- Tel: 858.663.9055
-
Email: info@nsjbio.com
- Tel: 858.663.9055
- Email: info@nsjbio.com
Related Products
|
Fas cell surface death receptor (FAS) is a type I transmembrane protein belonging to the tumor necrosis factor receptor superfamily, widely expressed on epithelial and immune cells where it localizes primarily to the plasma membrane with additional cytoplasmic distribution. The FAS Antibody / CD95 Apoptosis Receptor Antibody (clone FAS/3112) targets this critical regulator of programmed cell death, commonly referred to as CD95 or APO-1, and is widely studied for its role in extrinsic apoptosis signaling. FAS antibody, also referred to as CD95 antibody and APO-1 antibody in the literature, recognizes a receptor that initiates caspase activation following ligand binding, ultimately leading to controlled cellular elimination. This antibody is part of a collection of Human Protein Microarray validated antibodies that have been screened for specificity across thousands of proteins.
Functionally, FAS serves as a central mediator of immune homeostasis and tissue turnover by transmitting apoptotic signals upon engagement with its ligand FASL. This receptor is a member of the TNF receptor family and contains a cytoplasmic death domain that recruits adaptor proteins such as FADD, forming the death-inducing signaling complex and activating downstream caspases including CASP8. Through this mechanism, FAS signaling contributes to the removal of damaged or unwanted cells and plays an essential role in maintaining peripheral immune tolerance. Dysregulation of FAS expression or signaling is associated with autoimmune disease, lymphoproliferative disorders, and resistance to apoptosis in cancer cells.
Expression of FAS is observed in a wide range of tissues, including epithelial compartments such as colon, liver, and skin, as well as hematopoietic and lymphoid populations. In epithelial tissues, FAS is typically detected along the cell membrane with variable cytoplasmic staining reflecting receptor internalization and trafficking. In immune tissues, particularly lymph nodes and tonsil, strong expression is often observed in activated lymphocytes, consistent with its role in activation-induced cell death. The protein is encoded by the TNFRSF6 gene located on chromosome 10q24.1 and exists as multiple isoforms generated through alternative splicing, including membrane-bound and soluble variants that can modulate apoptotic signaling dynamics.
At the structural level, FAS contains an extracellular domain responsible for ligand binding, a single-pass transmembrane region, and a cytoplasmic death domain essential for signal transduction. Interactions with proteins such as FADD and caspase-8 occur within this intracellular region, enabling formation of the apoptotic signaling complex. FAS may also co-localize with membrane microdomains and signaling platforms that regulate receptor clustering and activation efficiency. In addition to apoptosis, emerging evidence suggests roles in non-apoptotic signaling pathways, including inflammation and cell proliferation under certain conditions.
This antibody demonstrates strong target specificity supported by protein microarray validation, showing a pronounced signal for FAS with minimal off-target binding. Such high specificity supports reliable detection of FAS expression across diverse tissue types. A FAS antibody is suitable for detecting this apoptosis receptor in research applications where accurate assessment of extrinsic cell death signaling and immune regulation is required.
This CD35 antibody is part of a broader CD antibody panel offered by NSJ Bioreagents.
Optimal dilution of the FAS Antibody / CD95 Apoptosis Receptor Antibody should be determined by the researcher.
A human recombinant partial protein (amino acids 26-96) was used as the immunogen for the Fas antibody.
Store the FAS antibody at 2-8oC (with azide) or aliquot and store at -20oC or colder (without azide).
CD95 antibody, APO-1 antibody, TNFRSF6 antibody, Fas receptor antibody, Death receptor 2 antibody
Your bulk quote request has been submitted successfully!
Please contact us if you have any questions.