Recombinant HIV1 gp120 Protein

Name: Recombinant HIV1 gp120 Protein
Brand: Beta LifeScience
SKU: BLA-11303P
Availability: InStock

Collections: Featured viral antigens molecules, Hiv, Recombinant proteins, Viral antigen

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Product Overview

Accession	P04578
Synonym	Glycoprotein 120 gp120 SU Surface protein
Description	Recombinant HIV1 gp120 Protein was expressed in Baculovirus infected insect cells. It is a Full length protein
Source	Baculovirus infected insect cells
AA Sequence	KLWVTVYYGVPVWKEATTTLFCASDAKAYDTEVHNVWATHACVPTDPNPQ EVVLVNVTENFNMWKNDMVEQMHEDIISLWDQSLKPCVKLTPLCVSLK CTDLKNDTNTNSSSGRMIMEKGEIKNCSFNISTSIRGKVQKEYAFFYK LDIIPIDNDTTSYKLTSCNTSVITQACPKVSFEPIPIHYCAPAGFAIL KCNNKTFNGTGPCTNVSTVQCTHGIRPVVSTQLLLNGSLAEEEVVIRS VNFTDNAKTIIVQLNTSVEINCTRPNNNTRKRIRIQRGPGRAFVTIGKIG NMRQAHCNISRAKWNNTLKQIASKLREQFGNNKTIIFKQSSGGDPEIV THSFNCGGEFFYCNSTQLFNSTWFNSTWSTEGSNNTEGSDTITLPCRI KQIINMWQKVGKAMYAPPISGQIRCSSNITGLLLTRDGGNSNNESEIF RPGGGDMRDNWRSELYKYKVVKIEPLGVAPTKAKRRVVQREKR
Molecular Weight	54 kDa
Purity	>90% SDS-PAGE.Purified under conditions that maintain the tertiary structure of the molecule. Sterile filtered solution.
Endotoxin	< 1.0 EU per μg of the protein as determined by the LAL method
Formulation	Liquid Solution
Stability	The recombinant protein samples are stable for up to 12 months at -80°C
Reconstitution	See related COA
Unit Definition	For Research Use Only
Storage Buffer	Shipped at 4°C. Store at -20°C. Avoid freeze / thaw cycle.

Target Details

Target Function	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 thereby activated by cellular furin or furin-like proteases to produce gp120 and gp41.; Attaches the virus to the host lymphoid cell by binding to the primary receptor CD4. This interaction induces a structural rearrangement creating a high affinity binding site for a chemokine coreceptor like CXCR4 and/or CCR5. Acts as a ligand for CD209/DC-SIGN and CLEC4M/DC-SIGNR, which are respectively found on dendritic cells (DCs), and on endothelial cells of liver sinusoids and lymph node sinuses. These interactions allow capture of viral particles at mucosal surfaces by these cells and subsequent transmission to permissive cells. HIV subverts the migration properties of dendritic cells to gain access to CD4+ T-cells in lymph nodes. Virus transmission to permissive T-cells occurs either in trans (without DCs infection, through viral capture and transmission), or in cis (following DCs productive infection, through the usual CD4-gp120 interaction), thereby inducing a robust infection. In trans infection, bound virions remain infectious over days and it is proposed that they are not degraded, but protected in non-lysosomal acidic organelles within the DCs close to the cell membrane thus contributing to the viral infectious potential during DCs' migration from the periphery to the lymphoid tissues. On arrival at lymphoid tissues, intact virions recycle back to DCs' cell surface allowing virus transmission to CD4+ T-cells.; Acts as a class I viral fusion protein. Under the current model, the protein has at least 3 conformational states: pre-fusion native state, pre-hairpin intermediate state, and post-fusion hairpin state. During fusion of viral and target intracellular membranes, the coiled coil regions (heptad repeats) assume a trimer-of-hairpins structure, positioning the fusion peptide in close proximity to the C-terminal region of the ectodomain. The formation of this structure appears to drive apposition and subsequent fusion of viral and target cell membranes. Complete fusion occurs in host cell endosomes and is dynamin-dependent, however some lipid transfer might occur at the plasma membrane. The virus undergoes clathrin-dependent internalization long before endosomal fusion, thus minimizing the surface exposure of conserved viral epitopes during fusion and reducing the efficacy of inhibitors targeting these epitopes. Membranes fusion leads to delivery of the nucleocapsid into the cytoplasm.
Subcellular Location	[Surface protein gp120]: Virion membrane; Peripheral membrane protein. Host cell membrane; Peripheral membrane protein. Host endosome membrane; Single-pass type I membrane protein.; [Transmembrane protein gp41]: Virion membrane; Single-pass type I membrane protein. Host cell membrane; Single-pass type I membrane protein. Host endosome membrane; Single-pass type I membrane protein.
Protein Families	HIV-1 env protein family
Database References	KEGG: vg:155971

