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Search results 101 to 200 out of 287 for Msl3

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Type Details Score
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: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:342607
       
First Author: Birgit Meldal and Sandra Orchard (1). (1) European Bioinformatics Institute (EBI), Hinxton, Cambridgeshire, United Kingdom
Year: 2023
Title: Manual transfer of experimentally-verified manual GO annotation data to homologous complexes by curator judgment of sequence, composition and function similarity
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Publication
10725249 | J:60984
First Author: Ko MS
Year: 2000
Journal: Development
Title: Large-scale cDNA analysis reveals phased gene expression patterns during preimplantation mouse development.
Volume: 127
Issue: 8
Pages: 1737-49
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Publication
- | J:188991
     
First Author: The Jackson Laboratory
Year: 2012
Journal: MGI Direct Data Submission
Title: Alleles produced for the KOMP project by The Jackson Laboratory
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Publication
- | J:80155
       
First Author: Mouse Genome Informatics Scientific Curators
Year: 2002
Title: Mouse Genome Informatics Computational Sequence to Gene Associations for FANTOM2 data
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Publication
34321999 | J:313619
 
First Author: Bedogni F
Year: 2021
Journal: Front Mol Neurosci
Title: Cell-Type-Specific Gene Expression in Developing Mouse Neocortex: Intermediate Progenitors Implicated in Axon Development.
Volume: 14
Pages: 686034
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Publication
- | J:148605
     
First Author: Wellcome Trust Sanger Institute
Year: 2009
Journal: MGI Direct Data Submission
Title: Alleles produced for the KOMP project by the Wellcome Trust Sanger Institute
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Publication
- | J:171409
     
First Author: GUDMAP Consortium
Year: 2004
Journal: www.gudmap.org
Title: GUDMAP: the GenitoUrinary Development Molecular Anatomy Project
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Publication
- | J:211773
     
First Author: Mouse Genome Informatics and the International Mouse Phenotyping Consortium (IMPC)
Year: 2014
Journal: Database Release
Title: Obtaining and Loading Phenotype Annotations from the International Mouse Phenotyping Consortium (IMPC) Database
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Publication
16602821 | J:162220
First Author: Magdaleno S
Year: 2006
Journal: PLoS Biol
Title: BGEM: an in situ hybridization database of gene expression in the embryonic and adult mouse nervous system.
Volume: 4
Issue: 4
Pages: e86
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Publication
38355793 | J:345621
First Author: Adams DJ
Year: 2024
Journal: Nature
Title: Genetic determinants of micronucleus formation in vivo.
Volume: 627
Issue: 8002
Pages: 130-136
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Publication
- | J:293217
       
First Author: GemPharmatech
Year: 2020
Title: GemPharmatech Website.
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Publication
21677750 | J:173534
First Author: Skarnes WC
Year: 2011
Journal: Nature
Title: A conditional knockout resource for the genome-wide study of mouse gene function.
Volume: 474
Issue: 7351
Pages: 337-42
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Publication
- | J:326541
       
First Author: Cyagen Biosciences Inc.
Year: 2022
Title: Cyagen Biosciences Website.
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Publication
- | J:342587
       
First Author: AgBase, BHF-UCL, Parkinson's UK-UCL, dictyBase, HGNC, Roslin Institute, FlyBase and UniProtKB curators
Year: 2011
Title: Manual transfer of experimentally-verified manual GO annotation data to orthologs by curator judgment of sequence similarity
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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:68900
     
First Author: The Jackson Laboratory Mouse Radiation Hybrid Database
Year: 2004
Journal: Database Release
Title: Mouse T31 Radiation Hybrid Data Load
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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
- | 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: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:155221
     
First Author: Mouse Genome Informatics
Year: 2010
Journal: Database Release
Title: Protein Ontology Association Load.
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Allele
Msl3l2<+> | MGI:3809853
 
