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Search results 1 to 87 out of 87 for Rpp21

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Hits by Strain

Type Details Score
Gene
79897 | RPP21
Type: gene
Organism: human
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Gene
448235 | rpp21
Type: gene
Organism: frog, western clawed
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Gene
104968464 | RPP21
Type: gene
Organism: cattle
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Gene
406230 | Rpp21
Type: gene
Organism: rat
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Gene
474824 | RPP21
Type: gene
Organism: dog, domestic
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Gene
471955 | RPP21
Type: gene
Organism: chimpanzee
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Gene
445136 | rpp21
Type: gene
Organism: zebrafish
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Gene
713056 | RPP21
Type: gene
Organism: macaque, rhesus
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Protein Coding Gene
MGI:1914926 | Rpp21
Type: protein_coding_gene
Organism: mouse, laboratory
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Publication
12671000 | J:82851
First Author: Takada T
Year: 2003
Journal: Genome Res
Title: Species-specific class I gene expansions formed the telomeric 1 mb of the mouse major histocompatibility complex.
Volume: 13
Issue: 4
Pages: 589-600
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Protein Coding Gene
MGP_CAROLIEiJ_G0021549 | -
Type: protein_coding_gene
Organism: Mus caroli
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Protein Coding Gene
MGP_129S1SvImJ_G0023672 | -
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGP_AJ_G0023629 | -
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGP_AKRJ_G0023600 | -
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGP_BALBcJ_G0023636 | -
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGP_C3HHeJ_G0023398 | -
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGI_C57BL6J_1914926 | -
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGP_C57BL6NJ_G0024074 | -
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGP_CASTEiJ_G0022887 | -
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGP_CBAJ_G0023376 | -
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGP_DBA2J_G0023500 | -
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGP_FVBNJ_G0023473 | -
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGP_LPJ_G0023579 | -
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGP_NODShiLtJ_G0023496 | -
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGP_NZOHlLtJ_G0024120 | -
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGP_PWKPhJ_G0022638 | -
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGP_WSBEiJ_G0022956 | -
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGP_PahariEiJ_G0020546 | -
Type: protein_coding_gene
Organism: Mus pahari
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Protein Coding Gene
MGP_SPRETEiJ_G0022458 | -
Type: protein_coding_gene
Organism: Mus spretus
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Publication
12045094 | J:88304
 
First Author: Xiao S
Year: 2002
Journal: Annu Rev Biochem
Title: Eukaryotic ribonuclease P: a plurality of ribonucleoprotein enzymes.
Volume: 71
Pages: 165-89
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Publication
- | J:157064
     
First Author: University of California, Davis
Year: 2010
Journal: MGI Direct Data Submission
Title: Alleles produced for the KOMP project by the University of California, Davis
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Publication
- | J:72245
       
First Author: GOA curators, MGI curators
Year: 2001
Title: Gene Ontology annotation based on Enzyme Commission mapping
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Publication
- | J:342604
       
First Author: UniProt-GOA
Year: 2012
Title: Gene Ontology annotation based on UniProtKB/Swiss-Prot Subcellular Location vocabulary mapping, accompanied by conservative changes to GO terms applied by UniProt
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Publication
- | J:78475
       
First Author: Mouse Genome Informatics Scientific Curators
Year: 2002
Title: Chromosome assignment of mouse genes using the Mouse Genome Sequencing Consortium (MGSC) assembly and the ENSEMBL Database
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Publication
11217851 | J:65060
First Author: Kawai J
Year: 2001
Journal: Nature
Title: Functional annotation of a full-length mouse cDNA collection.
Volume: 409
Issue: 6821
Pages: 685-90
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Publication
14610273 | J:86696
First Author: Zambrowicz BP
Year: 2003
Journal: Proc Natl Acad Sci U S A
Title: Wnk1 kinase deficiency lowers blood pressure in mice: a gene-trap screen to identify potential targets for therapeutic intervention.
Volume: 100
Issue: 24
Pages: 14109-14
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Publication
- | J:141210
     
First Author: Mouse Genome Informatics (MGI) and National Center for Biotechnology Information (NCBI)
Year: 2008
Journal: Database Download
Title: Mouse Gene Trap Data Load from dbGSS
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Publication
- | J:60000
       
