ; -.
PDBsum; 3SGK; -.
PDBsum; 3TV3; -.
PDBsum; 3TWC; -.
PDBsum; 3TYG; -.
PDBsum; 3U0W; -.
PDBsum; 3U7W; -.
PDBsum; 3U7Y; -.
PDBsum; 3V7M; -.
PDBsum; 3V8C; -.
PDBsum; 3V95; -.
PDBsum; 3WJJ; -.
PDBsum; 3WJL; -.
PDBsum; 3WKN; -.
PDBsum; 3WN5; -.
PDBsum; 4ACP; -.
PDBsum; 4B7I; -.
PDBsum; 4BM7; -.
PDBsum; 4BSV; -.
PDBsum; 4BSW; -.
PDBsum; 4BYH; -.
PDBsum; 4CDH; -.
PDBsum; 4D9Q; -.
PDBsum; 4D9R; -.
PDBsum; 4DAG; -.
PDBsum; 4DZ8; -.
PDBsum; 4EOW; -.
PDBsum; 4HIX; -.
PDBsum; 4J12; -.
PDBsum; 4KU1; -.
PDBsum; 4LLD; -.
PDBsum; 4LLM; -.
PDBsum; 4LLQ; -.
PDBsum; 4N0U; -.
PDBsum; 4NQS; -.
PDBsum; 4NQT; -.
PDBsum; 4NQU; -.
PDBsum; 4NWT; -.
PDBsum; 4NWU; -.
PDBsum; 4O4Y; -.
PDBsum; 4O51; -.
PDBsum; 4Q6Y; -.
PDBsum; 4Q74; -.
PDBsum; 4Q7D; -.
PDBsum; 4W4N; -.
PDBsum; 4W4O; -.
PDBsum; 4WI2; -.
PDBsum; 4WI3; -.
PDBsum; 4WI4; -.
PDBsum; 4WI5; -.
PDBsum; 4WI6; -.
PDBsum; 4WI7; -.
PDBsum; 4WI8; -.
PDBsum; 4WI9; -.
PDBsum; 4X4M; -.
PDBsum; 4X98; -.
PDBsum; 4X99; -.
PDBsum; 4XMP; -.
PDBsum; 4XNY; -.
PDBsum; 4XNZ; -.
PDBsum; 4XXD; -.
PDBsum; 4ZNE; -.
PDBsum; 5BW7; -.
PDBsum; 5D4Q; -.
PDBsum; 5D6D; -.
PDBsum; 5DI8; -.
PDBsum; 5DJ0; -.
PDBsum; 5DJ2; -.
PDBsum; 5DJ6; -.
PDBsum; 5DJ8; -.
PDBsum; 5DJA; -.
PDBsum; 5DJC; -.
PDBsum; 5DJD; -.
PDBsum; 5DJX; -.
PDBsum; 5DJY; -.
PDBsum; 5DJZ; -.
PDBsum; 5DK0; -.
PDBsum; 5DK2; -.
PDBsum; 5DVK; -.
PDBsum; 5DVL; -.
PDBsum; 5DVM; -.
PDBsum; 5DVN; -.
PDBsum; 5DVO; -.
PDBsum; 5HSF; -.
PDBsum; 5HY9; -.
PDBsum; 5HYE; -.
PDBsum; 5HYF; -.
PDBsum; 5HYI; -.
PDBsum; 5IQ7; -.
PDBsum; 5IQ9; -.
PDBsum; 5IW3; -.
PDBsum; 5IW6; -.
PDBsum; 5JIH; -.
PDBsum; 5JII; -.
PDBsum; 5JIK; -.
PDBsum; 5K33; -.
PDBsum; 5K8D; -.
PDBsum; 5KWG; -.
PDBsum; 5M3V; -.
PDBsum; 5U52; -.
PDBsum; 5U66; -.
PDBsum; 5V43; -.
PDBsum; 5V4E; -.
ProteinModelPortal; P01857; -.
SMR; P01857; -.
DIP; DIP-29187N; -.
IntAct; P01857; 90.
MINT; MINT-120799; -.
DrugBank; DB07883; (2-AMINO-3-PHENYL-BICYCLO[2.2.1]HEPT-2-YL)-PHENYL-METHANONE.
DrugBank; DB08294; 2-(4-HYDROXY-3-NITROPHENYL)ACETIC ACID.
DrugBank; DB07371; 3-(10-METHYL-ANTHRACEN-9-YL)-PROPIONIC ACID.
DrugBank; DB08562; 4-(4-STYRYL-PHENYLCARBAMOYL)-BUTYRIC ACID.
DrugBank; DB08409; 4-NITRO-BENZYLPHOSPHONOBUTANOYL-GLYCINE.
