|Positive WB detected in||A431 cells, L02 cells, Jurkat cells, HeLa cells, HepG2 cells, HEK-293 cells, Jurkat cells, THP-1 cells|
|Positive IHC detected in||human liver cancer tissue|
Note: suggested antigen retrieval with TE buffer pH 9.0; (*) Alternatively, antigen retrieval may be performed with citrate buffer pH 6.0
|Western Blot (WB)||WB : 1:5000-1:50000|
|Immunohistochemistry (IHC)||IHC : 1:550-1:2200|
|Sample-dependent, check data in validation data gallery|
66911-1-Ig targets MAVS; VISA in WB, IHC, IF, ELISA applications and shows reactivity with Human samples.
|Host / Isotype||Mouse / IgG1|
|Immunogen||MAVS; VISA fusion protein Ag5949|
|Full Name||mitochondrial antiviral signaling protein|
|Calculated molecular weight||57 kDa|
|Observed molecular weight||70-75 kDa, 50-55 kDa|
|GenBank accession number||BC044952|
|Gene ID (NCBI)||57506|
|Purification Method||Protein A purification|
|Storage Buffer||PBS with 0.02% sodium azide and 50% glycerol pH 7.3.|
|Storage Conditions||Store at -20°C. Stable for one year after shipment. Aliquoting is unnecessary for -20oC storage.|
Mitochondrial antiviral-signaling protein (MAVS) is also known as virus-induced-signaling adapter (VISA) or IFN beta promoter stimulator protein 1 (IPS-1), it is widely involved and required for innate immune defense against viruses. MAVS, present in T cells, monocytes, epithelial cells and hepatocytes, contains CARD and transmembrane domains which are essential for antiviral functions. MAVS is able to interact with various cellular proteins including DDX58/RIG-I, IFIH1/MDA5, TRAF2, TRAF6, TMEM173/MITA, IFIT3 and etc. It can undergoe phosphorylation on multiple sites and ubiquitination, which may together cause the molecular weight migrate to about 70 kDa despite the predicated 57 kDa.
Host protein, HSP90β, antagonizes IFN-β signaling pathway and facilitates the proliferation of encephalomyocarditis virus in vitro.
Encephalomyocarditis virus abrogates the IFN-β signaling pathway via its structural protein VP2.
Swine Acute Diarrhea Syndrome Coronavirus Nucleocapsid Protein Antagonizes Interferon-β Production via Blocking the Interaction Between TRAF3 and TBK1.