First Author: UniProt-GOA
Year: 2012
Title: Gene Ontology annotation based on UniProtKB/Swiss-Prot keyword mapping
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Publication
- | J:342605
       
First Author: GOA curators
Year: 2016
Title: Automatic transfer of experimentally verified manual GO annotation data to orthologs using Ensembl Compara
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Publication
12466851 | J:80000
First Author: Okazaki Y
Year: 2002
Journal: Nature
Title: Analysis of the mouse transcriptome based on functional annotation of 60,770 full-length cDNAs.
Volume: 420
Issue: 6915
Pages: 563-73
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Publication
- | J:164563
       
First Author: The Gene Ontology Consortium
Year: 2010
Title: Automated transfer of experimentally-verified manual GO annotation data to mouse-human orthologs
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Publication
21267068 | J:153498
First Author: Diez-Roux G
Year: 2011
Journal: PLoS Biol
Title: A high-resolution anatomical atlas of the transcriptome in the mouse embryo.
Volume: 9
Issue: 1
Pages: e1000582
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Publication
- | J:75000
       
First Author: Mouse Genome Informatics Scientific Curators
Year: 2002
Title: Mouse Genome Informatics Computational Sequence to Gene Associations
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Publication
- | J:157972
     
First Author: Mouse Genome Informatics Scientific Curators
Year: 2010
Journal: Database Download
Title: Mouse Microarray Data Integration in Mouse Genome Informatics, the Affymetrix GeneChip Mouse Genome U74 Array Platform (A, B, C v2).
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Publication
- | J:57747
     
First Author: MGI Genome Annotation Group and UniGene Staff
Year: 2015
Journal: Database Download
Title: MGI-UniGene Interconnection Effort
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Publication
- | J:161428
       
First Author: Marc Feuermann, Huaiyu Mi, Pascale Gaudet, Dustin Ebert, Anushya Muruganujan, Paul Thomas
Year: 2010
Title: Annotation inferences using phylogenetic trees
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Publication
- | J:63103
     
First Author: Mouse Genome Database and National Center for Biotechnology Information
Year: 2000
Journal: Database Release
Title: Entrez Gene Load
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Publication
- | J:262123
     
First Author: Allen Institute for Brain Science
Year: 2004
Journal: Allen Institute
Title: Allen Brain Atlas: mouse riboprobes
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Publication
- | J:144086
     
First Author: Mouse Genome Informatics Scientific Curators
Year: 2009
Journal: Database Download
Title: Mouse Microarray Data Integration in Mouse Genome Informatics, the Affymetrix GeneChip Mouse Gene 1.0 ST Array Platform
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Publication
- | J:155721
     
First Author: Mouse Genome Informatics (MGI) and The National Center for Biotechnology Information (NCBI)
Year: 2010
Journal: Database Download
Title: Consensus CDS project
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Publication
- | J:85324
     
First Author: Mouse Genome Informatics Group
Year: 2003
Journal: Database Procedure
Title: Automatic Encodes (AutoE) Reference
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Publication
- | J:53168
     
First Author: Bairoch A
Year: 1999
Journal: Database Release
Title: SWISS-PROT Annotated protein sequence database
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Publication
- | J:91388
       
First Author: Mouse Genome Informatics Scientific Curators
Year: 2005
Title: Obtaining and Loading Genome Assembly Coordinates from Ensembl Annotations
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Publication
- | J:155221
     
First Author: Mouse Genome Informatics
Year: 2010
Journal: Database Release
Title: Protein Ontology Association Load.
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Publication
- | J:90438
       
First Author: Mouse Genome Informatics Scientific Curators
Year: 2005
Title: Obtaining and loading genome assembly coordinates from NCBI annotations
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Publication
- | J:144087
     
