DOCSLIB.ORG

PDCD6 Antibody Order 021-34695924 [email protected] Support 400-6123-828 50Ul [email protected] 100 Ul √ √ Web

Total Page：16

File Type：pdf, Size：1020Kb

Download full-text PDF Read full-text
PDCD6 Antibody Order 021-34695924 Orders@Ab-Mart.Com Support 400-6123-828 50Ul Support1@Ab-Mart.Com 100 Ul √ √ Web TD7978 PDCD6 Antibody Order 021-34695924 [email protected] Support 400-6123-828 50ul [email protected] 100 uL √ √ Web www.ab-mart.com.cn Description: Calcium sensor that plays a key role in processes such as endoplasmic reticulum (ER)- Golgi vesicular transport, endosomal biogenesis or membrane repair. Acts as an adapter that bridges unrelated proteins or stabilizes weak protein-protein complexes in response to calcium: calcium-binding triggers exposure of apolar surface, promoting interaction with different sets of proteins thanks to 3 different hydrophobic pockets, leading to translocation to membranes. Involved in ER-Golgi transport by promoting the association between PDCD6IP and TSG101, thereby bridging together the ESCRT-III and ESCRT-I complexes. Together with PEF1, acts as calcium-dependent adapter for the BCR(KLHL12) complex, a complex involved in ER-Golgi transport by regulating the size of COPII coats. In response to cytosolic calcium increase, the heterodimer formed with PEF1 interacts with, and bridges together the BCR(KLHL12) complex and SEC31 (SEC31A or SEC31B), promoting monoubiquitination of SEC31 and subsequent collagen export, which is required for neural crest specification. Involved in the regulation of the distribution and function of MCOLN1 in the endosomal pathway. Promotes localization and polymerization of TFG at endoplasmic reticulum exit site. Required for T-cell receptor-, Fas-, and glucocorticoid- induced apoptosis (By similarity). May mediate Ca(2+)-regulated signals along the death pathway: interaction with DAPK1 can accelerate apoptotic cell death by increasing caspase-3 activity. Its role in apoptosis may however be indirect, as suggested by knockout experiments (By similarity). May inhibit KDR/VEGFR2-dependent angiogenesis; the function involves inhibition of VEGF-induced phosphorylation of the Akt signaling pathway. In case of infection by HIV-1 virus, indirectly inhibits HIV-1 production by affecting viral Gag expression and distribution.Has a lower Ca(2+) affinity than isoform 1 (By similarity). Uniprot:O75340 Alternative Names： AIP1; ALG 2; ALG-2-interacting protein 1; ALG2; ALIX; Apoptosis linked gene 2; Apoptosis linked gene 2 protein; Apoptosis-linked gene 2 protein; FLJ42309; FLJ46208; Hp95; KIAA1375; MA 3; MA3; MGC111017; MGC119050; MGC9123; PDCD 6; Pdcd6; PDCD6_HUMAN; PEF 1B; PEF1B; Probable calcium binding protein ALG 2; Probable calcium binding protein ALG2; Probable calcium-binding protein ALG-2; Programmed cell death 6; Programmed cell death 6-interacting protein; Programmed cell death protein 6; PS 2; PS2; Specificity: PDCD6 Antibody detects endogenous levels of total PDCD6. Reactivity:Human Source:Rabbit Mol.Wt.: 21kD; 22kDa(Calculated). Storage Condition: Store at -20 °C. Stable for 12 months from date of receipt. Application: WB 1:1000-1:2000；IHC/IF 1:50-1:500.
