COX15 Antibody Cat

Total Page：16

File Type：pdf, Size：1020Kb

COX15 Antibody Cat. No.: 15-661 COX15 Antibody Immunohistochemistry of paraffin-embedded rat spleen Immunohistochemistry of paraffin-embedded rat heart using COX15 antibody (15-661) at dilution of 1:100 (40x using COX15 antibody (15-661) at dilution of 1:100 (40x lens). lens). Immunohistochemistry of paraffin-embedded human lung Immunohistochemistry of paraffin-embedded human cancer using COX15 antibody (15-661) at dilution of 1:100 thyroid cancer using COX15 antibody (15-661) at dilution (40x lens). of 1:100 (40x lens). September 29, 2021 1 https://www.prosci-inc.com/cox15-antibody-15-661.html Immunohistochemistry of paraffin-embedded human Immunohistochemistry of paraffin-embedded mouse placenta using COX15 antibody (15-661) at dilution of 1:100 spleen using COX15 antibody (15-661) at dilution of (40x lens). 1:100 (40x lens). Immunohistochemistry of paraffin-embedded mouse heart Immunofluorescence analysis of L929 cells using COX15 using COX15 antibody (15-661) at dilution of 1:100 (40x Polyclonal Antibody (15-661) at dilution of 1:100 (40x lens). lens). Blue: DAPI for nuclear staining. Specifications HOST SPECIES: Rabbit SPECIES REACTIVITY: Human, Mouse, Rat A synthetic peptide corresponding to a sequence within amino acids 150-250 of human IMMUNOGEN: COX15 (NP_510870.1). TESTED APPLICATIONS: IF, IHC, WB WB: ,1:500 - 1:2000 APPLICATIONS: IHC: ,1:50 - 1:100 IF: ,1:50 - 1:100 POSITIVE CONTROL: 1) U-251MG 2) A-431 3) Jurkat 4) Mouse heart 5) Mouse kidney 6) Mouse lung PREDICTED MOLECULAR Observed: 60kDa WEIGHT: September 29, 2021 2 https://www.prosci-inc.com/cox15-antibody-15-661.html Properties PURIFICATION: Affinity purification CLONALITY: Polyclonal ISOTYPE: IgG CONJUGATE: Unconjugated PHYSICAL STATE: Liquid BUFFER: PBS with 0.02% sodium azide, 50% glycerol, pH7.3. STORAGE CONDITIONS: Store at -20˚C. Avoid freeze / thaw cycles. Additional Info OFFICIAL SYMBOL: COX15 ALTERNATE NAMES: COX15, CEMCOX2 GENE ID: 1355 USER NOTE: Optimal dilutions for each application to be determined by the researcher. Background and References Cytochrome c oxidase (COX), the terminal component of the mitochondrial respiratory chain, catalyzes the electron transfer from reduced cytochrome c to oxygen. This component is a heteromeric complex consisting of 3 catalytic subunits encoded by mitochondrial genes and multiple structural subunits encoded by nuclear genes. The mitochondrially-encoded subunits function in electron transfer, and the nuclear-encoded BACKGROUND: subunits may function in the regulation and assembly of the complex. This nuclear gene encodes a protein which is not a structural subunit, but may be essential for the biogenesis of COX formation and may function in the hydroxylation of heme O, according to the yeast mutant studies. This protein is predicted to contain 5 transmembrane domains localized in the mitochondrial inner membrane. Alternative splicing of this gene generates two transcript variants diverging in the 3' region. ANTIBODIES FOR RESEARCH USE ONLY. For additional information, visit ProSci's Terms & Conditions Page. September 29, 2021 3 https://www.prosci-inc.com/cox15-antibody-15-661.html.

