epitope corresponding to amino acids 311-400 mapping at the C-terminus of OAS1 p46 of human origin
Modification Notes
The 2'-, 5'- oligoadenylate synthetases (OASs) are interferon-induced proteins that play a putative role in mediating resistance to virus infection, control of cell growth, differentiation and apoptosis. OAS1, which functions as a homotetramer, is characterized by its capacity to catalyze the synthesis of 2'-, 5'- oligomers of adenosine (2-5As). OAS1 binds double-stranded RNA and polymerizes ATP into PPP(A2'P5'A)N oligomers, activating latent RNase L which, when activated, cleaves single-stranded RNAs. This RNase L activity leads to the inhibition of cellular protein synthesis a nd the impairment of viral replication. OAS1, a 400 amino acid containing protein, is also important in evaluating the interferon response in RNAi studies, and is implicated in diabetes mellitus susceptibility.
Key Feature
Clonality
Polyclonal
Isotype
IgG
Host Species
Rabbit
Tested Applications
WBIPIFELISA
recommended for detection of OAS1 of human origin by WB, IP, IF and ELISA:
Species Reactivity
HumanMouseRat
Concentration
1mg/ml
Purification
Affinity purified
Target Information
Alternative Names
epitope corresponding to amino acids 311-400 mapping at the C-terminus of OAS1 p46 of human origin
Tissue Specificity
epitope corresponding to amino acids 311-400 mapping at the C-terminus of OAS1 p46 of human origin