Non-secretory ribonuclease Recombinant Protein | RNASE2 recombinant protein

Recombinant Human Non-secretory ribonuclease

Cat. Num. AAA114100

• Gene Names: RNASE2; EDN; RAF3; RNS2
• Purity: Greater or equal to 85% purity as determined by SDS-PAGE.
• Synonyms: Non-secretory ribonuclease; N/A; Recombinant Human Non-secretory ribonuclease; Eosinophil-derived neurotoxin; RNase UpI-2; Ribonuclease 2; RNase 2; Ribonuclease US; RNASE2 recombinant protein

• Host: E Coli or Yeast or Baculovirus or Mammalian Cell
• Purity/Purification: Greater or equal to 85% purity as determined by SDS-PAGE.
• Form/Format: Lyophilized or liquid (Format to be determined during the manufacturing process)
• Sequence Positions: 28-161aa; Full Length of Mature Protein
• Sequence: KPPQFTWAQWFETQHINMTSQQCTNAMQVINNYQRRCKNQNTFLLTTFANVVNVCGNPNMTCPSNKTRKNCHHSGSQVPLIHCNLTTPSPQNISNCRYAQTPANMFYIVACDNRDQRRDPPQYPVVPVHLDRII

• Preparation and Storage: Store at -20 degree C, for extended storage, conserve at -20 degree C or -80 degree C.

SDS-PAGE

Related Product Information for RNASE2 recombinant protein

This is a non-secretory ribonuclease. It is a pyrimidine specific nuclease with a slight preference for U. Cytotoxin and helminthotoxin. Selectively chotactic for dendritic cells. Possesses a wide variety of biological activities.

