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Recombinant human CD4 Protein, Fc Tag, 200µg  

Recombinant human CD4 Protein, Fc Tag, 200µg

Recombinant Human CD4 Protein, Lys 26 - Pro 396, produced in human 293 cells (HEK293), Fc Tag

Recombinant human protein, CD4, CD-4, CD4mut, CD-4mut

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Availability: within 7 days

396,00 €

Cluster of Differentiation 4 (CD4), also known as T-cell surface antigen T4/Leu-3 (LEU-3) and CD4mut, is a single-pass type I membrane glycoprotein,and is a member of the immunoglobulin superfamily. CD4 expressed on the surface of T helper cells, monocytes, macrophages, and dendritic cells. It has four immunoglobulin domains (D1 to D4) that are exposed on the extracellular surface of the cell: D1 and D3 resemble immunoglobulin variable (IgV) domains. D2 and D4 resemble immunoglobulin constant (IgC) domains. CD4 is a co-receptor that assists the T cell receptor (TCR) with an antigen-presenting cell. Using its portion that resides inside the T cell, CD4 amplifies the signal generated by the TCR by recruiting an enzyme, known as the tyrosine kinase lck, which is essential for activating many molecules involved in the signaling cascade of an activated T cell. CD4 also interacts directly with MHC class II molecules on the surface of the antigen-presenting cell using its extracellular domain. The extracellular domain adopts an immunoglobulin-like beta-sandwich with seven strands in 2 beta sheets, in a Greek key topology.[1] CD4 has also been shown to interact with SPG21 ,[2] Lck[3-4] and Protein unc-119 homolog.[5] 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. Therefore, medical professionals refer to the CD4 count to decide when to begin treatment for HIV-infected patients.

Recombinant Human CD4 Protein, Fc Tag (Human CD4, Fc Tag) Lys 26 - Pro 396 (Accession # AAH25782) was produced in human 293 cells (HEK293).

Molecular Characterization
rhCD4-Fc, fused with Fc fragment Of human IgG1 at the C-terminus and has a calculated MW of 68 kDa expressed. The predicted N-terminus is Lys26. Protein migrates as 80 kDa in reduced SDS-PAGE due to glycosylation.

Less than 1.0 EU per μg of the rhCD4-Fc by the LAL method.

>95% as determined by SDS-PAGE.

Lyophilized from 0.22 μm filtered solution in 50 mM tris, 100 mM glycine, pH7.0. Normally Mannitol or Trehalose are added as protectants before lyophilization.

See Certificate of Analysis for details of reconstitution instruction and specific concentration.

Avoid repeated freeze-thaw cycles. No activity loss was observed after storage at:
In lyophilized state for 1 year (4C-8C); After reconstitution under sterile conditions for 1 month (4°C-8°C) or 3 months (-20°C to -70°C).

Measured by its binding ability in a functional ELISA. Immobilized HIV-1 GP120 (CN54), His Tag (Cat. No. GP4-V15227) at 5μg/mL(100 μL/well) can bind Human CD4, Fc Tag (Cat. No. CD4-H5259) with a linear range of 4.9-78 ng/mL (QC tested). Measured by its binding ability in a functional ELISA. Immobilized Human CD4, Fc Tag (Cat. No. CD4-H5259) at 10μg/mL (100 μL/well) can bind HIV-1 GP120 (CN54), His Tag (Cat. No. GP4-V15227) with a linear range of 0.15-1.25 μg/mL (QC tested).


(1) Brady RL, et al., 1993, Science 260 (5110): 979–83.
(2) Zeitlmann, L., et al., 2001, J. Biol. Chem. (United States) 276 (12): 9123–32.
(3) Rudd CE, et al., 2010, J. Immunol. 185 (5): 2645–9.
(4) Rudd CE, et al., 1988, Proc. Natl. Acad. Sci. U.S.A. 85 (14): 5190–4.
(5) Gorska MM, et al., 2004, J. Exp. Med. 199 (3): 369–79.