Antibody data
- Antibody Data
- Antigen structure
- References [13]
- Comments [0]
- Validations
- Western blot [1]
- Immunohistochemistry [1]
Submit
Validation data
Reference
Comment
Report error
- Product number
- NB100-351 - Provider product page
- Provider
- Novus Biologicals
- Proper citation
- Novus Cat#NB100-351, RRID:AB_10081934
- Product name
- Mouse Monoclonal RNase L Antibody
- Antibody type
- Monoclonal
- Description
- Protein G purified.
- Reactivity
- Human, Mouse, Rat, Hamster, Simian
- Host
- Mouse
- Isotype
- IgG
- Vial size
- 0.1 ml
- Concentration
- 1.0 mg/ml
- Storage
- Aliquot and store at -20C or -80C. Avoid freeze-thaw cycles.
Submitted references RNase L promotes the formation of unique ribonucleoprotein granules distinct from stress granules.
RNase L Reprograms Translation by Widespread mRNA Turnover Escaped by Antiviral mRNAs.
Regulation of p21/CIP1/WAF-1 mediated cell-cycle arrest by RNase L and tristetraprolin, and involvement of AU-rich elements.
RNase L controls terminal adipocyte differentiation, lipids storage and insulin sensitivity via CHOP10 mRNA regulation.
Alternative polyadenylation variants of the RNA binding protein, HuR: abundance, role of AU-rich elements and auto-Regulation.
Distinct antiviral roles for human 2',5'-oligoadenylate synthetase family members against dengue virus infection.
A phylogenetically conserved RNA structure in the poliovirus open reading frame inhibits the antiviral endoribonuclease RNase L.
Germline mutations in the ribonuclease L gene in families showing linkage with HPC1.
A bipartite model of 2-5A-dependent RNase L.
A bipartite model of 2-5A-dependent RNase L.
Elevated levels of 2',5'-linked oligoadenylate-dependent ribonuclease L occur as an early event in colorectal tumorigenesis.
2-5A-dependent RNase molecules dimerize during activation by 2-5A.
2-5A-dependent RNase molecules dimerize during activation by 2-5A.
Burke JM, Lester ET, Tauber D, Parker R
The Journal of biological chemistry 2020 Feb 7;295(6):1426-1438
The Journal of biological chemistry 2020 Feb 7;295(6):1426-1438
RNase L Reprograms Translation by Widespread mRNA Turnover Escaped by Antiviral mRNAs.
Burke JM, Moon SL, Matheny T, Parker R
Molecular cell 2019 Sep 19;75(6):1203-1217.e5
Molecular cell 2019 Sep 19;75(6):1203-1217.e5
Regulation of p21/CIP1/WAF-1 mediated cell-cycle arrest by RNase L and tristetraprolin, and involvement of AU-rich elements.
Al-Haj L, Blackshear PJ, Khabar KS
Nucleic acids research 2012 Sep;40(16):7739-52
Nucleic acids research 2012 Sep;40(16):7739-52
RNase L controls terminal adipocyte differentiation, lipids storage and insulin sensitivity via CHOP10 mRNA regulation.
Fabre O, Salehzada T, Lambert K, Boo Seok Y, Zhou A, Mercier J, Bisbal C
Cell death and differentiation 2012 Sep;19(9):1470-81
Cell death and differentiation 2012 Sep;19(9):1470-81
Alternative polyadenylation variants of the RNA binding protein, HuR: abundance, role of AU-rich elements and auto-Regulation.
Al-Ahmadi W, Al-Ghamdi M, Al-Haj L, Al-Saif M, Khabar KS
Nucleic acids research 2009 Jun;37(11):3612-24
Nucleic acids research 2009 Jun;37(11):3612-24
Distinct antiviral roles for human 2',5'-oligoadenylate synthetase family members against dengue virus infection.
Lin RJ, Yu HP, Chang BL, Tang WC, Liao CL, Lin YL
Journal of immunology (Baltimore, Md. : 1950) 2009 Dec 15;183(12):8035-43
Journal of immunology (Baltimore, Md. : 1950) 2009 Dec 15;183(12):8035-43
A phylogenetically conserved RNA structure in the poliovirus open reading frame inhibits the antiviral endoribonuclease RNase L.
Han JQ, Townsend HL, Jha BK, Paranjape JM, Silverman RH, Barton DJ
Journal of virology 2007 Jun;81(11):5561-72
Journal of virology 2007 Jun;81(11):5561-72
Germline mutations in the ribonuclease L gene in families showing linkage with HPC1.
Carpten J, Nupponen N, Isaacs S, Sood R, Robbins C, Xu J, Faruque M, Moses T, Ewing C, Gillanders E, Hu P, Bujnovszky P, Makalowska I, Baffoe-Bonnie A, Faith D, Smith J, Stephan D, Wiley K, Brownstein M, Gildea D, Kelly B, Jenkins R, Hostetter G, Matikainen M, Schleutker J, Klinger K, Connors T, Xiang Y, Wang Z, De Marzo A, Papadopoulos N, Kallioniemi OP, Burk R, Meyers D, Grönberg H, Meltzer P, Silverman R, Bailey-Wilson J, Walsh P, Isaacs W, Trent J
Nature genetics 2002 Feb;30(2):181-4
Nature genetics 2002 Feb;30(2):181-4
A bipartite model of 2-5A-dependent RNase L.
Dong B, Silverman RH
The Journal of biological chemistry 1997 Aug 29;272(35):22236-42
The Journal of biological chemistry 1997 Aug 29;272(35):22236-42
A bipartite model of 2-5A-dependent RNase L.
Dong B, Silverman RH
The Journal of biological chemistry 1997 Aug 29;272(35):22236-42
The Journal of biological chemistry 1997 Aug 29;272(35):22236-42
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
Clinical cancer research : an official journal of the American Association for Cancer Research 1995 Nov;1(11):1421-8
Clinical cancer research : an official journal of the American Association for Cancer Research 1995 Nov;1(11):1421-8
2-5A-dependent RNase molecules dimerize during activation by 2-5A.
Dong B, Silverman RH
The Journal of biological chemistry 1995 Feb 24;270(8):4133-7
The Journal of biological chemistry 1995 Feb 24;270(8):4133-7
2-5A-dependent RNase molecules dimerize during activation by 2-5A.
Dong B, Silverman RH
The Journal of biological chemistry 1995 Feb 24;270(8):4133-7
The Journal of biological chemistry 1995 Feb 24;270(8):4133-7
No comments: Submit comment
Supportive validation
- Submitted by
- Novus Biologicals (provider)
- Main image
- Experimental details
- Western Blot: RNase L Antibody (2E9) [NB100-351] - RNaseL in insect cell extracts transfected with recombinant human RNase L (0.1 ug) and Hey1B (100 ug)
Supportive validation
- Submitted by
- Novus Biologicals (provider)
- Main image
- Experimental details
- Immunohistochemistry: RNase L Antibody (2E9) [NB100-351] - RNase L antibody was tested in human colon using DAB with hematoxylin counterstain.