CHCHD2 Antibody Cat

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CHCHD2 Antibody Cat. No.: 19-066 CHCHD2 Antibody Specifications HOST SPECIES: Rabbit SPECIES REACTIVITY: Human IMMUNOGEN: A synthetic Peptide of human CHCHD2 TESTED APPLICATIONS: Flow, IHC, WB WB: ,1:200 - 1:500 APPLICATIONS: IHC: ,1:50 - 1:100 Flow: ,1:20 - 1:50 POSITIVE CONTROL: 1) A-549 2) MCF7 PREDICTED MOLECULAR Observed: 17kDa WEIGHT: Properties PURIFICATION: Affinity purification CLONALITY: Polyclonal September 30, 2021 1 https://www.prosci-inc.com/chchd2-antibody-19-066.html ISOTYPE: IgG CONJUGATE: Unconjugated PHYSICAL STATE: Liquid BUFFER: PBS with 0.02% sodium azide, pH7.3. STORAGE CONDITIONS: Store at 4˚C. Avoid freeze / thaw cycles. Additional Info OFFICIAL SYMBOL: CHCHD2 Coiled-coil-helix-coiled-coil-helix domain-containing protein 2, mitochondrial, Aging- ALTERNATE NAMES: associated gene 10 protein, HCV NS2 trans-regulated protein, NS2TP, CHCHD2, C7orf17 GENE ID: 51142 USER NOTE: Optimal dilutions for each application to be determined by the researcher. Background and References The protein encoded by this gene belongs to a class of eukaryotic CX(9)C proteins characterized by four cysteine residues spaced ten amino acids apart from one another. These residues form disulfide linkages that define a CHCH fold. In response to stress, the protein translocates from the mitochondrial intermembrane space to the nucleus where it binds to a highly conserved 13 nucleotide oxygen responsive element in the promoter of cytochrome oxidase 4I2, a subunit of the terminal enzyme of the electron transport BACKGROUND: chain. In concert with recombination signal sequence-binding protein J, binding of this protein activates the oxygen responsive element at four percent oxygen. In addition, it has been shown that this protein is a negative regulator of mitochondria-mediated apoptosis. In response to apoptotic stimuli, mitochondrial levels of this protein decrease, allowing BCL2-associated X protein to oligomerize and activate the caspase cascade. Pseudogenes of this gene are found on multiple chromosomes. Alternative splicing results in multiple transcript variants. ANTIBODIES FOR RESEARCH USE ONLY. For additional information, visit ProSci's Terms & Conditions Page. September 30, 2021 2 https://www.prosci-inc.com/chchd2-antibody-19-066.html.

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© 2019 Jan C. Lumibao
© 2019 Jan C. Lumibao CHCHD2 AND THE TUMOR MICROENVIRONMENT IN GLIOBLASTOMA BY JAN C. LUMIBAO DISSERTATION Submitted in partial fulfillment of the requirements for the degree of Doctor of Philosophy in Nutritional Sciences in the Graduate College of the University of Illinois at Urbana-Champaign, 2019 Urbana, Illinois Doctoral Committee: Professor Brendan A. Harley, Chair Professor H. Rex Gaskins, Director of Research Assistant Professor Andrew J. Steelman Professor Rodney W. Johnson Professor Emeritus John W. Erdman ABSTRACT Glioblastoma (GBM) is the most common, aggressive, and deadly form of primary brain tumor in adults, with a median survival time of only 14.6 months. GBM tumors present with chemo- and radio-resistance and rapid, diffuse invasion, making complete surgical resection impossible and resulting in nearly universal recurrence. While investigating the genomic landscape of GBM tumors has expanded understanding of brain tumor biology, targeted therapies against cellular pathways affected by the most common genetic aberrations have been largely ineffective at producing robust survival benefits. Currently, a major obstacle to more effective therapies is the impact of the surrounding tumor microenvironment on intracellular signaling, which has the potential to undermine targeted treatments and advance tumor malignancy, progression, and resistance to therapy. Additionally, mitochondria, generally regarded as putative energy sensors within cells, also play a central role as signaling organelles. Retrograde signaling occurring from
