TSEN54 Rabbit Pab Antibody

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TSEN54 rabbit pAb antibody

Catalog No :
Source:
Concentration :
Mol.Wt. (Da):

A22945
Rabbit
1 mg/ml
58819

Applications Reactivity Dilution

WB,IHC,ELISA Human WB: 1:500 - 1:2000. IHC: 1:100 - 1:300. ELISA: 1:20000. Not yet tested in other applications.

Storage

-20°C/1 year

Specificity

TSEN54 Polyclonal Antibody detects endogenous levels of TSEN54 protein.

Source / Purification

The antibody was affinity-purified from rabbit antiserum by affinitychromatography using epitope-specific immunogen.

Immunogen

The antiserum was produced against synthesized peptide derived from human TSEN54. AA range:261-310

Uniprot No

Q7Z6J9

Alternative names

TSEN54; SEN54; tRNA-splicing endonuclease subunit Sen54; SEN54 homolog; HsSEN54; tRNA-intron endonuclease Sen54

Form

Liquid in PBS containing 50% glycerol, 0.5% BSA and 0.02% sodium azide.

Clonality Isotype

Polyclonal IgG

Conjugation Background

tRNA splicing endonuclease subunit 54(TSEN54) Homo sapiens This gene encodes a subunit of the tRNA splicing endonuclease complex, which catalyzes the removal of introns from precursor tRNAs. The complex is also implicated in pre-mRNA 3-prime end processing. Mutations in this gene result in pontocerebellar hypoplasia type 2.[provided by RefSeq, Oct 2009],

Other

TSEN54, tRNA-splicing endonuclease subunit Sen54

Produtc Images

：

Application Key:

WB-Western IP-Immunoprecipitation IHC-Immunohistochemistry ChIP-Chromatin Immunoprecipitation

A
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FOR RESEARCH USE ONLY. NOT FOR HUMAN OR DIAGNOSTIC USE.

IF-Immunofluorescence F-Flow Cytometry E-P-ELISA-Peptide

Species Cross-Reactivity Key:

H-Human M-Mouse R-Rat Hm-Hamster Mk-Monkey Vir-Virus Mi-Mink C-Chicken Dm-D. melanogaster X-Xenopus Z-Zebrafish B-Bovine Dg-Dog Pg-Pig Sc-S. cerevisiae Ce-C. elegans Hr-Horse All-All Species Expected

Trademarks

All product names and trademarks are the property of their respective owners.

Regulatory Disclaimer

For life science research only. Not for use in diagnostic procedures.

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To ask questions, solve problems, suggest enhancements and report new applications, please visit our Online Technical Support Site. To call, write, fax, or email us, please visit www.aabsci.cn, contact information will be displayed.

A
AAB Biosciences Products
www.aabsci.cn
FOR RESEARCH USE ONLY. NOT FOR HUMAN OR DIAGNOSTIC USE.

Recommended publications

Brain Morphometry in Pontocerebellar Hypoplasia Type 2

Ekert et al. Orphanet Journal of Rare Diseases (2016) 11:100 DOI 10.1186/s13023-016-0481-4 RESEARCH Open Access Brain morphometry in Pontocerebellar Hypoplasia type 2 Kaspar Ekert1†, Samuel Groeschel1†, Iciar Sánchez-Albisua1*, Saskia Frölich1, Andrea Dieckmann2, Corinna Engel1 and Ingeborg Krägeloh-Mann1 Abstract Background: Pontocerebellar hypoplasia type 2 (PCH2) is caused by a defect in the TSEN54-gene and leads to severe and early disruption of brain development, especially of cerebellum and pons. The aim of this work was to quantify the infra- and supratentorial brain growth during postnatal brain development in children with PCH2. Methods: MRI data of 24 children with PCH2 (age 0.02–17 years., 13 females) were analysed volumetrically and compared to images of 24 typically developing age- and gender-matched children. All children with PCH2 had the homozygous p.A307S mutation in the TSEN54-gene. In 5 patients follow-up MRI investigations were available. Images of the children with PCH2 were available either on film (n = 12) or in digital format (n = 21). Images on film were digitalized. Brain structures were manually masked and further adjusted semi-automatically using intensity thresholding to exclude CSF. Volumes of cerebellum, brain stem, and pons were measured, as well as supratentorial brain and frontal lobe volume. For validation of the method part of the digital images were processed as images on film. In addition, intra- and inter-rater variabilities were tested. Results: Children with PCH2 showed reduced volumes of all measured brain structures compared to healthy controls. Severely hypoplastic cerebellum, pons and brain stem only slightly increased in size postnatally.
High-Resolution Annotation of the Mouse Preimplantation Embryo