DrugBank; DB08296; 5-(PARA-NITROPHENYL PHOSPHONATE)-PENTANOIC ACID.
DrugBank; DB08412; 6-{4-[HYDROXY-(4-NITRO-PHENOXY)-PHOSPHORYL]-BUTYRYLAMINO}-HEXANOIC ACID.
DrugBank; DB08332; [2'-CARBOXYLETHYL]-10-METHYL-ANTHRACENE ENDOPEROXIDE.
DrugBank; DB04473; Alpha-L-Fucose.
DrugBank; DB04639; Biphenylalanine.
DrugBank; DB07764; FLUORESCIN.
DrugBank; DB01631; Methyl Nonanoate (Ester).
DrugBank; DB07816; N-(P-CYANOPHENYL)-N'-DIPHENYLMETHYL-GUANIDINE-ACETIC ACID.
DrugBank; DB03740; N-acetyl-alpha-D-glucosamine.
DrugBank; DB07881; N-{[2-({[1-(4-CARBOXYBUTANOYL)AMINO]-2-PHENYLETHYL}-HYDROXYPHOSPHINYL)OXY]ACETYL}-2-PHENYLETHYLAMINE.
DrugBank; DB08410; PARA-NITROBENZYL GLUTARYL GLYCINIC ACID.
DrugBank; DB08377; PARA-NITROPHENYL PHOSPHONOBUTANOYL D-ALANINE.
DrugBank; DB08411; PARA-NITROPHENYL PHOSPHONOBUTANOYL L-ALANINE.
DrugBank; DB08394; PARA-NITROPHENYLPHOSPHONOBUTANOYL-GLYCINE.
DrugBank; DB07672; TRANS-2-(DIMETHYLPHENYLSILYL)-PIPERIDINE-N-OXIDE.
IMGT_GENE-DB; IGHG1; -.
iPTMnet; P01857; -.
PhosphoSitePlus; P01857; -.
SwissPalm; P01857; -.
UniCarbKB; P01857; -.
DMDM; 121039; -.
DOSAC-COBS-2DPAGE; P01857; -.
REPRODUCTION-2DPAGE; P01857; -.
UCD-2DPAGE; P01857; -.
EPD; P01857; -.
MaxQB; P01857; -.
PeptideAtlas; P01857; -.
PRIDE; P01857; -.
Ensembl; ENST00000390549; ENSP00000374991; ENSG00000211896.
Ensembl; ENST00000631466; ENSP00000488387; ENSG00000277633.
UCSC; uc059gdc.1; human.
DisGeNET; 3500; -.
EuPathDB; HostDB:ENSG00000211896.7; -.
GeneCards; IGHG1; -.
HGNC; HGNC:5525; IGHG1.
MalaCards; IGHG1; -.
MIM; 147100; gene.
MIM; 254500; phenotype.
neXtProt; NX_P01857; -.
OpenTargets; ENSG00000211896; -.
Orphanet; 67038; B-cell chronic lymphocytic leukemia.
GeneTree; ENSGT00530000063726; -.
HOVERGEN; HBG005814; -.
InParanoid; P01857; -.
PhylomeDB; P01857; -.
Reactome; R-HSA-166663; Initial triggering of complement.
Reactome; R-HSA-173623; Classical antibody-mediated complement activation.
Reactome; R-HSA-2029481; FCGR activation.
Reactome; R-HSA-2029482; Regulation of actin dynamics for phagocytic cup formation.
Reactome; R-HSA-2029485; Role of phospholipids in phagocytosis.
Reactome; R-HSA-6785807; Interleukin-4 and 13 signaling.
Reactome; R-HSA-977606; Regulation of Complement cascade.
EvolutionaryTrace; P01857; -.
PRO; PR:P01857; -.
Proteomes; UP000005640; Chromosome 14.
Bgee; ENSG00000211896; -.
CleanEx; HS_IGHG1; -.
ExpressionAtlas; P01857; baseline and differential.
Genevisible; P01857; HS.
GO; GO:0072562; C:blood microparticle; IDA:UniProtKB.
GO; GO:0009897; C:external side of plasma membrane; IBA:GO_Central.
GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
GO; GO:0005576; C:extracellular region; TAS:Reactome.
GO; GO:0005615; C:extracellular space; IDA:UniProtKB.
GO; GO:0042571; C:immunoglobulin complex, circulating; IBA:GO_Central.
GO; GO:0003823; F:antigen binding; TAS:UniProtKB.
GO; GO:0034987; F:immunoglobulin receptor binding; IBA:GO_Central.
GO; GO:0004252; F:serine-type endopeptidase activity; TAS:Reactome.