Gene Functions References

Data show that the cleavage-independent HIV envelope glycoprotein (Env) trimers exhibit quaternary protein structure. PMID: 29769533
Extracellular vesicles that carry Env seem to facilitate HIV infection. PMID: 28490736
Stabilization of the gp120 V3 loop through hydrophobic interactions reduces the immunodominant V3-directed non-neutralizing response to HIV-1 envelope trimers. PMID: 29222332
sequence coverage for Env provides semi-quantitative analysis of the glycosylation status at each glycosite. PMID: 28348411
Binding stability to beta2-microglobulin may confer to HLA-C the ability to preferentially act either as a conventional immune-competent molecule or as an accessory molecule involved in HIV-1 infectivity via viral envelope glycoprotein binding. PMID: 28051183
heptad region 1 connecting loop is a key determinant of HIV-1 trimer metastability PMID: 27349805
These findings highlight regions of cross talk between gp120 and gp41 and identify heptad repeat region 1(HR1) residues that play important roles in regulating CD4-induced conformational changes in Env. PMID: 29875245
Solution structure and membrane interaction of the cytoplasmic tail of HIV-1 gp41 protein has been described. PMID: 29056482
effective antibody that prevents immune escape must selectively bind to high escape cost residues that are surrounded by those where mutations incur a low fitness cost PMID: 29311326
Conserved residues from the signal peptide and residues downstream of the canonical cleavage site form an extended alpha-helix in the endoplasmic reticulum membrane, which covers the cleavage site, thus preventing cleavage. PMID: 28753126
In this study, the authors found the expression of MARCH2 to be upregulated upon HIV-1 infection. MARCH2 inhibits the production and infection of HIV-1 through ligase activity-dependent envelope protein degradation and/or intracellular retention. PMID: 29573664
These data indicate that GPI-scFvs can inhibit Env processing and function, thereby restricting production and infectivity of newly synthesized HIV. PMID: 29321330
Study uses molecular dynamics to provide insight into its structural dynamics and into how both protomer and glycan movements coordinate to shield the Env protein surface; results provide a microsecond-based understanding of the Env glycan shield. PMID: 28890362
The alpha helix 1 from the first conserved region of HIV1 gp120 is reconstructed in the short NQ21 peptide. PMID: 29273432
gp120IIIB promotes the downregulation of CHRFAM7A in neuronal cells. PMID: 26567012
These observations suggest that modulation of N332 glycan occupancy by the second amino acid position of the canonical glycosylation motif Asn-X-Ser plays a previously unappreciated role in viral escape from immune responses. PMID: 27258397
Study reported that DPF1, a short-degraded peptide fragment derived from native gp120-loaded rat hepatocytes, immediately forms fibrils by self-assembly and thus enhances HIV-1 infection. Furthermore, DPF1 accelerates the formation of seminal amyloid fibrils by PAP248-286 and SEM186-107. The newly formed amyloid fibrils retain the ability to enhance HIV-1 infection PMID: 28978437
Data suggest that, beyond hydrophobicity, preserving sequence order (the tandem repeat of the FLGFLG tripeptide) is an important feature for defining the secondary structures and oligomeric states adopted in membranes by the HIV fusion peptide of gp41. (Note that gp41 is coded with gp120 as one gp160 by the env gene of HIV.) PMID: 28930470
crystal structures of trimeric HIV envelope with entry inhibitors BMS-378806 and BMS-626529 PMID: 28825711
Upon gp120 binding to DC-SIGN, cellular NF-kappaB signaling was triggered, leading to the induction of matrix metalloproteinases, which subsequently degraded tight junction proteins and disrupted the blood-retinal barrier integrity. PMID: 27605665
The data data suggest that interactions between HIV-1 gp120 and A2 exist, though this interaction may be indirect. PMID: 27863502
Env regions that respond to CCR5 binding was located in the gp120 alpha1 helix and in the gp41 HR1 heptad repeat and membrane-proximal external region. PMID: 28521215
Glycosylation of V1V2 domain of HIV envelope protein determined its binding to alpha4ss7 integrin. PMID: 28577856
study revealed that while HIV-1 gp120 and Staph aureus LukED both target CCR5, they bind to different regions of the receptor, highlighting the divergence of the pathogens PMID: 27965453
Data suggest that core glycans of gp120 form of HIV-1 envelope protein are not essential for protein folding or viral infectivity; thus, the likely primary role of glycosylation of gp120 is enabling immune evasion. PMID: 28446609