ARTICLE https://doi.org/10.1038/s41467-020-16444-w OPEN High-resolution annotation of the mouse preimplantation embryo transcriptome using long-read sequencing ✉ Yunbo Qiao1,8 , Chao Ren2,8, Shisheng Huang3,4,8, Jie Yuan2,8, Xingchen Liu4,5,8, Jiao Fan6, Jianxiang Lin1, ✉ ✉ Susu Wu1, Qiuzhen Chen2,7, Xiaochen Bo2, Xiangyang Li3,4, Xingxu Huang3,4, Zhen Liu5 & Wenjie Shu 2 1234567890():,; The transcriptome of the preimplantation mouse embryo has been previously annotated by short-read sequencing, with limited coverage and accuracy. Here we utilize a low-cell number transcriptome based on the Smart-seq2 method to perform long-read sequencing. Our analysis describes additional novel transcripts and complexity of the preimplantation tran- scriptome, identifying 2280 potential novel transcripts from previously unannotated loci and 6289 novel splicing isoforms from previously annotated genes. Notably, these novel tran- scripts and isoforms with transcription start sites are enriched for an active promoter modiﬁcation, H3K4me3. Moreover, we generate a more complete and precise transcriptome by combining long-read and short-read data during early embryogenesis. Based on this approach, we identify a previously undescribed isoform of Kdm4dl with a modiﬁed mRNA reading frame and a novel noncoding gene designated XLOC_004958. Depletion of Kdm4dl or XLOC_004958 led to abnormal blastocyst development. Thus, our data provide a high- resolution and more precise transcriptome during preimplantation mouse embryogenesis. 1 Precise Genome Engineering Center, School of Life Sciences, Guangzhou University, 510006 Guangzhou, China. 2 Department of Biotechnology, Beijing Institute of Radiation Medicine, 100850 Beijing, China. 3 School of Life Science and Technology, ShanghaiTech University, 201210 Shanghai, China.
Platform Abstracts

American Society of Human Genetics 65th Annual Meeting October 6–10, 2015 Baltimore, MD PLATFORM ABSTRACTS Wednesday, October 7, 9:50-10:30am Abstract #’s Friday, October 9, 2:15-4:15 pm: Concurrent Platform Session D: 4. Featured Plenary Abstract Session I Hall F #1-#2 46. Hen’s Teeth? Rare Variants and Common Disease Ballroom I #195-#202 Wednesday, October 7, 2:30-4:30pm Concurrent Platform Session A: 47. The Zen of Gene and Variant 15. Update on Breast and Prostate Assessment Ballroom III #203-#210 Cancer Genetics Ballroom I #3-#10 48. New Genes and Mechanisms in 16. Switching on to Regulatory Variation Ballroom III #11-#18 Developmental Disorders and 17. Shedding Light into the Dark: From Intellectual Disabilities Room 307 #211-#218 Lung Disease to Autoimmune Disease Room 307 #19-#26 49. Statistical Genetics: Networks, 18. Addressing the Difficult Regions of Pathways, and Expression Room 309 #219-#226 the Genome Room 309 #27-#34 50. Going Platinum: Building a Better 19. Statistical Genetics: Complex Genome Room 316 #227-#234 Phenotypes, Complex Solutions Room 316 #35-#42 51. Cancer Genetic Mechanisms Room 318/321 #235-#242 20. Think Globally, Act Locally: Copy 52. Target Practice: Therapy for Genetic Hilton Hotel Number Variation Room 318/321 #43-#50 Diseases Ballroom 1 #243-#250 21. Recent Advances in the Genetic Basis 53. The Real World: Translating Hilton Hotel of Neuromuscular and Other Hilton Hotel Sequencing into the Clinic Ballroom 4 #251-#258 Neurodegenerative Phenotypes Ballroom 1 #51-#58 22. Neuropsychiatric Diseases of Hilton Hotel Friday, October 9, 4:30-6:30pm Concurrent Platform Session E: Childhood Ballroom 4 #59-#66 54.
TSEN54 Gene Trna Splicing Endonuclease Subunit 54