GO; GO:0050853; P:B cell receptor signaling pathway; IBA:GO_Central.
GO; GO:0006956; P:complement activation; TAS:Reactome.
GO; GO:0006958; P:complement activation, classical pathway; IBA:GO_Central.
GO; GO:0042742; P:defense response to bacterium; IBA:GO_Central.
GO; GO:0038096; P:Fc-gamma receptor signaling pathway involved in phagocytosis; TAS:Reactome.
GO; GO:0045087; P:innate immune response; IBA:GO_Central.
GO; GO:0006911; P:phagocytosis, engulfment; IBA:GO_Central.
GO; GO:0006910; P:phagocytosis, recognition; IBA:GO_Central.
GO; GO:0050871; P:positive regulation of B cell activation; IBA:GO_Central.
GO; GO:0030449; P:regulation of complement activation; TAS:Reactome.
Gene3D; 2.60.40.10; -; 3.
InterPro; IPR007110; Ig-like_dom.
InterPro; IPR013783; Ig-like_fold.
InterPro; IPR003006; Ig/MHC_CS.
InterPro; IPR003597; Ig_C1-set.
Pfam; PF07654; C1-set; 3.
SMART; SM00407; IGc1; 3.
SUPFAM; SSF48726; SSF48726; 3.
PROSITE; PS50835; IG_LIKE; 3.
PROSITE; PS00290; IG_MHC; 2.
1: Evidence at protein level;
3D-structure; Adaptive immunity; Cell membrane;
Chromosomal rearrangement; Complete proteome;
Direct protein sequencing; Disulfide bond; Glycoprotein; Immunity;
Immunoglobulin C region; Immunoglobulin domain; Membrane;
Polymorphism; Reference proteome; Secreted.
CHAIN <1 330 Immunoglobulin heavy constant gamma 1.
/FTId=PRO_0000153578.
DOMAIN 6 99 Ig-like 1. {ECO:0000255|PROSITE-
ProRule:PRU00114}.
DOMAIN 121 220 Ig-like 2. {ECO:0000255|PROSITE-
ProRule:PRU00114}.
DOMAIN 229 325 Ig-like 3. {ECO:0000255|PROSITE-
ProRule:PRU00114}.
REGION 1 98 CH1.
REGION 99 110 Hinge.
REGION 111 223 CH2.
REGION 224 330 CH3.
CARBOHYD 180 180 N-linked (GlcNAc...) (complex)
asparagine. {ECO:0000269|PubMed:19139490,
ECO:0000269|PubMed:19159218,
ECO:0000269|PubMed:19358553}.
DISULFID 27 83 {ECO:0000255|PROSITE-ProRule:PRU00114}.
DISULFID 103 103 Interchain (with light chain).
DISULFID 109 109 Interchain (with heavy chain).
DISULFID 112 112 Interchain (with heavy chain).
DISULFID 144 204 {ECO:0000255|PROSITE-ProRule:PRU00114}.
DISULFID 250 308 {ECO:0000255|PROSITE-ProRule:PRU00114}.
VARIANT 97 97 K -> R (in IMGT allele IGHG1*03).
/FTId=VAR_003886.
VARIANT 239 239 D -> E (in IMGT allele IGHG1*03).
/FTId=VAR_003887.
VARIANT 241 241 L -> M (in IMGT allele IGHG1*03).
/FTId=VAR_003888.
NON_TER 1 1
STRAND 7 14 {ECO:0000244|PDB:4LLD}.
STRAND 16 18 {ECO:0000244|PDB:4LLD}.
STRAND 22 35 {ECO:0000244|PDB:4LLD}.
STRAND 38 41 {ECO:0000244|PDB:4LLD}.
HELIX 42 44 {ECO:0000244|PDB:4LLD}.
STRAND 50 52 {ECO:0000244|PDB:4LLD}.
STRAND 63 72 {ECO:0000244|PDB:4LLD}.
HELIX 73 75 {ECO:0000244|PDB:4LLD}.
TURN 76 78 {ECO:0000244|PDB:4LLD}.
STRAND 82 87 {ECO:0000244|PDB:4LLD}.
HELIX 88 90 {ECO:0000244|PDB:4LLD}.
STRAND 92 97 {ECO:0000244|PDB:4LLD}.
HELIX 115 117 {ECO:0000244|PDB:3SGJ}.
STRAND 118 120 {ECO:0000244|PDB:1HZH}.
STRAND 122 126 {ECO:0000244|PDB:1L6X}.
HELIX 130 134 {ECO:0000244|PDB:1L6X}.
STRAND 136 138 {ECO:0000244|PDB:5IW3}.
STRAND 141 149 {ECO:0000244|PDB:1L6X}.
