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Envelope Glycoprotein Gp120 (gp120) Recombinant Protein

For Research Use Only. Not for use in diagnostic procedures. Catalog #: MBS1136560

Envelope glycoprotein gp160: Oligomerizes in the host endoplasmic reticulum into predominantly trimers. In a second time, gp160 transits in the host Golgi, where glycosylation is completed. The precursor is then proteolytically cleaved in the trans-Golgi and… More details

$455 / 0.02 mg (E-Coli) +1 FREE 8GB USB
Product Documentation
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Sample Manual Insert View PDF
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Material Safety Data Sheet View PDF
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Technical Datasheet View PDF
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Product Overview

Online Datasheet in PDF
Product Name
Envelope glycoprotein gp120, Recombinant Protein
Full Product Name
Recombinant Human immunodeficiency virus type 1 group M subtype B (isolate HXB2) (HIV-1) Envelope glycoprotein gp120
Product Gene Name
Product Synonym Names
Env polyprotein
Sequence
KLWVTVYYGV PVWKEATTTL FCASDAKAYD TEVHNVWATH ACVPTDPNPQ EVVLVNVTEN FNMWKNDMVE QMHEDIISLW DQSLKPCVKL TPLCVSLKCT DLKNDTNTNS SSGRMIMEKG EIKNCSFNIS TSIRGKVQKE YAFFYKLDII PIDNDTTSYK LTSCNTSVIT QACPKVSFEP IPIHYCAPAG FAILKCNNKT FNGTGPCTNV STVQCTHGIR PVVSTQLLLN GSLAEEEVVI RSVNFTDNAK TIIVQLNTSV EINCTRPNNN TRKRIRIQRG PGRAFVTIGK IGNMRQAHCN ISRAKWNNTL KQIASKLREQ FGNNKTIIFK QSSGGDPEIV THSFNCGGEF FYCNSTQLFN STWFNSTWST EGSNNTEGSD TITLPCRIKQ IINMWQKVGK AMYAPPISGQ IRCSSNITGL LLTRDGGNSN NESEIFRPGG GDMRDNWRSE LYKYKVVKIE PLGVAPTKAK RRVVQREKR
Host
E Coli or Yeast or Baculovirus or Mammalian Cell
Form/Format
Lyophilized or liquid (Format to be determined during the manufacturing process)
Purity/Purification
Greater or equal to 85% purity as determined by SDS-PAGE. (lot specific)
Preparation and Storage
Store at -20 degree C, for extended storage, conserve at -20 degree C or -80 degree C.
Molecular Weight
69.7 kDa
Sequence Positions
33-511aa. Partial,provide Surface protein gp120 chain
Tag Information
This protein contains an N-terminal tag and may also contain a C-terminal tag. Tag types are determined by various factors including tag-protein stability, please inquire for tag information.
Sterility
Sterile filter available upon request.
Endotoxin
Low endotoxin available upon request.
3D Structure
ModBase 3D Structure for P04578
ISO Certification
Manufactured in an ISO 9001:2015 Certified Laboratory.