Load more

Recommended publications
  • Farnesol-Induced Apoptosis in Human Lung Carcinoma Cells Is Coupled to the Endoplasmic Reticulum Stress Response
    Research Article Farnesol-Induced Apoptosis in Human Lung Carcinoma Cells Is Coupled to the Endoplasmic Reticulum Stress Response Joung Hyuck Joo,1 Grace Liao,1 Jennifer B. Collins,2 Sherry F. Grissom,2 and Anton M. Jetten1 1Cell Biology Section, LRB, and 2Microarray Group, Division of Intramural Research, National Institute of Environmental Health Sciences, NIH, Research Triangle Park, North Carolina Abstract range of fruits and vegetables (9, 10). Each isoprenoid has been Farnesol (FOH) and other isoprenoid alcohols induce apopto- shown to inhibit proliferation and induce apoptosis in a number of sis in various carcinoma cells and inhibit tumorigenesis in neoplastic cell lines from different origins (4, 11–14). In addition, in vivo these isoprenoids have been reported to be effective in chemo- several models. However, the mechanisms by which in vivo they mediate their effects are not yet fully understood. In this prevention and chemotherapy in various cancer models study, we show that FOH is an effective inducer of apoptosis in (10, 12, 15, 16). FOH has been reported to exhibit chemopreventive several lung carcinoma cells, including H460. This induction is effects in colon and pancreas carcinogenesis in rats (9, 17) whereas associated with activation of several caspases and cleavage of phase I and II clinical trials have indicated therapeutic potential poly(ADP-ribose) polymerase (PARP). To obtain insight into for POH (16, 18). The mechanisms by which these isoprenoids induce these effects are not yet fully understood. Isoprenoids have the mechanism involved in FOH-induced apoptosis, we compared the gene expression profiles of FOH-treated and been reported to inhibit posttranslational protein prenylation (19) control H460 cells by microarray analysis.
    [Show full text]
  • Multi-Targeted Mechanisms Underlying the Endothelial Protective Effects of the Diabetic-Safe Sweetener Erythritol
    Multi-Targeted Mechanisms Underlying the Endothelial Protective Effects of the Diabetic-Safe Sweetener Erythritol Danie¨lle M. P. H. J. Boesten1*., Alvin Berger2.¤, Peter de Cock3, Hua Dong4, Bruce D. Hammock4, Gertjan J. M. den Hartog1, Aalt Bast1 1 Department of Toxicology, Maastricht University, Maastricht, The Netherlands, 2 Global Food Research, Cargill, Wayzata, Minnesota, United States of America, 3 Cargill RandD Center Europe, Vilvoorde, Belgium, 4 Department of Entomology and UCD Comprehensive Cancer Center, University of California Davis, Davis, California, United States of America Abstract Diabetes is characterized by hyperglycemia and development of vascular pathology. Endothelial cell dysfunction is a starting point for pathogenesis of vascular complications in diabetes. We previously showed the polyol erythritol to be a hydroxyl radical scavenger preventing endothelial cell dysfunction onset in diabetic rats. To unravel mechanisms, other than scavenging of radicals, by which erythritol mediates this protective effect, we evaluated effects of erythritol in endothelial cells exposed to normal (7 mM) and high glucose (30 mM) or diabetic stressors (e.g. SIN-1) using targeted and transcriptomic approaches. This study demonstrates that erythritol (i.e. under non-diabetic conditions) has minimal effects on endothelial cells. However, under hyperglycemic conditions erythritol protected endothelial cells against cell death induced by diabetic stressors (i.e. high glucose and peroxynitrite). Also a number of harmful effects caused by high glucose, e.g. increased nitric oxide release, are reversed. Additionally, total transcriptome analysis indicated that biological processes which are differentially regulated due to high glucose are corrected by erythritol. We conclude that erythritol protects endothelial cells during high glucose conditions via effects on multiple targets.
