| Catalog No. | Size | Price (USD) |
| 60003-MM02-A-25 | 25 Tests | $162.92 |
| 60003-MM02-A-100 | 100 Tests | $325.84 |
General Information
| Product name | Anti-CD4 Antibody (APC), Mouse Monoclonal |
| Validated applications | FCM (FAQ Protocol) |
| Species reactivity | Reacts with: Ferret |
| Specificity | Ferret CD4 |
| Immunogen | Recombinant Ferret CD4 protein (Catalog#60003-F08H) |
| Preparation | This antibody was produced from a hybridoma resulting from the fusion of a mouse myeloma with B cells obtained from a mouse immunized with purified, recombinant Ferret CD4 (rFerret CD4; Catalog#60003-F08H; ABS50090.1; Met1-Leu401) and conjugated with APC under optimum conditions, the unreacted APC was removed. |
| Source | Monoclonal Mouse IgG1 Clone #02 |
| Purification | Protein A |
| Formulation | PBS solution containing 0.5% BSA and 0.03%ProClin300 |
| Concentration | 10 μl/Test, 0.1 mg/ml |
| Conjugate | APC |
| Form | Liquid |
| Shipping | This antibody is shipped as liquid solution at ambient temperature. Upon receipt, store it immediately at the temperature recommended below. |
| Storage | This antibody can be stored at 2℃-8℃ for twelve months without detectable loss of activity. Protected from prolonged exposure to light. Do not freeze ! |
Image / Experimental Information
| Image 1 Description | Analysis of CD4 expression on spleen lymphocytes. Ferret splenocytes were stained with APC-conjugated anti-Ferret CD4. The histogram were derived from the gated events based on light scattering characteristics of lymphocytes. |
| Image 1 Alt Text | Ferret CD4 Flow Cytometry (FC) 26309 |
| Image 1 URL | Source image |
Background Information
| Full Name | CD4 molecule |
| Description | 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. |
| Related Pathways |
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| References |
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title: A universal influenza mRNA vaccine candidate boosts T cell responses and reduces zoonotic influenza virus disease in ferrets
authors: Koen van de Ven; Josien Lanfermeijer; ...; Jørgen de Jonge
journal: Science Advances
date: 2022-12-01
pmid: 36516261
doi: 10.1126/sciadv.adc9937
pmcid: 9750153
cited_by_count: 37
techniques: Derivative Assay; Enzyme-linked Immunospot; Flow Cytometry; Staining
bioz_score: 90
title: Influenza Infection in Ferrets with SARS-CoV-2 Infection History
authors: Caroline Vilas Boas de Melo; Florence Peters; ...; Daniela S. Rajao
journal: Microbiology Spectrum
date: 2022-10-27
pmid: 36301107
doi: 10.1128/spectrum.01386-22
pmcid: 9784775
cited_by_count: 3
techniques: Flow Cytometry; Incubation; Staining
bioz_score: 90
title: Moving Forward: Recent Developments for the Ferret Biomedical Research Model
authors: Randy A. Albrecht; Wen-Chun Liu; ...; Stacey Schultz-Cherry
journal: mBio
date: 2018-09-05
doi: 10.1128/mbio.01113-18
cited_by_count: 51
techniques: Enzyme-linked Immunospot; Flow Cytometry; Ifn? elispot; Immunohistochemistry; Staining
bioz_score: 90