Copy Link

Recommended publications

Ncomms8214.Pdf
ARTICLE Received 20 Feb 2015 | Accepted 17 Apr 2015 | Published 26 May 2015 DOI: 10.1038/ncomms8214 OPEN Comprehensive survey of condition-specific reproductive isolation reveals genetic incompatibility in yeast Jing Hou1, Anne Friedrich1, Jean-Sebastien Gounot1 & Joseph Schacherer1 Genetic variation within a species could cause negative epistasis leading to reduced hybrid fitness and post-zygotic reproductive isolation. Recent studies in yeasts revealed chromo- somal rearrangements as a major mechanism dampening intraspecific hybrid fertility on rich media. Here, by analysing a large number of Saccharomyces cerevisiae crosses on different culture conditions, we show environment-specific genetic incompatibility segregates readily within yeast and contributes to reproductive isolation. Over 24% (117 out of 481) of cases tested show potential epistasis, among which 6.7% (32 out of 481) are severe, with at least 20% of progeny loss on tested conditions. Based on the segregation patterns, we further characterize a two-locus Dobzhansky–Mu¨ller incompatibility case leading to offspring respiratory deficiency caused by nonsense mutation in a nuclear-encoding mitochondrial gene and tRNA suppressor. We provide evidence that this precise configuration could be adaptive in fluctuating environments, highlighting the role of ecological selection in the onset of genetic incompatibility and reproductive isolation in yeast. 1 Department of Genetics, Genomics and Microbiology, University of Strasbourg/CNRS, UMR7156, 28 rue Goethe, 67083 Strasbourg, France. Correspondence
[Show full text]
Alterations of Genetic Variants and Transcriptomic Features of Response to Tamoxifen in the Breast Cancer Cell Line
Alterations of Genetic Variants and Transcriptomic Features of Response to Tamoxifen in the Breast Cancer Cell Line Mahnaz Nezamivand-Chegini Shiraz University Hamed Kharrati-Koopaee Shiraz University https://orcid.org/0000-0003-2345-6919 seyed taghi Heydari ( [email protected] ) Shiraz University of Medical Sciences https://orcid.org/0000-0001-7711-1137 Hasan Giahi Shiraz University Ali Dehshahri Shiraz University of Medical Sciences Mehdi Dianatpour Shiraz University of Medical Sciences Kamran Bagheri Lankarani Shiraz University of Medical Sciences Research Keywords: Tamoxifen, breast cancer, genetic variants, RNA-seq. Posted Date: August 17th, 2021 DOI: https://doi.org/10.21203/rs.3.rs-783422/v1 License: This work is licensed under a Creative Commons Attribution 4.0 International License. Read Full License Page 1/33 Abstract Background Breast cancer is one of the most important causes of mortality in the world, and Tamoxifen therapy is known as a medication strategy for estrogen receptor-positive breast cancer. In current study, two hypotheses of Tamoxifen consumption in breast cancer cell line (MCF7) were investigated. First, the effect of Tamoxifen on genes expression prole at transcriptome level was evaluated between the control and treated samples. Second, due to the fact that Tamoxifen is known as a mutagenic factor, there may be an association between the alterations of genetic variants and Tamoxifen treatment, which can impact on the drug response. Methods In current study, the whole-transcriptome (RNA-seq) dataset of four investigations (19 samples) were derived from European Bioinformatics Institute (EBI). At transcriptome level, the effect of Tamoxifen was investigated on gene expression prole between control and treatment samples.