Name: MSL3 like 2; wild type
Allele Type: Not Specified
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Protein Coding Gene
MGP_CAROLIEiJ_G0015325 | -
Type: protein_coding_gene
Organism: Mus caroli
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Protein Coding Gene
MGP_129S1SvImJ_G0017235 | -
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGP_AJ_G0017211 | -
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGP_AKRJ_G0017171 | -
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGP_BALBcJ_G0017172 | -
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGP_C3HHeJ_G0016995 | -
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGI_C57BL6J_1920640 | -
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGP_C57BL6NJ_G0017631 | -
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGP_CASTEiJ_G0016568 | -
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGP_CBAJ_G0016967 | -
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGP_DBA2J_G0017072 | -
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGP_FVBNJ_G0017067 | -
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGP_LPJ_G0017147 | -
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGP_NODShiLtJ_G0017096 | -
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGP_NZOHlLtJ_G0017668 | -
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGP_PWKPhJ_G0016349 | -
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGP_WSBEiJ_G0016633 | -
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGP_PahariEiJ_G0030742 | -
Type: protein_coding_gene
Organism: Mus pahari
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Protein Coding Gene
MGP_SPRETEiJ_G0016135 | -
Type: protein_coding_gene
Organism: Mus spretus
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HT Experiment
GSE235777 | Loss Of Function of Male-Specific Lethal 3 (Msl3) Does Not Affect Spermatogenesis in Rodents
 
Experiment Type: RNA-Seq
Study Type: WT vs. Mutant
Source: GEO
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DO Term
DOID:0111838 | Basilicata-Akhtar syndrome
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Protein Domain
IPR037922 | MSL2
Type: Family
Description: E3 ubiquitin-protein ligase MSL2 (MSL2; [intenz:6.3.2.-]) is an E3 ubiquitin ligase that promotes monoubiquitination of histone H2B at 'Lys-35' (H2BK34Ub), but not that of H2A. It is a component of MSL complex [].The male-specific lethal (MSL) complex is a histone acetyltransferase with specificity for histone H4 'lysine-16' in chromatin. The complex consists of MOF, MSL1, MSL2, and MSL3 []. The complex was first identified in Drosophila.
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Publication
10786633 | -
First Author: Neal KC
Year: 2000
Journal: Biochim Biophys Acta
Title: A new human member of the MYST family of histone acetyl transferases with high sequence similarity to Drosophila MOF.
Volume: 1490
Issue: 1-2
Pages: 170-4
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Protein Domain
IPR037906 | KAT8
Type: Family
Description: Histone acetyltransferase KAT8 () has activity directed towards histones H3, H2A and H4 []and is the active component of the MSL and NSL complexes []. KAT8 autoacetylates itself on Lys-274 which is a requirement for binding to histone H4 []. In Drosophila melanogaster this protein is known as 'males-absent on the first protein' (MOF) [].The male-specific lethal (MSL) complex is a histone acetyltransferase with specificity for histone H4 'lysine-16' in chromatin. The complex consists of MOF, MSL1, MSL2, and MSL3 []. The complex was first identified in Drosophila.
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Publication
23084835 | -
First Author: Hallacli E
Year: 2012
Journal: Mol Cell
Title: Msl1-mediated dimerization of the dosage compensation complex is essential for male X-chromosome regulation in Drosophila.
Volume: 48
Issue: 4
Pages: 587-600
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Publication
20620954 | -
First Author: Raja SJ
Year: 2010
Journal: Mol Cell
Title: The nonspecific lethal complex is a transcriptional regulator in Drosophila.
Volume: 38
Issue: 6
Pages: 827-41
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Publication
22020126 | -
First Author: Yuan H
Year: 2012
Journal: EMBO J
Title: MYST protein acetyltransferase activity requires active site lysine autoacetylation.
Volume: 31
Issue: 1
Pages: 58-70
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Publication
2662307 | -
First Author: Felder RA
Year: 1989
Journal: Semin Nephrol
Title: Role of endogenous dopamine on renal sodium excretion.
Volume: 9
Issue: 1
Pages: 91-3
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Publication
16364921 | -
First Author: Joshi AA
Year: 2005
Journal: Mol Cell
Title: Eaf3 chromodomain interaction with methylated H3-K36 links histone deacetylation to Pol II elongation.
Volume: 20
Issue: 6
Pages: 971-8
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Publication
20536842 | -
 
