- Catalog number
- PKSH033507-01
- Size / count
- 10 µg
- Dry ice
- No
- Hazardous
- No
- Discontinued
- No
- Background
- T-cell surface glycoprotein CD4, is a single-pass type I membrane protein. CD4 contains three Ig-like C2-type (immunoglobulin-like) domains and one Ig-like V-type (immunoglobulin-like) domain. CD4 is a glycoprotein expressed on the surface of T helper cells, regulatory T cells, monocytes, macrophages, and dendritic cells. The CD4 surface determinant, previously associated as a phenotypic marker for helper/inducer subsets of T lymphocytes, has now been critically identified as the binding/entry protein for human immunodeficiency viruses (HIV) . The human CD4 molecule is readily detectable on monocytes, T lymphocytes, and brain tissues. All human tissue sources of CD4 bind radiolabeled gp120 to the same relative degree; however, the murine homologous protein, L3T4, does not bind the HIV envelope protein. CD4 is a co-receptor that assists the T cell receptor (TCR) to activate its T cell following an interaction with an antigen-presenting cell. Using its portion that resides inside the T cell, CD4 amplifies the signal generated by the TCR. CD4 interacts directly with MHC class II molecules on the surface of the antigen-presenting cell via its extracellular domain. The CD4 molecule is currently the object of intense interest and investigation both because of its role in normal T-cell function, and because of its role in HIV infection. CD4 is a primary receptor used by HIV-1 to gain entry into host T cells. HIV infection leads to a progressive reduction of the number of T cells possessing CD4 receptors. Viral protein U (VpU) of HIV-1 plays an important role in downregulation of the main HIV-1 receptor CD4 from the surface of infected cells. Physical binding of VpU to newly synthesized CD4 in the endoplasmic reticulum is an early step in a pathway leading to proteasomal degradation of CD4. Amino acids in both helices found in the cytoplasmic region of VpU in membrane-mimicking detergent micelles experience chemical shift perturbations upon binding to CD4, whereas amino acids between the two helices and at the C-terminus of VpU show no or only small changes, respectively. Paramagnetic spin labels were attached at three sequence positions of a CD4 peptide comprising the transmembrane and cytosolic domains of the receptor. VpU binds to a membrane-proximal region in the cytoplasmic domain of CD4.
- Abbreviation
- CD4; LEU3
- Synonyms
- CD4; CD4mut; Scd4; T-cell surface antigen T4/Leu-3; T-cell surface glycoprotein CD4
- UniProt
- P01730
- Accession Number
- P01730
- Expression System
- HEK293 Cells
- Tag
- C-Fc
- Sequence
- Lys26-Trp390
- Field of Research
- Immunology; Stem cells
- Endotoxin
- < 1.0 EU per μg of the protein as determined by the LAL method.
- Purity
- > 95 % as determined by reducing SDS-PAGE.
- Bioactivity
- Not validated for activity
- Reconstitution
- Please refer to the printed manual for detailed information.
- Shipping Conditions
- This product is provided as lyophilized powder which is shipped with ice packs.
- Storage Conditions
- Generally, lyophilized proteins are stable for up to 12 months when stored at -20 to -80°C. Reconstituted protein solution can be stored at 4-8°C for 2-7 days. Aliquots of reconstituted samples are stable at < -20°C for 3 months.
- Calculated Molecular Weight
- 67.6 kDa
- Observed Molecular Weight
- 70-85 kDa
- Species
- Human