Product References and Citations for gp120 recombinant protein

Complete nucleotide sequences of functional clones of the AIDS virus.Ratner L., Fisher A., Jagodzinski L.L., Mitsuya H., Liou R.-S., Gallo R.C., Wong-Staal F.AIDS Res. Hum. Retroviruses 3:57-69(1987) Ratner L., Fisher A., Jagodzinski L.L., Mitsuya H., Liou R.-S., Gallo R.C., Wong-Staal F.Endoproteolytic cleavage of gp160 is required for the activation of human immunodeficiency virus.McCune J.M., Rabin L.B., Feinberg M.B., Lieberman M., Kosek J.C., Reyes G.R., Weissman I.L.Cell 53:55-67(1988) Changes in the transmembrane region of the human immunodeficiency virus type 1 gp41 envelope glycoprotein affect membrane fusion.Helseth E., Olshevsky U., Gabuzda D., Ardman B., Haseltine W., Sodroski J.J. Virol. 64:6314-6318(1990) Inhibition of furin-mediated cleavage activation of HIV-1 glycoprotein gp160.Hallenberger S., Bosch V., Angliker H., Shaw E., Klenk H.D., Garten W.Nature 360:358-361(1992) The immunosuppressive peptide of HIV-1 functional domains and immune response in AIDS patients.Denner J., Norley S., Kurth R.AIDS 8:1063-1072(1994) The human and simian immunodeficiency virus envelope glycoprotein transmembrane subunits are palmitoylated.Yang C., Spies C.P., Compans R.W.Proc. Natl. Acad. Sci. U.S.A. 92:9871-9875(1995) Human immunodeficiency virus type 1 infection of SK-N-MC cells domains of gp120 involved in entry into a CD4-negative, galactosyl ceramide/3' sulfo-galactosyl ceramide-positive cell line.Harouse J.M., Collman R.G., Gonzalez-Scarano F.J. Virol. 69:7383-7390(1995) Polarized human immunodeficiency virus budding in lymphocytes involves a tyrosine-based signal and favors cell-to-cell viral transmission.Deschambeault J., Lalonde J.P., Cervantes-Acosta G., Lodge R., Cohen E.A., Lemay G.J. Virol. 73:5010-5017(1999) A dendritic cell-specific intercellular adhesion molecule 3-grabbing nonintegrin (DC-SIGN) -related protein is highly expressed on human liver sinusoidal endothelial cells and promotes HIV-1 infection.Bashirova A.A., Geijtenbeek T.B.H., van Duijnhoven G.C.F., van Vliet S.J., Eilering J.B.G., Martin M.P., Wu L., Martin T.D., Viebig N., Knolle P.A., Kewalramani V.N., van Kooyk Y., Carrington M.J. Exp. Med. 193:671-678(2001) Pathogens target DC-SIGN to influence their fate DC-SIGN functions as a pathogen receptor with broad specificity.Geijtenbeek T.B., van Kooyk Y.APMIS 111:698-714(2003) Protein-disulfide isomerase-mediated reduction of two disulfide bonds of HIV envelope glycoprotein 120 occurs post-CXCR4 binding and is required for fusion.Barbouche R., Miquelis R., Jones I.M., Fenouillet E.J. Biol. Chem. 278:3131-3136(2003) Differential N-linked glycosylation of human immunodeficiency virus and Ebola virus envelope glycoproteins modulates interactions with DC-SIGN and DC-SIGNR.Lin G., Simmons G., Poehlmann S., Baribaud F., Ni H., Leslie G.J., Haggarty B.S., Bates P., Weissman D., Hoxie J.A., Doms R.W.J. Virol. 77:1337-1346(2003) Stoichiometry of envelope glycoprotein trimers in the entry of human immunodeficiency virus type 1.Yang X., Kurteva S., Ren X., Lee S., Sodroski J.J. Virol. 79:12132-12147(2005) The HIV Env-mediated fusion reaction.Gallo S.A., Finnegan C.M., Viard M., Raviv Y., Dimitrov A., Rawat S.S., Puri A., Durell S., Blumenthal R.Biochim. Biophys. Acta 1614:36-50(2003) Mechanisms of apoptosis induction by the HIV-1 envelope.Perfettini J.-L., Castedo M., Roumier T., Andreau K., Nardacci R., Piacentini M., Kroemer G.Cell Death Differ. 12:916-923(2005) V3 HIV's switch-hitter.Hartley O., Klasse P.J., Sattentau Q.J., Moore J.P.AIDS Res. Hum. Retroviruses 21:171-189(2005) Emerging drug targets for antiretroviral therapy.Reeves J.D., Piefer A.J.Drugs 65:1747-1766(2005) HIV and the chemokine system 10 years later.Lusso P.EMBO J. 25:447-456(2006) A conserved dileucine motif mediates clathrin and AP-2-dependent endocytosis of the HIV-1 envelope protein.Byland R., Vance P.J., Hoxie J.A., Marsh M.Mol. Biol. Cell 18:414-425(2007) The membrane-proximal external region of the human immunodeficiency virus type 1 envelope dominant site of antibody neutralization and target for vaccine design.Montero M., van Houten N.E., Wang X., Scott J.K.Microbiol. Mol. Biol. Rev. 72:54-84(2008) The HIV-1 envelope glycoprotein gp120 features four heparan sulfate binding domains, including the co-receptor binding site.Crublet E., Andrieu J.P., Vives R.R., Lortat-Jacob H.J. Biol. Chem. 283:15193-15200(2008) HIV enters cells via endocytosis and dynamin-dependent fusion with endosomes.Miyauchi K., Kim Y., Latinovic O., Morozov V., Melikyan G.B.Cell 137:433-444(2009) Modulation of cytokine release and gene expression by the immunosuppressive domain of gp41 of HIV-1.Denner J., Eschricht M., Lauck M., Semaan M., Schlaermann P., Ryu H., Akyuez L.PLoS ONE 8:E55199-E55199(2013) Core structure of gp41 from the HIV envelope glycoprotein.Chan