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CHCHD2 (NM 016139) Human Tagged ORF Clone Product Data
OriGene Technologies, Inc. 9620 Medical Center Drive, Ste 200 Rockville, MD 20850, US Phone: +1-888-267-4436 [email protected] EU: [email protected] CN: [email protected] Product datasheet for RC209806 CHCHD2 (NM_016139) Human Tagged ORF Clone Product data: Product Type: Expression Plasmids Product Name: CHCHD2 (NM_016139) Human Tagged ORF Clone Tag: Myc-DDK Symbol: CHCHD2 Synonyms: C7orf17; MIX17B; MNRR1; NS2TP; PARK22 Vector: pCMV6-Entry (PS100001) E. coli Selection: Kanamycin (25 ug/mL) Cell Selection: Neomycin ORF Nucleotide >RC209806 ORF sequence Sequence: Red=Cloning site Blue=ORF Green=Tags(s) TTTTGTAATACGACTCACTATAGGGCGGCCGGGAATTCGTCGACTGGATCCGGTACCGAGGAGATCTGCC GCCGCGATCGCC ATGCCGCGTGGAAGCCGAAGCCGCACCTCCCGCATGGCCCCTCCGGCCAGCCGGGCCCCTCAGATGAGAG CTGCACCCAGGCCAGCACCAGTCGCTCAGCCACCAGCAGCGGCACCCCCATCTGCAGTTGGCTCTTCTGC TGCTGCGCCCCGGCAGCCAGTTCTGATGGCCCAGATGGCAACCACTGCAGCTGGCGTGGCTGTGGGCTCT GCTGTGGGGCACACATTGGGTCACGCCATTACTGGGGGCTTCAGTGGAGGAAGTAATGCTGAGCCTGCGA GGCCTGACATCACTTACCAGGAGCCTCAGGGAACCCAGCCAGCACAGCAGCAGCAGCCTTGCCTCTATGA GATCAAACAGTTTCTGGAGTGTGCCCAGAACCAGGGTGACATCAAGCTCTGTGAGGGTTTCAATGAGGTG CTGAAACAGTGCCGACTTGCAAACGGATTGGCC ACGCGTACGCGGCCGCTCGAGCAGAAACTCATCTCAGAAGAGGATCTGGCAGCAAATGATATCCTGGATT ACAAGGATGACGACGATAAGGTTTAA Protein Sequence: >RC209806 protein sequence Red=Cloning site Green=Tags(s) MPRGSRSRTSRMAPPASRAPQMRAAPRPAPVAQPPAAAPPSAVGSSAAAPRQPVLMAQMATTAAGVAVGS AVGHTLGHAITGGFSGGSNAEPARPDITYQEPQGTQPAQQQQPCLYEIKQFLECAQNQGDIKLCEGFNEV LKQCRLANGLA TRTRPLEQKLISEEDLAANDILDYKDDDDKV Restriction Sites: SgfI-MluI This product
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Regulation of COX Assembly and Function by Twin CX9C Proteins—Implications for Human Disease
cells Review Regulation of COX Assembly and Function by Twin CX9C Proteins—Implications for Human Disease Stephanie Gladyck 1, Siddhesh Aras 1,2, Maik Hüttemann 1 and Lawrence I. Grossman 1,2,* 1 Center for Molecular Medicine and Genetics, Wayne State University School of Medicine, Detroit, MI 48201, USA; [email protected] (S.G.); [email protected] (S.A.); [email protected] (M.H.) 2 Perinatology Research Branch, Division of Obstetrics and Maternal-Fetal Medicine, Division of Intramural Research, Eunice Kennedy Shriver National Institute of Child Health and Human Development, National Institutes of Health, U.S. Department of Health and Human Services, Bethesda, Maryland and Detroit, MI 48201, USA * Correspondence: [email protected] Abstract: Oxidative phosphorylation is a tightly regulated process in mammals that takes place in and across the inner mitochondrial membrane and consists of the electron transport chain and ATP synthase. Complex IV, or cytochrome c oxidase (COX), is the terminal enzyme of the electron transport chain, responsible for accepting electrons from cytochrome c, pumping protons to contribute to the gradient utilized by ATP synthase to produce ATP, and reducing oxygen to water. As such, COX is tightly regulated through numerous mechanisms including protein–protein interactions. The twin CX9C family of proteins has recently been shown to be involved in COX regulation by assisting with complex assembly, biogenesis, and activity. The twin CX9C motif allows for the import of these proteins into the intermembrane space of the mitochondria using the redox import machinery of Mia40/CHCHD4. Studies have shown that knockdown of the proteins discussed in this review results in decreased or completely deﬁcient aerobic respiration in experimental models ranging from yeast to human cells, as the proteins are conserved across species.
