Recombinant Mouse CD4 His-tag Protein, CF Summary
Lys27-Thr394, with a C-terminal 6-His tag
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CF stands for Carrier Free (CF). We typically add Bovine Serum Albumin (BSA) as a carrier protein to our recombinant proteins. Adding a carrier protein enhances protein stability, increases shelf-life, and allows the recombinant protein to be stored at a more dilute concentration. The carrier free version does not contain BSA.
In general, we advise purchasing the recombinant protein with BSA for use in cell or tissue culture, or as an ELISA standard. In contrast, the carrier free protein is recommended for applications, in which the presence of BSA could interfere.
|Formulation||Lyophilized from a 0.2 μm filtered solution in PBS with Trehalose.|
|Reconstitution||Reconstitute at 500 μg/mL in PBS.|
|Shipping||The product is shipped at ambient temperature. Upon receipt, store it immediately at the temperature recommended below.|
|Stability & Storage:||Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
Immobilized Recombinant Mouse CD4 His-tag Protein (10476-CD) supports the adhesion of NIH-3T3 mouse embryonic fibroblast cells. The ED50 for this effect is 2-12 μg/mL.
2 μg/lane of Recombinant Mouse CD4 His-tag Protein (Catalog # 10476-CD) was resolved with SDS-PAGE under reducing (R) and non-reducing (NR) conditions and visualized by Coomassie® Blue staining, showing bands at 50-60 kDa.
CD4, also known as L3T4, T4, and W3/25, is an approximately 42-kDa type I transmembrane glycoprotein that is expressed predominantly on thymocytes and a subset of mature T lymphocytes. It is a standard phenotype marker for the identification of T cell populations (1). Mature mouse CD4 consists of a 394 amino acid (aa) extracellular region containing four immunoglobulin-like domains, a 22 aa transmembrane segment, and a 39 aa cytoplasmic domain (2). Within the ECD, mouse CD4 shares approximately 52% and 73% aa sequence identity with human and rat CD4, respectively. CD4 is expressed along with CD8 on double positive T cells during their development in the thymus. Either CD4 or CD8 expression is then lost, giving rise to single positive (SP) CD4+ or CD8+ mature T cells (3). CD4+ SP cells, also known as T helper cells, further differentiate into multiple subsets of CD4+ cells including Th1, Th2, Th17, Tfh, and Treg cells which regulate humoral and cellular immunity (4). CD4 is reexpressed on circulating CD8+ T cells upon activation and contributes to their cytotoxic effector activity (5). CD4 distribution between species cannot be assumed as demonstrated by its presence on macrophages in human and rat but not in mouse (6). CD4 binds directly to MHC class II molecules on antigen presenting cells (10). This interaction contributes to the formation of the immunological synapse which is focused around the TCR-MHC class II-antigenic peptide interaction (1, 11). Palmitoylation of two cysteine residues in the cytoplasmic tail of CD4 promotes the localization of CD4 in lipid rafts and its ability to augment TCR signaling via activation of the tyrosine kinase Lck (12). CD4 also functions as a chemotactic receptor for IL-16 and, in human, as a co-receptor for the gp120 surface glycoprotein of HIV-1 (7, 13-15).
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