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> Recombinant Protein > Human Cell Expressed > Human Immunodeficiency Virus type 1 gp140 Protein Human Immunodeficiency Virus type 1 gp140 Protein
| Catalog | Size (Price) | Quantity | In Stock | Operation | Other Information |
| 11677-V02H |
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YES |
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Human Immunodeficiency Virus Type 1 gp140 Protein
HIV-1 gp140 Protein Price Inquiry ( Available Sizes )
- 50μg: Inquiring Price;
- 200μg: Inquiring Price;
- ≥1mg Bulk: Inquiring Price
HIV-1 gp140 Protein Product Information
| Synonym : |
gp140 |
| Protein Construction: |
A DNA sequence encoding the HIV-1 envelope glycoprotein gp160 extracellular domain ( Ala 29 - Ser 661 ), termed as gp140, was fused with the Fc region of human IgG1 at the C-terminus and a signal peptide at the N-terminus |
| Source: |
Human Immunodeficiency Virus type 1 (HIV-1) |
| Strain : | Similar to 97CN001 |
| Expression Host: | Human Cells |
HIV-1 gp140 Protein QC Testing
| Purity: |
> 95 % as determined by SDS-PAGE |
SDS-PAGE:![]() gp140 protein |
|
Bio-activity: |
Using the Octet RED System , the affinity constant ( Kd ) of gp140-Fc bound to human CD4 is 0.3 μM | |
| Endotoxin: | < 1.0 EU per μg of the protein as determined by the LAL method. | |
| Stability: | Samples are stable for up to twelve months from date of receipt at -70℃ | |
| Predicted N terminal: |
Ala 29 |
|
| Molecular Mass: | The recombinant HIV-1 gp140 consists of 874 amino acids after removal of the signal peptide and has a predicted molecular mass of 98 kDa. The apparent molecular mass of the recombinant protein is approximately 210 - 230 kDa in SDS-PAGE under reducing conditions | |
| Formulation: | Lyophilized from sterile PBS , pH 7.4
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HIV-1 gp140 Protein Usage Guide
| Storage: | Store it under sterile conditions at -70℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles. |
| Reconstitution: | A hardcopy of COA with reconstitution instruction is sent along with the products. Please refer to it for detailed information. |
HIV-1 gp140 Protein Related Products & Topics
HIV-1 gp140 Protein Description
Human Immunodeficiency Virus (HIV) can be divided into two major types, HIV type 1 (HIV-1) and HIV type 2 (HIV-2). HIV-1 is related to viruses found in chimpanzees and gorillas living in western Africa. HIV-2 is related to viruses found in sooty mangabeys. HIV-1 viruses may be further divided into groups. The HIV-1 group M viruses predominate and are responsible for the AIDS pandemic. Some of the HIV-1 group M subtypes are known to be more virulent or are resistant to different medications. HIV-2 viruses are thought to be less virulent and transmissible than HIV-1 M group viruses.
The HIV-1 envelope glycoprotein gp160, also known as Glycoprotein 160, is cleaved into two chains: the surface protein gp120 and the transmembrane protein gp41. The mature envelope protein (Env) consists of a homotrimer of non-covalently associated gp120-gp41 heterodimers. The 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. Surface protein gp120 is a ligand for CD209 / DC-SIGN and CLEC4M / DC-SIGNR. It may target the virus to gut-associated lymphoid tissue (GALT) by binding host ITGA4/ITGB7 (alpha-4/beta-7 integrins), a complex that mediates T-cell migration to the GALT. The transmembrane protein gp41 (TM) acts as a class I viral fusion protein, and membranes fusion leads to delivery of the nucleocapsid into the cytoplasm. The external domains of the HIV-1 envelope glycoprotein (gp120 and the gp41 ectodomain, collectively known as gp140) contain all known viral neutralization epitopes.
References
- Robertson, DL. et al.,1995, J. Mol. Evol. 40 (3): 249-59.
- Gallo SA., et al., 2003, Biochim. Biophys. Acta. 1614: 36-50.
- Bobkov, AF. et al., 2004, J. Med. Virol. 74 (2): 191-6.
- Yang X., J. et al., 2005, Virol. 79: 12132-47.
- Beddows, S. et al., 2007, Virology. 360 (2): 329-40.
- Du, SX. et al., 2009, Virology. 395 (1): 33-44.
- Mendu, DR. et al., 2007, Biochem Biophys Res Commun. 363 (3): 466-71.
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