Cytokine and Growth Factor Catalog
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Fgf17b and FGF18 Have Different Midbrain Regulatory Properties from Fgf8b Or Activated FGF Receptors Aimin Liu1,2, James Y
Research article 6175 FGF17b and FGF18 have different midbrain regulatory properties from FGF8b or activated FGF receptors Aimin Liu1,2, James Y. H. Li2, Carrie Bromleigh2, Zhimin Lao2, Lee A. Niswander1 and Alexandra L. Joyner2,* 1Howard Hughes Medical Institute, Developmental Biology Program, Memorial Sloan Kettering Cancer Center, New York, NY 10021, USA 2Howard Hughes Medical Institute and Skirball Institute of Biomolecular Medicine, Departments of Cell Biology, and Physiology and Neuroscience, NYU School of Medicine, New York, NY 10016, USA *Author for correspondence (e-mail: [email protected]) Accepted 28 August 2003 Development 130, 6175-6185 Published by The Company of Biologists 2003 doi:10.1242/dev.00845 Summary Early patterning of the vertebrate midbrain and region in the midbrain, correlating with cerebellum cerebellum is regulated by a mid/hindbrain organizer that development. By contrast, FGF17b and FGF18 mimic produces three fibroblast growth factors (FGF8, FGF17 FGF8a by causing expansion of the midbrain and and FGF18). The mechanism by which each FGF upregulating midbrain gene expression. This result is contributes to patterning the midbrain, and induces a consistent with Fgf17 and Fgf18 being expressed in the cerebellum in rhombomere 1 (r1) is not clear. We and midbrain and not just in r1 as Fgf8 is. Third, analysis of others have found that FGF8b can transform the midbrain gene expression in mouse brain explants with beads soaked into a cerebellum fate, whereas FGF8a can promote in FGF8b or FGF17b showed that the distinct activities of midbrain development. In this study we used a chick FGF17b and FGF8b are not due to differences in the electroporation assay and in vitro mouse brain explant amount of FGF17b protein produced in vivo. -
The TNF and TNF Receptor Review Superfamilies: Integrating Mammalian Biology
Cell, Vol. 104, 487±501, February 23, 2001, Copyright 2001 by Cell Press The TNF and TNF Receptor Review Superfamilies: Integrating Mammalian Biology Richard M. Locksley,*²³k Nigel Killeen,²k The receptors and ligands in this superfamily have and Michael J. Lenardo§k unique structural attributes that couple them directly to *Department of Medicine signaling pathways for cell proliferation, survival, and ² Department of Microbiology and Immunology differentiation. Thus, they have assumed prominent ³ Howard Hughes Medical Institute roles in the generation of tissues and transient microen- University of California, San Francisco vironments. Most TNF/TNFR SFPs are expressed in the San Francisco, California 94143 immune system, where their rapid and potent signaling § Laboratory of Immunology capabilities are crucial in coordinating the proliferation National Institute of Allergy and Infectious Diseases and protective functions of pathogen-reactive cells. National Institutes of Health Here, we review the organization of the TNF/TNFR SF Bethesda, Maryland 20892 and how these proteins have been adapted for pro- cesses as seemingly disparate as host defense and or- ganogenesis. In interpreting this large and highly active Introduction area of research, we have focused on common themes that unite the actions of these genes in different tissues. Three decades ago, lymphotoxin (LT) and tumor necro- We also discuss the evolutionary success of this super- sis factor (TNF) were identified as products of lympho- familyÐsuccess that we infer from its expansion across cytes and macrophages that caused the lysis of certain the mammalian genome and from its many indispens- types of cells, especially tumor cells (Granger et al., able roles in mammalian biology. -
