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Search results 101 to 183 out of 183 for Ddb2

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Type Details Score
DO Term
DOID:0110846 | xeroderma pigmentosum group E
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Publication
20128879 | -
First Author: Biedermann S
Year: 2010
Journal: Plant J
Title: The DDB1a interacting proteins ATCSA-1 and DDB2 are critical factors for UV-B tolerance and genomic integrity in Arabidopsis thaliana.
Volume: 62
Issue: 3
Pages: 404-15
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Strain
MGI:6770688 | C57BL/6JSmoc-Ddb2<em1Smoc>/Smoc
Attribute String: coisogenic, endonuclease-mediated mutation, mutant strain
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Publication
25578727 | -
First Author: Zhang L
Year: 2015
Journal: Cell Rep
Title: The deubiquitinating enzyme USP24 is a regulator of the UV damage response.
Volume: 10
Issue: 2
Pages: 140-7
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Publication
26568301 | -
First Author: Wang YC
Year: 2016
Journal: Oncogene
Title: Variants of ubiquitin-specific peptidase 24 play a crucial role in lung cancer malignancy.
Volume: 35
Issue: 28
Pages: 3669-80
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Publication
25814533 | -
First Author: Peterson LF
Year: 2015
Journal: Blood
Title: Targeting deubiquitinase activity with a novel small-molecule inhibitor as therapy for B-cell malignancies.
Volume: 125
Issue: 23
Pages: 3588-97
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Publication
29695420 | -
 
First Author: Sun Y
Year: 2018
Journal: J Virol
Title: Human Cytomegalovirus Protein pUL38 Prevents Premature Cell Death by Binding to Ubiquitin-Specific Protease 24 and Regulating Iron Metabolism.
Volume: 92
Issue: 13
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Protein Domain
IPR033382 | USP24
Type: Family
Description: Ubiquitin-specific peptidase 24 (USP24, MEROPS identifier C19.047) is a de-ubiquitinating enzyme that is associated with late-onset Parkinson's Disease []. The enzyme is known to remove ubiquitin from damage-specific DNA-binding protein 2 (DDB2), increasing its stability. DDB2 is involved in DNA damage recognition in the nucleotide excision repair pathway, and is a component of an E3 ligase that targets XPC, histones and DDB2 itself []. USP24 also de-ubiquitinates p53, and cells are resistant to apoptosis following UV irradiation if USP24 is depleted because p53 is stabilized []. Single-nucleotide polymorphisms of the USP24 gene have been identified in lung cancer malignancy and could be diagnostic markers for the disease []. The USP24 gene is up-regulated when the USP9X gene is down-regulated by shRNA, leading to increased survival of B-cell myeloma cells []. USP24 positively regulates ferritinophagy, a process in which ferritin is degraded in lysosomes and releases free iron [].
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Publication
19481525 | J:150427
First Author: Liu L
Year: 2009
Journal: Mol Cell
Title: CUL4A abrogation augments DNA damage response and protection against skin carcinogenesis.
Volume: 34
Issue: 4
Pages: 451-60
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Publication
20302855 | -
First Author: Wu YR
Year: 2010
Journal: Clin Chim Acta
Title: Ubiquitin specific proteases USP24 and USP40 and ubiquitin thiolesterase UCHL1 polymorphisms have synergic effect on the risk of Parkinson's disease among Taiwanese.
Volume: 411
Issue: 13-14
Pages: 955-8
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Protein
Q8BX58
Organism: Mus musculus/domesticus
Length: 313  
Fragment?: false
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Publication
23689509 | J:201926
First Author: Liu C
Year: 2013
Journal: J Biol Chem
Title: COP9 signalosome subunit Csn8 is involved in maintaining proper duration of the G1 phase.
Volume: 288
Issue: 28
Pages: 20443-52
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Publication
18298797 | -
First Author: Oren-Giladi P
Year: 2008
Journal: Genes Cells
Title: Cop9 signalosome subunit 8 (CSN8) is essential for Drosophila development.
Volume: 13
Issue: 3
Pages: 221-31
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Publication
11418127 | -
First Author: Hong X
Year: 2001
Journal: FEBS Lett
Title: CSN3 interacts with IKKgamma and inhibits TNF- but not IL-1-induced NF-kappaB activation.