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Chchd10, a Novel Bi-Organellar Regulator of Cellular Metabolism: Implications in Neurodegeneration
Wayne State University Wayne State University Dissertations January 2018 Chchd10, A Novel Bi-Organellar Regulator Of Cellular Metabolism: Implications In Neurodegeneration Neeraja Purandare Wayne State University, [email protected] Follow this and additional works at: https://digitalcommons.wayne.edu/oa_dissertations Part of the Molecular Biology Commons Recommended Citation Purandare, Neeraja, "Chchd10, A Novel Bi-Organellar Regulator Of Cellular Metabolism: Implications In Neurodegeneration" (2018). Wayne State University Dissertations. 2125. https://digitalcommons.wayne.edu/oa_dissertations/2125 This Open Access Dissertation is brought to you for free and open access by DigitalCommons@WayneState. It has been accepted for inclusion in Wayne State University Dissertations by an authorized administrator of DigitalCommons@WayneState. CHCHD10, A NOVEL BI-ORGANELLAR REGULATOR OF CELLULAR METABOLISM: IMPLICATIONS IN NEURODEGENERATION by NEERAJA PURANDARE DISSERTATION Submitted to the Graduate School of Wayne State University, Detroit, Michigan in partial fulfillment of the requirements for the degree of DOCTOR OF PHILOSOPHY 2018 MAJOR: MOLECULAR BIOLOGY AND GENETICS Approved By: Advisor Date © COPYRIGHT BY NEERAJA PURANDARE 2018 All Rights Reserved ACKNOWLEDGEMENTS First, I would I like to express the deepest gratitude to my mentor Dr. Grossman for the advice and support and most importantly your patience. Your calm and collected approach during our discussions provided me much needed perspective towards prioritizing and planning my work and I hope to carry this composure in my future endeavors. Words cannot describe my gratefulness for the support of Dr. Siddhesh Aras. You epitomize the scientific mind. I hope that I have inculcated a small fraction of your scientific thought process and I will carry this forth not just in my career, but for everything else that I do.
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[KO Validated] CHCHD2 Rabbit Pab
Leader in Biomolecular Solutions for Life Science [KO Validated] CHCHD2 Rabbit pAb Catalog No.: A16645 KO Validated Basic Information Background Catalog No. The protein encoded by this gene belongs to a class of eukaryotic CX(9)C proteins A16645 characterized by four cysteine residues spaced ten amino acids apart from one another. These residues form disulfide linkages that define a CHCH fold. In response to stress, the Observed MW protein translocates from the mitochondrial intermembrane space to the nucleus where 16kDa it binds to a highly conserved 13 nucleotide oxygen responsive element in the promoter of cytochrome oxidase 4I2, a subunit of the terminal enzyme of the electron transport Calculated MW chain. In concert with recombination signal sequence-binding protein J, binding of this 15kDa protein activates the oxygen responsive element at four percent oxygen. In addition, it has been shown that this protein is a negative regulator of mitochondria-mediated Category apoptosis. In response to apoptotic stimuli, mitochondrial levels of this protein decrease, allowing BCL2-associated X protein to oligomerize and activate the caspase Primary antibody cascade. Pseudogenes of this gene are found on multiple chromosomes. Alternative splicing results in multiple transcript variants. Applications WB, IHC, IF Cross-Reactivity Human, Mouse, Rat Recommended Dilutions Immunogen Information WB 1:500 - 1:2000 Gene ID Swiss Prot 51142 Q9Y6H1 IHC 1:50 - 1:200 Immunogen 1:50 - 1:200 IF Recombinant fusion protein containing a sequence corresponding to amino acids 75-145 of human CHCHD2 (NP_057223.1). Synonyms CHCHD2;C7orf17;MNRR1;NS2TP;PARK22 Contact Product Information www.abclonal.com Source Isotype Purification Rabbit IgG Affinity purification Storage Store at -20℃.
