Viral Protein U Antibody Summary
| Immunogen |
Synthetic peptide from amino acids 58-80 corresponding to Vpu peptide (amino acid seq: egd qee lsa lme mgh hap wnv nd), was selected from the unique region of the Vpu protein, peptide was post-synthetically modified to achieve highest antigenicity before used for coupling to KLH using heterobifunctional cross linker for immunogen preparation. |
| Specificity |
This antibody is specific to the Viral Protein U found in HIV-1 |
| Clonality |
Polyclonal |
| Host |
Rabbit |
| Gene |
VPU |
| Purity |
Immunogen affinity purified |
| Innovator's Reward |
Test in a species/application not listed above to receive a full credit towards a future purchase. |
Applications/Dilutions
| Dilutions |
- ELISA 1:50000
- Immunocytochemistry/ Immunofluorescence 1:250
- Immunohistochemistry
- Immunohistochemistry-Paraffin 1:250
- Immunoprecipitation 1:250
- Western Blot 1:1000
|
| Application Notes |
This antibody is useful for ELISA, Western Blot, Immunohistochemistry-Paraffin, Immunofluorescence and Immunoprecipitation. |
Reactivity Notes
This antibody reacts with Human Immmunodeficiency Viruse One (HIV-1).
Packaging, Storage & Formulations
| Storage |
Store at -20C. Avoid freeze-thaw cycles. |
| Buffer |
Tris/Glycine buffer pH 7.5-7.9, stabilizing protein, and glycerol |
| Preservative |
0.02% Sodium Azide |
| Purity |
Immunogen affinity purified |
Alternate Names for Viral Protein U Antibody
Background
Retroviruses have several characteristic structural and catalytic proteins, one such auxiliary protein is a viral protein U (Vpu) which enhances virion release from human cells and also involved in the degradation of CD4, the cellular surface receptor of HIV-1. The Vpu has no homolog in less pathogenic HIV-2 virus. Vpu is an 81 amino acid class I membrane integral protein that is unique to human and simian immunodeficiency virus isolated from Chimpanzee and few other monkey species. The 16kDa protein Vpu protein consist of an N-terminal hydrophobic membrane anchor of 27 amino acids and a charged C-terminal hydrophilic domain of 54 amino acids that extents to the cytoplasm. The cytoplasmic domain has a conserved dual serine phosphorylation site (S52 GXX &S56 motif) that is phosphorylated by casein kinase II (1). Vpu is involved in viral replication an degradation of its cellular receptor CD4 and enhancement of viral particle release from macrophages and primary lymphocytes. The degradation of CD4 receptor is achieved by hijacking of protein degradation machinery of the host cells that involves ubiquitin ligases that ensures the selection of proteins to be degraded. Vpu binds to CD4 and simultaneously recruits the BetaTrCP subunit of the SCFBetaTrCP ubiquitin ligase complex through its constitutively phosphorylated DS52GXXS56 motif. In this process, Vpu was found to escape degradation, while inhibiting the degradation of BetaTrCP natural targets such as Beta-catenin and I'Balpha (2). Interestingly, the Vpu activity was not observed in simian cells probably due to its ability to counter act host cell restriction factor specific for human cells and may depend on Vpu binding to host channel TASK-1 protein (3). Vpu is degraded in cells arrested in early mitosis by nacodazole, the degradation process require phosphorylation of the serine 61 residue adjacent to the bTrCP-binding motif (3). Vpu has all the characteristics of signal peptide sequences (hydrophobic N-terminal and a hydrophilic C-terminal tail) when cleaved by signal peptidases stays with lipids of the signal peptidase complex, after further processing the N-0terminal region is released into cytosol where it interacts with calmodulin and preprolactin.
Limitations
This product is for research use only and is not approved for use in humans or in clinical diagnosis. Primary Antibodies are
guaranteed for 1 year from date of receipt.
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