    [Show full text]
  • 1 Supporting Information for a Microrna Network Regulates
    Supporting Information for A microRNA Network Regulates Expression and Biosynthesis of CFTR and CFTR-ΔF508 Shyam Ramachandrana,b, Philip H. Karpc, Peng Jiangc, Lynda S. Ostedgaardc, Amy E. Walza, John T. Fishere, Shaf Keshavjeeh, Kim A. Lennoxi, Ashley M. Jacobii, Scott D. Rosei, Mark A. Behlkei, Michael J. Welshb,c,d,g, Yi Xingb,c,f, Paul B. McCray Jr.a,b,c Author Affiliations: Department of Pediatricsa, Interdisciplinary Program in Geneticsb, Departments of Internal Medicinec, Molecular Physiology and Biophysicsd, Anatomy and Cell Biologye, Biomedical Engineeringf, Howard Hughes Medical Instituteg, Carver College of Medicine, University of Iowa, Iowa City, IA-52242 Division of Thoracic Surgeryh, Toronto General Hospital, University Health Network, University of Toronto, Toronto, Canada-M5G 2C4 Integrated DNA Technologiesi, Coralville, IA-52241 To whom correspondence should be addressed: Email: [email protected] (M.J.W.); yi- [email protected] (Y.X.); Email: [email protected] (P.B.M.) This PDF file includes: Materials and Methods References Fig. S1. miR-138 regulates SIN3A in a dose-dependent and site-specific manner. Fig. S2. miR-138 regulates endogenous SIN3A protein expression. Fig. S3. miR-138 regulates endogenous CFTR protein expression in Calu-3 cells. Fig. S4. miR-138 regulates endogenous CFTR protein expression in primary human airway epithelia. Fig. S5. miR-138 regulates CFTR expression in HeLa cells. Fig. S6. miR-138 regulates CFTR expression in HEK293T cells. Fig. S7. HeLa cells exhibit CFTR channel activity. Fig. S8. miR-138 improves CFTR processing. Fig. S9. miR-138 improves CFTR-ΔF508 processing. Fig. S10. SIN3A inhibition yields partial rescue of Cl- transport in CF epithelia.
    [Show full text]
  • Downloaded from URL: Δ Δ Nated ALG-2 GF122) and GST-ALG-2 GF122 Was Cium.Uhnres.Utoronto.Ca/Vgm
    Inuzuka et al. BMC Structural Biology 2010, 10:25 http://www.biomedcentral.com/1472-6807/10/25 RESEARCH ARTICLE Open Access Molecular basis for defect in Alix-binding by alternatively spliced isoform of ALG-2 (ALG-2ΔGF122) and structural roles of F122 in target recognition Tatsutoshi Inuzuka1, Hironori Suzuki1,2, Masato Kawasaki2, Hideki Shibata1, Soichi Wakatsuki2, Masatoshi Maki1* Abstract Background: ALG-2 (a gene product of PDCD6) belongs to the penta-EF-hand (PEF) protein family and Ca2 +-dependently interacts with various intracellular proteins including mammalian Alix, an adaptor protein in the ESCRT system. Our previous X-ray crystal structural analyses revealed that binding of Ca2+ to EF3 enables the side chain of R125 to move enough to make a primary hydrophobic pocket (Pocket 1) accessible to a short fragment of Alix. The side chain of F122, facing a secondary hydrophobic pocket (Pocket 2), interacts with the Alix peptide. An alternatively spliced shorter isoform, designated ALG-2ΔGF122, lacks Gly121Phe122 and does not bind Alix, but the structural basis of the incompetence has remained to be elucidated. Results: We solved the X-ray crystal structure of the PEF domain of ALG-2ΔGF122 in the Ca2+-bound form and compared it with that of ALG-2. Deletion of the two residues shortened a-helix 5 (a5) and changed the configuration of the R125 side chain so that it partially blocked Pocket 1. A wall created by the main chain of 121- GFG-123 and facing the two pockets was destroyed. Surprisingly, however, substitution of F122 with Ala or Gly, but not with Trp, increased the Alix-binding capacity in binding assays.