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Loss of Parkinson&Rsquo;S Disease-Associated
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NOVEL FUNCTIONS OF MITOCHONDRIAL PROTEINS IN HEALTH AND DISEASE A Dissertation Presented to the Faculty of the Weill Cornell Graduate School of Medical Sciences in Partial Fulfillment of the Requirements for the Degree of Doctor of Philosophy by Suzanne R. Burstein June 2017 © 2017 Suzanne R. Burstein NOVEL FUNCTIONS OF MITOCHONDRIAL PROTEINS IN HEALTH AND DISEASE Suzanne R. Burstein, Ph.D. Cornell University 2017 Mitochondria are organelles critical for many cellular functions including energy production, ion homeostasis, cellular protein trafficking, and apoptosis induction. While the mitochondrial protein machinery that performs these roles has been studied for many years, the functions of many of these proteins have not been fully elucidated. This dissertation is focused on understanding the functions of two proteins in mitochondria, and their involvement in disease. We describe a novel function for estrogen receptor beta (ERβ) in brain mitochondria. We find that ERβ modulates cyclophilin D-dependent mitochondrial permeability transition (MPT) in brain. MPT is critical in cell death following brain injuries, such as stroke. Based on sex differences in ERβ modulation of MPT, we suggest that it may contribute to sex differences in cellular responses to ischemia. We also explore the protein CHCHD10, a mitochondrial protein with yet unknown function. This protein is of particular interest, as its mutations have been recently associated with familial myopathy and neurodegenerative diseases, such as ALS. We find that CHCHD10 binds to its homolog CHCHD2, and both of these proteins bind to the mitochondrial protein P32. Transient silencing of CHCHD10 expression in HEK293 cells triggers the induction of mitochondria-dependent apoptosis.
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ARTICLE Received 22 Aug 2016 | Accepted 7 Apr 2017 | Published 6 Jun 2017 DOI: 10.1038/ncomms15558 OPEN Loss of function CHCHD10 mutations in cytoplasmic TDP-43 accumulation and synaptic integrity Jung-A. A. Woo1,2,*, Tian Liu1,2,*, Courtney Trotter1,2,*, Cenxiao C. Fang1,2, Emillio De Narvaez1,2, Patrick LePochat1,2, Drew Maslar1,2, Anusha Bukhari1,2, Xingyu Zhao1,2, Andrew Deonarine3, Sandy D. Westerheide3 & David E. Kang1,2,4 Although multiple CHCHD10 mutations are associated with the spectrum of familial and sporadic frontotemporal dementia–amyotrophic lateral sclerosis (FTD–ALS) diseases, neither the normal function of endogenous CHCHD10 nor its role in the pathological milieu (that is, TDP-43 pathology) of FTD/ALS have been investigated. In this study, we made a series of observations utilizing Caenorhabditis elegans models, mammalian cell lines, primary neurons and mouse brains, demonstrating that CHCHD10 normally exerts a protective role in mitochondrial and synaptic integrity as well as in the retention of nuclear TDP-43, whereas FTD/ALS-associated mutations (R15L and S59L) exhibit loss of function phenotypes in C. elegans genetic complementation assays and dominant negative activities in mammalian systems, resulting in mitochondrial/synaptic damage and cytoplasmic TDP-43 accumulation. As such, our results provide a pathological link between CHCHD10-associated mitochon- drial/synaptic dysfunction and cytoplasmic TDP-43 inclusions. 1 USF Health Byrd Alzheimer’s Institute, University of South Florida, Morsani College of Medicine, Tampa, Florida 33613, USA. 2 Department of Molecular Medicine, University of South Florida, Morsani College of Medicine, Tampa, Florida 33613, USA. 3 Department of Cell Biology, Microbiology & Molecular Biology, University of South Florida, College of Arts and Sciences, Tampa, Florida 33620, USA.