Volume: 499
Issue: 1-2
Pages: 133-6
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Protein Domain
IPR045237 | COPS7/eIF3m
Type: Family
Description: This entry includes eIF3m and COPS7A/B. eIF3m is a component of the eukaryotic translation initiation factor 3 (eIF-3) complex, which is involved in protein synthesis and, together with other initiation factors, stimulates binding of mRNA and methionyl-tRNAi to the 40S ribosome []. The COP9 signalosome (CSN) is a conserved protein complex that regulates the ubiquitin (Ubl) conjugation pathway by mediating the deneddylation of the cullin subunits of SCF-type E3 ligase complexes [], which leads to a decrease in Ubl ligase activity of SCF-type complexes such as SCF, CSA or DDB2 []. Protein kinases CK2 and D, which phosphorylate proteins such as cJun and p53 resulting in their degradation by the ubiquitin-26S proteasome system, also binds to CSN [, ]. The mammalian CSN typically consistis of eight subunits designated CSN1-CSN8. The fission yeast possesses a smaller version of the CSN, consisting only of six subunits, whereas a more distant CSN-like complex has been described in Saccharomyces cerevisiae [].
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Protein Domain
IPR027530 | Csn7B
Type: Family
Description: The COP9 signalosome (CSN) is a conserved protein complex that regulates the ubiquitin (Ubl) conjugation pathway by mediating the deneddylation of the cullin subunits of SCF-type E3 ligase complexes [], which leads to a decrease in Ubl ligase activity of SCF-type complexes such as SCF, CSA or DDB2 []. Protein kinases CK2 and D, which phosphorylate proteins such as cJun and p53 resulting in their degradation by the ubiquitin-26S proteasome system, also binds to CSN [, ]. The mammalian CSN typically consistis of eight subunits designated CSN1-CSN8. The fission yeast possesses a smaller version of the CSN, consisting only of six subunits, whereas a more distant CSN-like complex has been described in Saccharomyces cerevisiae [].In mammals, the CSN7 subunit is encoded by two similar genes, CSN7a and CSN7b []. This entry represents subunit CSN7b.
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Protein Domain
IPR037750 | COPS2
Type: Family
Description: The COP9 signalosome (CSN) is a conserved protein complex that regulates the ubiquitin (Ubl) conjugation pathway by mediating the deneddylation of the cullin subunits of SCF-type E3 ligase complexes [], which leads to a decrease in Ubl ligase activity of SCF-type complexes such as SCF, CSA or DDB2 []. Protein kinases CK2 and D, which phosphorylate proteins such as cJun and p53 resulting in their degradation by the ubiquitin-26S proteasome system, also binds to CSN [, ]. The mammalian CSN typically consistis of eight subunits designated CSN1-CSN8. The fission yeast possesses a smaller version of the CSN, consisting only of six subunits, whereas a more distant CSN-like complex has been described in Saccharomyces cerevisiae [].This entry includes the COP9 signalosome complex (CSN) subunits 2 and 10. Subunit 10 is found only in some yeasts and is uncharacterized.
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Protein Domain
IPR037753 | CSN3
Type: Family
Description: The COP9 signalosome (CSN) is a conserved protein complex that regulates the ubiquitin (Ubl) conjugation pathway by mediating the deneddylation of the cullin subunits of SCF-type E3ligase complexes [], which leads to a decrease in Ubl ligase activity of SCF-type complexes such as SCF, CSA or DDB2 []. Protein kinases CK2 and D, which phosphorylate proteins such as cJun and p53 resulting in their degradation by the ubiquitin-26S proteasome system, also binds to CSN [, ]. The mammalian CSN typically consistis of eight subunits designated CSN1-CSN8. The fission yeast possesses a smaller version of the CSN, consisting only of six subunits, whereas a more distant CSN-like complex has been described in Saccharomyces cerevisiae [].This entry includes the COP9 signalosome complex (CSN) subunit 3 (CSN3). Interactions have been identified between CSN3 and IKKgamma, which prevents activation of transcription factor nuclear factor kappaB (NF-kappaB) []; and the Int-6 protein subunit of the eIF3 translation initiation factor [].