    [Show full text]
  • PDCD6IP (Human) Recombinant Protein (P01)
    PDCD6IP (Human) Recombinant Preparation Method: in vitro wheat germ expression Protein (P01) system Purification: Glutathione Sepharose 4 Fast Flow Catalog Number: H00010015-P01 Storage Buffer: 50 mM Tris-HCI, 10 mM reduced Regulation Status: For research use only (RUO) Glutathione, pH=8.0 in the elution buffer. Product Description: Human PDCD6IP full-length ORF Storage Instruction: Store at -80°C. Aliquot to avoid ( AAH20066, 1 a.a. - 868 a.a.) recombinant protein with repeated freezing and thawing. GST-tag at N-terminal. Entrez GeneID: 10015 Sequence: MATFISVQLKKTSEVDLAKPLVKFIQQTYPSGGEEQAQ Gene Symbol: PDCD6IP YCRAAEELSKLRRAAVGRPLDKHEGALETLLRYYDQIC SIEPKFPFSENQICLTFTWKDAFDKGSLFGGSVKLALA Gene Alias: AIP1, Alix, DRIP4, HP95, MGC17003 SLGYEKSCVLFNCAALASQIAAEQNLDNDEGLKIAAKH YQFASGAFLHIKETVLSALSREPTVDISPDTVGTLSLIM Gene Summary: This gene encodes a protein thought LAQAQEVFFLKATRDKMKDAIIAKLANQAADYFGDAFK to participate in programmed cell death. Studies using QCQYKDTLPKEVFPVLAAKHCIMQANAEYHQSILAKQ mouse cells have shown that overexpression of this QKKFGEEIARLQHAAELIKTVASRYDEYVNVKDFSDKI protein can block apoptosis. In addition, the product of NRALAAAKKDNDFIYHDRVPDLKDLDPIGKATLVKSTP this gene binds to the product of the PDCD6 gene, a VNVPISQKFTDLFEKMVPVSVQQSLAAYNQRKADLVN protein required for apoptosis, in a calcium-dependent RSIAQMREATTLANGVLASLNLPAAIEDVSGDTVPQSIL manner. This gene product also binds to endophilins, TKSRSVIEQGGIQTVDQLIKELPELLQRNREILDESLRLL proteins that regulate membrane shape during DEEEATDNDLRAKFKERWQRTPSNELYKPLRAEGTNF endocytosis.
    [Show full text]
  • Anti-PEF1 / Peflin Antibody (ARG42993)
    Product datasheet [email protected] ARG42993 Package: 100 μl anti-PEF1 / Peflin antibody Store at: -20°C Summary Product Description Rabbit Polyclonal antibody recognizes PEF1 / Peflin Tested Reactivity Hu, Ms, Rat Tested Application FACS, WB Host Rabbit Clonality Polyclonal Isotype IgG Target Name PEF1 / Peflin Antigen Species Human Immunogen Synthetic peptide of Human PEF1 / Peflin. Conjugation Un-conjugated Alternate Names ABP32; PEF1A; Peflin; PEF protein with a long N-terminal hydrophobic domain; Penta-EF hand domain- containing protein 1 Application Instructions Application table Application Dilution FACS 1:20 WB 1:1000 - 1:5000 Application Note * The dilutions indicate recommended starting dilutions and the optimal dilutions or concentrations should be determined by the scientist. Positive Control K562 Calculated Mw 30 kDa Observed Size ~ 31 kDa Properties Form Liquid Purification Affinity purified. Buffer 50 nM Tris-Glycine (pH 7.4), 0.15M NaCl, 0.01% Sodium azide, 40% Glycerol and 0.05% BSA. Preservative 0.01% Sodium azide Stabilizer 40% Glycerol and 0.05% BSA Storage instruction For continuous use, store undiluted antibody at 2-8°C for up to a week. For long-term storage, aliquot and store at -20°C. Storage in frost free freezers is not recommended. Avoid repeated freeze/thaw cycles. Suggest spin the vial prior to opening. The antibody solution should be gently mixed before use. www.arigobio.com 1/2 Note For laboratory research only, not for drug, diagnostic or other use. Bioinformation Gene Symbol PEF1 Gene Full Name penta-EF-hand domain containing 1 Background This gene encodes a calcium-binding protein belonging to the penta-EF-hand protein family.
