RNH1 Antibody (C-term)
Peptide Affinity Purified Rabbit Polyclonal Antibody (Pab)
|Application ||WB, IF, E|
|Other Accession||NP_976318.1, NP_976317.1|
|Calculated MW||49973 Da|
|Antigen Region||425-454 aa|
|Other Names||Ribonuclease inhibitor, Placental ribonuclease inhibitor, Placental RNase inhibitor, Ribonuclease/angiogenin inhibitor 1, RAI, RNH1, PRI, RNH|
|Target/Specificity||This RNH1 antibody is generated from rabbits immunized with a KLH conjugated synthetic peptide between 425-454 amino acids from the C-terminal region of human RNH1.|
|Format||Purified polyclonal antibody supplied in PBS with 0.09% (W/V) sodium azide. This antibody is purified through a protein A column, followed by peptide affinity purification.|
|Storage||Maintain refrigerated at 2-8°C for up to 2 weeks. For long term storage store at -20°C in small aliquots to prevent freeze-thaw cycles.|
|Precautions||RNH1 Antibody (C-term) is for research use only and not for use in diagnostic or therapeutic procedures.|
|Function||Ribonuclease inhibitor which inhibits RNASE1, RNASE2 and ANG. May play a role in redox homeostasis.|
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Provided below are standard protocols that you may find useful for product applications.
Placental ribonuclease inhibitor (PRI) is a member of a family of proteinaceous cytoplasmic RNase inhibitors that occur in many tissues and bind to both intracellular and extracellular RNases (summarized by Lee et al., 1988 [PubMed 3219362]). In addition to control of intracellular RNases, the inhibitor may have a role in the regulation of angiogenin (MIM 105850). Ribonuclease inhibitor, of 50,000 Da, binds to ribonucleases and holds them in a latent form. Since neutral and alkaline ribonucleases probably play a critical role in the turnover of RNA in eukaryotic cells, RNH may be essential for control of mRNA turnover; the interaction of eukaryotic cells with ribonuclease may be reversible in vivo.
Martins-de-Souza, D., et al. J Psychiatr Res 44(14):989-991(2010)
Martins-de-Souza, D., et al. J Neural Transm 116(3):275-289(2009)
Turcotte, R.F., et al. Biochem. Biophys. Res. Commun. 377(2):512-514(2008)
Johnson, R.J., et al. Biochemistry 46(45):13131-13140(2007)
Johnson, R.J., et al. J. Mol. Biol. 368(2):434-449(2007)
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