The HIV gp160 envelope protein carries out two major functions, membrane fusion and immune suppression. (Review) PMID: 27793589
The transferred nuclear Overhauser effect (TRNOE) crosspeaks in the ternary complex were assigned to the specific Tyr protons in the human C-C chemokine receptor 5 (CCR5) chemokine receptor peptide and to methyl protons, predominantly of isoleucine residues, and also of leucine and/or valine residues of HIV-1 gp120 envelope protein. PMID: 27701820
initial contact of CD4 with the HIV-1 Env trimer at 6.8-A resolution, is reported. PMID: 28218750
Stabilization of a soluble, native-like trimeric form of an efficiently cleaved Indian HIV-1 clade C envelope glycoprotein.( PMID: 28283570
The increased HIV-1 sensitivity to anti-gp41 antibodies and peptides suggests that SER5 also delays refolding of the remaining fusion-competent Env trimers. PMID: 28179429
Broadly neutralizing antibodies (bnAbs) PGT145 recognizes a quaternary epitope at the apical 3-fold symmetry axis of the envelope (Env) trimer. PMID: 28423342
Key features of the HIV-1 envelope protein that are associated with viral resistance to the IFITM3 protein. PMID: 28100616
The GP120 Phe 43 cavity modulates recognition of CRF01_AE HIV-1-infected cells by serum antibodies isolated from RV144 vaccinees. PMID: 28100618
The authors have found that the hydrophobicity of residue 69 is important for Env processing, CD4 binding, and its transition to the CD4-bound conformation. PMID: 27384653
We report on the production and analysis of HIV-1 Env-specific human monoclonal antibodies. PMID: 27630232
the bilayer curvature modifying properties of a synthetic variant of the HIV-1 gp41 fusion peptide with lipid bilayer vesicles composed of a mixture of dimyristoyl phosphatidylcholine (DMPC) and dimyristoyl phosphatidylserine (DMPS) were studied PMID: 28104377
Ficolin-2 protein could bind with HIV-1 envelope glycoprotein gp120, and subsequently induce complement dependent cytotoxicity. PMID: 27576476
Residue 22 in the envelope glycoprotein V3 region of HIV-1B significantly influences the infectivity of the virus. PMID: 27815696
These results provide evidence that cytoplasmic domains can induce conformational changes in functional regions of gp120 and determine receptor tropism but do not modulate HIV-1 co-receptor specificity. PMID: 27488878
Study presents the 3.4 A structure of a fully glycosylated HIV-1 pre-fusion trimer from clade G and characterize the organization of glycans and clustering of oligomannose residues. Additionally, the 3.7 A structures of fully glycosylated HIV-1 pre-fusion trimers from clades A and B are presented and carried out molecular dynamics simulations and other analyses to provide insight into antibody-glycan interactions. PMID: 27114034
N-linked glycans may impact the infectivity of HIV-1; the distribution of potential N-linked glycosylation sites in gp120 differs among major HIV-1 subtypes circulating in China. PMID: 26384088
The authors provide the first evidence that shows CCR5 interaction with a dual-tropic HIV-1 Env played a significant role in Env-induced depletion of CD4 T cells. PMID: 27026376
These results show how a transmembrane domain anchors, stabilizes, and modulates a viral envelope spike and suggest that its influence on Env conformation is an important consideration for HIV-1 immunogen design. PMID: 27338706
findings suggested that HIV-1 gp41-I90 ectodomain can enhance the transmigration of THP-1 through Cn-infected BBB, which may be mediated by CD44. PMID: 26897523
mechanism by which gp41's function alternates from membrane fusion facilitation to suppression of TCR activation. PMID: 26823547
Taken together, these results suggest that HIV-1 gp120 induces hippocampal neuron apoptosis by enhancement of the Ik, which might be associated with increased Kv2.1 expression via the p38 MAPK pathway. PMID: 26393286
Data suggest that HIV-1 gp41 transmembrane domain (TMD) directly interacts with TMDs of the T-cell receptor and it's CD3-antigen co-receptors (delta, gamma, and epsilon); these interactions appear to be involved in immune evasion mechanism of HIV-1. PMID: 26828096
IFITM2 and IFITM3 specifically antagonize the HIV-1 envelope glycoprotein (Env), thereby inhibiting viral infection. PMID: 26387945
HIV-1 JRCSF variant makes functionally critical contacts with human CCR5 coreceptor amino terminus and extracellular loop 1 (ECL1) and adaptation to murine ECL1 requires multiple mutations in the crown of gp120's V3 loop. PMID: 26114311
Here, the authors show that a highly conserved tryptophan at position 69 of the gp120 inner domain is important for antibody-dependent cellular cytotoxicity mediated by anti-cluster A antibodies and sera from HIV-1-infected individuals. PMID: 26637462

