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- Tel: 858.663.9055
- Email: info@nsjbio.com
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Fas cell surface death receptor (FAS), also known as CD95, is a transmembrane receptor of the tumor necrosis factor receptor family that plays a central role in regulating apoptosis within the immune system. The CD95 Antibody / FAS Immune Apoptosis Marker Antibody (clone FAS/3588) targets this receptor, which is predominantly localized to the cell membrane with additional cytoplasmic presence due to receptor trafficking and turnover. CD95 antibody, also referred to as FAS antibody and APO-1 antibody in the literature, detects a key mediator of activation-induced cell death, particularly within lymphoid tissues. This antibody is part of a collection of Human Protein Microarray validated antibodies that have been screened for specificity across thousands of proteins.
CD95 signaling is critical for maintaining immune homeostasis by eliminating activated or autoreactive lymphocytes. Upon binding to its ligand FASL, CD95 undergoes trimerization and recruits adaptor proteins such as FADD, leading to activation of initiator caspases and subsequent apoptotic cascades. This pathway is essential for regulating immune responses and preventing excessive lymphocyte accumulation. Disruption of CD95 signaling is associated with autoimmune syndromes, including autoimmune lymphoproliferative syndrome, as well as tumor immune evasion mechanisms in cancer.
Expression of CD95 is especially prominent in lymphoid organs such as tonsil, lymph node, and spleen, where it is highly expressed on activated T and B cells. In these tissues, staining is typically observed with a membranous pattern accompanied by cytoplasmic signal reflecting receptor internalization. CD95 is also expressed in epithelial tissues, including the gastrointestinal tract, where it contributes to epithelial turnover and response to cellular stress. The TNFRSF6 gene encoding CD95 is located on chromosome 10q24.1 and produces multiple isoforms, including soluble variants that can modulate ligand binding and apoptotic signaling.
Structurally, CD95 consists of an extracellular ligand-binding domain, a transmembrane region, and a cytoplasmic death domain required for downstream signaling. Interaction with FADD and caspase-8 drives formation of the death-inducing signaling complex, leading to apoptosis. CD95 may also interact with additional signaling pathways that influence inflammation and cell survival depending on cellular context. Co-localization with membrane signaling complexes further regulates receptor activation and function.
This antibody shows strong and reliable detection of CD95 expression in lymphoid tissues, making it well suited for studying immune cell apoptosis and regulation. While protein microarray validation demonstrates good specificity, the strength of this antibody lies in its ability to highlight physiologically relevant CD95 expression patterns in immune-rich environments. A CD95 antibody is suitable for detecting this apoptosis receptor in research applications focused on immune regulation, lymphocyte biology, and programmed cell death.
For highly specific detection supported by extensive protein microarray validation, see our FAS antibody FAS/3112.
Optimal dilution of the CD95 Antibody / FAS Immune Apoptosis Marker Antibody should be determined by the researcher.
A human recombinant partial protein (amino acids 26-96) was used as the immunogen for the CD95 antibody.
Store the CD95 antibody at 2-8oC (with azide) or aliquot and store at -20oC or colder (without azide).
FAS antibody, APO-1 antibody, TNFRSF6 antibody, Fas receptor antibody, Death receptor 2 antibody
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