TSEN54 gene tRNA splicing endonuclease subunit 54 Normal Function The TSEN54 gene provides instructions for making one part (subunit) of an enzyme called the tRNA splicing endonuclease complex. This complex helps process several types of RNA molecules, which are chemical cousins of DNA. The tRNA splicing endonuclease complex is particularly important for the normal processing of a form of RNA known as transfer RNA (tRNA). tRNA molecules help assemble protein building blocks called amino acids into full-length proteins. However, before they can assemble proteins, tRNAs must be processed into mature molecules. In particular, regions called introns need to be removed from some tRNAs for the molecules to be functional. The tRNA splicing endonuclease complex recognizes and then removes introns to help produce mature tRNA molecules. Studies suggest that the tRNA splicing endonuclease complex may also be involved in processing another form of RNA known as messenger RNA (mRNA). mRNA serves as a genetic blueprint for making proteins. Researchers suspect that the tRNA splicing endonuclease complex cuts (cleaves) one end of mRNA molecules so a string of adenines (one of the building blocks of RNA) can be added. This process is known as polyadenylation, and the string of adenines is known as a poly(A) tail. The poly(A) tail signals the stopping point for protein production and protects mRNA from being broken down before protein production occurs. Health Conditions Related to Genetic Changes Pontocerebellar hypoplasia Several mutations in the TSEN54 gene have been identified in people with a disorder of brain development called pontocerebellar hypoplasia. The major features of this condition include delayed development, problems with movement, and intellectual disability.
Supplementary Table 1 Double Treatment Vs Single Treatment

Supplementary table 1 Double treatment vs single treatment Probe ID Symbol Gene name P value Fold change TC0500007292.hg.1 NIM1K NIM1 serine/threonine protein kinase 1.05E-04 5.02 HTA2-neg-47424007_st NA NA 3.44E-03 4.11 HTA2-pos-3475282_st NA NA 3.30E-03 3.24 TC0X00007013.hg.1 MPC1L mitochondrial pyruvate carrier 1-like 5.22E-03 3.21 TC0200010447.hg.1 CASP8 caspase 8, apoptosis-related cysteine peptidase 3.54E-03 2.46 TC0400008390.hg.1 LRIT3 leucine-rich repeat, immunoglobulin-like and transmembrane domains 3 1.86E-03 2.41 TC1700011905.hg.1 DNAH17 dynein, axonemal, heavy chain 17 1.81E-04 2.40 TC0600012064.hg.1 GCM1 glial cells missing homolog 1 (Drosophila) 2.81E-03 2.39 TC0100015789.hg.1 POGZ Transcript Identified by AceView, Entrez Gene ID(s) 23126 3.64E-04 2.38 TC1300010039.hg.1 NEK5 NIMA-related kinase 5 3.39E-03 2.36 TC0900008222.hg.1 STX17 syntaxin 17 1.08E-03 2.29 TC1700012355.hg.1 KRBA2 KRAB-A domain containing 2 5.98E-03 2.28 HTA2-neg-47424044_st NA NA 5.94E-03 2.24 HTA2-neg-47424360_st NA NA 2.12E-03 2.22 TC0800010802.hg.1 C8orf89 chromosome 8 open reading frame 89 6.51E-04 2.20 TC1500010745.hg.1 POLR2M polymerase (RNA) II (DNA directed) polypeptide M 5.19E-03 2.20 TC1500007409.hg.1 GCNT3 glucosaminyl (N-acetyl) transferase 3, mucin type 6.48E-03 2.17 TC2200007132.hg.1 RFPL3 ret finger protein-like 3 5.91E-05 2.17 HTA2-neg-47424024_st NA NA 2.45E-03 2.16 TC0200010474.hg.1 KIAA2012 KIAA2012 5.20E-03 2.16 TC1100007216.hg.1 PRRG4 proline rich Gla (G-carboxyglutamic acid) 4 (transmembrane) 7.43E-03 2.15 TC0400012977.hg.1 SH3D19
Gnomad Lof Supplement