    [Show full text]
  • Characterizing the Chlamydia Trachomatis Inclusion Membrane Proteome
    Characterizing the Chlamydia trachomatis inclusion membrane proteome Mary Dickinson A dissertation submitted in partial fulfillment of the requirements for the degree of Doctor of Philosophy University of Washington 2019 Reading committee Kevin Hybiske, Chair Lee Ann Campbell David Sherman Program Authorized to Offer Degree: Pathobiology ©Copyright 2019 Mary Dickinson ii University of Washington Abstract Characterizing the Chlamydia trachomatis inclusion membrane proteome Mary Dickinson Chair of the Supervisory Committee: Kevin Hybiske Pathobiology Program, Department of Medicine Chlamydia trachomatis is the most common cause of bacterial sexually transmitted infection, responsible for millions of infections each year. Despite this high prevalence, the elucidation of the molecular mechanisms of Chlamydia pathogenesis has been difficult due to limitations in genetic tools and its intracellular developmental cycle. Within a host epithelial cell, chlamydiae replicate within a vacuole called the inclusion. Many Chlamydia–host interactions are thought to be mediated by the Inc family of type III secreted proteins that are anchored in the inclusion membrane, but their array of host targets are largely unknown. To investigate how the inclusion membrane proteome changes over the course of an infected cell, we have adapted the APEX system of proximity-dependent biotinylation. APEX is capable of specifically labeling proteins within a 20 nm radius in living cells. We transformed C. trachomatis to express the enzyme APEX fused to known inclusion membrane proteins, allowing biotinylation and purification of inclusion-associated proteins. Using quantitative mass spectrometry against APEX labeled samples, we identified over 400 proteins associated with the inclusion membrane at early, middle, and late stages of epithelial cell infection. This system was iii sensitive enough to detect inclusion interacting proteins early in the developmental cycle, at 8 hours post infection, a previously intractable time point.
    [Show full text]
  • Functional Dependency Analysis Identifies Potential Druggable
    cancers Article Functional Dependency Analysis Identifies Potential Druggable Targets in Acute Myeloid Leukemia 1, 1, 2 3 Yujia Zhou y , Gregory P. Takacs y , Jatinder K. Lamba , Christopher Vulpe and Christopher R. Cogle 1,* 1 Division of Hematology and Oncology, Department of Medicine, College of Medicine, University of Florida, Gainesville, FL 32610-0278, USA; yzhou1996@ufl.edu (Y.Z.); gtakacs@ufl.edu (G.P.T.) 2 Department of Pharmacotherapy and Translational Research, College of Pharmacy, University of Florida, Gainesville, FL 32610-0278, USA; [email protected]fl.edu 3 Department of Physiological Sciences, College of Veterinary Medicine, University of Florida, Gainesville, FL 32610-0278, USA; cvulpe@ufl.edu * Correspondence: [email protected]fl.edu; Tel.: +1-(352)-273-7493; Fax: +1-(352)-273-5006 Authors contributed equally. y Received: 3 November 2020; Accepted: 7 December 2020; Published: 10 December 2020 Simple Summary: New drugs are needed for treating acute myeloid leukemia (AML). We analyzed data from genome-edited leukemia cells to identify druggable targets. These targets were necessary for AML cell survival and had favorable binding sites for drug development. Two lists of genes are provided for target validation, drug discovery, and drug development. The deKO list contains gene-targets with existing compounds in development. The disKO list contains gene-targets without existing compounds yet and represent novel targets for drug discovery. Abstract: Refractory disease is a major challenge in treating patients with acute myeloid leukemia (AML). Whereas the armamentarium has expanded in the past few years for treating AML, long-term survival outcomes have yet to be proven. To further expand the arsenal for treating AML, we searched for druggable gene targets in AML by analyzing screening data from a lentiviral-based genome-wide pooled CRISPR-Cas9 library and gene knockout (KO) dependency scores in 15 AML cell lines (HEL, MV411, OCIAML2, THP1, NOMO1, EOL1, KASUMI1, NB4, OCIAML3, MOLM13, TF1, U937, F36P, AML193, P31FUJ).