Supplemental Figure 1. Vimentin
Double mutant specific genes Transcript gene_assignment Gene Symbol RefSeq FDR Fold- FDR Fold- FDR Fold- ID (single vs. Change (double Change (double Change wt) (single vs. wt) (double vs. single) (double vs. wt) vs. wt) vs. single) 10485013 BC085239 // 1110051M20Rik // RIKEN cDNA 1110051M20 gene // 2 E1 // 228356 /// NM 1110051M20Ri BC085239 0.164013 -1.38517 0.0345128 -2.24228 0.154535 -1.61877 k 10358717 NM_197990 // 1700025G04Rik // RIKEN cDNA 1700025G04 gene // 1 G2 // 69399 /// BC 1700025G04Rik NM_197990 0.142593 -1.37878 0.0212926 -3.13385 0.093068 -2.27291 10358713 NM_197990 // 1700025G04Rik // RIKEN cDNA 1700025G04 gene // 1 G2 // 69399 1700025G04Rik NM_197990 0.0655213 -1.71563 0.0222468 -2.32498 0.166843 -1.35517 10481312 NM_027283 // 1700026L06Rik // RIKEN cDNA 1700026L06 gene // 2 A3 // 69987 /// EN 1700026L06Rik NM_027283 0.0503754 -1.46385 0.0140999 -2.19537 0.0825609 -1.49972 10351465 BC150846 // 1700084C01Rik // RIKEN cDNA 1700084C01 gene // 1 H3 // 78465 /// NM_ 1700084C01Rik BC150846 0.107391 -1.5916 0.0385418 -2.05801 0.295457 -1.29305 10569654 AK007416 // 1810010D01Rik // RIKEN cDNA 1810010D01 gene // 7 F5 // 381935 /// XR 1810010D01Rik AK007416 0.145576 1.69432 0.0476957 2.51662 0.288571 1.48533 10508883 NM_001083916 // 1810019J16Rik // RIKEN cDNA 1810019J16 gene // 4 D2.3 // 69073 / 1810019J16Rik NM_001083916 0.0533206 1.57139 0.0145433 2.56417 0.0836674 1.63179 10585282 ENSMUST00000050829 // 2010007H06Rik // RIKEN cDNA 2010007H06 gene // --- // 6984 2010007H06Rik ENSMUST00000050829 0.129914 -1.71998 0.0434862 -2.51672 -
IL17RB Antibody Cat
IL17RB Antibody Cat. No.: 62-448 IL17RB Antibody Formalin-fixed and paraffin-embedded human colon Flow cytometric analysis of HepG2 cells using IL17RB carcinoma reacted with IL17RB Antibody , which was Antibody (bottom histogram) compared to a negative peroxidase-conjugated to the secondary antibody, control cell (top histogram). FITC-conjugated goat-anti- followed by DAB staining. rabbit secondary antibodies were used for the analysis. Specifications HOST SPECIES: Rabbit SPECIES REACTIVITY: Human This IL17_ antibody is generated from rabbits immunized with a KLH conjugated synthetic IMMUNOGEN: peptide between 207-234 amino acids from the Central region of human IL17_. TESTED APPLICATIONS: Flow, IHC-P, WB For WB starting dilution is: 1:1000 APPLICATIONS: For IHC-P starting dilution is: 1:10~50 For FACS starting dilution is: 1:10~50 September 25, 2021 1 https://www.prosci-inc.com/il17rb-antibody-62-448.html PREDICTED MOLECULAR 56 kDa WEIGHT: Properties This antibody is prepared by Saturated Ammonium Sulfate (SAS) precipitation followed by PURIFICATION: dialysis CLONALITY: Polyclonal ISOTYPE: Rabbit Ig CONJUGATE: Unconjugated PHYSICAL STATE: Liquid BUFFER: Supplied in PBS with 0.09% (W/V) sodium azide. CONCENTRATION: batch dependent Store at 4˚C for three months and -20˚C, stable for up to one year. As with all antibodies STORAGE CONDITIONS: care should be taken to avoid repeated freeze thaw cycles. Antibodies should not be exposed to prolonged high temperatures. Additional Info OFFICIAL SYMBOL: IL17RB Interleukin-17 receptor B, IL-17 receptor B, IL-17RB, Cytokine receptor-like 4, IL-17 ALTERNATE NAMES: receptor homolog 1, IL-17Rh1, IL17Rh1, Interleukin-17B receptor, IL-17B receptor, IL17RB, CRL4, EVI27, IL17BR ACCESSION NO.: Q9NRM6 PROTEIN GI NO.: 21263748 GENE ID: 55540 USER NOTE: Optimal dilutions for each application to be determined by the researcher. -