1 gnomAD supplement gnomAD supplement 1 Data processing 4 Alignment and read processing 4 Variant Calling 4 Coverage information 5 Data processing 5 Sample QC 7 Hard filters 7 Supplementary Table 1 | Sample counts before and after hard and release filters 8 Supplementary Table 2 | Counts by data type and hard filter 9 Platform imputation for exomes 9 Supplementary Table 3 | Exome platform assignments 10 Supplementary Table 4 | Confusion matrix for exome samples with Known platform labels 11 Relatedness filters 11 Supplementary Table 5 | Pair counts by degree of relatedness 12 Supplementary Table 6 | Sample counts by relatedness status 13 Population and subpopulation inference 13 Supplementary Figure 1 | Continental ancestry principal components. 14 Supplementary Table 7 | Population and subpopulation counts 16 Population- and platform-specific filters 16 Supplementary Table 8 | Summary of outliers per population and platform grouping 17 Finalizing samples in the gnomAD v2.1 release 18 Supplementary Table 9 | Sample counts by filtering stage 18 Supplementary Table 10 | Sample counts for genomes and exomes in gnomAD subsets 19 Variant QC 20 Hard filters 20 Random Forest model 20 Features 21 Supplementary Table 11 | Features used in final random forest model 21 Training 22 Supplementary Table 12 | Random forest training examples 22 Evaluation and threshold selection 22 Final variant counts 24 Supplementary Table 13 | Variant counts by filtering status 25 Comparison of whole-exome and whole-genome coverage in coding regions 25 Variant annotation 30 Frequency and context annotation 30 2 Functional annotation 31 Supplementary Table 14 | Variants observed by category in 125,748 exomes 32 Supplementary Figure 5 | Percent observed by methylation.
Natural Course of Pontocerebellar Hypoplasia Type 2A Iciar Sánchez-Albisua1*, Saskia Frölich1, Peter G Barth2, Maja Steinlin3 and Ingeborg Krägeloh-Mann1

Sánchez-Albisua et al. Orphanet Journal of Rare Diseases 2014, 9:70 http://www.ojrd.com/content/9/1/70 RESEARCH Open Access Natural course of pontocerebellar hypoplasia type 2A Iciar Sánchez-Albisua1*, Saskia Frölich1, Peter G Barth2, Maja Steinlin3 and Ingeborg Krägeloh-Mann1 Abstract Introduction: Pontocerebellar hypoplasia Type 2 (PCH2) is a rare autosomal recessive condition, defined on MRI by a small cerebellum and ventral pons. Clinical features are severe developmental delay, microcephaly and dyskinesia. Ninety percent carry a p.A307S mutation in the TSEN54-gene. Our aim was to describe the natural course including neurological and developmental features and other aspects of care in a homogeneous group of PCH2 patients all carrying the p.A307S mutation. Patients and methods: Patients were recruited via the German patients' organizations. Inclusion criteria were imaging findings of PCH2 and a p.A307S mutation. Data were collected using medical reports and patient questionnaires discussed in a standardized telephone interview. Results: Thirty-three patients were included. When considering survival until age 11 years, 53% of children had died Weight, length and head circumference, mostly in the normal range at birth, became abnormal, especially head circumference (-5.58 SD at age 5 yrs). Neurologic symptoms: Choreathetosis was present in 88% (62% with pyramidal signs), 12% had pure spasticity. Epileptic seizures were manifest in 82%, status epilepticus in 39%. Non-epileptic dystonic attacks occurred in 33%. General symptoms: feeding difficulties were recorded in 100%, sleep disorder in 96%, apneas in 67% and recurrent infections in 52%; gastroesophageal reflux disease was diagnosed in 73%, 67% got percutaneous endoscopic gastrostomy and 36% a Nissen-fundoplication.
Natural Course of Pontocerebellar Hypoplasia Type 2A Iciar Sánchez-Albisua1*, Saskia Frölich1, Peter G Barth2, Maja Steinlin3 and Ingeborg Krägeloh-Mann1