[Show full text]
Supplementary Materials
Supplementary materials Supplementary Table S1: MGNC compound library Ingredien Molecule Caco- Mol ID MW AlogP OB (%) BBB DL FASA- HL t Name Name 2 shengdi MOL012254 campesterol 400.8 7.63 37.58 1.34 0.98 0.7 0.21 20.2 shengdi MOL000519 coniferin 314.4 3.16 31.11 0.42 -0.2 0.3 0.27 74.6 beta- shengdi MOL000359 414.8 8.08 36.91 1.32 0.99 0.8 0.23 20.2 sitosterol pachymic shengdi MOL000289 528.9 6.54 33.63 0.1 -0.6 0.8 0 9.27 acid Poricoic acid shengdi MOL000291 484.7 5.64 30.52 -0.08 -0.9 0.8 0 8.67 B Chrysanthem shengdi MOL004492 585 8.24 38.72 0.51 -1 0.6 0.3 17.5 axanthin 20- shengdi MOL011455 Hexadecano 418.6 1.91 32.7 -0.24 -0.4 0.7 0.29 104 ylingenol huanglian MOL001454 berberine 336.4 3.45 36.86 1.24 0.57 0.8 0.19 6.57 huanglian MOL013352 Obacunone 454.6 2.68 43.29 0.01 -0.4 0.8 0.31 -13 huanglian MOL002894 berberrubine 322.4 3.2 35.74 1.07 0.17 0.7 0.24 6.46 huanglian MOL002897 epiberberine 336.4 3.45 43.09 1.17 0.4 0.8 0.19 6.1 huanglian MOL002903 (R)-Canadine 339.4 3.4 55.37 1.04 0.57 0.8 0.2 6.41 huanglian MOL002904 Berlambine 351.4 2.49 36.68 0.97 0.17 0.8 0.28 7.33 Corchorosid huanglian MOL002907 404.6 1.34 105 -0.91 -1.3 0.8 0.29 6.68 e A_qt Magnogrand huanglian MOL000622 266.4 1.18 63.71 0.02 -0.2 0.2 0.3 3.17 iolide huanglian MOL000762 Palmidin A 510.5 4.52 35.36 -0.38 -1.5 0.7 0.39 33.2 huanglian MOL000785 palmatine 352.4 3.65 64.6 1.33 0.37 0.7 0.13 2.25 huanglian MOL000098 quercetin 302.3 1.5 46.43 0.05 -0.8 0.3 0.38 14.4 huanglian MOL001458 coptisine 320.3 3.25 30.67 1.21 0.32 0.9 0.26 9.33 huanglian MOL002668 Worenine
[Show full text]
Supplementary Data Table 1. Genes Upregulated in N-Myc-Overexpressing Mouse Mac1+/Gr1+ BM Cells
Supplementary Data Table 1. Genes upregulated in N-Myc-overexpressing mouse Mac1+/Gr1+ BM cells Probeset C-myc / N-myc / N-myc / C- Gene Title Representative 430v2 Vector Fold Vector Fold myc Fold Public ID Change Change Change 1435368_a_at 2.3 4.6 2.1 poly (ADP-ribose) polymerase family, member 1 BB767586 1455648_at 1.3 3.0 2.1 similar to reduced expression 2 /// similar to reduced expression 2 BG244780 1438973_x_at 2.5 9.8 4.0 gap junction membrane channel protein alpha 1 BB043407 1419915_at 2.0 3.0 2.1 DNA segment, Chr 10, ERATO Doi 438, expressed AW538011 1454842_a_at 1.6 4.0 2.3 UDP-GalNAc:betaGlcNAc beta 1,3-galactosaminyltransferase, AI853240 polypeptide 2 1436704_x_at 2.1 9.2 3.2 methylenetetrahydrofolate dehydrogenase (NADP+ dependent), AV215673 methenyltetrahydrofolate cyclohydrolase, formyltetrahydrofolate synthase 1423142_a_at 2.0 2.5 2.1 GTP binding protein 4 AI987834 1420043_s_at 2.5 5.7 2.8 THO complex 1 AW107924 1439444_x_at 1.5 4.3 2.5 transmembrane emp24-like trafficking protein 10 (yeast) /// similar to AV213456 transmembrane trafficking protein 1438610_a_at 1.9 4.9 2.3 Crystallin, zeta BB793369 1434291_a_at 2.5 4.3 2.8 small EDRK-rich factor 1 AA709993 1422716_a_at 2.8 6.5 2.6 acid phosphatase 1, soluble AW554436 1447895_x_at -1.3 2.3 2.6 PAN3 polyA specific ribonuclease subunit homolog (S. cerevisiae) AV368189 1434097_at 1.5 3.2 2.5 Transcribed locus BM218328 1420982_at 1.1 3.5 2.6 RNA-binding region (RNP1, RRM) containing 2 NM_133242 1433853_at 2.6 7.5 2.6 mindbomb homolog 1 (Drosophila) BG063791 1419824_a_at 1.6 4.0 2.1 RIKEN cDNA A230062G08 gene AI875121 1453797_at 7.5 14.9 2.1 phosphatase, orphan 2 AK010147 1440803_x_at 2.3 4.0 2.3 tachykinin receptor 3 BB498416 1455737_at -2.0 1.1 2.8 RIKEN cDNA C030002B11 gene AU040848 1450954_at -1.5 2.8 4.6 YME1-like 1 (S.