First Author: Mouse Genome Informatics Scientific Curators
Year: 2009
Journal: Database Download
Title: Mouse Microarray Data Integration in Mouse Genome Informatics, the Affymetrix GeneChip Mouse Genome 430 2.0 Array Platform
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Protein
Q80XY2
Organism: Mus musculus/domesticus
Length: 71  
Fragment?: false
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Protein
Q8R040
Organism: Mus musculus/domesticus
Length: 150  
Fragment?: false
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Protein
G3UWS0
Organism: Mus musculus/domesticus
Length: 51  
Fragment?: true
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Publication
11497433 | -
First Author: Jarrous N
Year: 2001
Journal: RNA
Title: Function and subnuclear distribution of Rpp21, a protein subunit of the human ribonucleoprotein ribonuclease P.
Volume: 7
Issue: 8
Pages: 1153-64
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Publication
10523674 | -
First Author: Cai T
Year: 1999
Journal: Mol Cell Biol
Title: Mutagenesis of SNM1, which encodes a protein component of the yeast RNase MRP, reveals a role for this ribonucleoprotein endoribonuclease in plasmid segregation.
Volume: 19
Issue: 11
Pages: 7857-69
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Publication
11880623 | -
First Author: Houser-Scott F
Year: 2002
Journal: Proc Natl Acad Sci U S A
Title: Interactions among the protein and RNA subunits of Saccharomyces cerevisiae nuclear RNase P.
Volume: 99
Issue: 5
Pages: 2684-9
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Protein Domain
IPR007175 | Rpr2/Snm1/Rpp21
Type: Family
Description: This entry contains ribonuclease P (Rnp) proteins from eukaryotes and archaea. Rnp is a ubiquitous ribozyme that catalyzes a Mg2 -dependent hydrolysis to remove the 5'-leader sequence of precursor tRNA (pre-tRNA) [, ]. Archaeal and eukaryotic RNase P consist of a single RNA and archaeal RNase P has four or five proteins, while eukaryotic RNase P consists of 9 or 10 proteins. Eukaryotic and archaeal RNase P RNAs cooperatively function with protein subunits in catalysis []. Human RNase P is composed of a singular protein Pop1 and three subcomplexes, the Rpp20-Rpp25 heterodimer, Pop5-Rpp14-(Rpp30)2-Rpp40 heteropentamer, and Rpp21-Rpp29-Rpp38 heterotrimer. Although both Pop5 and Rpp14 have similar protein structure, they share a very limited sequence similarity. Moreover, the C-terminal fragments after the conserved beta sheets in Pop5 and Rpp14 exhibit distinct structural features that mediate interactions with Pop1 and Rpp40, respectively [].In the hyperthermophilic archaeon Pyrococcus horikoshii OT3, RNase P is composed of the RNase P RNA (pRNA) and five proteins (PhoPop5, PhoRpp38, PhoRpp21, PhoRpp29, and PhoRpp30) [, ].This entry includes Rpp21 from animals, Snm1/Rpr2 from yeasts and RNP4 from archaea [, ]. Snm1 is a subunit of RNase MRP (mitochondrial RNA processing), a ribonucleoprotein endoribonuclease that has roles in both mitochondrial DNA replication and nuclear 5.8S rRNA processing. Snm1 is an RNA binding protein that binds the MRP RNA specifically []. This subunit possibly binds the precursor tRNA [].
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Publication
21956908 | -
First Author: Mattijssen S
Year: 2010
Journal: Wiley Interdiscip Rev RNA
Title: RNase MRP and disease.
Volume: 1
Issue: 1
Pages: 102-16
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Publication
28115465 | -
First Author: Goldfarb KC
Year: 2017
Journal: Genes Dev
Title: Targeted CRISPR disruption reveals a role for RNase MRP RNA in human preribosomal RNA processing.
Volume: 31
Issue: 1
Pages: 59-71
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Publication
15518563 | -
First Author: Sidote DJ
Year: 2004
Journal: Biochemistry
Title: Crystal structure of archaeal ribonuclease P protein aRpp29 from Archaeoglobus fulgidus.
Volume: 43
Issue: 44
Pages: 14128-38
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Protein Domain
IPR016819 | RNase_P/MRP_POP5
Type: Family