View metadata, citation and similar papers at core.ac.uk brought to you by CORE provided by Bern Open Repository and Information System (BORIS) Sánchez-Albisua et al. Orphanet Journal of Rare Diseases 2014, 9:70 http://www.ojrd.com/content/9/1/70 RESEARCH Open Access Natural course of pontocerebellar hypoplasia type 2A Iciar Sánchez-Albisua1*, Saskia Frölich1, Peter G Barth2, Maja Steinlin3 and Ingeborg Krägeloh-Mann1 Abstract Introduction: Pontocerebellar hypoplasia Type 2 (PCH2) is a rare autosomal recessive condition, defined on MRI by a small cerebellum and ventral pons. Clinical features are severe developmental delay, microcephaly and dyskinesia. Ninety percent carry a p.A307S mutation in the TSEN54-gene. Our aim was to describe the natural course including neurological and developmental features and other aspects of care in a homogeneous group of PCH2 patients all carrying the p.A307S mutation. Patients and methods: Patients were recruited via the German patients' organizations. Inclusion criteria were imaging findings of PCH2 and a p.A307S mutation. Data were collected using medical reports and patient questionnaires discussed in a standardized telephone interview. Results: Thirty-three patients were included. When considering survival until age 11 years, 53% of children had died Weight, length and head circumference, mostly in the normal range at birth, became abnormal, especially head circumference (-5.58 SD at age 5 yrs). Neurologic symptoms: Choreathetosis was present in 88% (62% with pyramidal signs), 12% had pure spasticity. Epileptic seizures were manifest in 82%, status epilepticus in 39%. Non-epileptic dystonic attacks occurred in 33%. General symptoms: feeding difficulties were recorded in 100%, sleep disorder in 96%, apneas in 67% and recurrent infections in 52%; gastroesophageal reflux disease was diagnosed in 73%, 67% got percutaneous endoscopic gastrostomy and 36% a Nissen-fundoplication.
Mutations in Drosophila Trna Processing Factors Cause Phenotypes Similar

bioRxiv preprint doi: https://doi.org/10.1101/2021.07.09.451847; this version posted July 10, 2021. The copyright holder for this preprint (which was not certified by peer review) is the author/funder, who has granted bioRxiv a license to display the preprint in perpetuity. It is made available under aCC-BY-NC 4.0 International license. Mutations in Drosophila tRNA processing factors cause phenotypes similar to Pontocerebellar Hypoplasia Casey A. Schmidt+1, Lucy Y. Min+2, Michelle H. McVay2, Joseph D. Giusto2, John C. Brown3, Harmony R. Salzler3, and A. Gregory Matera1,2,3,4,5* 1Curriculum in Genetics and Molecular Biology, University of North Carolina, Chapel Hill, NC, USA 2Department of Biology, University of North Carolina, Chapel Hill, NC, USA 3Integrative Program for Biological and Genome Sciences, University of North Carolina, Chapel Hill, NC, USA 4Department of Genetics, University of North Carolina, Chapel Hill, NC, USA 5Lineberger Comprehensive Cancer Center, University of North Carolina, Chapel Hill, NC, USA +These authors contributed equally *Corresponding Author Email: [email protected] (AGM) 1 bioRxiv preprint doi: https://doi.org/10.1101/2021.07.09.451847; this version posted July 10, 2021. The copyright holder for this preprint (which was not certified by peer review) is the author/funder, who has granted bioRxiv a license to display the preprint in perpetuity. It is made available under aCC-BY-NC 4.0 International license. Abstract Mature tRNAs are generated by multiple RNA processing events, which can include the excision of intervening sequences. The tRNA splicing endonuclease (TSEN) complex is responsible for cleaving these intron-containing pre-tRNA transcripts.
Assembly Defects of the Human Trna Splicing Endonuclease Contribute to Impaired

bioRxiv preprint doi: https://doi.org/10.1101/2020.08.03.234229; this version posted August 3, 2020. The copyright holder for this preprint (which was not certified by peer review) is the author/funder, who has granted bioRxiv a license to display the preprint in perpetuity. It is made available under aCC-BY-NC-ND 4.0 International license. 1 Assembly defects of the human tRNA splicing endonuclease contribute to impaired 2 pre-tRNA processing in pontocerebellar hypoplasia 3 4 Samoil Sekulovski1,†, Pascal Devant1,7,†, Silvia Panizza2,†, Tasos Gogakos5, Anda Pitiriciu1, Katharina 5 Heitmeier1, Ewan Phillip Ramsay3, Marie Barth4, Carla Schmidt4, Stefan Weitzer2, Thomas Tuschl5, 6 Frank Baas6, Javier Martinez2,* & Simon Trowitzsch1,** 7 8 1 Institute of Biochemistry, Biocenter, Goethe University Frankfurt, Max-von-Laue Strasse 9, 60438 9 Frankfurt/Main, Germany. 10 2 Max Perutz Labs, Medical University of Vienna, Vienna Biocenter (VBC), Dr. Bohr-Gasse 9/2, 1030 11 Vienna, Austria. 12 3 The Institute of Cancer Research, 237 Fulham Road, London, SW3 6JB, United Kingdom 13 4 Interdisciplinary research center HALOmem, Charles Tanford Protein Center, Institute for 14 Biochemistry and Biotechnology, Martin Luther University Halle-Wittenberg, Kurt-Mothes-Strasse 3a, 15 06120 Halle, Germany. 16 5 Laboratory for RNA Molecular Biology, The Rockefeller University, 1230 York Avenue, New York, NY 17 10065, USA. 18 6 Department of Clinical Genetics, Leiden University, Albinusdreef 2, 2333 ZA Leiden, Netherlands. 19 7 Ph.D. Program in Virology, Harvard Medical School, Boston, MA 02115, USA & Harvard Medical 20 School and Division of Gastroenterology, Boston Children’s Hospital, Boston, 300 Longwood Avenue, 21 MA 02115, USA.
Chromosomal Instability Selects Gene Copy-Number Variants Encoding Core Regulators of Proliferation in Erþ Breast Cancer