[Show full text]
Gene Ontology Functional Annotations and Pleiotropy
Network based analysis of genetic disease associations Sarah Gilman Submitted in partial fulfillment of the requirements for the degree of Doctor of Philosophy under the Executive Committee of the Graduate School of Arts and Sciences COLUMBIA UNIVERSITY 2014 © 2013 Sarah Gilman All Rights Reserved ABSTRACT Network based analysis of genetic disease associations Sarah Gilman Despite extensive efforts and many promising early findings, genome-wide association studies have explained only a small fraction of the genetic factors contributing to common human diseases. There are many theories about where this “missing heritability” might lie, but increasingly the prevailing view is that common variants, the target of GWAS, are not solely responsible for susceptibility to common diseases and a substantial portion of human disease risk will be found among rare variants. Relatively new, such variants have not been subject to purifying selection, and therefore may be particularly pertinent for neuropsychiatric disorders and other diseases with greatly reduced fecundity. Recently, several researchers have made great progress towards uncovering the genetics behind autism and schizophrenia. By sequencing families, they have found hundreds of de novo variants occurring only in affected individuals, both large structural copy number variants and single nucleotide variants. Despite studying large cohorts there has been little recurrence among the genes implicated suggesting that many hundreds of genes may underlie these complex phenotypes. The question
[Show full text]
MOCHI Enables Discovery of Heterogeneous Interactome Modules in 3D Nucleome
Downloaded from genome.cshlp.org on October 4, 2021 - Published by Cold Spring Harbor Laboratory Press MOCHI enables discovery of heterogeneous interactome modules in 3D nucleome Dechao Tian1,# , Ruochi Zhang1,# , Yang Zhang1, Xiaopeng Zhu1, and Jian Ma1,* 1Computational Biology Department, School of Computer Science, Carnegie Mellon University, Pittsburgh, PA 15213, USA #These two authors contributed equally *Correspondence: [email protected] Contact To whom correspondence should be addressed: Jian Ma School of Computer Science Carnegie Mellon University 7705 Gates-Hillman Complex 5000 Forbes Avenue Pittsburgh, PA 15213 Phone: +1 (412) 268-2776 Email: [email protected] 1 Downloaded from genome.cshlp.org on October 4, 2021 - Published by Cold Spring Harbor Laboratory Press Abstract The composition of the cell nucleus is highly heterogeneous, with different constituents forming complex interactomes. However, the global patterns of these interwoven heterogeneous interactomes remain poorly understood. Here we focus on two different interactomes, chromatin interaction network and gene regulatory network, as a proof-of-principle, to identify heterogeneous interactome modules (HIMs), each of which represents a cluster of gene loci that are in spatial contact more frequently than expected and that are regulated by the same group of transcription factors. HIM integrates transcription factor binding and 3D genome structure to reflect “transcriptional niche” in the nucleus. We develop a new algorithm MOCHI to facilitate the discovery of HIMs based on network motif clustering in heterogeneous interactomes. By applying MOCHI to five different cell types, we found that HIMs have strong spatial preference within the nucleus and exhibit distinct functional properties. Through integrative analysis, this work demonstrates the utility of MOCHI to identify HIMs, which may provide new perspectives on the interplay between transcriptional regulation and 3D genome organization.
[Show full text]
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.
[Show full text]
Role of Cytochrome C Oxidase Nuclear-Encoded Subunits in Health and Disease
Physiol. Res. 69: 947-965, 2020 https://doi.org/10.33549/physiolres.934446 REVIEW Role of Cytochrome c Oxidase Nuclear-Encoded Subunits in Health and Disease Kristýna ČUNÁTOVÁ1, David PAJUELO REGUERA1, Josef HOUŠTĚK1, Tomáš MRÁČEK1, Petr PECINA1 1Department of Bioenergetics, Institute of Physiology, Czech Academy of Sciences, Prague, Czech Republic Received February 2, 2020 Accepted September 13, 2020 Epub Ahead of Print November 2, 2020 Summary [email protected] and Tomáš Mráček, Department of Cytochrome c oxidase (COX), the terminal enzyme of Bioenergetics, Institute of Physiology CAS, Vídeňská 1083, 142 mitochondrial electron transport chain, couples electron transport 20 Prague 4, Czech Republic. E-mail: [email protected] to oxygen with generation of proton gradient indispensable for the production of vast majority of ATP molecules in mammalian Cytochrome c oxidase cells. The review summarizes current knowledge of COX structure and function of nuclear-encoded COX subunits, which may Energy demands of mammalian cells are mainly modulate enzyme activity according to various conditions. covered by ATP synthesis carried out by oxidative Moreover, some nuclear-encoded subunits possess tissue-specific phosphorylation apparatus (OXPHOS) located in the and development-specific isoforms, possibly enabling fine-tuning central bioenergetic organelle, mitochondria. OXPHOS is of COX function in individual tissues. The importance of nuclear- composed of five multi-subunit complexes embedded in encoded subunits is emphasized by recently discovered the inner mitochondrial membrane (IMM). Electron pathogenic mutations in patients with severe mitopathies. In transport from reduced substrates of complexes I and II to addition, proteins substoichiometrically associated with COX were cytochrome c oxidase (COX, complex IV, CIV) is found to contribute to COX activity regulation and stabilization of achieved by increasing redox potential of individual the respiratory supercomplexes.
