Tyrosine Kinase Panel

Total Page:16

File Type:pdf, Size:1020Kb

Tyrosine Kinase Panel KinaseSeeker™ TK Panel (126 Wild-Type and Full-Length Kinases) Kinase Group Kinase Group ABL1 TK EPHA3 intracellular module TK ABL1 full-length TK EPHA4 TK ABL2 TK EPHA4 intracellular module TK ALK TK EPHA5 TK AXL TK EPHA5 intracellular module TK BLK TK EPHA6 TK BLK full-length TK EPHA6 intracellular module TK BMX TK EPHA7 TK BTK TK EPHA7 intracellular module TK BTK full-length TK EPHA8 TK CSF1R TK EPHA8 intracellular module TK CSF1R intracellular module TK EPHB2 TK CSK TK EPHB3 TK CSK full-length TK EPHB3 intracellular module TK DDR1 TK EPHB4 TK DDR1 intracellular module TK EPHB4 intracellular module TK DDR2 TK EPHB6 TK DDR2 intracellular module TK ERBB2 TK EGFR TK ERBB2 intracellular module TK EGFR intracellular module TK ERBB3 TK EPHA1 TK ERBB4 intracellular module TK EPHA1 intracellular module TK FAK TK EPHA2 TK FAK full-length TK EPHA2 intracellular module TK FER TK EPHA3 TK FES TK Legend: Full-Length: Construct contains Full-length kinase Intracellular Module: Construct contains Cytoplasmic Region in Receptor Tyrosine Kinases Page 1 of 3 KinaseSeeker™ TK Panel (126 Wild-Type and Full-Length Kinases) Kinase Group Kinase Group FGFR2 TK INSRR TK FGFR2 intracellular module TK ITK TK FGFR3 TK JAK2 TK FGFR3 intracellular module TK JAK3 TK FGFR4 TK KIT TK FGR TK KIT intracellular module TK FGR full-length TK LCK TK FLT1 TK LCK full-length TK FLT1 intracellular module TK LYN TK FLT2 TK LYN full-length TK FLT2 intracellular module TK MET TK FLT3 TK MET intracellular module TK FLT4 TK MST1R/RON TK FLT4 intracellular module TK MUSK TK FRK TK MUSK intracellular module TK FRK full-length TK NTRK1 TK FYN TK NTRK2 TK FYN full-length TK NTRK2 intracellular module TK HCK TK NTRK3 TK HCK full-length isoform1 TK NTRK3 intracellular module TK HCK full-length isoform2 TK PDGFRA TK IGF1R TK PDGFRA intracellular module TK IGF1R intracellular module TK PDGFRB TK INSR TK PDGFRB intracellular module TK INSR intracellular module TK PTK6 TK Legend: Full-Length: Construct contains Full-length kinase Intracellular Module: Construct contains Cytoplasmic Region in Receptor Tyrosine Kinases Page 2 of 3 KinaseSeeker™ TK Panel (126 Wild-Type and Full-Length Kinases) Kinase Group Kinase Group PTK6 full-length TK YES1 full-length TK PYK2 TK PYK2 full-length TK RET TK To place an order or request a quote, please RET intracellular module TK contact us at: ROS1 TK Phone: (520) 495-0161 ROS1 intracellular module TK Email: [email protected] SRC TK SRC full-length TK SRMS TK SYK TK TEC TK TIE1 TK TIE1 intracellular module TK TIE2 TK TIE2 intracellular module TK TNK1 TK TNK1 full-length TK TNK2 TK TXK TK TYRO3 TK TYRO3 intracellular module TK VEGFR2 TK VEGFR2 intracellular module TK YES1 TK Legend: Full-Length: Construct contains Full-length kinase Intracellular Module: Construct contains Cytoplasmic Region in Receptor Tyrosine Kinases Page 3 of 3 .