    [Show full text]
  • ALIX / PDCD6IP Antibody Cat
    ALIX / PDCD6IP Antibody Cat. No.: 18-578 ALIX / PDCD6IP Antibody Immunohistochemistry of paraffin- embedded rat kidney using ALIX / Immunohistochemistry of paraffin-embedded human prostate using ALIX / PDCD6IP antibody (18-578) at PDCD6IP antibody (18-578) at dilution of 1:100 (40x lens). dilution of 1:100 (40x lens). Immunohistochemistry of paraffin- embedded human stomach using ALIX / PDCD6IP antibody (18-578) at dilution of 1:100 (40x lens). Specifications HOST SPECIES: Rabbit September 24, 2021 1 https://www.prosci-inc.com/alix-pdcd6ip-antibody-18-578.html SPECIES REACTIVITY: Human, Mouse, Rat Recombinant fusion protein containing a sequence corresponding to amino acids 1-180 of IMMUNOGEN: human ALIX / PDCD6IP (NP_037506.2). TESTED APPLICATIONS: IHC, WB WB: ,1:200 - 1:2000 APPLICATIONS: IHC: ,1:50 - 1:200 POSITIVE CONTROL: 1) HeLa 2) LO2 3) Jurkat 4) Rat brain PREDICTED MOLECULAR Observed: 105kDa WEIGHT: 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: PDCD6IP Programmed cell death 6-interacting protein, PDCD6-interacting protein, ALG-2- ALTERNATE NAMES: interacting protein 1, ALG-2-interacting protein X, Hp95, PDCD6IP, AIP1, ALIX, KIAA1375 GENE ID: 10015 USER NOTE: Optimal dilutions for each application to be determined by the researcher. Background and References September 24, 2021 2 https://www.prosci-inc.com/alix-pdcd6ip-antibody-18-578.html This gene encodes a protein that functions within the ESCRT pathway in the abscission stage of cytokinesis, in intralumenal endosomal vesicle formation, and in enveloped virus budding.
    [Show full text]
  • Atlas Journal
    Atlas of Genetics and Cytogenetics in Oncology and Haematology Home Genes Leukemias Solid Tumours Cancer-Prone Deep Insight Portal Teaching X Y 1 2 3 4 5 6 7 8 9 10 11 12 13 14 15 16 17 18 19 20 21 22 NA Atlas Journal Atlas Journal versus Atlas Database: the accumulation of the issues of the Journal constitutes the body of the Database/Text-Book. TABLE OF CONTENTS Volume 12, Number 5, Sep-Oct 2008 Previous Issue / Next Issue Genes XAF1 (XIAP associated factor-1) (17p13.2). Stéphanie Plenchette, Wai Gin Fong, Robert G Korneluk. Atlas Genet Cytogenet Oncol Haematol 2008; 12 (5): 668-673. [Full Text] [PDF] URL : http://atlasgeneticsoncology.org/Genes/XAF1ID44095ch17p13.html WWP1 (WW domain containing E3 ubiquitin protein ligase 1) (8q21.3). Ceshi Chen. Atlas Genet Cytogenet Oncol Haematol 2008; 12 (5): 674-680. [Full Text] [PDF] URL : http://atlasgeneticsoncology.org/Genes/WWP1ID42993ch8q21.html TSPAN1 (tetraspanin 1) (1p34.1). David Murray, Peter Doran. Atlas Genet Cytogenet Oncol Haematol 2008; 12 (5): 681-683. [Full Text] [PDF] URL : http://atlasgeneticsoncology.org/Genes/TSPAN1ID44178ch1p34.html TCL1B (T-cell leukemia/lymphoma 1B) (14q32.13). Herbert Eradat, Michael A Teitell. Atlas Genet Cytogenet Oncol Haematol 2008; 12 (5): 684-686. [Full Text] [PDF] URL : http://atlasgeneticsoncology.org/Genes/TCL1BID354ch14q32.html PVRL4 (poliovirus receptor-related 4) (1q23.3). Marc Lopez. Atlas Genet Cytogenet Oncol Haematol 2008; 12 (5): 687-690. [Full Text] [PDF] URL : http://atlasgeneticsoncology.org/Genes/PVRL4ID44141ch1q23.html PTTG1IP (pituitary tumor-transforming 1 interacting protein) (21q22.3). Vicki Smith, Chris McCabe. Atlas Genet Cytogenet Oncol Haematol 2008; 12 (5): 691-694.