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Protein Domain
IPR033205 | COP9_CSN8
Type: Family
Description: The COP9 signalosome (CSN) is a conserved protein complex that regulates the ubiquitin (Ubl) conjugation pathway by mediating the deneddylation of the cullin subunits of SCF-type E3 ligase complexes [], which leads to a decrease in Ubl ligase activity of SCF-type complexes such as SCF, CSA or DDB2 []. Protein kinases CK2 and D, which phosphorylate proteins such as cJun and p53 resulting in their degradation by the ubiquitin-26S proteasome system, also binds to CSN [, ]. The mammalian CSN typically consistis of eight subunits designated CSN1-CSN8. The fission yeast possesses a smaller version of the CSN, consisting only of six subunits, whereas a more distant CSN-like complex has been described in Saccharomyces cerevisiae [].In the complex, CSN8, which is the smallest subunit, probably interacts directly with CSN3, CSN4 and CSN7 (CSN7A or CSN7B). It is necessary for assembly of the complex []. CSN8 plays an important role in maintaining the proper duration of the G1 phase of the cell cycle [].
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Protein
D6RI85
Organism: Mus musculus/domesticus
Length: 103  
Fragment?: false
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Protein
D6RH36
Organism: Mus musculus/domesticus
Length: 62  
Fragment?: false
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Protein
D3Z6T8
Organism: Mus musculus/domesticus
Length: 199  
Fragment?: true
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Publication
11564863 | J:320036
First Author: Martinez E
Year: 2001
Journal: Mol Cell Biol
Title: Human STAGA complex is a chromatin-acetylating transcription coactivator that interacts with pre-mRNA splicing and DNA damage-binding factors in vivo.
Volume: 21
Issue: 20
Pages: 6782-95
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Publication
30297359 | J:271163
First Author: Chan CH
Year: 2019
Journal: Mol Cancer Res
Title: DNA Damage, Liver Injury, and Tumorigenesis: Consequences of DDX3X Loss.
Volume: 17
Issue: 2
Pages: 555-566
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Publication
22705887 | J:202206
First Author: Durik M
Year: 2012
Journal: Circulation
Title: Nucleotide excision DNA repair is associated with age-related vascular dysfunction.
Volume: 126
Issue: 4
Pages: 468-78
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Publication
37716414 | J:343192
 
First Author: Yang Z
Year: 2023
Journal: Toxicol Appl Pharmacol
Title: NAT10 regulates the repair of UVB-induced DNA damage and tumorigenicity.
Volume: 477
Pages: 116688
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Publication
34452996 | J:309589
 
First Author: Yang Z
Year: 2021
Journal: Proc Natl Acad Sci U S A
Title: METTL14 facilitates global genome repair and suppresses skin tumorigenesis.
Volume: 118
Issue: 35
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Publication
11337588 | -
First Author: Lyapina S
Year: 2001
Journal: Science
Title: Promotion of NEDD-CUL1 conjugate cleavage by COP9 signalosome.
Volume: 292
Issue: 5520
Pages: 1382-5
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Publication
12628923 | -
First Author: Uhle S
Year: 2003
Journal: EMBO J
Title: Protein kinase CK2 and protein kinase D are associated with the COP9 signalosome.
Volume: 22
Issue: 6
Pages: 1302-12
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Publication
11285227 | -
First Author: Bech-Otschir D
Year: 2001
Journal: EMBO J
Title: COP9 signalosome-specific phosphorylation targets p53 to degradation by the ubiquitin system.
Volume: 20
Issue: 7
Pages: 1630-9
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Publication
18926707 | -
First Author: Wei N
Year: 2008
Journal: Trends Biochem Sci
Title: The COP9 signalosome: more than a protease.
Volume: 33
Issue: 12
Pages: 592-600
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Protein
D3Z0S0
Organism: Mus musculus/domesticus
Length: 79  
Fragment?: true
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Publication
18850735 | -
First Author: Fang L
Year: 2008
Journal: J Proteome Res
Title: Characterization of the human COP9 signalosome complex using affinity purification and mass spectrometry.
Volume: 7
Issue: 11
Pages: 4914-25
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Publication
12220626 | -
First Author: Hoareau Alves K
Year: 2002
Journal: FEBS Lett
Title: Association of the mammalian proto-oncoprotein Int-6 with the three protein complexes eIF3, COP9 signalosome and 26S proteasome.