ARTICLES Fibroblast Growth Factors 1, 2, 17, and 19 Are The
0031-3998/07/6103-0267 PEDIATRIC RESEARCH Vol. 61, No. 3, 2007 Copyright © 2007 International Pediatric Research Foundation, Inc. Printed in U.S.A. ARTICLES Fibroblast Growth Factors 1, 2, 17, and 19 Are the Predominant FGF Ligands Expressed in Human Fetal Growth Plate Cartilage PAVEL KREJCI, DEBORAH KRAKOW, PERTCHOUI B. MEKIKIAN, AND WILLIAM R. WILCOX Medical Genetics Institute [P.K., D.K., P.B.M., W.R.W.], Cedars-Sinai Medical Center, Los Angeles, California 90048; Department of Obstetrics and Gynecology [D.K.] and Department of Pediatrics [W.R.W.], UCLA School of Medicine, Los Angeles, California 90095 ABSTRACT: Fibroblast growth factors (FGF) regulate bone growth, (G380R) or TD (K650E) mutations (4–6). When expressed at but their expression in human cartilage is unclear. Here, we deter- physiologic levels, FGFR3-G380R required, like its wild-type mined the expression of entire FGF family in human fetal growth counterpart, ligand for activation (7). Similarly, in vitro cul- plate cartilage. Using reverse transcriptase PCR, the transcripts for tivated human TD chondrocytes as well as chondrocytes FGF1, 2, 5, 8–14, 16–19, and 21 were found. However, only FGF1, isolated from Fgfr3-K644M mice had an identical time course 2, 17, and 19 were detectable at the protein level. By immunohisto- of Fgfr3 activation compared with wild-type chondrocytes and chemistry, FGF17 and 19 were uniformly expressed within the showed no receptor activation in the absence of ligand (8,9). growth plate. In contrast, FGF1 was found only in proliferating and hypertrophic chondrocytes whereas FGF2 localized predominantly to Despite the importance of the FGF ligand for activation of the resting and proliferating cartilage. -
Cytokine Nomenclature
RayBiotech, Inc. The protein array pioneer company Cytokine Nomenclature Cytokine Name Official Full Name Genbank Related Names Symbol 4-1BB TNFRSF Tumor necrosis factor NP_001552 CD137, ILA, 4-1BB ligand receptor 9 receptor superfamily .2. member 9 6Ckine CCL21 6-Cysteine Chemokine NM_002989 Small-inducible cytokine A21, Beta chemokine exodus-2, Secondary lymphoid-tissue chemokine, SLC, SCYA21 ACE ACE Angiotensin-converting NP_000780 CD143, DCP, DCP1 enzyme .1. NP_690043 .1. ACE-2 ACE2 Angiotensin-converting NP_068576 ACE-related carboxypeptidase, enzyme 2 .1 Angiotensin-converting enzyme homolog ACTH ACTH Adrenocorticotropic NP_000930 POMC, Pro-opiomelanocortin, hormone .1. Corticotropin-lipotropin, NPP, NP_001030 Melanotropin gamma, Gamma- 333.1 MSH, Potential peptide, Corticotropin, Melanotropin alpha, Alpha-MSH, Corticotropin-like intermediary peptide, CLIP, Lipotropin beta, Beta-LPH, Lipotropin gamma, Gamma-LPH, Melanotropin beta, Beta-MSH, Beta-endorphin, Met-enkephalin ACTHR ACTHR Adrenocorticotropic NP_000520 Melanocortin receptor 2, MC2-R hormone receptor .1 Activin A INHBA Activin A NM_002192 Activin beta-A chain, Erythroid differentiation protein, EDF, INHBA Activin B INHBB Activin B NM_002193 Inhibin beta B chain, Activin beta-B chain Activin C INHBC Activin C NM005538 Inhibin, beta C Activin RIA ACVR1 Activin receptor type-1 NM_001105 Activin receptor type I, ACTR-I, Serine/threonine-protein kinase receptor R1, SKR1, Activin receptor-like kinase 2, ALK-2, TGF-B superfamily receptor type I, TSR-I, ACVRLK2 Activin RIB ACVR1B -
FGF14 Regulates Presynaptic Ca2+ Channels and Synaptic Transmission