Recommended publications
  • Gene Symbol Gene Description ACVR1B Activin a Receptor, Type IB
    Table S1. Kinase clones included in human kinase cDNA library for yeast two-hybrid screening Gene Symbol Gene Description ACVR1B activin A receptor, type IB ADCK2 aarF domain containing kinase 2 ADCK4 aarF domain containing kinase 4 AGK multiple substrate lipid kinase;MULK AK1 adenylate kinase 1 AK3 adenylate kinase 3 like 1 AK3L1 adenylate kinase 3 ALDH18A1 aldehyde dehydrogenase 18 family, member A1;ALDH18A1 ALK anaplastic lymphoma kinase (Ki-1) ALPK1 alpha-kinase 1 ALPK2 alpha-kinase 2 AMHR2 anti-Mullerian hormone receptor, type II ARAF v-raf murine sarcoma 3611 viral oncogene homolog 1 ARSG arylsulfatase G;ARSG AURKB aurora kinase B AURKC aurora kinase C BCKDK branched chain alpha-ketoacid dehydrogenase kinase BMPR1A bone morphogenetic protein receptor, type IA BMPR2 bone morphogenetic protein receptor, type II (serine/threonine kinase) BRAF v-raf murine sarcoma viral oncogene homolog B1 BRD3 bromodomain containing 3 BRD4 bromodomain containing 4 BTK Bruton agammaglobulinemia tyrosine kinase BUB1 BUB1 budding uninhibited by benzimidazoles 1 homolog (yeast) BUB1B BUB1 budding uninhibited by benzimidazoles 1 homolog beta (yeast) C9orf98 chromosome 9 open reading frame 98;C9orf98 CABC1 chaperone, ABC1 activity of bc1 complex like (S. pombe) CALM1 calmodulin 1 (phosphorylase kinase, delta) CALM2 calmodulin 2 (phosphorylase kinase, delta) CALM3 calmodulin 3 (phosphorylase kinase, delta) CAMK1 calcium/calmodulin-dependent protein kinase I CAMK2A calcium/calmodulin-dependent protein kinase (CaM kinase) II alpha CAMK2B calcium/calmodulin-dependent
    [Show full text]
  • Abnormal Embryonic Lymphatic Vessel Development in Tie1 Hypomorphic Mice Xianghu Qu, Kevin Tompkins, Lorene E
    © 2014. Published by The Company of Biologists Ltd | Development (2014) 141, 1417 doi:10.1242/dev.108969 CORRECTION Abnormal embryonic lymphatic vessel development in Tie1 hypomorphic mice Xianghu Qu, Kevin Tompkins, Lorene E. Batts, Mira Puri and H. Scott Baldwin There was an error published in Development 137, 1285-1295. Author name H. Scott Baldwin was incomplete. The correct author list appears above. The authors apologise to readers for this mistake. 1417 RESEARCH ARTICLE 1285 Development 137, 1285-1295 (2010) doi:10.1242/dev.043380 © 2010. Published by The Company of Biologists Ltd Abnormal embryonic lymphatic vessel development in Tie1 hypomorphic mice Xianghu Qu1, Kevin Tompkins1, Lorene E. Batts1, Mira Puri2 and Scott Baldwin1,3,* SUMMARY Tie1 is an endothelial receptor tyrosine kinase that is essential for development and maintenance of the vascular system; however, the role of Tie1 in development of the lymphatic vasculature is unknown. To address this question, we first documented that Tie1 is expressed at the earliest stages of lymphangiogenesis in Prox1-positive venous lymphatic endothelial cell (LEC) progenitors. LEC Tie1 expression is maintained throughout embryonic development and persists in postnatal mice. We then generated two lines of Tie1 mutant mice: a hypomorphic allele, which has reduced expression of Tie1, and a conditional allele. Reduction of Tie1 levels resulted in abnormal lymphatic patterning and in dilated and disorganized lymphatic vessels in all tissues examined and in impaired lymphatic drainage in embryonic skin. Homozygous hypomorphic mice also exhibited abnormally dilated jugular lymphatic vessels due to increased production of Prox1-positive LECs during initial lymphangiogenesis, indicating that Tie1 is required for the early stages of normal lymphangiogenesis.
