Human CD4 (His & Fc Tag) recombinant protein

Human CD4 (His & Fc Tag) recombinant protein

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• Material Safety Data Sheets (MSDS)

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.

cDNA FLJ50658, highly similar to T-cell surface glycoprotein CD4

CD4; L3T4; CD4MUT; LY-4

P01730

Human Cells

A DNA sequence encoding the human CD4 (NP_000607.1) extracellular domain (Met 1-Trp 390) was fused with the C-terminal polyhistidine-tagged Fc region of human IgG1 at the C-terminus.

Human

The recombinant human CD4/Fc is a disulfide-linked homodimer. The reduced monomer consists of 612 amino acids and has a predicted molecular mass of 68.7 kDa. In SDS-PAGE under reducing conditions, the apparent molecular mass of rh CD4/Fc monomer is approximately 75 kDa due to glycosylation.

> 92 % as determined by SDS-PAGE

1. Measured by the ability of the immobilized protein to support the adhesion of NIH-3T3 mouse embryonic fibroblast cells. When 5 × 10E4 cells/well areadded to CD4-Fch coated plates (1.25μg/mL and 100μL/well), approximately >50% will adhere specifically after 30 minutes at 37℃.
2. Measured by its binding ability in a functional ELISA. Immobilized human CD4 at 10 μg/mL (100 μL/well) can bind biotinylated GP140-His (Tri) (Cat: 504682) with a linear range of 0.16-1.25μg/mL.