D.C., Fass D., Berger J.M., Kim P.S.Cell 89:263-273(1997) Structure of an HIV gp120 envelope glycoprotein in complex with the CD4 receptor and a neutralizing human antibody.Kwong P.D., Wyatt R., Robinson J., Sweet R.W., Sodroski J., Hendrickson W.A.Nature 393:648-659(1998) Helical interactions in the HIV-1 gp41 core reveal structural basis for the inhibitory activity of gp41 peptides.Shu W., Liu J., Ji H., Radigen L., Jiang S., Lu M.Biochemistry 39:1634-1642(2000) Interactions between HIV-1 gp41 core and detergents and their implications for membrane fusion.Shu W., Ji H., Lu M.J. Biol. Chem. 275:1839-1845(2000) Structures of HIV-1 gp120 envelope glycoproteins from laboratory-adapted and primary isolates.Kwong P.D., Wyatt R., Majeed S., Robinson J., Sweet R.W., Sodroski J., Hendrickson W.A.Structure 8:1329-1339(2000) Interhelical interactions in the gp41 core implications for activation of HIV-1 membrane fusion.Wang S., York J., Shu W., Stoller M.O., Nunberg J.H., Lu M.Biochemistry 41:7283-7292(2002) Short constrained peptides that inhibit HIV-1 entry.Sia S.K., Carr P.A., Cochran A.G., Malashkevich V.N., Kim P.S.Proc. Natl. Acad. Sci. U.S.A. 99:14664-14669(2002) Structural analysis of the epitope of the anti-HIV antibody 2F5 sheds light into its mechanism of neutralization and HIV fusion.Barbato G., Bianchi E., Ingallinella P., Hurni W.H., Miller M.D., Ciliberto G., Cortese R., Bazzo R., Shiver J.W., Pessi A.J. Mol. Biol. 330:1101-1115(2003) Structural basis of tyrosine sulfation and VH-gene usage in antibodies that recognize the HIV type 1 coreceptor-binding site on gp120.Huang C.C., Venturi M., Majeed S., Moore M.J., Phogat S., Zhang M.Y., Dimitrov D.S., Hendrickson W.A., Robinson J., Sodroski J., Wyatt R., Choe H., Farzan M., Kwong P.D.Proc. Natl. Acad. Sci. U.S.A. 101:2706-2711(2004) Structural definition of a conserved neutralization epitope on HIV-1 gp120.Zhou T., Xu L., Dey B., Hessell A.J., Van Ryk D., Xiang S.H., Yang X., Zhang M.Y., Zwick M.B., Arthos J., Burton D.R., Dimitrov D.S., Sodroski J., Wyatt R., Nabel G.J., Kwong P.D.Nature 445:732-737(2007) HIV-1 broadly neutralizing antibody extracts its epitope from a kinked gp41 ectodomain region on the viral membrane.Sun Z.Y., Oh K.J., Kim M., Yu J., Brusic V., Song L., Qiao Z., Wang J.H., Wagner G., Reinherz E.L.Immunity 28:52-63(2008) Structural details of HIV-1 recognition by the broadly neutralizing monoclonal antibody 2F5 epitope conformation, antigen-recognition loop mobility, and anion-binding site.Julien J.P., Bryson S., Nieva J.L., Pai E.F.J. Mol. Biol. 384:377-392(2008) Molecular architecture of native HIV-1 gp120 trimers.Liu J., Bartesaghi A., Borgnia M.J., Sapiro G., Subramaniam S.Nature 455:109-113(2008) Structural basis of immune evasion at the site of CD4 attachment on HIV-1 gp120.Chen L., Kwon Y.D., Zhou T., Wu X., O'Dell S., Cavacini L., Hessell A.J., Pancera M., Tang M., Xu L., Yang Z.Y., Zhang M.Y., Arthos J., Burton D.R., Dimitrov D.S., Nabel G.J., Posner M.R., Sodroski J., Wyatt R., Mascola J.R., Kwong P.D.Science 326:1123-1127(2009) Crystal structure and size-dependent neutralization properties of HK20, a human monoclonal antibody binding to the highly conserved heptad repeat 1 of gp41.Sabin C., Corti D., Buzon V., Seaman M.S., Lutje Hulsik D., Hinz A., Vanzetta F., Agatic G., Silacci C., Mainetti L., Scarlatti G., Sallusto F., Weiss R., Lanzavecchia A., Weissenhorn W.PLoS Pathog. 6:E1001195-E1001195(2010) A potent and broad neutralizing antibody recognizes and penetrates the HIV glycan shield.Pejchal R., Doores K.J., Walker L.M., Khayat R., Huang P.S., Wang S.K., Stanfield R.L., Julien J.P., Ramos A., Crispin M., Depetris R., Katpally U., Marozsan A., Cupo A., Maloveste S., Liu Y., McBride R., Ito Y., Sanders R.W., Ogohara C., Paulson J.C., Feizi T., Scanlan C.N., Wong C.H., Moore J.P., Olson W.C., Ward A.B., Poignard P., Schief W.R., Burton D.R., Wilson I.A.Science 334:1097-1103(2011) Broad antiviral activity and crystal structure of HIV-1 fusion inhibitor sifuvirtide.Yao X., Chong H., Zhang C., Waltersperger S., Wang M., Cui S., He Y.J. Biol. Chem. 287:6788-6796(2012) Rational HIV immunogen design to target specific germline B cell receptors.Jardine J., Julien J.P., Menis S., Ota T., Kalyuzhniy O., McGuire A., Sok D., Huang P.S., MacPherson S., Jones M., Nieusma T., Mathison J., Baker D., Ward A.B., Burton D.R., Stamatatos L., Nemazee D., Wilson I.A., Schief W.R.Science 340:711-716(2013) Disruption of helix-capping residues 671 and 674 reveals a role in HIV-1 entry for a specialized hinge segment of the membrane proximal external region of gp41.Sun Z.Y., Cheng Y., Kim M., Song L., Choi J., Kudahl U.J., Brusic V., Chowdhury B., Yu L., Seaman M.S., Bellot G., Shih W.M., Wagner G., Reinherz E.L.J. Mol. Biol. 426:1095-1108(2014) +Additional computationally mapped references.<p>Provides general information on the entry.