Published OnlineFirst June 26, 2014; DOI: 10.1158/0008-5472.CAN-13-2664 Cancer Tumor and Stem Cell Biology Research Chromosomal Instability Selects Gene Copy-Number Variants Encoding Core Regulators of Proliferation in ERþ Breast Cancer David Endesfelder1,2, Rebecca A. Burrell3, Nnennaya Kanu4, Nicholas McGranahan3, Mike Howell7, Peter J. Parker5,6, Julian Downward8, Charles Swanton3,4, and Maik Kschischo1 Abstract Chromosomal instability (CIN) is associated with poor outcome in epithelial malignancies, including breast þ carcinomas. Evidence suggests that prognostic signatures in estrogen receptor–positive (ER ) breast cancer define tumors with CIN and high proliferative potential. Intriguingly, CIN induction in lower eukaryotic cells and human cells is context dependent, typically resulting in a proliferation disadvantage but conferring a fitness benefit under strong selection pressures. We hypothesized that CIN permits accelerated genomic evolution through the generation of diverse DNA copy-number events that may be selected during disease development. In support of this hypothesis, we found evidence for selection of gene amplification of core regulators of proliferation in CIN-associated cancer genomes. Stable DNA copy-number amplifications of the core regulators TPX2 and UBE2C were associated with expression of a gene module involved in proliferation. The module genes were þ enriched within prognostic signature gene sets for ER breast cancer, providing a logical connection between CIN and prognostic signature expression. Our results provide a framework to decipher the impact of intratumor heterogeneity on key cancer phenotypes, and they suggest that CIN provides a permissive landscape for selection of copy-number alterations that drive cancer proliferation. Cancer Res; 74(17); 1–11.
Generation DNA Sequencing to the Identification of Rare Variants in Congenital Disorders

UNIVERSITY OF CALIFORNIA Los Angeles Applications of Next-Generation DNA Sequencing to the Identification of Rare Variants in Congenital DisorDers of the Intestine anD Brain A Dissertation submitteD in partial satisfaction of the requirements for the Degree of Doctor of Philosophy in Human Genetics by Michael Yourshaw 2014 © Copyright by Michael Yourshaw 2014 ABSTRACT OF THE DISSERTATION Applications of Next-Generation DNA Sequencing to the Identification of Rare Variants in Congenital DisorDers of the Intestine anD Brain by Michael Yourshaw Doctor of Philosophy in Human Genetics University of California, Los Angeles, 2014 Professor Stanley F. Nelson, Chair High throughput, massively parallel DNA sequencing proviDes a powerful technology to stuDy the human genome anD to iDentify variations in DNA that cause disease. Sequencing the protein coDing region of the genome (‘whole-exome sequencing’) is a cost effective methoD to search the part of the genome that is most likely to harbor Disease relateD mutations. We DevelopeD software methoDs to process sequencing data and to annotate variants with Data on genes, function, conservation, expression, Diseases, pathways, anD protein structure. We applieD whole-exome sequencing to search for the molecular basis of Disease in three projects: 1) a cohort of patients with congenital diarrheal disorders (CDDs); 2) a cohort of patients with congenital chronic intestinal pseuDo-obstruction (CIPO) or the relateD Disease, megacystis-microcolon-intestinal hypoperistalsis syndrome (MMIH); anD 3) four siblings with infantile pontocerebellar hypoplasia and spinal motor neuron Degeneration. ii We sequenceD 45 probanDs from Diverse ethnic backgrounDs who were DiagnoseD with a variety of CDDs of probable, but unknown genetic cause.