    [Show full text]
  • Discovery of Orphan Receptor Tie1 and Angiopoietin Ligands Ang1 and Ang4 As Novel GAG-Binding Partners
    78 Chapter 3 Discovery of Orphan Receptor Tie1 and Angiopoietin Ligands Ang1 and Ang4 as Novel GAG-Binding Partners 79 3.1 Abstract The Tie/Ang signaling axis is necessary for proper vascular development and remodeling. However, the mechanisms that modulate signaling through this receptor tyrosine kinase pathway are relatively unclear. In particular, the role of the orphan receptor Tie1 is highly disputed. Although this protein is required for survival, Tie1 has been found both to inhibit and yet be necessary for Tie2 signaling. While differing expression levels have been put forth as an explanation for its context-specific activity, the lack of known endogenous ligands for Tie1 has severely hampered understanding its molecular mode of action. Here we describe the discovery of orphan receptor Tie1 and angiopoietin ligands Ang1 and Ang4 as novel GAG binding partners. We localize the binding site of GAGs to the N- terminal region of Tie1, which may provide structural insights into the importance of this interaction regarding the formation of Tie1-Tie2 heterodimerization. Furthermore, we use our mutagenesis studies to guide the generation of a mouse model that specifically ablates GAG-Tie1 binding in vivo for further characterization of the functional outcomes of GAG-Tie1 binding. We also show that GAGs can form a trimeric complex with Ang1/4 and Tie2 using our microarray technology. Finally, we use our HaloTag glycan engineering platform to modify the cell surface of endothelial cells and demonstrate that HS GAGs can potentiate Tie2 signaling in a sulfation-specific manner, providing the first evidence of the involvement of HS GAGs in Tie/Ang signaling and delineating further the integral role of HS GAGs in angiogenesis.
    [Show full text]
  • Mutation-Specific and Common Phosphotyrosine Signatures of KRAS G12D and G13D Alleles Anticipated Graduation August 1St, 2018
    MUTATION-SPECIFIC AND COMMON PHOSPHOTYROSINE SIGNATURES OF KRAS G12D AND G13D ALLELES by Raiha Tahir A dissertation submitted to The Johns Hopkins University in conformity with the requirement of the degree of Doctor of Philosophy Baltimore, MD August 2018 © 2018 Raiha Tahir All Rights Reserved ABSTRACT KRAS is one of the most frequently mutated genes across all cancer subtypes. Two of the most frequent oncogenic KRAS mutations observed in patients result in glycine to aspartic acid substitution at either codon 12 (G12D) or 13 (G13D). Although the biochemical differences between these two predominant mutations are not fully understood, distinct clinical features of the resulting tumors suggest involvement of disparate signaling mechanisms. When we compared the global phosphotyrosine proteomic profiles of isogenic colorectal cancer cell lines bearing either G12D or G13D KRAS mutations, we observed both shared as well as unique signaling events induced by the two KRAS mutations. Remarkably, while the G12D mutation led to an increase in membrane proximal and adherens junction signaling, the G13D mutation led to activation of signaling molecules such as non-receptor tyrosine kinases, MAPK kinases and regulators of metabolic processes. The importance of one of the cell surface molecules, MPZL1, which found to be hyperphosphorylated in G12D cells, was confirmed by cellular assays as its knockdown led to a decrease in proliferation of G12D but not G13D expressing cells. Overall, our study reveals important signaling differences across two common KRAS mutations and highlights the utility of our approach to systematically dissect the subtle differences between related oncogenic mutants and potentially lead to individualized treatments.