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Proteins are sensitive to heat, and freeze-drying can preserve the activity of the majority of proteins. It improves protein stability, extends storage time, and reduces shipping costs. However, freeze-drying can also lead to the loss of the active portion of the protein and cause aggregation and denaturation issues. Nonetheless, these adverse effects can be minimized by incorporating protective agents such as stabilizers, additives, and excipients, and by carefully controlling various lyophilization conditions.

Commonly used protectant include saccharides, polyols, polymers, surfactants, some proteins and amino acids etc. We usually add 8% (mass ratio by volume) of trehalose and mannitol as lyoprotectant. Trehalose can significantly prevent the alter of the protein secondary structure, the extension and aggregation of proteins during freeze-drying process; mannitol is also a universal applied protectant and fillers, which can reduce the aggregation of certain proteins after lyophilization.

Our protein products do not contain carrier protein or other additives (such as bovine serum albumin (BSA), human serum albumin (HSA) and sucrose, etc., and when lyophilized with the solution with the lowest salt content, they often cannot form A white grid structure, but a small amount of protein is deposited in the tube during the freeze-drying process, forming a thin or invisible transparent protein layer.

Reminder: Before opening the tube cap, we recommend that you quickly centrifuge for 20-30 seconds in a small centrifuge, so that the protein attached to the tube cap or the tube wall can be aggregated at the bottom of the tube. Our quality control procedures ensure that each tube contains the correct amount of protein, and although sometimes you can't see the protein powder, the amount of protein in the tube is still very precise.

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