06-203 | Anti-SHC Antibody

06-203
250 µg  
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      Overview

      Replacement Information

      Key Spec Table

      Species ReactivityKey ApplicationsHostFormatAntibody Type
      H, M, Po, RIHC, IP, WBRbPurifiedPolyclonal Antibody
      Description
      Catalogue Number06-203
      Brand Family Upstate
      Trade Name
      • Upstate
      DescriptionAnti-SHC Antibody
      References
      Product Information
      FormatPurified
      Control
      • Positive Control Included: Non-Stim A431 Cell Lysate (12-301)
      PresentationImmunoaffinity Purified immunoglobulin in 0.2 Tris-glycine, pH 7.4, 0.15M NaCl, 0.05% sodium azide before the addition of glycerol to 30%
      Applications
      ApplicationAnti-SHC Antibody is an antibody against SHC for use in IH, IP & WB.
      Key Applications
      • Immunohistochemistry
      • Immunoprecipitation
      • Western Blotting
      Biological Information
      ImmunogenRecombinant GST fusion protein corresponding to amino acids 366-473 of human SHC-SH2
      ConcentrationPlease refer to the Certificate of Analysis for the lot-specific concentration.
      HostRabbit
      SpecificityRecognizes SHC proteins.
      IsotypeIgG
      Species Reactivity
      • Human
      • Mouse
      • Pig
      • Rat
      Antibody TypePolyclonal Antibody
      Entrez Gene Number
      Gene Symbol
      • SHC1
      • p66SHC
      • SHCA
      • p66
      • SHC
      • FLJ26504
      • p52SHC
      Purification MethodProtein A Purfied
      UniProt Number
      UniProt SummaryFUNCTION: SwissProt: P29353 # Signaling adapter that couples activated growth factor receptors to signaling pathway. Isoform p46Shc and isoform p52Shc, once phosphorylated, couple activated receptor tyrosine kinases to Ras via the recruitment of the GRB2/SOS complex and are implicated in the cytoplasmic propagation of mitogenic signals. Isoform p46Shc and isoform p52Shc may thus function as initiators of the Ras signaling cascade in various non-neuronal systems. Isoform p66Shc does not mediate Ras activation, but is involved in signal transduction pathways that regulate the cellular response to oxidative stress and life span. Isoform p66Shc acts as a downstream target of the tumor suppressor p53 and is indispensable for the ability of stress-activated p53 to induce elevation of intracellular oxidants, cytochrome c release and apoptosis. The expression of isoform p66Shc has been correlated with life span (By similarity).
      SIZE: 583 amino acids; 62852 Da
      SUBUNIT: Interacts with the Trk receptors in a phosphotyrosine- dependent manner. Interacts with the NPXY motif of tyrosine- phosphorylated IGF1R and INSR in vitro via the PID domain. Once activated, binds to GRB2. Interacts with tyrosine-phosphorylated CD3T. Interacts with the N-terminal region of APS. Interacts with phosphorylated LRP1. Interacts with INPP5D/SHIP1 and INPPL1/SHIP2.
      SUBCELLULAR LOCATION: Cytoplasm. & Isoform p46Shc: Mitochondrion matrix. Note=Localized to the mitochondria matrix. Targeting of isoform p46Shc to mitochondria is mediated by its first 32 amino acids, which behave as a bona fide mitochondrial targeting sequence. Isoform p52Shc and isoform p66Shc, that contain the same sequence but more internally located, display a different subcellular localization.
      TISSUE SPECIFICITY: Widely expressed. Expressed in neural stem cells but absent in mature neurons.
      DOMAIN: SwissProt: P29353 In response to a variety of growth factors, isoform p46Shc and isoform p52Shc bind to phosphorylated Trk receptors through their phosphotyrosine binding (PID) and/or SH2 domains. The PID and SH2 domains bind to specific phosphorylated tyrosine residues in the Asn-Pro-Xaa-Tyr(P) motif of the Trk receptors. Isoform p46Shc and isoform p52Shc are in turn phosphorylated on three tyrosine residues within the extended proline-rich domain. These phosphotyrosines act as docking site for GRB2 and thereby are involved in Ras activation (By similarity).
      PTM: Phosphorylated by activated epidermal growth factor receptor. Isoform p46Shc and isoform p52Shc are phosphorylated on tyrosine residues of the Pro-rich domain. Isoform p66Shc is phosphorylated on Ser-36 upon treatment with insulin, hydrogen peroxide or irradiation with ultraviolet light (By similarity).
      SIMILARITY: Contains 1 PID domain. & Contains 1 SH2 domain.
      Molecular Weight46, 52, 66 kDa
      Physicochemical Information
      Dimensions
      Materials Information
      Toxicological Information
      Safety Information according to GHS
      Safety Information
      Product Usage Statements
      Quality Assuranceroutinely evaluated by immunoblot on RIPA lysates from human A431 carcinoma cells or mouse 3T3 RIPA cell lysate
      Usage Statement
      • Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.
      Storage and Shipping Information
      Storage ConditionsMaintain for 2 years at -20°C from date of shipment. Aliquot to avoid repeated freezing and thawing. For maximum recovery of product, centrifuge the original vial after thawing and prior to removing the cap.
      Packaging Information
      Material Size250 µg
      Transport Information
      Supplemental Information
      Specifications