    [Show full text]
  • Cytokine Signaling Through the Novel Tyrosine Kinase RAFTK in Kaposi's
    Cytokine Signaling Through the Novel Tyrosine Kinase RAFTK in Kaposi’s Sarcoma Cells Zhong-Ying Liu,* Ramesh K. Ganju,*Jian-Feng Wang,* Mel A. Ona,* William C. Hatch,* Tong Zheng,‡ Shalom Avraham,* Parkash Gill,‡ and Jerome E. Groopman* *Divisions of Experimental Medicine and Hematology/Oncology, Beth Israel Deaconess Medical Center, Harvard Medical School, Boston, Massachusetts 02215; and ‡Division of Hematology/Oncology, Norris Cancer Center, University of Southern California, Los Angeles, California 90033 Abstract believed to be from the lymphatic endothelium (1–2). Etiolog- ical factors implicated in KS include the recently discovered A number of cytokines, including basic fibroblast growth human herpesvirus 8 (HHV-8)/Kaposi’s sarcoma herpesvirus factor (bFGF), vascular endothelial growth factor (VEGF), (KSHV) and TAT, the soluble transcriptional activator of oncostatin M (OSM), IL-6, and tumor necrosis factor alpha HIV (3–7). Considerable data indicate a role for endogenous (TNF-a), have been postulated to have a role in the patho- and exogenous cytokines in the pathogenesis of KS (8–16). genesis of Kaposi’s sarcoma (KS). The proliferative effects Growth factors such as basic fibroblast growth factor (bFGF) of bFGF and OSM may be via their reported activation of and vascular endothelial growth factor (VEGF), which are the c-Jun NH2-terminal kinase (JNK) signaling pathway in known to stimulate the mitogenesis of certain types of endo- KS cells. We now report that KS cells express a recently thelium, as well as Oncostatin M (OSM), IL-6, and tumor ne- identified focal adhesion kinase termed RAFTK which ap- crosis factor alpha (TNF-a) which are elaborated during in- pears in other cell systems to coordinate surface signals be- flammatory conditions, have been implicated in promoting KS tween cytokine and integrin receptors and the cytoskeleton cell growth (17–25).
    [Show full text]
  • Effects of Simultaneous Knockdown of HER2 and PTK6 on Malignancy and Tumor Progression in Human Breast Cancer Cells
    Published OnlineFirst January 30, 2013; DOI: 10.1158/1541-7786.MCR-12-0378 Molecular Cancer Oncogenes and Tumor Suppressors Research Effects of Simultaneous Knockdown of HER2 and PTK6 on Malignancy and Tumor Progression in Human Breast Cancer Cells Natalie Ludyga1, Natasa Anastasov2, Michael Rosemann2, Jana Seiler1, Nadine Lohmann1, Herbert Braselmann3, Karin Mengele4, Manfred Schmitt4, Heinz Ho€fler1,5, and Michaela Aubele1 Abstract Breast cancer is the most common malignancy in women of the Western world. One prominent feature of breast cancer is the co- and overexpression of HER2 and protein tyrosine kinase 6 (PTK6). According to the current clinical cancer therapy guidelines, HER2-overexpressing tumors are routinely treated with trastuzumab, a humanized monoclonal antibody targeting HER2. Approximately, 30% of HER2-overexpressing breast tumors at least initially respond to the anti-HER2 therapy, but a subgroup of these tumors develops resistance shortly after the administration of trastuzumab. A PTK6-targeted therapy does not yet exist. Here, we show for the first time that the simultaneous knockdown in vitro, compared with the single knockdown of HER2 and PTK6, in particular in the trastuzumab-resistant JIMT-1 cells, leads to a significantly decreased phosphorylation of crucial signaling proteins: mitogen-activated protein kinase 1/3 (MAPK 1/3, ERK 1/2) and p38 MAPK, and (phosphatase and tensin homologue deleted on chromosome ten) PTEN that are involved in tumorigenesis. In addition, dual knockdown strongly reduced the migration and invasion of the JIMT-1 cells. Moreover, the downregulation of HER2 and PTK6 led to an induction of p27, and the dual knockdown significantly diminished cell proliferation in JIMT-1 and T47D cells.