Product Categories/Family for RNASE2 recombinant protein

Immunology

References

Sequence of human eosinophil-derived neurotoxin cDNA identity of deduced amino acid sequence with human nonsecretory ribonucleases.Hamann K.J., Barker R.L., Loegering D.A., Pease L.R., Gleich G.J.Gene 83:161-167(1989) Eosinophil cationic protein cDNA. Comparison with other toxic cationic proteins and ribonucleases.Barker R.L., Loegering D.A., Ten R.M., Hamann K.J., Pease L.R., Gleich G.J.J. Immunol. 143:952-955(1989) Molecular cloning of the human eosinophil-derived neurotoxin a member of the ribonuclease gene family.Rosenberg H.F., Tenen D.G., Ackerman S.J.Proc. Natl. Acad. Sci. U.S.A. 86:4460-4464(1989) Structure and chromosome localization of the human eosinophil-derived neurotoxin and eosinophil cationic protein genes evidence for intronless coding sequences in the ribonuclease gene superfamily.Hamann K.J., Ten R.M., Loegering D.A., Jenkins R.B., Heise M.T., Schad C.R., Pease L.R., Gleich G.J., Barker R.L.Genomics 7:535-546(1990) Sequence variation at two eosinophil-associated ribonuclease loci in humans.Zhang J., Rosenberg H.F.Genetics 156:1949-1958(2000) Simonsen C.C., Kennedy J., Comstock L., Ashton N., McGrogan M. Amino acid sequence of the nonsecretory ribonuclease of human urine.Beintema J.J., Hofsteenge J., Iwama M., Morita T., Ohgi K., Irie M., Sugiyama R.H., Schieven G.L., Dekker C.A., Glitz D.G.Biochemistry 27:4530-4538(1988) Biochemical and functional similarities between human eosinophil-derived neurotoxin and eosinophil cationic protein homology with ribonuclease.Gleich G.J., Loegering D.A., Bell M.P., Checkel J.L., Ackerman S.J., McKean D.J.Proc. Natl. Acad. Sci. U.S.A. 83:3146-3150(1986) Purification and properties of bovine kidney ribonucleases.Niwata Y., Ohgi K., Sanda A., Takizawa Y., Irie M.J. Biochem. 97:923-934(1985) Purification and characterization of a ribonuclease from human liver.Sorrentino S., Tucker G.K., Glitz D.G.J. Biol. Chem. 263:16125-16131(1988) Characterization of a unique nonsecretory ribonuclease from urine of pregnant women.Sakakibara R., Hashida K., Kitahara T., Ishiguro M.J. Biochem. 111:325-330(1992) Characterisation of UGP and its relationship with beta-core fragment.Kardana A., Bagshawe K.D., Coles B., Read D., Taylor M.Br. J. Cancer 67:686-692(1993) New type of linkage between a carbohydrate and a protein C-glycosylation of a specific tryptophan residue in human RNase Us.Hofsteenge J., Mueller D.R., de Beer T., Loeffler A., Richter W.J., Vliegenthart J.F.G.Biochemistry 33:13524-13530(1994) The hexopyranosyl residue that is C-glycosidically linked to the side chain of tryptophan-7 in human RNase Us is alpha-mannopyranose.de Beer T., Vliegenthart J.F.G., Loeffler A., Hofsteenge J.Biochemistry 34:11785-11789(1995) Recognition signal for C-mannosylation of Trp-7 in RNase 2 consists of sequence Trp-x-x-Trp.Krieg J., Hartmann S., Vicentini A., Glasner W., Hess D., Hofsteenge J.Mol. Biol. Cell 9:301-309(1998) Mutational analysis of the complex of human RNase inhibitor and human eosinophil-derived neurotoxin (RNase 2) .Teufel D.P., Kao R.Y., Acharya K.R., Shapiro R.Biochemistry 42:1451-1459(2003) Eosinophil-derived neurotoxin (EDN) , an antimicrobial protein with chemotactic activities for dendritic cells.Yang D., Rosenberg H.F., Chen Q., Dyer K.D., Kurosaka K., Oppenheim J.J.Blood 102:3396-3403(2003) Post-translational tyrosine nitration of eosinophil granule toxins mediated by eosinophil peroxidase.Ulrich M., Petre A., Youhnovski N., Proemm F., Schirle M., Schumm M., Pero R.S., Doyle A., Checkel J., Kita H., Thiyagarajan N., Acharya K.R., Schmid-Grendelmeier P., Simon H.-U., Schwarz H., Tsutsui M., Shimokawa H., Bellon G., Lee J.J., Przybylski M., Doering G.J. Biol. Chem. 283:28629-28640(2008) An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome.Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.J. Proteomics 96:253-262(2014) X-ray crystallographic structure of recombinant eosinophil-derived neurotoxin at 1.83-A resolution.Mosimann S.C., Newton D.L., Youle R.J., James M.N.G.J. Mol. Biol. 260:540-552(1996) Mapping the ribonucleolytic active site of eosinophil-derived neurotoxin (EDN) . High resolution crystal structures of EDN complexes with adenylic nucleotide inhibitors.Leonidas D.D., Boix E., Prill R., Suzuki M., Turton R., Minson K., Swaminathan G.J., Youle R.J., Acharya K.R.J. Biol. Chem. 276:15009-15017(2001) Molecular recognition of human eosinophil-derived neurotoxin (RNase 2) by placental ribonuclease inhibitor.Iyer S., Holloway D.E., Kumar K., Shapiro R., Acharya K.R.J. Mol. Biol. 347:637-655(2005) Crystal structures of eosinophil-derived neurotoxin (EDN) in complex with the inhibitors 5'-ATP, Ap3A, Ap4A, and Ap5A.Baker M.D., Holloway D.E., Swaminathan G.J., Acharya K.R.Biochemistry 45:416-426(2006)

NCBI and Uniprot Product Information

• NCBI GI #: 4506549
• NCBI GeneID: 6036
• NCBI Accession #: NP_002925.1
• NCBI GenBank Nucleotide #: NM_002934.2
• UniProt Accession #: P10153; Q52M39; Q9H2B7; Q9UCG7
• Molecular Weight: 19.5 kDa
• NCBI Official Full Name: non-secretory ribonuclease
• NCBI Official Synonym Full Names: ribonuclease A family member 2
• NCBI Official Symbol: RNASE2
• NCBI Official Synonym Symbols: EDN; RAF3; RNS2
• NCBI Protein Information: non-secretory ribonuclease
• UniProt Protein Name: Non-secretory ribonuclease
• UniProt Gene Name: RNASE2
• UniProt Synonym Gene Names: EDN; RNS2; RNase 2
• UniProt Entry Name: RNAS2_HUMAN