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Identification of CHCHD2 Mutations in Patients with Alzheimer's Disease, Amyotrophic Lateral Sclerosis and Frontotemporal Dementia in China
MOLECULAR MEDICINE REPORTS 18: 461-466, 2018 Identification ofCHCHD2 mutations in patients with Alzheimer's disease, amyotrophic lateral sclerosis and frontotemporal dementia in China XIXI LIU1, BIN JIAO1‑3, WEIWEI ZHANG1, TINGTING XIAO1, LIHUA HOU1, CHUZHENG PAN1, BEISHA TANG1-6 and LU SHEN1‑3,7 1Department of Neurology, Xiangya Hospital; 2Key Laboratory of Hunan Province in Neurodegenerative Disorders, Central South University, Changsha, Hunan 410008; 3National Clinical Research Center for Geriatric Diseases, Changsha, Hunan 410078; 4Parkinson's Disease Center of Beijing Institute for Brain Disorders, Beijing 100069; 5Collaborative Innovation Center for Brain Science, Shanghai 200032; 6Collaborative Innovation Center for Genetics and Development, Shanghai 200433; 7Key Laboratory of Organ Injury, Aging and Regenerative Medicine of Hunan, Changsha, Hunan 410008, P.R. China Received December 1, 2017; Accepted April 26, 2018 DOI: 10.3892/mmr.2018.8962 Abstract. Recently, the coiled-coil-helix-coiled-coil-helix important functions. Mutations of CHCHD genes have been domain 2 (CHCHD2) gene was identified as a possible causative identified to be associated with various human neurodegenera- gene for Parkinson's disease (PD). Three other neurodegenera- tive diseases (1). CHCHD10, which is a CHCHD protein, was tive diseases, Alzheimer's disease (AD), amyotrophic lateral identified to be associated with amyotrophic lateral sclerosis sclerosis (ALS) and frontotemporal dementia (FTD), share (ALS), frontotemporal dementia (FTD) and Alzheimer's significant overlaps with PD in clinical phenotypes, patho- disease (AD) in Chinese population (2,3). Recently, the logical features and genetic heredities, and it is still unclear CHCHD2 gene was identified as a possible causative gene for whether CHCHD2 variants could explain these three diseases.
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Systematic analysis of rare variants in mitochondrial function-associated genes for autosomal-dominant Parkinson’s disease in a Chinese population Yongping Chen Sichuan University West China Hospital Xiaojing Gu Sichuan University West China Hospital Ruwei Ou Sichuan University West China Hospital Lingyu Zhang Sichuan University West China Hospital Yanbing Hou Sichuan University West China Hospital Kuncheng Liu Sichuan University West China Hospital Bei Cao Sichuan University West China Hospital Qianqian Wei Sichuan University West China Hospital Wei Song Sichuan University West China Hospital Bi Zhao Sichuan University West China Hospital Ying Wu Sichuan University West China Hospital Jingqiu Cheng Sichuan University West China Hospital huifang shang ( [email protected] ) Sichuan University West China Hospital Department of Neurology https://orcid.org/0000-0003-0947-1151 Research article Keywords: Parkinson’s disease, autosomal dominant, mitochondrial function-associated genes, HTRA2, CHCHD2, burden analysis Posted Date: April 28th, 2020 DOI: https://doi.org/10.21203/rs.3.rs-23120/v1 License: This work is licensed under a Creative Commons Attribution 4.0 International License. Read Full License Page 1/11 Abstract Background Mitochondrial dysfunction is involved in the pathogenicity of Parkinson’s disease (PD). However, the genetic roles of mitochondrial function-associated genes responsible for PD need to be replicated in different cohorts. Methods Whole-exome and Sanger sequencing were used to identify the genetic etiology of 400 autosomal dominant-inherited PD (ADPD) patients. Variants in six dominant inherited mitochondrial function-associated genes, including HTRA2, CHCHD2, CHCHD10, TRAP1, HSPA9 and RHOT1, were analyzed. Results A total of 12 rare variants identied in the ve genes accounted for 3% of ADPD cases, including 0.5% in HTRA2, 0.8% in CHCHD2, 1% in TRAP1, 0.3% in RHOT1 and 0.5% in HSPA9.
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Table S1. 103 Ferroptosis-Related Genes Retrieved from the Genecards
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