Manufacturer |
GENWAY
|
Category |
|
Type |
Antibody |
Specific against |
other |
Clone |
H398 |
Applications |
FC |
Amount |
0.025 mg |
Item no. |
20-783-310055 |
eClass 6.1 |
32160702 |
eClass 9.0 |
32160702 |
Available |
|
Genway ID: |
GWB-CA3025 |
Specificity: |
CD120aNCBI |
Gene ID: |
7132 |
Isotype: |
IgG2a |
Clone: |
H398 |
Immunogen: |
Purified human tumour necrosis factor receptor type 1 |
Fusion Partner: |
Spleen cells from immunised BALB/c mice were fused with cells of the mouse NSO myeloma cell line. |
Preparation: |
Purified IgG prepared by affinity chromatography on Protein A from tissue culture supernatant |
Buffer Solution: |
Phosphate buffered saline pH7. 4 |
|
Preservative Stabilisers: |
| 0. 09%Sodium Azide1%Bovine Serum AlbuminSuggested |
Flow Cytometry: |
Use 10ul of the suggested working dilution to label 106 cells or 100ul whole blood. Suggested |
Dilution: |
Flow Cytometry - Neat |
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. Contributes to the induction of non-cytocidal TNF effects including anti-viral state and activation of the acid sphingomyelinase. |
Subunit: |
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. Interacts with BAG4 BRE FEM1B GRB2 SQSTM1 and TRPC4AP. Interacts with HCV core protein. |
Subcellular Location: |
Cell membrane; Single-pass type I membrane protein. Secreted. |
Domain: |
The domain that induces A-SMASE is probably identical to the death domain. The N-SMASE activation domain (NSD) is both necessary and sufficient for activation of N-SMASE. |
Domain: |
Both the cytoplasmic membrane-proximal region and the C-terminal region containing the death domain are involved in the interaction with TRPC4AP (By similarity). |
Ptm: |
The soluble form is produced from the membrane form by proteolytic processing. |
Disease: |
Defects in TNFRSF1A are the cause of familial hibernian fever (FHF) [MIM:142680]; also known as tumor necrosis factor receptor-associated periodic syndrome (TRAPS). FHF is a hereditary periodic fever syndrome characterized by recurrent fever abdominal pain localized tender skin lesions and myalgia. Reactive amyloidosis is the main complication and occurs in 25% of cases. |
Similarity: |
Contains 1 death domain. |
Similarity: |
Contains 4 TNFR-Cys repeats. 1. Thoma. B. et al. (1990) Identification of a 60-kD tumor necrosis factor (TNF) receptor as the major signal transducing component in TNF responses. 2. Menegazzi. R. et al. (1994) Evidence that tumor necrosis factor alpha (TNF)-induced activation of neutrophil respiratory burst on biologic surfaces is mediated by the p55 TNF receptor. 3. Dri. P. et al. (1999) Role of the 75-kDa TNF receptor in TNF-induced activation of neutrophil respiratory burst. 4. Kohrgruber. N. et al. (1999) Survival. maturation. and function of CD11c- and CD11c+ peripheral blood dendritic cells are differentially regulated by cytokines. 5. Weigart. N. et al. (1996) Gastrin secretion from primary cultures of rabbit antral G cells; stimulation by inflammatory cytokines. |
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