First Author: Chen M
Year: 2010
Journal: Ann N Y Acad Sci
Title: Emerging role of the MORF/MRG gene family in various biological processes, including aging.
Volume: 1197
Pages: 134-41
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Publication
17173057 | -
First Author: Straub T
Year: 2007
Journal: Nat Rev Genet
Title: Dosage compensation: the beginning and end of generalization.
Volume: 8
Issue: 1
Pages: 47-57
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Publication
22421046 | -
First Author: Conrad T
Year: 2012
Journal: Dev Cell
Title: The MOF chromobarrel domain controls genome-wide H4K16 acetylation and spreading of the MSL complex.
Volume: 22
Issue: 3
Pages: 610-24
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Publication
22285924 | -
First Author: Eissenberg JC
Year: 2012
Journal: Gene
Title: Structural biology of the chromodomain: form and function.
Volume: 496
Issue: 2
Pages: 69-78
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Protein Domain
IPR008676 | MRG
Type: Family
Description: This entry represents MRG protein family, whose members include MORF4L1/2 (MRG15/MRGX) and MSL3L1/2 from humans, ESA1-associated factor 3 (Eaf3) from yeasts and male-specific lethal 3 (MSL3) from flies. They contain an N-terminal chromodomain that binds H3K36me3, a histone mark associated with transcription elongation []. Saccharomyces cerevisiae Eaf3 is a component of both NuA4 histone acetyltransferase and Rpd3S histone deacetylase complexes [, ]. It was found that Eaf3 mediates preferential deacetylation of coding regions through an interaction between the Eaf3 chromodomain and methylated H3-K36 that presumably results in preferential association of the Rpd3 complex []. The Drosophila MSL proteins (MSL1, MSL2, MSL3, MLE, and MOF) are essential for elevating transcription of the single X chromosome in the male (X chromosome dosage compensation) []. Together with two partlyredundant non-coding RNAs, roX1 and roX2, they form the MSL complex, also known as dosage compensation complex or DCC. MSL complex upregulates transcription by spreading the histone H4 Lys16 (H4K16) acetyl mark []and allows compensation for the loss of one X-chromosomal allele by increasing the transcription from the retained allele []. The MSL3 chromodomain has been shown to bind DNA and methylated H4K20 in vitro []. Human MORF4L1, also known as MRG15, is a component of the NuA4 histone acetyltransferase complex that transcriptional activates genes by acetylation of nucleosomal histones H4 and H2A. This modification may both alter nucleosome - DNA interactions and promote interaction of the modified histones with other proteins which positively regulate transcription. NuA4 complex may also play a direct role in DNA repair when directly recruited to sites of DNA damage. MRG15 is also a component of the mSin3A/Pf1/HDAC complex which acts to repress transcription by deacetylation of nucleosomal histones. MRG15 was found to interact with PALB2, a tumour suppressor protein that plays a crucial role in DNA damage repair by homologous recombination []. Furthermore, MRG15 play a role in the response to double strand breaks (DSBs) by recruiting the BRCA complex (BRCA1, PALB2, BRCA2 and RAD51) to sites of damaged DNA [, ].
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Protein Domain
IPR000953 | Chromo/chromo_shadow_dom
Type: Domain
Description: The CHROMO (CHRromatin Organization MOdifier) domain [, , , ]is a conserved region of around 60 amino acids, originally identified in Drosophila modifiers of variegation. These are proteins that alter the structure of chromatin to the condensed morphology of heterochromatin, a cytologically visible condition where gene expression is repressed. In one of these proteins, Polycomb, the chromo domain has been shown to be important for chromatin targeting. Proteins that contain a chromo domain appear to fall into 3 classes. The first class includes proteins having an N-terminal chromo domain followed by a region termed the chromo shadow domain, with weak but significant sequence similarity to the N-terminal chromo domain [], eg. Drosophila and human heterochromatin protein Su(var)205 (HP1). The second class includes proteins with a single chromo domain, eg. Drosophila protein Polycomb (Pc); mammalian modifier 3; human Mi-2 autoantigen and several yeast and Caenorhabditis elegans hypothetical proteins. In the third class paired tandem chromo domains are found, eg. in mammalian DNA-binding/helicase proteins CHD-1 to CHD-4 and yeast protein CHD1.Functional dissections of chromo domain proteins suggests a mechanistic role for chromo domains in targeting chromo domain proteins to specific regions of the nucleus. The mechanism of targeting may involve protein-protein and/or protein/nucleic acid interactions. Hence, several line of evidence show that the HP1 chromo domain is a methyl-specific histone binding module, whereas the chromo domain of two protein components of the drosophila dosage compensation complex, MSL3 and MOF, contain chromo domains that bind to RNA in vitro [].The high resolution structures of HP1-family protein chromo and chromo shadow domain reveal a conserved chromo domain fold motif consisting of three β-strands packed against an α-helix. The chromo domain fold belongs to the OB (oligonucleotide/oligosaccharide binding)-fold class found in a variety of prokaryotic and eukaryotic nucleic acid binding protein [].
