protein

Recombinant Human Ig gamma-1 chain C region

MBS717608

0.05 mg (E-Coli)

190 USD

Recombinant Protein

Recombinant Human Ig gamma-1 chain C region

Ig gamma-1 chain C region

Ig gamma-1 chain C region; Ig gamma-1 chain C region; immunoglobulin heavy constant gamma 1 (G1m marker)

IGHG1

IGHG1; IGHG1

IGHG1_HUMAN

E Coli or Yeast or Baculovirus or Mammalian Cell

1-479

330

MKFGLSWIFLPAILKGVQCEVQLVESGGGLVKAGGSLRL
SCAASGFSFSDAWMSWARQPPGKGLEWLGRIKRKSDGGT
TEYAAHVKGRFIISRDDSKYMVYMQMNSLKTEDTAVYYC
NTDARSVGSLEWPNYYHGMNVWGEGTTVTVSSASTKGPS
VFPLAPSSKSTSGGTAALGCLVKDYFPEPVTVSWNSGAL
TSGVHTFPAVLQSSGLYSLSSVVTVPSSSLGTQTYICNV
NHKPSNTKVDKKVEPKSCDKT

Greater than 90% as determined by SDS-PAGE.

Liquid containing glycerol; lyophilization may be available upon request.

Store at -20 degree C, for extended storage, conserve at -20 degree C or -80 degree C.

Immunology

The nucleotide sequence of a human immunoglobulin C gamma1 gene.Ellison J.W., Berson B.J., Hood L.E.Nucleic Acids Res. 10:4071-4079(1982) The covalent structure of a human gamma G-immunoglobulin. VII. Amino acid sequence of heavy-chain cyanogen bromide fragments H1-H4.Cunningham B.A., Rutishauser U., Gall W.E., Gottlieb P.D., Waxdal M.J., Edelman G.M.Biochemistry 9:3161-3170(1970) The covalent structure of a human gamma G-immunoglobulin. 8. Amino acid sequence of heavy-chain cyanogen bromide fragments H5-H7.Rutishauser U., Cunningham B.A., Bennett C., Konigsberg W.H., Edelman G.M.Biochemistry 9:3171-3181(1970) 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.Ponstingl H., Hilschmann N.Hoppe-Seyler's Z. Physiol. Chem. 357:1571-1604(1976) Three-dimensional structure determination of antibodies. Primary structure of crystallized monoclonal immunoglobulin IgG1 KOL, I.Schmidt W.E., Jung H.-D., Palm W., Hilschmann N.Hoppe-Seyler's Z. Physiol. Chem. 364:713-747(1983) The covalent structure of a human gamma G-immunoglobulin. X. Intrachain disulfide bonds.Gall W.E., Edelman G.M.Biochemistry 9:3188-3196(1970) 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.Dreker L., Schwarz J., Reichel W., Hilschmann N.Hoppe-Seyler's Z. Physiol. Chem. 357:1515-1540(1976) Site-specific glycoprofiling of N-linked glycopeptides using MALDI-TOF MS strong correlation between signal strength and glycoform quantities.Thaysen-Andersen M., Mysling S., Hojrup P.Anal. Chem. 81:3933-3943(2009) Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry.Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.J. Proteome Res. 8:651-661(2009) A strategy for precise and large scale identification of core fucosylated glycoproteins.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.Mol. Cell. Proteomics 8:913-923(2009) Initial characterization of the human central proteome.Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.BMC Syst. Biol. 5:17-17(2011) An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome.Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.J. Proteomics 96:253-262(2014) 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.Deisenhofer J.Biochemistry 20:2361-2370(1981) Promiscuous translocations into immunoglobulin heavy chain switch regions in multiple myeloma.Bergsagel P.L., Chesi M., Nardini E., Brents L.A., Kirby S.L., Kuehl W.M.Proc. Natl. Acad. Sci. U.S.A. 93:13931-13936(1996) Translocations of 14q32 and deletions of 13q14 are common chromosomal abnormalities in systemic amyloidosis.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.Br. J. Haematol. 117:427-435(2002)

121039

P01857.1

P01857

68.48kD

Classical Antibody-mediated Complement Activation Pathway (1269246); Complement Cascade Pathway (1269241); Creation Of C4 And C2 Activators Pathway (1269243); FCGR Activation Pathway (1269280); Fcgamma Receptor (FCGR) Dependent Phagocytosis Pathway (1269279); IL4-mediated Signaling Events Pathway (137933); Immune System Pathway (1269170); Initial Triggering Of Complement Pathway (1269242); Innate Immune System Pathway (1269203); Regulation Of Actin Dynamics For Phagocytic Cup Formation Pathway (1269281)

IGHG1: Defects in IGHG1 are a cause of multiple myeloma (MM). MM is 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. 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. Protein type: Immunoglobulin superfamily. Chromosomal Location of Human Ortholog: 14q32.33. Cellular Component: external side of plasma membrane; extracellular region; extracellular space. Molecular Function: antigen binding; protein binding. Biological Process: B cell receptor signaling pathway; complement activation; complement activation, classical pathway; defense response to bacterium; innate immune response; phagocytosis, engulfment; phagocytosis, recognition; positive regulation of B cell activation. Disease: Myeloma, Multiple

0.05 mg (E-Coli)

190 USD

0.2 mg (E-Coli)

460

0.5 mg (E-Coli)

750

0.05 mg (Baculovirus)

1090

1 mg (E-Coli)

1180