Description: Ribonuclease P (Rnp) is a ubiquitous ribozyme that catalyzes a Mg2 -dependent hydrolysis to remove the 5'-leader sequence of precursor tRNA (pre-tRNA) in all three domains of life []. In bacteria, the catalytic RNA (typically ~120kDa) is aided by a small protein cofactor (~14kDa) []. Archaeal and eukaryote RNase P consist of a single RNA and archaeal RNase P has four or five proteins, while eukaryotic RNase P consists of 9 or 10 proteins. Eukaryotic and archaeal RNase P RNAs cooperatively function with protein subunits in catalysis [].Eukaryotic nuclear RNase P shares most of its protein components with another essential RNP enzyme, nucleolar RNase MRP []. RNase MRP (mitochondrial RNA processing) is an rRNA processing enzyme that cleaves various RNAs, including ribosomal, messenger, and mitochondrial RNAs. It can cleave a specific site within precursor rRNA to generate the mature 5'-end of 5.8S rRNA []. Despite its name, the vast majority of RNase MRP is localized in the nucleolus []. RNase MRP has been shown to cleave primers for mitochondrial DNA replication and CLB2 mRNA. In yeast, RNase MRP possesses one putatively catalytic RNA and at least 9 protein subunits (Pop1, Pop3-Pop8, Rpp1, Snm1 and Rmp1) []. Human RNase MRP complex consists of 267 nucleotides and supports the interaction with and among at least seven protein components: hPop1, hPop5, Rpp20, Rpp25, Rpp30, Rpp38, and Rpp40) and three additional proteins, hPop4, Rpp21 and Rpp14, have been reported to be associated with at least a subset of RNase MRP complexes [].This entry represents the Pop5 from eukaryotes and related proteins from archaea.
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Protein Domain
IPR016848 | RNase_P/MRP_Rpp29-subunit
Type: Family
Description: Ribonuclease P (Rnp) is a ubiquitous ribozyme that catalyzes a Mg2 -dependent hydrolysis to remove the 5'-leader sequence of precursor tRNA (pre-tRNA) in all three domains of life []. In bacteria, the catalytic RNA (typically ~120kDa) is aided by a small protein cofactor (~14kDa) []. Archaeal and eukaryote RNase P consist of a single RNA and archaeal RNase P has four or five proteins, while eukaryotic RNase P consists of 9 or 10 proteins. Eukaryotic and archaeal RNase P RNAs cooperatively function with protein subunits in catalysis [].Eukaryotic nuclear RNase P shares most of its protein components with another essential RNP enzyme, nucleolar RNase MRP []. RNase MRP (mitochondrial RNA processing) is an rRNA processing enzyme that cleaves various RNAs, including ribosomal, messenger, and mitochondrial RNAs. It can cleave a specific site within precursor rRNA to generate the mature 5'-end of 5.8S rRNA []. Despite its name, the vast majority of RNase MRP is localized in the nucleolus []. RNase MRP has been shown to cleave primers for mitochondrial DNA replication and CLB2 mRNA. In yeast, RNase MRP possesses one putatively catalytic RNA and at least 9 protein subunits (Pop1, Pop3-Pop8, Rpp1, Snm1 and Rmp1) []. Human RNase MRP complex consists of 267 nucleotides and supports the interaction with and among at least seven protein components: hPop1, hPop5, Rpp20, Rpp25, Rpp30, Rpp38, and Rpp40) and three additional proteins, hPop4, Rpp21 and Rpp14, have been reported to be associated with at least a subset of RNase MRP complexes [].This entry represents the p29 subunit (also known as Rpp29 or Pop4) of the related ribonucleoproteins ribonuclease (RNase) P and RNase MRP from eukaryotes []. Rpp29 has a conserved C-terminal domain with an Sm-like fold []. Rpp29 () catalyses the endonucleolytic cleavage of RNA, removing 5'-extranucleotides from tRNA precursor. It interacts with the Rpp25 and Pop5 subunits.
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Protein Domain
IPR042848 | Rpp38
Type: Family
Description: Ribonuclease P (Rnp) is a ubiquitous ribozyme that catalyzes a Mg2 -dependent hydrolysis to remove the 5'-leader sequence of precursor tRNA (pre-tRNA) in all three domains of life []. In bacteria, the catalytic RNA (typically ~120kDa) is aided by a small protein cofactor (~14kDa) []. Archaeal and eukaryote RNase P consist of a single RNA and archaeal RNase P has four or five proteins, while eukaryotic RNase P consists of 9 or 10 proteins. Eukaryotic and archaeal RNase P RNAs cooperatively function with protein subunits in catalysis [].Eukaryotic nuclear RNase P shares most of its protein components with another essential RNP enzyme, nucleolar RNase MRP []. RNase MRP (mitochondrial RNA processing) is an rRNA processing enzyme that cleaves various RNAs, including ribosomal, messenger, and mitochondrial RNAs. It can cleave a specific site within precursor rRNA to generate the mature 5'-end of 5.8S rRNA []. Despite its name, the vast majority of RNase MRP is localized in the nucleolus []. RNase MRP has been shown to cleave primers for mitochondrial DNA replication and CLB2 mRNA. In yeast, RNase MRP possesses one putatively catalytic RNA and at least 9 protein subunits (Pop1, Pop3-Pop8, Rpp1, Snm1 and Rmp1) []. Human RNase MRP complex consists of 267 nucleotides and supports the interaction with and among at least seven protein components: hPop1, hPop5, Rpp20, Rpp25, Rpp30, Rpp38, and Rpp40) and three additional proteins, hPop4, Rpp21 and Rpp14, have been reported to be associated with at least a subset of RNase MRP complexes [].This entry includes animal Rpp38, which is a component of the Rnp and the MRP ribonuclease complexes [].