Other Notes

Small volumes of gp120 recombinant protein vial(s) may occasionally become entrapped in the seal of the product vial during shipment and storage. If necessary, briefly centrifuge the vial on a tabletop centrifuge to dislodge any liquid in the container`s cap. Certain products may require to ship with dry ice and additional dry ice fee may apply.

Searchable Terms for gp120 purchase

MBS1136560 is a recombinant protein targeting gp120. Also known as Recombinant Human immunodeficiency virus type 1 group M subtype B (isolate HXB2) (HIV-1) Envelope glycoprotein gp120. Host: E Coli or Yeast or Baculovirus or Mammalian Cell.

Additional Details

NCBI/Uniprot data below describe general gene information for gp120. It may not necessarily be applicable to this product.

NCBI GI #
NCBI GeneID
NCBI Accession #
UniProt Primary Accession #
UniProt Secondary Accession #
UniProt Related Accession #
GenBank Nucleotide #
NCBI Official Full Name
Envelope surface glycoprotein gp160
NCBI Official Symbol
env
UniProt Protein Name
Envelope glycoprotein gp160
UniProt Synonym Protein Names
Env polyprotein
UniProt Gene Name
env
UniProt Synonym Gene Names
SU; gp120; TM; gp41
UniProt Entry Name
ENV_HV1H2
NCBI Protein Information
gp160; envelope glycoprotein

UniProt Comments for gp120

gp160: The gp120-gp41 heterodimer allows rapid transcytosis of the virus through CD4 negative cells such as simple epithelial monolayers of the intestinal, rectal and endocervical epithelial barriers. Both gp120 and gp41 specifically recognize glycosphingolipids galactosyl-ceramide (GalCer) or 3' sulfo-galactosyl-ceramide (GalS) present in the lipid rafts structures of epithelial cells. Binding to these alternative receptors allows the rapid transcytosis of the virus through the epithelial cells. This transcytotic vesicle-mediated transport of virions from the apical side to the basolateral side of the epithelial cells does not involve infection of the cells themselves

Protein type: Membrane protein, integral; Apoptosis
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Precautions

All of MyBioSource's Products are for scientific laboratory research purposes and are not for diagnostic, therapeutics, prophylactic or in vivo use. Through your purchase, you expressly represent and warrant to MyBioSource that you will properly test and use any Products purchased from MyBioSource in accordance with industry standards. MyBioSource and its authorized distributors reserve the right to refuse to process any order where we reasonably believe that the intended use will fall outside of our acceptable guidelines.

Disclaimer

While every efforts were made to ensure the accuracy of the information provided in this datasheet, MyBioSource will not be liable for any omissions or errors contained herein. MyBioSource reserves the right to make changes to this datasheet at any time without prior notice.

It is the responsibility of the customer to report product performance issues to MyBioSource within 30 days of receipt of the product. Please visit our Terms & Conditions page for more information.

Product Note

Select online data sheet information is drawn from bioinformatics databases, occasionally resulting in ambiguous or non-relevant product information. It is the responsibility of the customer to review, verify, and evaluate the information to make sure it matches their requirements before purchasing the kit. Our ELISA Kit assays are dynamic research tools and sometimes they may be updated and improved. If the format of this assay is important to you then please request the current manual or contact our technical support team with a presales inquiry before placing an order. We will confirm the current details of the assay. We cannot guarantee the sample manual posted online is the most current manual, it is intended to serve as an example only. Please refer to the instructions For Use provided with the assay kit for precise details.

Product PubMed Publications

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