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Protein Domain
IPR023780 | Chromo_domain
Type: Domain
Description: The CHROMO (CHRromatin Organization MOdifier) domain [, , , ]is a conserved region of around 60 amino acids, originally identified in Drosophila modifiers of variegation. These are proteins that alter the structure of chromatin to the condensed morphology of heterochromatin, a cytologically visible condition where gene expression is repressed. In one of these proteins, Polycomb, the chromo domain has been shown to be important for chromatin targeting. Proteins that contain a chromo domain appear to fall into 3 classes. The first class includes proteins having an N-terminal chromo domain followed by a region termed the chromo shadow domain, with weak but significant sequence similarity to the N-terminal chromo domain [], eg. Drosophila and human heterochromatin protein Su(var)205 (HP1). The second class includes proteins with a single chromo domain, eg. Drosophila protein Polycomb (Pc); mammalian modifier 3; human Mi-2 autoantigen and several yeast and Caenorhabditis elegans hypothetical proteins. In the third class paired tandem chromo domains are found, eg. in mammalian DNA-binding/helicase proteins CHD-1 to CHD-4 and yeast protein CHD1.Functional dissections of chromo domain proteins suggests a mechanistic role for chromo domains in targeting chromo domain proteins to specific regions of the nucleus. The mechanism of targeting may involve protein-protein and/or protein/nucleic acid interactions. Hence, several line of evidence show that the HP1 chromo domain is a methyl-specific histone binding module, whereas the chromo domain of two protein components of the drosophila dosage compensation complex, MSL3 and MOF, contain chromo domains that bind to RNA in vitro [].The high resolution structures of HP1-family protein chromo and chromo shadow domain reveal a conserved chromo domain fold motif consisting of three β-strands packed against an α-helix. The chromo domain fold belongs to the OB (oligonucleotide/oligosaccharide binding)-fold class found in a variety of prokaryotic and eukaryotic nucleic acid binding protein [].
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Protein Domain
IPR023779 | Chromodomain_CS
Type: Conserved_site
Description: The CHROMO (CHRromatin Organization MOdifier) domain [, , , ]is a conserved region of around 60 amino acids, originally identified in Drosophila modifiers of variegation. These are proteins that alter the structure of chromatin to the condensed morphology of heterochromatin, a cytologically visible condition where gene expression is repressed. In one of these proteins, Polycomb, the chromo domain has been shown to be important for chromatin targeting. Proteins that contain a chromo domain appear to fall into 3 classes. The first class includes proteins having an N-terminal chromo domain followed by a region termed the chromo shadow domain, with weak but significant sequence similarity to the N-terminal chromo domain [], eg. Drosophila and human heterochromatin protein Su(var)205 (HP1). The second class includes proteins with a single chromo domain, eg. Drosophila protein Polycomb (Pc); mammalian modifier 3; human Mi-2 autoantigen and several yeast and Caenorhabditis elegans hypothetical proteins. In the third class paired tandem chromo domains are found, eg. in mammalian DNA-binding/helicase proteins CHD-1 to CHD-4 and yeast protein CHD1.Functional dissections of chromo domain proteins suggests a mechanistic role for chromo domains in targeting chromo domain proteins to specific regions of the nucleus. The mechanism of targeting may involve protein-protein and/or protein/nucleic acid interactions. Hence, several line of evidence show that the HP1 chromo domain is a methyl-specific histone binding module, whereas the chromo domain of two protein components of the drosophila dosage compensation complex, MSL3 and MOF, contain chromo domains that bind to RNA in vitro [].The high resolution structures of HP1-family protein chromo and chromo shadow domain reveal a conserved chromo domain fold motif consisting of three β-strands packed against an α-helix. The chromo domain fold belongs to the OB (oligonucleotide/oligosaccharide binding)-fold class found in a variety of prokaryotic and eukaryotic nucleic acid binding protein [].This entry represents a conserved site in the chromo domain.
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Publication
11574148 | -
First Author: Eissenberg JC
Year: 2001
Journal: Gene
Title: Molecular biology of the chromo domain: an ancient chromatin module comes of age.
Volume: 275
Issue: 1
Pages: 19-29
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Protein
Q9D5D8
Organism: Mus musculus/domesticus
Length: 503  
Fragment?: false
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Publication