[Show full text]
Human Mitochondrial Pathologies of the Respiratory Chain and ATP Synthase: Contributions from Studies of Saccharomyces Cerevisiae
life Review Human Mitochondrial Pathologies of the Respiratory Chain and ATP Synthase: Contributions from Studies of Saccharomyces cerevisiae Leticia V. R. Franco 1,2,* , Luca Bremner 1 and Mario H. Barros 2 1 Department of Biological Sciences, Columbia University, New York, NY 10027, USA; [email protected] 2 Department of Microbiology,Institute of Biomedical Sciences, Universidade de Sao Paulo, Sao Paulo 05508-900, Brazil; [email protected] * Correspondence: [email protected] Received: 27 October 2020; Accepted: 19 November 2020; Published: 23 November 2020 Abstract: The ease with which the unicellular yeast Saccharomyces cerevisiae can be manipulated genetically and biochemically has established this organism as a good model for the study of human mitochondrial diseases. The combined use of biochemical and molecular genetic tools has been instrumental in elucidating the functions of numerous yeast nuclear gene products with human homologs that affect a large number of metabolic and biological processes, including those housed in mitochondria. These include structural and catalytic subunits of enzymes and protein factors that impinge on the biogenesis of the respiratory chain. This article will review what is currently known about the genetics and clinical phenotypes of mitochondrial diseases of the respiratory chain and ATP synthase, with special emphasis on the contribution of information gained from pet mutants with mutations in nuclear genes that impair mitochondrial respiration. Our intent is to provide the yeast mitochondrial specialist with basic knowledge of human mitochondrial pathologies and the human specialist with information on how genes that directly and indirectly affect respiration were identified and characterized in yeast. Keywords: mitochondrial diseases; respiratory chain; yeast; Saccharomyces cerevisiae; pet mutants 1.
[Show full text]
Leigh Syndrome
Leigh syndrome What is Leigh syndrome? Leigh syndrome is an inherited progressive neurodegenerative disease characterized by developmental delays or regression, low muscle tone, neuropathy, and severe episodes of illness that can lead to early death.1,2 Individuals with Leigh syndrome have defects in one of many proteins involved in the mitochondrial respiratory chain complexes that produce energy in cells.1 These protein defects cause lesions in tissues that require large amounts of energy, including the brainstem, thalamus, basal ganglia, cerebellum, and spinal cord.1 Clinical symptoms depend on which areas of the central nervous system are involved.1,2 Leigh syndrome is also known as subacute necrotizing encephalomyelopathy.3 What are the symptoms of Leigh syndrome and what treatment is available? Leigh syndrome is a disease that varies in age at onset and rate of progression. Signs of Leigh syndrome can be seen before birth, but are usually noticed soon after birth. Signs and symptoms may include: 2,3,4 • Hypotonia (low muscle tone) • Intellectual and physical developmental delay and regression • Digestive problems and failure to thrive • Cerebellar ataxia (difficulty coordinating movements) • Peripheral neuropathy (disease affecting nerves) • Hypertrophic cardiomyopathy • Breathing problems, leading to respiratory failure • Metabolic or neurological crisis (serious episode of illness) often triggered by an infection During a crisis, symptoms can progress to respiratory problems, seizures, coma, and possibly death. There is no cure for Leigh syndrome. Treatment is supportive. Approximately 50% of affected individuals die by three years of age, although some patients may survive beyond childhood.4 How is Leigh Syndrome inherited? Autosomal recessive Leigh syndrome is caused by mutations in at least 36 different genes,3 including FOXRED1, NDUFAF2, NDUFS4, NDUFS7, NDUFV1, COX15, SURF1 and LRPPRC.