Volume: 527
Issue: 1-3
Pages: 15-21
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Protein
A2A701
Organism: Mus musculus/domesticus
Length: 143  
Fragment?: true
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Protein
A0A087WPM5
Organism: Mus musculus/domesticus
Length: 80  
Fragment?: true
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Publication
17337451 | -
First Author: da Silva Correia J
Year: 2007
Journal: J Biol Chem
Title: The subunit CSN6 of the COP9 signalosome is cleaved during apoptosis.
Volume: 282
Issue: 17
Pages: 12557-65
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Publication
18060501 | -
First Author: Hetfeld BK
Year: 2008
Journal: Apoptosis
Title: The COP9 signalosome-mediated deneddylation is stimulated by caspases during apoptosis.
Volume: 13
Issue: 2
Pages: 187-95
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Publication
22575649 | J:184509
First Author: Zhang H
Year: 2012
Journal: FEBS Lett
Title: The crystal structure of the MPN domain from the COP9 signalosome subunit CSN6.
Volume: 586
Issue: 8
Pages: 1147-53
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Publication
12183637 | -
First Author: Cope GA
Year: 2002
Journal: Science
Title: Role of predicted metalloprotease motif of Jab1/Csn5 in cleavage of Nedd8 from Cul1.
Volume: 298
Issue: 5593
Pages: 608-11
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Publication
21102408 | -
First Author: Granata A
Year: 2011
Journal: EMBO J
Title: CSN complex controls the stability of selected synaptic proteins via a torsinA-dependent process.
Volume: 30
Issue: 1
Pages: 181-93
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Publication
12020345 | -
First Author: Wang Y
Year: 2002
Journal: Biochem J
Title: Polyamine-modulated factor 1 binds to the human homologue of the 7a subunit of the Arabidopsis COP9 signalosome: implications in gene expression.
Volume: 366
Issue: Pt 1
Pages: 79-86
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Protein Domain
IPR037754 | CSN4
Type: Family
Description: The COP9 signalosome (CSN) is a conserved protein complex that regulates the ubiquitin (Ubl) conjugation pathway by mediating the deneddylation of the cullin subunits of SCF-type E3 ligase complexes [], which leads to a decrease in Ubl ligase activity of SCF-type complexes such as SCF, CSA or DDB2 []. Protein kinases CK2 and D, which phosphorylate proteins such as cJun and p53 resulting in their degradation by the ubiquitin-26S proteasome system, also binds to CSN [, ]. The mammalian CSN typically consistis of eight subunits designated CSN1-CSN8. The fission yeast possesses a smaller version of the CSN, consisting only of six subunits, whereas a more distant CSN-like complex has been described in Saccharomyces cerevisiae [].This entry includes the COP9 signalosome complex (CSN) subunit 4 (CSN4). CSN4 also binds to the AAA+ ATPase torsinA, and CSN4 and torsinA in turn stabilize snapin, which is phosphorylated by protein kinase D, and stonin 2, which is neddylated. A mutation in torsinA leads to DYT1 dystonia, and overexpression of the mutant leads to a reduction of stonin 2 expression, suggesting that the mutant compromises the role of torsinA in protein stabilization and synaptic vesicle recycling [].
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Protein Domain
IPR037757 | COPS7A
Type: Family
Description: The COP9 signalosome (CSN) is a conserved protein complex that regulates the ubiquitin (Ubl) conjugation pathway by mediating the deneddylation of the cullin subunits of SCF-type E3 ligase complexes [], which leads to a decrease in Ubl ligase activity of SCF-type complexes such as SCF, CSA or DDB2 []. Protein kinases CK2 and D, which phosphorylate proteins such as cJun and p53 resulting in their degradation by the ubiquitin-26S proteasome system, also binds to CSN [, ]. The mammalian CSN typically consistis of eight subunits designated CSN1-CSN8. The fission yeast possesses a smaller version of the CSN, consisting only of six subunits, whereas a more distant CSN-like complex has been described in Saccharomyces cerevisiae [].In mammals, the CSN7 subunit is encoded by two similar genes, CSN7A and CSN7B []. This entry irepresents the COP9 signalosome complex (CSN) subunit 7a (CSN7A). Either CSN7A or CSN7B can be a component of CSN. CSN7A binds to polyamine-modulated factor 1, and each competes with the other for binding to NF-E2 related factor-2 (Nrf-2). Binding to Nrf-2 regulates transcription of spermidine/spermine N(1)-acetyltransferase []. CSN7A also binds the Int-6 protein subunit of the eIF3 translation initiation factor []; and protein kinases CK2 and D, which phosphorylate proteins such as cJun and p53, resulting in their degradation by the ubiquitin-26S proteasome system [].