    [Show full text]
  • Profiling Data
    Compound Name DiscoveRx Gene Symbol Entrez Gene Percent Compound Symbol Control Concentration (nM) JNK-IN-8 AAK1 AAK1 69 1000 JNK-IN-8 ABL1(E255K)-phosphorylated ABL1 100 1000 JNK-IN-8 ABL1(F317I)-nonphosphorylated ABL1 87 1000 JNK-IN-8 ABL1(F317I)-phosphorylated ABL1 100 1000 JNK-IN-8 ABL1(F317L)-nonphosphorylated ABL1 65 1000 JNK-IN-8 ABL1(F317L)-phosphorylated ABL1 61 1000 JNK-IN-8 ABL1(H396P)-nonphosphorylated ABL1 42 1000 JNK-IN-8 ABL1(H396P)-phosphorylated ABL1 60 1000 JNK-IN-8 ABL1(M351T)-phosphorylated ABL1 81 1000 JNK-IN-8 ABL1(Q252H)-nonphosphorylated ABL1 100 1000 JNK-IN-8 ABL1(Q252H)-phosphorylated ABL1 56 1000 JNK-IN-8 ABL1(T315I)-nonphosphorylated ABL1 100 1000 JNK-IN-8 ABL1(T315I)-phosphorylated ABL1 92 1000 JNK-IN-8 ABL1(Y253F)-phosphorylated ABL1 71 1000 JNK-IN-8 ABL1-nonphosphorylated ABL1 97 1000 JNK-IN-8 ABL1-phosphorylated ABL1 100 1000 JNK-IN-8 ABL2 ABL2 97 1000 JNK-IN-8 ACVR1 ACVR1 100 1000 JNK-IN-8 ACVR1B ACVR1B 88 1000 JNK-IN-8 ACVR2A ACVR2A 100 1000 JNK-IN-8 ACVR2B ACVR2B 100 1000 JNK-IN-8 ACVRL1 ACVRL1 96 1000 JNK-IN-8 ADCK3 CABC1 100 1000 JNK-IN-8 ADCK4 ADCK4 93 1000 JNK-IN-8 AKT1 AKT1 100 1000 JNK-IN-8 AKT2 AKT2 100 1000 JNK-IN-8 AKT3 AKT3 100 1000 JNK-IN-8 ALK ALK 85 1000 JNK-IN-8 AMPK-alpha1 PRKAA1 100 1000 JNK-IN-8 AMPK-alpha2 PRKAA2 84 1000 JNK-IN-8 ANKK1 ANKK1 75 1000 JNK-IN-8 ARK5 NUAK1 100 1000 JNK-IN-8 ASK1 MAP3K5 100 1000 JNK-IN-8 ASK2 MAP3K6 93 1000 JNK-IN-8 AURKA AURKA 100 1000 JNK-IN-8 AURKA AURKA 84 1000 JNK-IN-8 AURKB AURKB 83 1000 JNK-IN-8 AURKB AURKB 96 1000 JNK-IN-8 AURKC AURKC 95 1000 JNK-IN-8
    [Show full text]
  • Itk Tyrosine Kinase Substrate Docking Is Mediated by a Nonclassical SH2 Domain Surface of PLC␥1
    Itk tyrosine kinase substrate docking is mediated by a nonclassical SH2 domain surface of PLC␥1 Lie Min, Raji E. Joseph, D. Bruce Fulton, and Amy H. Andreotti1 Department of Biochemistry, Biophysics, and Molecular Biology, Iowa State University, Ames, IA 50011 Edited by Susan S. Taylor, University of California at San Diego, La Jolla, CA, and approved October 20, 2009 (received for review October 1, 2009) Interleukin-2 tyrosine kinase (Itk) is a Tec family tyrosine kinase that We have previously shown that the PLC␥1 SH2C domain mediates signaling processes after T cell receptor engagement. Acti- (spanning residues 659–756 within full-length PLC␥1) binds di- vation of Itk requires recruitment to the membrane via its pleckstrin rectly to the Itk kinase domain and is required for efficient homology domain, phosphorylation of Itk by the Src kinase, Lck, and phosphorylation of Y783 by Itk (26). Fragments of PLC␥1 that binding of Itk to the SLP-76/LAT adapter complex. After activation, Itk contain Y783 but not the SH2C domain are not efficiently phos- phosphorylates and activates phospholipase C-␥1 (PLC-␥1), leading to phorylated by Itk. Moreover, phosphorylation of PLC␥1 substrate production of two second messengers, DAG and IP3. We have previ- fragments that contain both SH2C and Y783 (spanning 659–789, ously shown that phosphorylation of PLC-␥1 by Itk requires a direct, hereafter referred to as PLC␥1 SH2C-linker) can be inhibited by phosphotyrosine-independent interaction between the Src homol- titration with isolated PLC␥1 SH2C domain (26). The excess, free ogy 2 (SH2) domain of PLC-␥1 and the kinase domain of Itk.
