|Other Names||Ribonuclease pancreatic, HP-RNase, RIB-1, RNase UpI-1, Ribonuclease 1, RNase 1, Ribonuclease A, RNase A, RNASE1, RIB1, RNS1|
|Target/Specificity||The synthetic peptide sequence is selected from aa 29-42 of HUMAN RNASE1|
|Format||Synthetic peptide was lyophilized with 100% acetonitrile and is supplied as a powder. Reconstitute with 0.1 ml DI water for a final concentration of 1 mg/ml.|
|Storage||Maintain refrigerated at 2-8°C for up to 6 months. For long term storage store at -20°C.|
|Precautions||This product is for research use only. Not for use in diagnostic or therapeutic procedures.|
|Function||Endonuclease that catalyzes the cleavage of RNA on the 3' side of pyrimidine nucleotides. Acts on single-stranded and double-stranded RNA.|
|Tissue Location||Pancreas and other tissues and body fluids (indicating it may have other physiological functions besides its role in digestion)|
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Provided below are standard protocols that you may find useful for product applications.
This gene encodes a member of the pancreatic-type of secretory ribonucleases, a subset of the ribonuclease A superfamily. The encoded endonuclease cleaves internal phosphodiester RNA bonds on the 3'-side of pyrimidine bases. It prefers poly(C) as a substrate and hydrolyzes 2',3'-cyclic nucleotides, with a pH optimum near 8.0. The encoded protein is monomeric and more commonly acts to degrade ds-RNA over ss-RNA. Alternative splicing occurs at this locus and four transcript variants encoding the same protein have been identified. [provided by RefSeq].
D'Alessio, G. Biopolymers 91(12):989-994(2009)
Kover, K.E., et al. J. Mol. Biol. 379(5):953-965(2008)
Ueki, M., et al. Biochem. Genet. 46 (3-4), 145-153 (2008) :
Johnson, R.J., et al. Biochemistry 46(36):10308-10316(2007)
Cybulski, C., et al. Urol. Int. 79(1):44-49(2007)
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