Cell Reports Article FGF14 Regulates Presynaptic Ca2+ Channels and Synaptic Transmission Haidun Yan,1,3 Juan L. Pablo,2,3 and Geoffrey S. Pitt1,2,3,* 1Division of Cardiology, Department of Medicine, Duke University Medical Center, Durham, NC 27710, USA 2Department of Neurobiology, Duke University Medical Center, Durham, NC 27710, USA 3Ion Channel Research Unit, Duke University Medical Center, Durham, NC 27710, USA *Correspondence: [email protected] http://dx.doi.org/10.1016/j.celrep.2013.06.012 This is an open-access article distributed under the terms of the Creative Commons Attribution-NonCommercial-No Derivative Works License, which permits non-commercial use, distribution, and reproduction in any medium, provided the original author and source are credited. SUMMARY data pinpointed FGF14 as the locus for spinocerebellar ataxia 27 (SCA27). Fibroblast growth factor homologous factors (FHFs) Focus on FHF regulation of neuronal excitability began when are not growth factors, but instead bind to voltage- Fgf14–/– mice showed ataxia (Wang et al., 2002), providing + gated Na channels (NaV) and regulate their function. a basis for exploring the implications of a linkage analysis that Mutations in FGF14, an FHF that is the locus for identified a F150S missense mutation in a ‘‘b’’ splice variant of F150S F145S spinocerebellar ataxia 27 (SCA27), are believed to FGF14 (FGF14b ; termed FGF14 in some studies that be pathogenic because of a dominant-negative used numbering based on the alternatively spliced FGF14a variant) as the etiology of the autosomal-dominant SCA27 in reduction of Na currents in cerebellar granule cells. V an extended Dutch family (van Swieten et al., 2003). -
Role and Regulation of Pdgfra Signaling in Liver Development and Regeneration
The American Journal of Pathology, Vol. 182, No. 5, May 2013 ajp.amjpathol.org GROWTH FACTORS, CYTOKINES, AND CELL CYCLE MOLECULES Role and Regulation of PDGFRa Signaling in Liver Development and Regeneration Prince K. Awuah,* Kari N. Nejak-Bowen,* and Satdarshan P.S. Monga*y From the Division of Experimental Pathology,* Department of Pathology, and the Department of Medicine,y University of Pittsburgh, Pittsburgh, Pennsylvania Accepted for publication January 22, 2013. Aberrant platelet-derived growth factor receptor-a (PDGFRa) signaling is evident in a subset of hepato- cellular cancers (HCCs). However, its role and regulation in hepatic physiology remains elusive. In the Address correspondence to a fi Satdarshan P.S. Monga, M.D., current study, we examined PDGFR signaling in liver development and regeneration. We identi ed a a Divisions of Experimental notable PDGFR activation in hepatic morphogenesis that, when interrupted by PDGFR -blocking anti- Pathology, Pathology and body, led to decreased hepatoblast proliferation and survival in embryonic liver cultures. We also identified Medicine, University of Pitts- temporal PDGFRa overexpression, which is regulated by epidermal growth factor (EGF) and tumor necrosis burgh School of Medicine, 200 factor a, and its activation at 3 to 24 hours after partial hepatectomy. Through generation of hepatocyte- Lothrop St., S-422 BST, Pitts- specific PDGFRA knockout (KO) mice that lack an overt phenotype, we show that absent PDGFRa burgh, PA 15261. E-mail: compromises extracelluar signal-regulated kinases and AKT activation 3 hours after partial hepatectomy, [email protected]. which, however, is alleviated by temporal compensatory increases in the EGF receptor (EGFR) and the hepatocyte growth factor receptor (Met) expression and activation along with rebound activation of extracellular signal-regulated kinases and AKT at 24 hours. -