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Publication
15916546 | -
First Author: Walker SC
Year: 2005
Journal: Biochem Soc Trans
Title: Probing the structure of Saccharomyces cerevisiae RNase MRP.
Volume: 33
Issue: Pt 3
Pages: 479-81
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Publication
21665995 | -
First Author: Marvin MC
Year: 2011
Journal: RNA
Title: Accumulation of noncoding RNA due to an RNase P defect in Saccharomyces cerevisiae.
Volume: 17
Issue: 8
Pages: 1441-50
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Publication
20627997 | -
First Author: Esakova O
Year: 2010
Journal: RNA
Title: Of proteins and RNA: the RNase P/MRP family.
Volume: 16
Issue: 9
Pages: 1725-47
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Protein Domain
IPR002730 | Rpp29/RNP1
Type: Family
Description: Ribonuclease P (Rnp) is a ubiquitous ribozyme that catalyzes a Mg2 -dependent hydrolysis to remove the 5'-leader sequence of precursor tRNA (pre-tRNA) in all three domains of life []. In bacteria, the catalytic RNA (typically ~120kDa) is aided by a small protein cofactor (~14kDa) []. Archaeal and eukaryote RNase P consist of a single RNA and archaeal RNase P has four or five proteins, while eukaryotic RNase P consists of 9 or 10 proteins. Eukaryotic and archaeal RNase P RNAs cooperatively function with protein subunits in catalysis [].Eukaryotic nuclear RNase P shares most of its protein components with another essential RNP enzyme, nucleolar RNase MRP []. RNase MRP (mitochondrial RNA processing) is an rRNA processing enzyme that cleaves various RNAs, including ribosomal, messenger, and mitochondrial RNAs. It can cleave a specific site within precursor rRNA to generate the mature 5'-end of 5.8S rRNA []. Despite its name, the vast majority of RNase MRP is localized in the nucleolus []. RNase MRP has been shown to cleave primers for mitochondrial DNA replication and CLB2 mRNA. In yeast, RNase MRP possesses one putatively catalytic RNA and at least 9 protein subunits (Pop1, Pop3-Pop8, Rpp1, Snm1 and Rmp1) []. Human RNase MRP complex consists of 267 nucleotides and supports the interaction with and among at least seven protein components: hPop1, hPop5, Rpp20, Rpp25, Rpp30, Rpp38, and Rpp40) and three additional proteins, hPop4, Rpp21 and Rpp14, have been reported to be associated with at least a subset of RNase MRP complexes [].This entry includes p29 subunit (also known as Rpp29 or Pop4) of the Ribonuclease P complex []. Its homologues from eukaryotes are also a subunit of the RNase MRP complex. The structure of the RNase P subunit, Rpp29, from Methanobacterium thermoautotrophicum has been determined. Mth Rpp29 is a member of the oligonucleotide/oligosaccharide binding fold family. It contains a structured β-barrel core and unstructured N- and C-terminal extensions bearing several highly conserved amino acid residues that could be involved in RNA contacts in the protein-RNA complex []. Rpp29 () catalyses the endonucleolytic cleavage of RNA, removing 5'-extranucleotides from tRNA precursor. It interacts with the Rpp25 and Pop5 subunits.
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Protein
Q9CR08
Organism: Mus musculus/domesticus
Length: 221  
Fragment?: false
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Publication
10352175 | -
First Author: van Eenennaam H
Year: 1999
Journal: Nucleic Acids Res
Title: hPop4: a new protein subunit of the human RNase MRP and RNase P ribonucleoprotein complexes.
Volume: 27
Issue: 12
Pages: 2465-72
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Publication
14673079 | -
First Author: Boomershine WP
Year: 2003
Journal: Proc Natl Acad Sci U S A
Title: Structure of Mth11/Mth Rpp29, an essential protein subunit of archaeal and eukaryotic RNase P.
Volume: 100
Issue: 26
Pages: 15398-403
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Publication
28971852 | -
First Author: Gopalan V
Year: 2018
Journal: RNA
Title: Chance and necessity in the evolution of RNase P.
Volume: 24
Issue: 1
Pages: 1-5
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Publication
30262633 | -
 