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Protein Domain
IPR037740 | CSN5
Type: Family
Description: The COP9 signalosome (CSN) is a conserved protein complex that regulates the ubiquitin (Ubl) conjugation pathway by mediating the deneddylation of the cullin subunits of SCF-type E3 ligase complexes [], which leads to a decrease in Ubl ligase activity of SCF-type complexes such as SCF, CSA or DDB2 []. Protein kinases CK2 and D, which phosphorylate proteins such as cJun and p53 resulting in their degradation by the ubiquitin-26S proteasome system, also binds to CSN [, ]. The mammalian CSN typically consistis of eight subunits designated CSN1-CSN8. The fission yeast possesses a smaller version of the CSN, consisting only of six subunits, whereas a more distant CSN-like complex has been described in Saccharomyces cerevisiae [].COP9 signalosome complex subunit 5 (Rri1, CSN5 or JAB1) is a metallo-isopeptidase (MEROPS identifier M67.002) that releases the ubiquitin-like protein Nedd8 from the Cul1 subunit of SCF ubiquitin ligases []. Rri1 binds a zinc ion via the histidines in an HXH motif and an aspartic acid C-terminal to this motif []. This entry includes CSN5 homologues from yeast to human.
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Protein Domain
IPR033859 | MPN_CSN6
Type: Family
Description: The COP9 signalosome (CSN) is a conserved protein complex that regulates the ubiquitin (Ubl) conjugation pathway by mediating the deneddylation of the cullin subunits of SCF-type E3 ligase complexes [], which leads to a decrease in Ubl ligase activity of SCF-type complexes such as SCF, CSA or DDB2 []. Protein kinases CK2 and D, which phosphorylate proteins such as cJun and p53 resulting in their degradation by the ubiquitin-26S proteasome system, also binds to CSN [, ]. The mammalian CSN typically consistis of eight subunits designated CSN1-CSN8. The fission yeast possesses a smaller version of the CSN, consisting only of six subunits, whereas a more distant CSN-like complex has been described in Saccharomyces cerevisiae [].CSN6 (COP9 signalosome subunit 6; COP9 subunit 6; MOV34 homolog, 34 kD; MEROPS identifier M67.972) is one of the eight subunits of COP9 signalosome. CSN6 is an MPN-domain protein that directly interacts with the MPN+-domain subunit CSN5 []. It is cleaved during apoptosis by activated caspases. CSN6 processing occurs in CSN/CRL (cullin-RING Ub ligase) complexes and is followed by the cleavage of Rbx1, the direct interaction partner of CSN6 []. CSN6 cleavage enhances CSN-mediated deneddylating activity (i.e. cleavage of ubiquitin-like protein Nedd8 (neural precursor cell expressed, developmentally downregulated 8)) in the cullin 1 in cells []. The cleavage of Rbx1 and increased deneddylation of cullins inactivate CRLs and presumably stabilize pro-apoptotic factors for final apoptotic steps. While CSN6 shows a typical MPN metalloprotease fold, it lacks the canonical JAMM motif, and therefore does not show catalytic isopeptidase activity.