IL-12 Abrogates Calcineurin-Dependent Immune Evasion During Leukemia Progression
Author Manuscript Published OnlineFirst on May 29, 2019; DOI: 10.1158/0008-5472.CAN-18-3800 Author manuscripts have been peer reviewed and accepted for publication but have not yet been edited. IL-12 abrogates calcineurin-dependent immune evasion during leukemia progression Jennifer L. Rabe,1* Lori Gardner,2* Rae Hunter,3 Jairo A. Fonseca,3 Jodi Dougan,3 Christy M. Gearheart,2 Michael S. Leibowitz,2 Cathy Lee-Miller,2 Dmitry Baturin,2 Susan P. Fosmire,2 Susan E. Zelasko,2 Courtney L. Jones,2 Jill E. Slansky,4 Manali Rupji,5 Bhakti Dwivedi,5 Curtis J. Henry,3,5,6 and Christopher C. Porter3,5,6 Affiliations: 1Molecular Biology Program, University of Colorado Denver, Aurora, CO. 2Department of Pediatrics, University of Colorado, Aurora, CO 3Department of Pediatrics, Emory University School of Medicine, Atlanta, GA 4Integrated Department of Immunology, University of Colorado School of Medicine, Aurora, CO 5Winship Cancer Institute, Emory University, Atlanta, GA 6Aflac Cancer and Blood Disorders Center, Children’s Healthcare of Atlanta, GA JR and LAG contributed equally to this study. Corresponding Author: Christopher C. Porter, MD Emory University School of Medicine 1760 Haygood Drive, E370 Atlanta, GA 30322 Phone: 404-727-4881 Fax: 404-727-4455 [email protected] Running title: Leukemia-cell calcineurin drives immune evasion Conflict of interest statement The authors have declared that no conflicts of interest exist. Abstract: 199 words Main Text: 5797 words (excluding figure legends and references) Downloaded from cancerres.aacrjournals.org on October 2, 2021. © 2019 American Association for Cancer Research. Author Manuscript Published OnlineFirst on May 29, 2019; DOI: 10.1158/0008-5472.CAN-18-3800 Author manuscripts have been peer reviewed and accepted for publication but have not yet been edited. -
Fibroblast Growth Factor 12 Is Expressed in Spiral and Vestibular
www.nature.com/scientificreports OPEN Fibroblast growth factor 12 is expressed in spiral and vestibular ganglia and necessary for auditory Received: 5 February 2018 Accepted: 26 June 2018 and equilibrium function Published: xx xx xxxx Yukiko Hanada1,2, Yukiko Nakamura1, Yoshiyuki Ozono2, Yusuke Ishida1,3, Yasumitsu Takimoto1,2,4, Manabu Taniguchi5, Kazuya Ohata1,2, Yoshihisa Koyama1, Takao Imai2, Tetsuo Morihana2,6, Makoto Kondo1, Takashi Sato2, Hidenori Inohara2 & Shoichi Shimada1 We investigated fbroblast growth factor 12 (FGF12) as a transcript enriched in the inner ear by searching published cDNA library databases. FGF12 is a fbroblast growth factor homologous factor, a subset of the FGF superfamily. To date, its localisation and function in the inner ear have not been determined. Here, we show that FGF12 mRNA is localised in spiral ganglion neurons (SGNs) and the vestibular ganglion. We also show that FGF12 protein is localised in SGNs, the vestibular ganglion, and nerve fbres extending beneath hair cells. Moreover, we investigated FGF12 function in auditory and vestibular systems using Fgf12-knockout (FGF12-KO) mice generated with CRISPR/Cas9 technology. Our results show that the inner ear morphology of FGF12-KO mice is not signifcantly diferent compared with wild-type mice. However, FGF12-KO mice exhibited an increased hearing threshold, as measured by the auditory brainstem response, as well as defcits in rotarod and balance beam performance tests. These results suggest that FGF12 is necessary for normal auditory and equilibrium function. Hearing loss is a common problem in people of all ages. Te World Health Organization reports that 360 million people worldwide have hearing loss, with 32 million being children1. -