[Show full text]
(-)-Oleocanthal As a Dual C-MET-COX2 Inhibitor for The
nutrients Article (−)-Oleocanthal as a Dual c-MET-COX2 Inhibitor for the Control of Lung Cancer Abu Bakar Siddique 1 , Phillip C.S.R. Kilgore 2, Afsana Tajmim 1 , Sitanshu S. Singh 1 , Sharon A. Meyer 1, Seetharama D. Jois 1, Urska Cvek 2, Marjan Trutschl 2 and Khalid A. El Sayed 1,* 1 School of Basic Pharmaceutical and Toxicological Sciences, College of Pharmacy, University of Louisiana at Monroe, 1800 Bienville Drive, Monroe, LA 71201, USA; [email protected] (A.B.S.); [email protected] (A.T.); [email protected] (S.S.S.); [email protected] (S.A.M.); [email protected] (S.D.J.) 2 Department of Computer Science, Louisiana State University Shreveport, Shreveport, LA 71115, USA; [email protected] (P.C.S.R.K.); [email protected] (U.C.); [email protected] (M.T.) * Correspondence: [email protected]; Tel.: +1-318-342-1725 Received: 14 May 2020; Accepted: 9 June 2020; Published: 11 June 2020 Abstract: Lung cancer (LC) represents the topmost mortality-causing cancer in the U.S. LC patients have overall poor survival rate with limited available treatment options. Dysregulation of the mesenchymal epithelial transition factor (c-MET) and cyclooxygenase 2 (COX2) initiates aggressive LC proﬁle in a subset of patients. The Mediterranean extra-virgin olive oil (EVOO)-rich diet already documented to reduce multiple malignancies incidence. (-)-Oleocanthal (OC) is a naturally occurring phenolic secoiridoid exclusively occurring in EVOO and showed documented anti-breast and other cancer activities via targeting c-MET. This study shows the novel ability of OC to suppress LC progression and metastasis through dual targeting of c-MET and COX-2.
[Show full text]
COX15 Mouse Monoclonal Antibody [Clone ID: 6H2.B4] 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 TA328075 COX15 Mouse Monoclonal Antibody [Clone ID: 6H2.B4] Product data: Product Type: Primary Antibodies Clone Name: 6H2.B4 Applications: IF, IP Recommend Dilution: IP, ICFC, IF, ICC Reactivity: Human, Mouse, Rat Host: Mouse Isotype: IgG1, kappa Clonality: Monoclonal Immunogen: Rat cyt c-OVA Formulation: This antibody is provided in phosphate-buffered solution, pH 7.2, containing 0.09% sodium azide. Final antibody concentration is 0.5 mg/ml. Concentration: 0.5 mg/ml Purification: The antibody was purified by affinity chromatography. Predicted Protein Size: 15 kD Gene Name: COX15 cytochrome c oxidase assembly homolog Database Link: NP_004367 Entrez Gene 226139 MouseEntrez Gene 309391 RatEntrez Gene 1355 Human Background: Cytochrome c is a 15 kD protein found in the mitochondrial intermembrane space with a heme-binding domain. Cytochrome c is a component of the electron transport chain; the heme group transfers electrons from cytochrome b-c1 complex to cytochrome oxidase complex. Cytochrome c initiates apoptosis by release to cytoplasm and binding Apaf-1 which activates procaspase 9. Cytochrome c interacts with the cytochrome b-c1 complex, cytochrome oxidase complex, heme, Apaf-1, and Caspase 9 proteins. The 6H2.B4 monoclonal antibody recognizes human, mouse, and rat cytochrome-c and has been shown to be useful for intracellular flow cytometric staining, Western blotting, immunoprecipitation, and immunofluorescence staining. Synonyms: CEMCOX2 Protein Families: Transmembrane Protein Pathways: Metabolic pathways, Oxidative phosphorylation, Porphyrin and chlorophyll metabolism This product is to be used for laboratory only.
[Show full text]