      Documentation

      SDS

      Title

      Safety Data Sheet (SDS) 

      Certificates of Analysis

      TitleLot Number
      Anti-SHC (rabbit polyclonal IgG) - 2388927 2388927
      Anti-SHC (rabbit polyclonal IgG) - 2424747 2424747
      Anti-SHC (rabbit polyclonal IgG) - 2189943 2189943
      Anti-SHC - 15785 15785
      Anti-SHC - 17710 17710
      Anti-SHC - 18399 18399
      Anti-SHC - 19704 19704
      Anti-SHC - 21554 21554
      Anti-SHC - 23039 23039
      Anti-SHC - 2828570 2828570

      References

      Reference overviewApplicationPub Med ID
      Constitutive and ligand-induced EGFR signalling triggers distinct and mutually exclusive downstream signalling networks.
      Chakraborty, S; Li, L; Puliyappadamba, VT; Guo, G; Hatanpaa, KJ; Mickey, B; Souza, RF; Vo, P; Herz, J; Chen, MR; Boothman, DA; Pandita, TK; Wang, DH; Sen, GC; Habib, AA
      Nature communications  5  5811  2014

      Show Abstract
      25503978 25503978
      Iron modulates cell survival in a Ras- and MAPK-dependent manner in ovarian cells.
      Bauckman, KA; Haller, E; Flores, I; Nanjundan, M
      Cell death & disease  4  e592  2013

      Show Abstract
      Western Blotting23598404 23598404
      SnoN/SkiL expression is modulated via arsenic trioxide-induced activation of the PI3K/AKT pathway in ovarian cancer cells.
      Kodigepalli, KM; Dutta, PS; Bauckman, KA; Nanjundan, M
      FEBS letters  587  5-16  2013

      Show Abstract
      23178716 23178716
      Arginase-II induces vascular smooth muscle cell senescence and apoptosis through p66Shc and p53 independently of its l-arginine ureahydrolase activity: implications for atherosclerotic plaque vulnerability.
      Xiong, Y; Yu, Y; Montani, JP; Yang, Z; Ming, XF
      Journal of the American Heart Association  2  e000096  2013

      Show Abstract
      23832324 23832324
      Blockade of phospholipid scramblase 1 with its N-terminal domain antibody reduces tumorigenesis of colorectal carcinomas in vitro and in vivo.
      Fan, CW; Chen, CY; Chen, KT; Shen, CR; Kuo, YB; Chen, YS; Chou, YP; Wei, WS; Chan, EC
      Journal of translational medicine  10  254  2012

      Show Abstract
      23259795 23259795
      Phosphatidylinositol 3-kinase (PI3K) activity bound to insulin-like growth factor-I (IGF-I) receptor, which is continuously sustained by IGF-I stimulation, is required for IGF-I-induced cell proliferation.
      Fukushima, T; Nakamura, Y; Yamanaka, D; Shibano, T; Chida, K; Minami, S; Asano, T; Hakuno, F; Takahashi, S
      The Journal of biological chemistry  287  29713-21  2012

      Show Abstract
      22767591 22767591
      Identification of MET and SRC activation in melanoma cell lines showing primary resistance to PLX4032.
      Vergani, E; Vallacchi, V; Frigerio, S; Deho, P; Mondellini, P; Perego, P; Cassinelli, G; Lanzi, C; Testi, MA; Rivoltini, L; Bongarzone, I; Rodolfo, M
      Neoplasia (New York, N.Y.)  13  1132-42  2011

      Show Abstract
      22241959 22241959
      Increased Level of Phosphorylated ShcA Measured by Chemiluminescence-Linked Immunoassay Is a Predictor of Good Prognosis in Primary Breast Cancer Expressing Low Levels of Estrogen Receptor.
      Cicenas, J; Küng, W; Eppenberger, U; Eppenberger-Castori, S
      Cancers  2  153-64  2010

      Show Abstract
      24281038 24281038
      Coordinate regulation of estrogen-mediated fibronectin matrix assembly and epidermal growth factor receptor transactivation by the G protein-coupled receptor, GPR30.
      Quinn, JA; Graeber, CT; Frackelton, AR; Kim, M; Schwarzbauer, JE; Filardo, EJ
      Molecular endocrinology (Baltimore, Md.)  23  1052-64  2009

      Show Abstract Full Text Article
      19342448 19342448
      Activation of platelet-activating factor receptor and pleiotropic effects on tyrosine phospho-EGFR/Src/FAK/paxillin in ovarian cancer.
      Margarita Aponte, Wei Jiang, Montaha Lakkis, Ming-Jiang Li, Dale Edwards, Lina Albitar, Allison Vitonis, Samuel C Mok, Daniel W Cramer, Bin Ye
      Cancer research  68  5839-48  2008

      Show Abstract Full Text Article
      18632638 18632638

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      Included Positive Control

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      Categories

      Life Science Research > Antibodies and Assays > Primary Antibodies