    [Show full text]
  • Novel Protein-Tyrosine Kinase Gene (Hck) Preferentially Expressed in Cells of Hematopoietic Origin STEVEN F
    MOLECULAR AND CELLULAR BIOLOGY, June 1987, p. 2276-2285 Vol. 7, No. 6 0270-7306/87/062276-10$02.00/0 Copyright © 1987, American Society for Microbiology Novel Protein-Tyrosine Kinase Gene (hck) Preferentially Expressed in Cells of Hematopoietic Origin STEVEN F. ZIEGLER,"12 JAMEY D. MARTH,"', DAVID B. LEWIS,4 AND ROGER M. PERLMUTTER' 2,5* Howard Hughes Medical Institute' and the Departments ofBiochemistry,2 Medicine,s Pediatrics,4 and Pharmacology,3 University of Washington School of Medicine, Seattle, Washington 98195 Received 16 December 1986/Accepted 18 March 1987 Protein-tyrosine kinases are implicated in the control of cell growth by virtue of their frequent appearance as products of retroviral oncogenes and as components of growth factor receptors. Here we report the characterization of a novel human protein-tyrosine kinase gene (hck) that is primarily expressed in hematopoietic cells, particularly granulocytes. The hck gene encodes a 505-residue polypeptide that is closely related to pp56kk, a lymphocyte-specific protein-tyrosine kinase. The exon breakpoints of the hck gene, partially defined by using murine genomic clones, demonstrate that hck is a member of the src gene family and has been subjected to strong selection pressure during mammalian evolution. High-level expression of hck transcripts in granulocytes is especially provocative since these cells are terminally differentiated and typically survive in vivo for only a few hours. Thus the hck gene, like other members of the src gene family, appears to function primarily in cells with little growth potential. Specific phosphorylation of proteins on tyrosine residues line Ml induces monocytoid differentiation (18), presumably was first detected in lysates of cells infected with acutely as a result of activation of endogenous pp60csrc (7).
    [Show full text]
  • Src-Family Kinases Impact Prognosis and Targeted Therapy in Flt3-ITD+ Acute Myeloid Leukemia
    Src-Family Kinases Impact Prognosis and Targeted Therapy in Flt3-ITD+ Acute Myeloid Leukemia Title Page by Ravi K. Patel Bachelor of Science, University of Minnesota, 2013 Submitted to the Graduate Faculty of School of Medicine in partial fulfillment of the requirements for the degree of Doctor of Philosophy University of Pittsburgh 2019 Commi ttee Membership Pa UNIVERSITY OF PITTSBURGH SCHOOL OF MEDICINE Commi ttee Membership Page This dissertation was presented by Ravi K. Patel It was defended on May 31, 2019 and approved by Qiming (Jane) Wang, Associate Professor Pharmacology and Chemical Biology Vaughn S. Cooper, Professor of Microbiology and Molecular Genetics Adrian Lee, Professor of Pharmacology and Chemical Biology Laura Stabile, Research Associate Professor of Pharmacology and Chemical Biology Thomas E. Smithgall, Dissertation Director, Professor and Chair of Microbiology and Molecular Genetics ii Copyright © by Ravi K. Patel 2019 iii Abstract Src-Family Kinases Play an Important Role in Flt3-ITD Acute Myeloid Leukemia Prognosis and Drug Efficacy Ravi K. Patel, PhD University of Pittsburgh, 2019 Abstract Acute myelogenous leukemia (AML) is a disease characterized by undifferentiated bone-marrow progenitor cells dominating the bone marrow. Currently the five-year survival rate for AML patients is 27.4 percent. Meanwhile the standard of care for most AML patients has not changed for nearly 50 years. We now know that AML is a genetically heterogeneous disease and therefore it is unlikely that all AML patients will respond to therapy the same way. Upregulation of protein-tyrosine kinase signaling pathways is one common feature of some AML tumors, offering opportunities for targeted therapy.
