Recombinant Human immunodeficiency virus type 1 group M subtype B Envelope glycoprotein gp160 (env), partial

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Code CSB-EP361302HKP
Size $224
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  • (Tris-Glycine gel) Discontinuous SDS-PAGE (reduced) with 5% enrichment gel and 15% separation gel.

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Product Details

Greater than 90% as determined by SDS-PAGE.
Target Names
Uniprot No.
Research Area
Alternative Names
envEnvelope glycoprotein gp160; Env polyprotein) [Cleaved into: Surface protein gp120; SU; Glycoprotein 120; gp120); Transmembrane protein gp41; TM; Glycoprotein 41; gp41)]
Human immunodeficiency virus type 1 group M subtype B (isolate HXB2) (HIV-1)
Expression Region
Target Protein Sequence
Note: The complete sequence including tag sequence, target protein sequence and linker sequence could be provided upon request.
Mol. Weight
69.7 kDa
Protein Length
Tag Info
N-terminal 6xHis-SUMO-tagged
Liquid or Lyophilized powder
Note: We will preferentially ship the format that we have in stock, however, if you have any special requirement for the format, please remark your requirement when placing the order, we will prepare according to your demand.
If the delivery form is liquid, the default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol.
Note: If you have any special requirement for the glycerol content, please remark when you place the order.
If the delivery form is lyophilized powder, the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, pH 8.0.
We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Please reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL.We recommend to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20°C/-80°C. Our default final concentration of glycerol is 50%. Customers could use it as reference.
Troubleshooting and FAQs
Storage Condition
Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. Avoid repeated freeze-thaw cycles.
Shelf Life
The shelf life is related to many factors, storage state, buffer ingredients, storage temperature and the stability of the protein itself.
Generally, the shelf life of liquid form is 6 months at -20°C/-80°C. The shelf life of lyophilized form is 12 months at -20°C/-80°C.
Lead Time
3-7 business days
Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.
Datasheet & COA
Please contact us to get it.

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Target Background

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.
Gene References into Functions
  1. Data show that the cleavage-independent HIV envelope glycoprotein (Env) trimers exhibit quaternary protein structure. PMID: 29769533
  2. Extracellular vesicles that carry Env seem to facilitate HIV infection. PMID: 28490736
  3. Stabilization of the gp120 V3 loop through hydrophobic interactions reduces the immunodominant V3-directed non-neutralizing response to HIV-1 envelope trimers. PMID: 29222332
  4. sequence coverage for Env provides semi-quantitative analysis of the glycosylation status at each glycosite. PMID: 28348411
  5. 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
  6. heptad region 1 connecting loop is a key determinant of HIV-1 trimer metastability PMID: 27349805
  7. 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
  8. Solution structure and membrane interaction of the cytoplasmic tail of HIV-1 gp41 protein has been described. PMID: 29056482
  9. 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
  10. 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
  11. 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
  12. These data indicate that GPI-scFvs can inhibit Env processing and function, thereby restricting production and infectivity of newly synthesized HIV. PMID: 29321330
  13. 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
  14. The alpha helix 1 from the first conserved region of HIV1 gp120 is reconstructed in the short NQ21 peptide. PMID: 29273432
  15. gp120IIIB promotes the downregulation of CHRFAM7A in neuronal cells. PMID: 26567012
  16. 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
  17. 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
  18. 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
  19. crystal structures of trimeric HIV envelope with entry inhibitors BMS-378806 and BMS-626529 PMID: 28825711
  20. 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
  21. The data data suggest that interactions between HIV-1 gp120 and A2 exist, though this interaction may be indirect. PMID: 27863502
  22. 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
  23. Glycosylation of V1V2 domain of HIV envelope protein determined its binding to alpha4ss7 integrin. PMID: 28577856
  24. 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
  25. 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
  26. The HIV gp160 envelope protein carries out two major functions, membrane fusion and immune suppression. (Review) PMID: 27793589
  27. 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
  28. initial contact of CD4 with the HIV-1 Env trimer at 6.8-A resolution, is reported. PMID: 28218750
  29. Stabilization of a soluble, native-like trimeric form of an efficiently cleaved Indian HIV-1 clade C envelope glycoprotein.( PMID: 28283570
  30. 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
  31. Broadly neutralizing antibodies (bnAbs) PGT145 recognizes a quaternary epitope at the apical 3-fold symmetry axis of the envelope (Env) trimer. PMID: 28423342
  32. Key features of the HIV-1 envelope protein that are associated with viral resistance to the IFITM3 protein. PMID: 28100616
  33. The GP120 Phe 43 cavity modulates recognition of CRF01_AE HIV-1-infected cells by serum antibodies isolated from RV144 vaccinees. PMID: 28100618
  34. 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
  35. We report on the production and analysis of HIV-1 Env-specific human monoclonal antibodies. PMID: 27630232
  36. 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
  37. Ficolin-2 protein could bind with HIV-1 envelope glycoprotein gp120, and subsequently induce complement dependent cytotoxicity. PMID: 27576476
  38. Residue 22 in the envelope glycoprotein V3 region of HIV-1B significantly influences the infectivity of the virus. PMID: 27815696
  39. 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
  40. 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
  41. 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
  42. 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
  43. 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
  44. 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
  45. mechanism by which gp41's function alternates from membrane fusion facilitation to suppression of TCR activation. PMID: 26823547
  46. 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
  47. 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
  48. IFITM2 and IFITM3 specifically antagonize the HIV-1 envelope glycoprotein (Env), thereby inhibiting viral infection. PMID: 26387945
  49. 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
  50. 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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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 Links

KEGG: vg:155971

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