Human IL12A / NKSF1 Protein (His Tag)
Human IL12A / NKSF1 Protein (His Tag) Catalog Number: 10021-H08H General Information SDS-PAGE: Gene Name Synonym: CLMF; IL-12A; NFSK; NKSF1; P35 Protein Construction: A DNA sequence encoding the p35 subunit of human IL12, termed as IL12A (P29459) (Met 1-Ser 219) was expressed, fused with a polyhistidine tag at the C-terminus. Source: Human Expression Host: HEK293 Cells QC Testing Purity: > 92 % as determined by SDS-PAGE Bio Activity： Protein Description Measured by its ability to bind Human IL12B-his in functional ELISA. Interleukin-12 subunit alpha (IL12A/IL-12p35) is also known as Cytotoxic lymphocyte maturation factor 35 kDa subunit, cytotoxic lymphocyte Endotoxin: maturation factor 1, p35, NK cell stimulatory factor chain 1, and interleukin- 12 alpha chain. IL12A/IL-12p35 is a subunit of a cytokine that acts on T < 1.0 EU per μg of the protein as determined by the LAL method and natural killer cells, and has a broad array of biological activities. The cytokine is a disulfide-linked heterodimer composed of the 35-kD subunit Stability: encoded by this gene, and a 40-kD subunit that is a member of the Samples are stable for up to twelve months from date of receipt at -70 ℃ cytokine receptor family. IL12A/IL-12p35 is required for the T-cell- independent induction of IFN-gamma, and is important for the Predicted N terminal: Arg 23 differentiation of both Th1 and Th2 cells. The responses of lymphocytes to this cytokine are mediated by the activator of transcription protein STAT4. Molecular Mass: Nitric oxide synthase 2A (NOS2A/NOS2) is found to be required for the signaling process of this cytokine in innate immunity. -
Single-Cell RNA Sequencing Demonstrates the Molecular and Cellular Reprogramming of Metastatic Lung Adenocarcinoma
ARTICLE https://doi.org/10.1038/s41467-020-16164-1 OPEN Single-cell RNA sequencing demonstrates the molecular and cellular reprogramming of metastatic lung adenocarcinoma Nayoung Kim 1,2,3,13, Hong Kwan Kim4,13, Kyungjong Lee 5,13, Yourae Hong 1,6, Jong Ho Cho4, Jung Won Choi7, Jung-Il Lee7, Yeon-Lim Suh8,BoMiKu9, Hye Hyeon Eum 1,2,3, Soyean Choi 1, Yoon-La Choi6,10,11, Je-Gun Joung1, Woong-Yang Park 1,2,6, Hyun Ae Jung12, Jong-Mu Sun12, Se-Hoon Lee12, ✉ ✉ Jin Seok Ahn12, Keunchil Park12, Myung-Ju Ahn 12 & Hae-Ock Lee 1,2,3,6 1234567890():,; Advanced metastatic cancer poses utmost clinical challenges and may present molecular and cellular features distinct from an early-stage cancer. Herein, we present single-cell tran- scriptome profiling of metastatic lung adenocarcinoma, the most prevalent histological lung cancer type diagnosed at stage IV in over 40% of all cases. From 208,506 cells populating the normal tissues or early to metastatic stage cancer in 44 patients, we identify a cancer cell subtype deviating from the normal differentiation trajectory and dominating the metastatic stage. In all stages, the stromal and immune cell dynamics reveal ontological and functional changes that create a pro-tumoral and immunosuppressive microenvironment. Normal resident myeloid cell populations are gradually replaced with monocyte-derived macrophages and dendritic cells, along with T-cell exhaustion. This extensive single-cell analysis enhances our understanding of molecular and cellular dynamics in metastatic lung cancer and reveals potential diagnostic and therapeutic targets in cancer-microenvironment interactions. 1 Samsung Genome Institute, Samsung Medical Center, Seoul 06351, Korea.