    [Show full text]
  • Recombinant Human Epha8 Fc Chimera Catalog Number: 6828-A8
    Recombinant Human EphA8 Fc Chimera Catalog Number: 6828-A8 DESCRIPTION Source Mouse myeloma cell line, NS0­derived Human EphA8 Human IgG (Glu31­Thr542) IEGRMD 1 (Pro100­Lys330) Accession # NP_065387 N­terminus C­terminus N­terminal Sequence Glu31 Analysis Structure / Form Disulfide­linked homodimer Predicted Molecular 83.2 kDa (monomer) Mass SPECIFICATIONS SDS­PAGE 94 kDa, reducing conditions Activity Measured by its binding ability in a functional ELISA. When Recombinant Human EphA8 Fc Chimera is coated at 2 μg/mL (100 μL/well), the concentration of Biotinylayed Recombinant Human Ephrin­A5 Fc Chimera (Catalog # BT374) that produces 50% of the optimal binding response is 2­12 ng/mL. Endotoxin Level <0.01 EU per 1 μg of the protein by the LAL method. Purity >90%, by SDS­PAGE under reducing conditions and visualized by silver stain. Formulation Supplied as a 0.2 μm filtered solution in MES, NaCl, PEG, CHAPS and Imidazole. See Certificate of Analysis for details. PREPARATION AND STORAGE Shipping The product is shipped with dry ice or equivalent. Upon receipt, store it immediately at the temperature recommended below. Stability & Storage Use a manual defrost freezer and avoid repeated freeze­thaw cycles. l 12 months from date of receipt, ­70 °C as supplied. l 1 month, 2 to 8 °C under sterile conditions after opening. l 3 months, ­20 to ­70 °C under sterile conditions after opening. BACKGROUND EphA8, also known as Hek3 and Eek, is a 120 kDa glycosylated member of the Eph family of transmembrane receptor tyrosine kinases (1, 2). The A and B classes of Eph proteins are distinguished by Ephrin ligand binding preference but have a common structural organization.
    [Show full text]
  • Anti-INSRR / IRR (Beta Chain) Antibody (ARG40358)
    Product datasheet [email protected] ARG40358 Package: 100 μl anti-INSRR / IRR (beta chain) antibody Store at: -20°C Summary Product Description Rabbit Polyclonal antibody recognizes INSRR / IRR (beta chain) Tested Reactivity Hu Tested Application IHC-P, WB Host Rabbit Clonality Polyclonal Isotype IgG Target Name INSRR / IRR (beta chain) Antigen Species Human Immunogen KLH-conjugated synthetic peptide corresponding to aa. 668-702 of Human INSRR. Conjugation Un-conjugated Alternate Names Insulin receptor-related protein; IRR; EC 2.7.10.1; IR-related receptor; Insulin Receptor R Application Instructions Application table Application Dilution IHC-P 1:25 WB 1:1000 Application Note * The dilutions indicate recommended starting dilutions and the optimal dilutions or concentrations should be determined by the scientist. Positive Control HeLa Calculated Mw 144 kDa Properties Form Liquid Purification Purification with Protein A and immunogen peptide. Buffer PBS and 0.09% (W/V) Sodium azide. Preservative 0.09% (W/V) Sodium azide. 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 or below. 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. Note For laboratory research only, not for drug, diagnostic or other use. www.arigobio.com 1/2 Bioinformation Gene Symbol INSRR Gene Full Name insulin receptor-related receptor Function Receptor with tyrosine-protein kinase activity. Functions as a pH sensing receptor which is activated by increased extracellular pH.
    [Show full text]