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Phospho-mouse TNFR(S299) Antibody Blocking peptide
Synthetic peptide
- SPECIFICATION
- CITATIONS
- PROTOCOLS
- BACKGROUND
| Primary Accession | P25118 |
|---|---|
| Clone Names | 4100210 |
| Gene ID | 21937 |
|---|---|
| Other Names | Tumor necrosis factor receptor superfamily member 1A, Tumor necrosis factor receptor 1, TNF-R1, Tumor necrosis factor receptor type I, TNF-RI, TNFR-I, p55, p60, CD120a, Tnfrsf1a, Tnfr-1, Tnfr1 |
| Target/Specificity | The synthetic peptide sequence used to generate the antibody AP3275a was selected from the region of human Mouse Phospho-TNFR-S299. A 10 to 100 fold molar excess to antibody is recommended. Precise conditions should be optimized for a particular assay. |
| Format | Peptides are lyophilized in a solid powder format. Peptides can be reconstituted in solution using the appropriate buffer as needed. |
| Storage | Maintain refrigerated at 2-8°C for up to 6 months. For long term storage store at -20°C. |
| Precautions | This product is for research use only. Not for use in diagnostic or therapeutic procedures. |
| Name | Tnfrsf1a |
|---|---|
| Synonyms | Tnfr-1, Tnfr1 |
| Function | Receptor for TNFSF2/TNF-alpha and homotrimeric TNFSF1/lymphotoxin-alpha. The adapter molecule FADD recruits caspase-8 to the activated receptor. The resulting death-inducing signaling complex (DISC) performs caspase-8 proteolytic activation which initiates the subsequent cascade of caspases (aspartate-specific cysteine proteases) mediating apoptosis (By similarity). |
| Cellular Location | Cell membrane; Single-pass type I membrane protein. Golgi apparatus membrane; Single-pass type I membrane protein |
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Provided below are standard protocols that you may find useful for product applications.
Background
TNFR1 is a receptor for TNFSF2/TNF-alpha and homotrimeric TNFSF1/lymphotoxin-alpha. The adapter molecule FADD recruits caspase-8 to the activated receptor. The resulting death-inducing signaling complex (DISC) performs caspase-8 proteolytic activation which initiates the subsequent cascade of caspases (aspartate-specific cysteine proteases) mediating apoptosis. Binding of TNF to the extracellular domain leads to homotrimerization. The aggregated death domains provide a novel molecular interface that interacts specifically with the death domain of TRADD. Various TRADD-interacting proteins such as TRAFS, RIPK1 and possibly FADD, are recruited to the complex by their association with TRADD. This complex activates at least two distinct signaling cascades, apoptosis and NF-kappa-B signaling.
References
1. J. Immunol. 175 (8), 5024-5033 (2005) 2. J Leukoc Biol. 2005 Dec;78(6):1233-41. 3. Mol. Cell. Biol. 11:3020-3026(1991).
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