First Author: Lan P
Year: 2018
Journal: Science
Title: Structural insight into precursor tRNA processing by yeast ribonuclease P.
Volume: 362
Issue: 6415
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Publication
7731988 | -
First Author: Bussey H
Year: 1995
Journal: Proc Natl Acad Sci U S A
Title: The nucleotide sequence of chromosome I from Saccharomyces cerevisiae.
Volume: 92
Issue: 9
Pages: 3809-13
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Publication
10024167 | -
First Author: Jarrous N
Year: 1999
Journal: RNA
Title: Rpp14 and Rpp29, two protein subunits of human ribonuclease P.
Volume: 5
Issue: 2
Pages: 153-7
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Protein
Q9DB28
Organism: Mus musculus/domesticus
Length: 169  
Fragment?: false
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Protein
Q80UU2
Organism: Mus musculus/domesticus
Length: 280  
Fragment?: false
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Protein
A2AJG0
Organism: Mus musculus/domesticus
Length: 280  
Fragment?: false
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Protein
Q8BX36
Organism: Mus musculus/domesticus
Length: 266  
Fragment?: true
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Publication
16829535 | -
First Author: Terada A
Year: 2006
Journal: J Biochem
Title: Characterization of the archaeal ribonuclease P proteins from Pyrococcus horikoshii OT3.
Volume: 140
Issue: 2
Pages: 293-8
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Publication
28715256 | -
First Author: Kimura M
Year: 2017
Journal: Biosci Biotechnol Biochem
Title: Structural basis for activation of an archaeal ribonuclease P RNA by protein cofactors.
Volume: 81
Issue: 9
Pages: 1670-1680
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Publication
19468303 | -
First Author: Church DM
Year: 2009
Journal: PLoS Biol
Title: Lineage-specific biology revealed by a finished genome assembly of the mouse.
Volume: 7
Issue: 5
Pages: e1000112
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MouseMine is a collaboration between MGI at The Jackson Laboratory and the InterMine project at the Cambridge Systems Biology Centre. MouseMine is funded through a grant from the NIH/NHGRI.The Jackson Laboratory makes no representation about the suitability or accuracy of this software or data for any purpose, and makes no warranties, either express or implied, including merchantability and fitness for a particular purpose or that the use of this software or data will not infringe any third party patents, copyrights, trademarks, or other rights. the software and data are provided "as is". This software and data are provided to enhance knowledge and encourage progress in the scientific community and are to be used only for research and educational purposes. Any reproduction or use for commercial purpose is prohibited without the prior express written permission of the Jackson Laboratory.

Copyright © 2017 by The Jackson Laboratory. All Rights Reserved

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