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Protein
Q9CZ04
Organism: Mus musculus/domesticus
Length: 275  
Fragment?: false
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Protein
Q8BV13
Organism: Mus musculus/domesticus
Length: 264  
Fragment?: false
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Protein
D3YVI6
Organism: Mus musculus/domesticus
Length: 176  
Fragment?: true
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Protein
D3Z440
Organism: Mus musculus/domesticus
Length: 226  
Fragment?: true
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Protein
Q3TDL0
Organism: Mus musculus/domesticus
Length: 264  
Fragment?: false
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Protein
D3Z1R9
Organism: Mus musculus/domesticus
Length: 206  
Fragment?: true
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Protein
D3YV99
Organism: Mus musculus/domesticus
Length: 244  
Fragment?: true
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Protein
O88543
Organism: Mus musculus/domesticus
Length: 423  
Fragment?: false
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Protein
Q8VBV7
Organism: Mus musculus/domesticus
Length: 209  
Fragment?: false
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Protein
F6YCA7
Organism: Mus musculus/domesticus
Length: 244  
Fragment?: true
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Protein
Q3UQL2
Organism: Mus musculus/domesticus
Length: 423  
Fragment?: false
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Protein
Q3TEA5
Organism: Mus musculus/domesticus
Length: 134  
Fragment?: true
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Protein
A2A702
Organism: Mus musculus/domesticus
Length: 242  
Fragment?: false
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Protein
O88544
Organism: Mus musculus/domesticus
Length: 406  
Fragment?: false
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Protein
O35864
Organism: Mus musculus/domesticus
Length: 334  
Fragment?: false
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Protein
P61202
Organism: Mus musculus/domesticus
Length: 443  
Fragment?: false
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Protein
O88545
Organism: Mus musculus/domesticus
Length: 324  
Fragment?: false
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Protein
Q99JX4
Organism: Mus musculus/domesticus
Length: 374  
Fragment?: false
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Protein
D3Z0F5
Organism: Mus musculus/domesticus
Length: 297  
Fragment?: false
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Protein
Q14AI7
Organism: Mus musculus/domesticus
Length: 406  
Fragment?: false
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Protein
Q3V0K7
Organism: Mus musculus/domesticus
Length: 220  
Fragment?: false
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Protein
A2AQE4
Organism: Mus musculus/domesticus
Length: 402  
Fragment?: false
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Protein
Q3V3N6
Organism: Mus musculus/domesticus
Length: 450  
Fragment?: false
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Protein
A0A087WQA8
Organism: Mus musculus/domesticus
Length: 210  
Fragment?: true
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Protein
Q3TIJ1
Organism: Mus musculus/domesticus
Length: 406  
Fragment?: false
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Protein
Q3UIT2
Organism: Mus musculus/domesticus
Length: 324  
Fragment?: false
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Protein
A0A087WQ60
Organism: Mus musculus/domesticus
Length: 147  
Fragment?: true
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Protein
Q3UK65
Organism: Mus musculus/domesticus
Length: 443  
Fragment?: false
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Protein
F6QTS1
Organism: Mus musculus/domesticus
Length: 253  
Fragment?: true
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Publication
8995409 | -
First Author: Asano K
Year: 1997
Journal: J Biol Chem
Title: Conservation and diversity of eukaryotic translation initiation factor eIF3.
Volume: 272
Issue: 2
Pages: 1101-9
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Protein
B1AY13
Organism: Mus musculus/domesticus
Length: 2617  
Fragment?: false
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Protein
E9PV45
Organism: Mus musculus/domesticus
Length: 2618  
Fragment?: false
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Publication
11042159 | J:68323
First Author: Carninci P
Year: 2000
Journal: Genome Res
Title: Normalization and subtraction of cap-trapper-selected cDNAs to prepare full-length cDNA libraries for rapid discovery of new genes.
Volume: 10
Issue: 10
Pages: 1617-30
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Publication
10349636 | J:80645
 
First Author: Carninci P
Year: 1999
Journal: Methods Enzymol
Title: High-efficiency full-length cDNA cloning.
Volume: 303
Pages: 19-44
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Publication
11076861 | J:68324
First Author: Shibata K
Year: 2000
Journal: Genome Res
Title: RIKEN integrated sequence analysis (RISA) system--384-format sequencing pipeline with 384 multicapillary sequencer.
Volume: 10
Issue: 11
Pages: 1757-71
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Publication
16141073 | -
First Author: Katayama S
Year: 2005
Journal: Science
Title: Antisense transcription in the mammalian transcriptome.
Volume: 309
Issue: 5740
Pages: 1564-6
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Publication
15489334 | -
First Author: Gerhard DS
Year: 2004
Journal: Genome Res
Title: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).
Volume: 14
Issue: 10B
Pages: 2121-7
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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.

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