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MABS2055-100UG
Sigma-AldrichAnti-RNase L Antibody, clone 2E9
Anti-RNase L, clone 2E9, Cat. No. MABS2055, is a mouse monoclonal antibody that detects 2-5A-dependent ribonuclease(RNase L) and has been tested for use in ELISA, Immunohistochemistry (Paraffin), and Western Blotting.
More>>Anti-RNase L, clone 2E9, Cat. No. MABS2055, is a mouse monoclonal antibody that detects 2-5A-dependent ribonuclease(RNase L) and has been tested for use in ELISA, Immunohistochemistry (Paraffin), and Western Blotting. Less<<
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Description
Catalogue Number
MABS2055-100UG
Description
Anti-RNase L Antibody, clone 2E9
Alternate Names
2-5A-dependent ribonuclease
2-5A-dependent RNase
Ribonuclease 4
Ribonuclease L
Background Information
2-5A-dependent ribonuclease (UniProt: Q05823; also known as 2-5A-dependent RNase, Ribonuclease 4, Ribonuclease L, RNase L) is encoded by the RNASEL (also known as RNS4) gene (Gene ID: 6041) in human. RNAse L is a virally induced endoribonuclease that functions in the interferon antiviral response. It is highly expressed in spleen and thymus followed by prostate, testis, uterus, small intestine, colon, and peripheral blood leukocytes. It is present in cells in a latent form and requires short 5 - phosphorylated, 2-5A for its activity. Activation of RNAse L results in inhibition of viral proliferation. It mediates its antiviral effects through a combination of direct cleavage of single-stranded viral RNAs, inhibition of protein synthesis through the degradation of rRNA, induction of apoptosis, and induction of other antiviral genes. Activation of RNAse L has also been shown to degrade RNA in a manganese or magnesium dependent process. It has a relatively broad specificity for cleaving single-stranded RNA but prefers UU and UA dinucleotides. RNase-mediated apoptosis results from a JNK-dependent stress-response pathway leading to cytochrome c release from mitochondria and caspase-dependent apoptosis. RNAse L contains nine ankyrin repeats, which constitute the N-terminus 2-5A binding domain. It also has a C6-type zinc finger domain (aa 395-444). Its ribonuclease domain is located in the C-terminus and a single active nuclease domain in a dimer is shown to be sufficient for its ribonuclease activity. Mutations in RNASEL gene are reported in cancers of the prostate and other tissues. (Ref.: Wang, L., et al. (1995). Clin. Can. Res. 1 (11); 1421-1428; Dong, B., and Silverman, RH (1995). J. Biol. Chem. 270(8); 4133-4137; Chakrabarti, A et al. (2011). J. Interferon Cytokine Res.31(1); 49-57).
References
Product Information
Format
Purified
Presentation
Purified mouse monoclonal antibody IgG1 in buffer containing 0.1 M Tris-Glycine (pH 7.4), 150 mM NaCl with 0.05% sodium azide.
Applications
Application
Anti-RNase L, clone 2E9, Cat. No. MABS2055, is a mouse monoclonal antibody that detects 2-5A-dependent ribonuclease(RNase L) and has been tested for use in ELISA, Immunohistochemistry (Paraffin), and Western Blotting.
Key Applications
ELISA
Immunohistochemistry (Paraffin)
Western Blotting
Application Notes
Immunohistochemistry (Paraffin) Analysis: A 1:50 dilution from a representative lot detected RNase L in human stomach tissue sections.
Western Blotting Analysis: A representative lot detected RNase L in Western Blotting applications (Dong, B., et. al. (1995). J Biol Chem. 270(8):4133-7).
ELISA Analysis: A representative lot detected RNase L in ELISA applications (Dong, B., et. al. (1995). J Biol Chem. 270(8):4133-7).
Immunohistochemistry Analysis: A representative lot detected RNase L in Immunohistochemistry applications (Wang, L., et. al. (1995). Clin Cancer Res. 1(11):1421-8).
Biological Information
Immunogen
Full length recombinant human 2-5A-dependent ribonuclease (RNase L).
Clone
2E9
Concentration
Please refer to lot specific datasheet.
Host
Mouse
Specificity
Clone 2E9 is a mouse monoclonal antibody that detects Ribonuclease L in human cells.
Evaluated by Immunohistochemistry (Paraffin) in human prostate tissue sections.
Immunohistochemistry (Paraffin) Analysis: A 1:50 dilution of this antibody detected RNase L in human prostate tissue sections.
Usage Statement
Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.
Elevated levels of 2',5'-linked oligoadenylate-dependent ribonuclease L occur as an early event in colorectal tumorigenesis. Wang, L; Zhou, A; Vasavada, S; Dong, B; Nie, H; Church, JM; Williams, BR; Banerjee, S; Silverman, RH Clin Cancer Res
2
1421-9
1996
RNA decay in IFN-treated cells is controlled by 2'5'-linked oligoadenylate (2-5A)-dependent RNase (RNase L), a uniquely regulated endoribonuclease that requires short 5'-phosphorylated, 2-5A for its activity. Because RNase L is also implicated in the regulation of cell proliferation, we monitored its expression in colorectal adenocarcinomas and noncancerous polyps from familial adenomatous polyposis patients. Elevated levels of RNase L mRNA and activity were found in 17 of 20 tumors compared with corresponding normal mucosa. An mAb against RNase L revealed elevated amounts of this RNase in sections of the tumors, largely in the base of the villi. The occurrence of elevated levels of RNase L seems to be an early event in colorectal tumorigenesis, suggesting that control of RNA turnover is an important step in tumor progression. These data also indicate that regulating RNase L activity may be a useful strategy in treating colorectal carcinomas.
2-5A-dependent RNase is an interferon-inducible enzyme that requires 5'-phosphorylated, 2',5'-linked oligoadenylates (2-5A) for its endoribonuclease activity against single-stranded RNAs. We demonstrate here that recombinant, human 2-5A-dependent RNase forms stable homodimers during its stimulation by 2-5A. The protein dimers were observed to form only upon binding to 2-5A, as shown using gel filtration chromatography and chemical cross-linking and after centrifugation in glycerol gradients. A monoclonal antibody to 2-5A-dependent RNase was prepared and used to probe the subunit structure of the enzyme in the presence or absence of 2-5A. Using oligoadenylates of different length, structure, and 5'-phosphorylation states we determined that conversion of 2-5A-dependent RNase from its monomeric, inactive form to its homodimeric, active form required the presence of functional 2-5A. These results demonstrate that the catalytically active form of 2-5A-dependent RNase is a homodimer.