1708124 | J:32398
First Author: Singh PB
Year: 1991
Journal: Nucleic Acids Res
Title: A sequence motif found in a Drosophila heterochromatin protein is conserved in animals and plants.
Volume: 19
Issue: 4
Pages: 789-94
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Protein
Q9WTK2
Organism: Mus musculus/domesticus
Length: 593  
Fragment?: false
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Protein
Q9QXV1
Organism: Mus musculus/domesticus
Length: 362  
Fragment?: false
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Protein
P30658
Organism: Mus musculus/domesticus
Length: 519  
Fragment?: false
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Protein
Q3ULG7
Organism: Mus musculus/domesticus
Length: 359  
Fragment?: true
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Protein
A0A0G2JFK1
Organism: Mus musculus/domesticus
Length: 74  
Fragment?: true
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Protein
Q9CU16
Organism: Mus musculus/domesticus
Length: 150  
Fragment?: true
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Protein
F7CDZ7
Organism: Mus musculus/domesticus
Length: 333  
Fragment?: true
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Protein
Q3UQV4
Organism: Mus musculus/domesticus
Length: 503  
Fragment?: false
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Protein
F6WJA6
Organism: Mus musculus/domesticus
Length: 180  
Fragment?: true
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Protein
D3Z5F6
Organism: Mus musculus/domesticus
Length: 133  
Fragment?: false
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Protein
A0A0G2JEP1
Organism: Mus musculus/domesticus
Length: 120  
Fragment?: true
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Protein
Q3UX18
Organism: Mus musculus/domesticus
Length: 168  
Fragment?: true
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Protein
Q3TZG6
Organism: Mus musculus/domesticus
Length: 519  
Fragment?: false
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Protein
D3Z329
Organism: Mus musculus/domesticus
Length: 127  
Fragment?: true
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Protein
Q7TQ22
Organism: Mus musculus/domesticus
Length: 503  
Fragment?: false
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Publication
7667093 | -
First Author: Aasland R
Year: 1995
Journal: Nucleic Acids Res
Title: The chromo shadow domain, a second chromo domain in heterochromatin-binding protein 1, HP1.
Volume: 23
Issue: 16
Pages: 3168-73
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Publication
7501439 | -
First Author: Koonin EV
Year: 1995
Journal: Nucleic Acids Res
Title: The chromo superfamily: new members, duplication of the chromo domain and possible role in delivering transcription regulators to chromatin.
Volume: 23
Issue: 21
Pages: 4229-33
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Publication
1982376 | -
First Author: Paro R
Year: 1990
Journal: Trends Genet
Title: Imprinting a determined state into the chromatin of Drosophila.
Volume: 6
Issue: 12
Pages: 416-21
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Protein
A0A087WNL5
Organism: Mus musculus/domesticus
Length: 100  
Fragment?: false
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Protein
H3BK45
Organism: Mus musculus/domesticus
Length: 121  
Fragment?: true
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Protein
D3Z0U2
Organism: Mus musculus/domesticus
Length: 42  
Fragment?: true
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Protein
Q8C9F3
Organism: Mus musculus/domesticus
Length: 347  
Fragment?: true
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Protein
D3Z1A9
Organism: Mus musculus/domesticus
Length: 71  
Fragment?: false
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Protein
A0A0U1RNW7
Organism: Mus musculus/domesticus
Length: 176  
Fragment?: true
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Protein
Q8VDS3
Organism: Mus musculus/domesticus
Length: 158  
Fragment?: false
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Protein
P83917
Organism: Mus musculus/domesticus
Length: 185  
Fragment?: false
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Protein
P23198
Organism: Mus musculus/domesticus
Length: 183  
Fragment?: false
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Protein
Q61686
Organism: Mus musculus/domesticus
Length: 191  
Fragment?: false
•
•
•
•
•
Protein
Q3TYA6
Organism: Mus musculus/domesticus
Length: 858  
Fragment?: false
•
•
•
•
•
Protein
O55187
Organism: Mus musculus/domesticus
Length: 551  
Fragment?: false
•
•
•
•
•
Protein
Q9DBY5
Organism: Mus musculus/domesticus
Length: 414  
Fragment?: false
•
•
•
•
•
Protein
Q9DCC5
Organism: Mus musculus/domesticus
Length: 183  
Fragment?: false
•
•
•
•
•
Protein
Q3UK98
Organism: Mus musculus/domesticus
Length: 396  
Fragment?: false
•
•
•
•
•
Protein
Q7TPM0
Organism: Mus musculus/domesticus
Length: 138  
Fragment?: false
•
•
•
•
•
Protein
Q9JJB4
Organism: Mus musculus/domesticus
Length: 843  
Fragment?: false
•
•
•
•
•




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.

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