STRAND 151 153 {ECO:0000244|PDB:1L6X}.
STRAND 157 162 {ECO:0000244|PDB:1L6X}.
STRAND 165 167 {ECO:0000244|PDB:1L6X}.
STRAND 170 172 {ECO:0000244|PDB:4WI6}.
STRAND 173 175 {ECO:0000244|PDB:1H3W}.
STRAND 176 178 {ECO:0000244|PDB:5DI8}.
STRAND 179 181 {ECO:0000244|PDB:4WI7}.
STRAND 183 190 {ECO:0000244|PDB:1L6X}.
HELIX 193 197 {ECO:0000244|PDB:1L6X}.
STRAND 202 207 {ECO:0000244|PDB:1L6X}.
STRAND 211 213 {ECO:0000244|PDB:1L6X}.
STRAND 215 219 {ECO:0000244|PDB:1L6X}.
STRAND 230 234 {ECO:0000244|PDB:5HSF}.
HELIX 240 242 {ECO:0000244|PDB:5HSF}.
STRAND 243 258 {ECO:0000244|PDB:5HSF}.
STRAND 261 266 {ECO:0000244|PDB:5HSF}.
STRAND 269 271 {ECO:0000244|PDB:1L6X}.
STRAND 272 276 {ECO:0000244|PDB:5HSF}.
STRAND 283 285 {ECO:0000244|PDB:3V8C}.
STRAND 287 296 {ECO:0000244|PDB:5HSF}.
HELIX 297 301 {ECO:0000244|PDB:5HSF}.
STRAND 306 311 {ECO:0000244|PDB:5HSF}.
STRAND 313 315 {ECO:0000244|PDB:1FCC}.
STRAND 318 324 {ECO:0000244|PDB:5HSF}.
SEQUENCE 330 AA; 36106 MW; 3770EE106C2FA33D CRC64;
ASTKGPSVFP LAPSSKSTSG GTAALGCLVK DYFPEPVTVS WNSGALTSGV HTFPAVLQSS
GLYSLSSVVT VPSSSLGTQT YICNVNHKPS NTKVDKKVEP KSCDKTHTCP PCPAPELLGG
PSVFLFPPKP KDTLMISRTP EVTCVVVDVS HEDPEVKFNW YVDGVEVHNA KTKPREEQYN
STYRVVSVLT VLHQDWLNGK EYKCKVSNKA LPAPIEKTIS KAKGQPREPQ VYTLPPSRDE
LTKNQVSLTC LVKGFYPSDI AVEWESNGQP ENNYKTTPPV LDSDGSFFLY SKLTVDKSRW
QQGNVFSCSV MHEALHNHYT QKSLSLSPGK


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EIAAB44568 Homo sapiens,Human,T-cell receptor gamma chain V region PT-gamma-1_2,TCRB,TRGV3
E0996h ELISA Gamma-1-globin,Hb F Agamma,HBG1,Hemoglobin gamma-1 chain,Hemoglobin gamma-A chain,Hemoglobin subunit gamma-1,Homo sapiens,Human,PRO2979 96T
E0996h ELISA kit Gamma-1-globin,Hb F Agamma,HBG1,Hemoglobin gamma-1 chain,Hemoglobin gamma-A chain,Hemoglobin subunit gamma-1,Homo sapiens,Human,PRO2979 96T
U0996h CLIA Gamma-1-globin,Hb F Agamma,HBG1,Hemoglobin gamma-1 chain,Hemoglobin gamma-A chain,Hemoglobin subunit gamma-1,Homo sapiens,Human,PRO2979 96T
E1579m ELISA kit Fc gamma receptor IIB,Fc-gamma RII,Fc-gamma-RIIB,Fcgr2,Fcgr2b,FcRII,IgG Fc receptor II beta,Low affinity immunoglobulin gamma Fc region receptor II,Ly-17,Ly-17,Lymphocyte antigen 17,Mouse,M 96T
E1579m ELISA Fc gamma receptor IIB,Fc-gamma RII,Fc-gamma-RIIB,Fcgr2,Fcgr2b,FcRII,IgG Fc receptor II beta,Low affinity immunoglobulin gamma Fc region receptor II,Ly-17,Ly-17,Lymphocyte antigen 17,Mouse,Mus mu 96T
U1579m CLIA Fc gamma receptor IIB,Fc-gamma RII,Fc-gamma-RIIB,Fcgr2,Fcgr2b,FcRII,IgG Fc receptor II beta,Low affinity immunoglobulin gamma Fc region receptor II,Ly-17,Ly-17,Lymphocyte antigen 17,Mouse,Mus mus 96T


 

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