    [Show full text]
  • PDCD6 Antibody (Center) Purified Rabbit Polyclonal Antibody (Pab) Catalog # Ap20782c
    10320 Camino Santa Fe, Suite G San Diego, CA 92121 Tel: 858.875.1900 Fax: 858.622.0609 PDCD6 Antibody (Center) Purified Rabbit Polyclonal Antibody (Pab) Catalog # AP20782c Specification PDCD6 Antibody (Center) - Product Information Application WB,E Primary Accession O75340 Other Accession P12815 Reactivity Mouse Host Rabbit Clonality Polyclonal Isotype Rabbit Ig Calculated MW 21868 PDCD6 Antibody (Center) - Additional Information Gene ID 10016 Other Names Programmed cell death protein 6, Apoptosis-linked gene 2 protein, Probable Western blot analysis of lysate from mouse calcium-binding protein ALG-2, PDCD6, liver tissue lysate, using PDCD6 Antibody ALG2 (Center)(Cat. #AP20782c). AP20782c was diluted at 1:1000. A goat anti-rabbit IgG Target/Specificity H&L(HRP) at 1:5000 dilution was used as the This PDCD6 antibody is generated from a secondary antibody. Lysate at 35ug. rabbit immunized with a KLH conjugated synthetic peptide between 103-137 amino acids from the Central region of human PDCD6 Antibody (Center) - Background PDCD6. Calcium-binding protein required for T-cell Dilution receptor-, Fas-, and glucocorticoid-induced cell WB~~1:1000 death. May mediate Ca(2+)- regulated signals along the death pathway (By similarity). Format Purified polyclonal antibody supplied in PBS Calcium-dependent adapter necessary for the with 0.09% (W/V) sodium azide. This association between PDCD6IP and TSG101. antibody is purified through a protein A Interaction with DAPK1 can accelerate column, followed by peptide affinity apoptotic cell death by increasing caspase-3 purification. activity. May inhibit KDR/VEGFR2-dependent angiogenesis; the function involves inhibition Storage of VEGF-induced phosphoprylation of the Akt Maintain refrigerated at 2-8°C for up to 2 signaling pathway.
    [Show full text]
  • Association of PDCD6 Polymorphisms with the Risk of Cancer: Evidence from a Meta-Analysis
    www.oncotarget.com Oncotarget, 2018, Vol. 9, (No. 37), pp: 24857-24868 Review Association of PDCD6 polymorphisms with the risk of cancer: Evidence from a meta-analysis Mohammad Hashemi1,2, Gholamreza Bahari2, Jarosław Markowski3, Andrzej Małecki4, Marek J. Łos5,8 and Saeid Ghavami6,7 1Cellular and Molecular Research Center, Zahedan University of Medical Sciences, Zahedan, Iran 2Department of Clinical Biochemistry, School of Medicine, Zahedan University of Medical Sciences, Zahedan, Iran 3ENT Department, School of Medicine, Medical University of Silesia in Katowice, Katowice, Poland 4Faculty of Physiotherapy, The Jerzy Kukuczka Academy of Physical Education in Katowice, Katowice, Poland 5Department of Molecular Biology, School of Pharmacy with the Division of Laboratory Medicine in Sosnowiec, Medical University of Silesia in Katowice, Katowice, Poland 6Department of Human Anatomy and Cell Science, Max Rady College of Medicine, Rady Faculty of Health Sciences, University of Manitoba, Winnipeg, MB, Canada 7Health Policy Research Center, Institute of Health, Shiraz University of Medical Sciences, Shiraz, Iran 8Centre de Biophysique Moléculaire, CNRS, Rue Charles Sadron, Orleans, France Correspondence to: Mohammad Hashemi, email: [email protected]; [email protected] Marek J. Łos, email: [email protected] Keywords: PDCD6; meta-analysis; cancer; risk; endometrial cancer Received: January 08, 2018 Accepted: April 12, 2018 Published: May 15, 2018 Copyright: Hashemi et al. This is an open-access article distributed under the terms of the Creative Commons Attribution License 3.0 (CC BY 3.0), which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited. ABSTRACT This study was designed to evaluate the relationship between Programmed cell death protein 6 (PDCD6) polymorphisms and cancer susceptibility.
    [Show full text]