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AB49079

Recombinant HIV1 p17 + p24 + gp120 + gp41 protein (Tag Free)

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Recombinant HIV1 p17 + p24 + gp120 + gp41 protein (Tag Free) is a HIV-1 M:B_HXB2R Fragment protein, expressed in Escherichia coli, with >95%, suitable for ELISA, WB.

주요 정보

Purity

>95% SDS-PAGE

발현 시스템

Escherichia coli

Tags

Tag free

Applications

WB, ELISA

applications

Biologically active

No

Accession

P04578-1

Animal free

No

Carrier free

No

Species

HIV-1 M:B_HXB2R

보관 버퍼

pH: 7.2 - 7.6 Preservative: 0.01% Sodium azide Constituents: 50% Glycerol (glycerin, glycerine), 9% Urea, 0.395% Tris HCl, 0.0292% EDTA

storage-buffer

Reactivity 정보

{ "title": "Reactivity Data", "filters": { "stats": ["", "Reactivity", "Dilution Info", "Notes"] }, "values": { "ELISA": { "reactivity":"TESTED_AND_REACTS", "dilution-info":"", "notes":"<p></p>" }, "WB": { "reactivity":"TESTED_AND_REACTS", "dilution-info":"", "notes":"<p></p>" } } }

서열 정보

[{"linker":null,"sequence":"","proteinLength":"Fragment","predictedMolecularWeight":null,"actualMolecularWeight":null,"aminoAcidEnd":0,"aminoAcidStart":0,"nature":"Recombinant","expressionSystem":null,"accessionNumber":"P04578","tags":[]}]

특성 및 보관 정보

제형
Liquid
배송 시 보관 조건
Blue Ice
적절한 단기 보관 조건
-20°C
적절한 장기 보관 조건
-20°C
분주 정보
Upon delivery aliquot
보관 정보
Avoid freeze / thaw cycle
False

추가 정보

This supplementary information is collated from multiple sources and compiled automatically.

HIV1 p17 p24 gp120 and gp41 are important structural proteins of the human immunodeficiency virus-1 (HIV-1). The HIV envelope glycoproteins gp120 and gp41 form a complex that is essential for viral entry into host cells. Gp120 has a mass of about 120 kDa while gp41 is approximately 41 kDa. These proteins facilitate the fusion of the viral envelope with the host cell membrane a critical step in infection. The proteins p17 and p24 are core proteins of the HIV-1 particle. P17 (also known as matrix protein) supports viral assembly and is about 17 kDa whereas p24 is a capsid protein with a mass of 24 kDa essential for forming the core of the virus. These proteins are expressed in infected cells and virions.
Biological function summary

These HIV-1 proteins play roles in enabling the virus to infect and replicate within human immune cells. Gp120 and gp41 interact with the CD4 receptor and co-receptors like CCR5 or CXCR4 on the host cell surface facilitating viral entry. P24 and p17 are significant in viral assembly and maturation processes interacting with other viral components to form a complete virion. While not part of a classic multiprotein complex in the host cell these proteins together contribute to the infectious cycle of HIV-1.

Pathways

These HIV-1 proteins are integral in the viral replication and life cycle pathway which includes attachment fusion uncoating reverse transcription integration and assembly. The interaction of gp120 with CD4 is an important step in the entry pathway leading to conformational changes necessary for fusion with the host membrane. P24 plays an important role in the assembly pathway where it associates with the Gag polyprotein a precursor protein that is cleaved during virus maturation for proper capsid formation.

These proteins are central to HIV infection and acquired immunodeficiency syndrome (AIDS) which leads to the gradual decline in immune function. The progression of HIV infection to AIDS involves immense destruction of CD4 T-cells leaving individuals susceptible to opportunistic infections. P24 being a major component of the capsid is frequently measured in diagnostics to quantify viral load in infected individuals. The correlation of gp120 with the CD4 receptor signifies potential targets for therapeutic interventions aimed at blocking the virus from entering host cells.

일반 정보

기능

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 thereby activated by cellular furin or furin-like proteases to produce gp120 and gp41.. Surface protein gp120. 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.. Transmembrane protein gp41. 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.

서열 유사성

Belongs to the HIV-1 env protein family.

Post-translational modifications

Palmitoylation of the transmembrane protein and of Env polyprotein (prior to its proteolytic cleavage) is essential for their association with host cell membrane lipid rafts. Palmitoylation is therefore required for envelope trafficking to classical lipid rafts, but not for viral replication.. Highly glycosylated by host. The high number of glycan on the protein is reffered to as 'glycan shield' because it contributes to hide protein sequence from adaptive immune system.. Specific enzymatic cleavages in vivo yield mature proteins. Envelope glycoproteins are synthesized as an inactive precursor that is heavily N-glycosylated and processed likely by host cell furin in the Golgi to yield the mature SU and TM proteins. The cleavage site between SU and TM requires the minimal sequence [KR]-X-[KR]-R. About 2 of the 9 disulfide bonds of gp41 are reduced by P4HB/PDI, following binding to CD4 receptor.

제품 프로토콜

타겟 정보

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 thereby activated by cellular furin or furin-like proteases to produce gp120 and gp41.. Surface protein gp120. 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.. Transmembrane protein gp41. 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.
See full target information env

Additional targets

gag-pol,

대체 명칭 보기

Envelope glycoprotein gp160, Env polyprotein, env, Gag-Pol polyprotein, Pr160Gag-Pol, gag-pol, Gag polyprotein, Pr55Gag, gag

Product promise

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