CD4 (26-396) Human

CD4 (26-396) Human Recombinant
Cat. No.
BT29153
Source
E.coli.
Synonyms
CD4 Molecule, T-Cell Surface Glycoprotein CD4, T-Cell Surface Antigen T4/Leu-3, CD4 Antigen (P55), CD4 Receptor, CD4 Antigen, CD4mut, T-cell surface glycoprotein CD4.
Appearance
Sterile Filtered colorless solution.
Purity
Greater than 85% as determined by SDS-PAGE.
Usage
THE BioTek's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
Shipped with Ice Packs
In Stock

Description

CD4 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 396 amino acids (26-396 a.a) and having a molecular mass of 44kDa.
CD4 is fused to a 25 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Product Specs

Introduction
CD4 is a cell surface glycoprotein present on mature helper T cells, immature thymocytes, monocytes, and macrophages. Some cytotoxic T cells also express CD4. Approximately 65% of blood T cells are CD4+, meaning they have CD4 protein on their membrane. Mature T cells express either CD4 or CD8, but not both. During development, T cells initially express both CD4 and CD8 but undergo differentiation in the thymus to become more specialized.
Description
Recombinant human CD4, produced in E. coli, is a single, non-glycosylated polypeptide chain comprising 396 amino acids (residues 26-396). It has a molecular weight of 44 kDa. This CD4 protein is fused to a 25 amino acid His-tag at the N-terminus and purified using proprietary chromatographic techniques.
Physical Appearance
A clear, colorless, and sterile filtered solution.
Formulation
The CD4 protein solution has a concentration of 0.25 mg/ml and is formulated in a buffer containing 20mM Tris-HCl (pH 8.0) and 10% glycerol.
Stability
For short-term storage (up to 2-4 weeks), store at 4°C. For long-term storage, freeze at -20°C. Adding a carrier protein like HSA or BSA (0.1%) is recommended for extended storage. Avoid repeated freeze-thaw cycles.
Purity
The purity of the CD4 protein is greater than 85% as determined by SDS-PAGE analysis.
Synonyms
CD4 Molecule, T-Cell Surface Glycoprotein CD4, T-Cell Surface Antigen T4/Leu-3, CD4 Antigen (P55), CD4 Receptor, CD4 Antigen, CD4mut, T-cell surface glycoprotein CD4.
Source
E.coli.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSHMKKVVL GKKGDTVELT CTASQKKSIQ FHWKNSNQIK ILGNQGSFLT KGPSKLNDRA DSRRSLWDQG NFPLIIKNLK IEDSDTYICE VEDQKEEVQL LVFGLTANSD THLLQGQSLT LTLESPPGSS PSVQCRSPRG KNIQGGKTLS VSQLELQDSG TWTCTVLQNQ KKVEFKIDIV VLAFQKASSI VYKKEGEQVE FSFPLAFTVE KLTGSGELWW QAERASSSKS WITFDLKNKE VSVKRVTQDP KLQMGKKLPL HLTLPQALPQ YAGSGNLTLA LEAKTGKLHQ EVNLVVMRAT QLQKNLTCEV WGPTSPKLML SLKLENKEAK VSKREKAVWV LNPEAGMWQC LLSDSGQVLL ESNIKVLPTW STPVQP.

Product Science Overview

Introduction

CD4, also known as T-cell surface glycoprotein CD4, is a critical protein in the immune system. It is primarily found on the surface of helper T cells, monocytes, macrophages, and dendritic cells. The CD4 molecule plays a significant role in the immune response by acting as a co-receptor that assists the T-cell receptor (TCR) in communicating with antigen-presenting cells (APCs).

Structure and Function

The CD4 protein is a member of the immunoglobulin superfamily and consists of four extracellular domains (D1 to D4). The recombinant human CD4 (26-396) refers to a specific fragment of the CD4 protein, encompassing amino acids 26 to 396. This fragment includes the extracellular portion of the protein, which is crucial for its interaction with major histocompatibility complex (MHC) class II molecules.

CD4 functions primarily as a co-receptor that enhances the sensitivity of TCRs to antigens presented by MHC class II molecules. This interaction is essential for the activation of helper T cells, which in turn play a pivotal role in orchestrating the immune response by activating other immune cells, including B cells and cytotoxic T cells.

Production and Purification

Recombinant human CD4 (26-396) is typically produced using various expression systems, such as HEK 293 cells or E. coli. The protein is expressed as a single, non-glycosylated polypeptide chain and is purified using chromatographic techniques to achieve high purity levels. For instance, the recombinant CD4 protein expressed in HEK 293 cells has a purity of ≥95% and an endotoxin level of ≤0.005 EU/µg . Similarly, the protein produced in E. coli is fused to a 25 amino acid His-tag at the N-terminus and purified to a purity greater than 85% .

Applications

Recombinant CD4 (26-396) is widely used in research to study the immune response, particularly the interactions between T cells and APCs. It is also utilized in the development of therapeutic agents and vaccines. The protein’s ability to bind to MHC class II molecules makes it a valuable tool for investigating the mechanisms of antigen presentation and T cell activation.

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