07-156 | Anti-phospho-Caldesmon (Ser789) Antibody

100 µg  
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      Replacement Information

      Key Spec Table

      Species ReactivityKey ApplicationsHostFormatAntibody Type
      Ca, Ft, PoEnzyme Assays, WBRbPurifiedPolyclonal Antibody
      Catalogue Number07-156
      Brand Family Upstate
      Trade Name
      • Upstate
      DescriptionAnti-phospho-Caldesmon (Ser789) Antibody
      Product Information
      PresentationPurified rabbit polyclonal in buffer containing 0.1 M Tris-Glycine (pH 7.4, 150 mM NaCl) with 0.05% sodium azide.
      ApplicationDetect phospho-Caldesmon (Ser789) using this Anti-phospho-Caldesmon Antibody validated for use in EA & WB.
      Key Applications
      • Enzyme Assays
      • Western Blotting
      Biological Information
      Immunogenpeptide corresponding to amino acids 782-793 (C-QSVDKVT[pS]PTKV) of human Caldesmon
      SpecificityCaldesmon phosphorylated on serine 789
      Species Reactivity
      • Canine
      • Ferret
      • Pig
      Antibody TypePolyclonal Antibody
      Entrez Gene Number
      Entrez Gene SummaryThis gene encodes a calmodulin- and actin-binding protein that plays an essential role in the regulation of smooth muscle and nonmuscle contraction. The conserved domain of this protein possesses the binding activities to Ca(2+)-calmodulin, actin, tropomyosin, myosin, and phospholipids. This protein is a potent inhibitor of the actin-tropomyosin activated myosin MgATPase, and serves as a mediating factor for Ca(2+)-dependent inhibition of smooth muscle contraction. Alternative splicing of this gene results in multiple transcript variants encoding distinct isoforms.
      Gene Symbol
      • CALD1
      • Caldesmon
      • CAD
      • CDM
      • L-CAD
      • MGC21352
      • NAG22
      • H-CAD
      • Phosphorylation
      Purification MethodProtein A chromatography
      UniProt Number
      UniProt SummaryFUNCTION: SwissProt: Q05682 # Actin- and myosin-binding protein implicated in the regulation of actomyosin interactions in smooth muscle and nonmuscle cells (could act as a bridge between myosin and actin filaments). Stimulates actin binding of tropomyosin which increases the stabilization of actin filament structure. In muscle tissues, inhibits the actomyosin ATPase by binding to F-actin. This inhibition is attenuated by calcium-calmodulin and is potentiated by tropomyosin. Interacts with actin, myosin, two molecules of tropomyosin and with calmodulin. Also play an essential role during cellular mitosis and receptor capping.
      SIZE: 793 amino acids; 93250 Da
      SUBCELLULAR LOCATION: Note=On thin filaments in smooth muscle and on stress fibers in fibroblasts (nonmuscle) (By similarity).
      TISSUE SPECIFICITY: High-molecular-weight caldesmon (isoform 1) is predominantly expressed in smooth muscles, whereas low-molecular- weight caldesmon (isoforms 2, 3, 4 and 5) are widely distributed in non-muscle tissues and cells. Not expressed in skeletal muscle or heart.
      DOMAIN: SwissProt: Q05682 The N-terminal part seems to be a myosin/calmodulin- binding domain, and the C-terminal a tropomyosin/actin/calmodulin- binding domain. These two domains are separated by a central helical region in the smooth-muscle form.
      PTM: In non-muscle cells, phosphorylation by CDC2 during mitosis causes caldesmon to dissociate from microfilaments. Phosphorylation reduces caldesmon binding to actin, myosin, and calmodulin as well as its inhibition of actomyosin ATPase activity. Phosphorylation also occurs in both quiescent and dividing smooth muscle cells with similar effects on the interaction with actin and calmodulin and on microfilaments reorganization (By similarity).
      SIMILARITY: Belongs to the caldesmon family.
      Molecular Weight140kDa and lower molecular weight isoforms
      Physicochemical Information
      Materials Information
      Toxicological Information
      Safety Information according to GHS
      Safety Information
      Product Usage Statements
      Quality Assuranceroutinely evaluated by immunoblot on a RIPA lysate of EGF stimulated human A431 cells; pretreatment of blots with lambda phosphatase prior to incubation abolished the detection of Caldesmon
      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 ConditionsStable for 1 year at 2-8°C from date of receipt.
      Packaging Information
      Material Size100 µg
      Transport Information
      Supplemental Information




      Safety Data Sheet (SDS) 

      Certificates of Analysis

      TitleLot Number
      Anti-phospho-Caldesmon (Ser789) 2476970
      Anti-phospho-Caldesmon (Ser789) (rabbit polyclonal IgG) - 2424688 2424688
      Anti-phospho-Caldesmon (Ser789) (rabbit polyclonal IgG) 3058470
      Anti-phospho-Caldesmon (Ser789) (rabbit polyclonal IgG) 2902701
      Anti-phospho-Caldesmon (Ser789) (rabbit polyclonal IgG) - 2316467 2316467
      Anti-phospho-Caldesmon (Ser789) (rabbit polyclonal IgG) - 2364190 2364190
      Anti-phospho-Caldesmon (Ser789) - 20246 20246
      Anti-phospho-Caldesmon (Ser789) - 27776 27776
      Anti-phospho-Caldesmon (Ser789) - DAM1754437 DAM1754437
      Anti-phospho-Caldesmon (Ser789) - JBC1856607 JBC1856607


      Reference overviewPub Med ID
      Smooth muscle tension induces invasive remodeling of the zebrafish intestine.
      Seiler, C; Davuluri, G; Abrams, J; Byfield, FJ; Janmey, PA; Pack, M
      PLoS biology  10  e1001386  2012

      Show Abstract
      22973180 22973180
      Phasic phosphorylation of caldesmon and ERK 1/2 during contractions in human myometrium.
      Paul, J; Maiti, K; Read, M; Hure, A; Smith, J; Chan, EC; Smith, R
      PloS one  6  e21542  2011

      Show Abstract Full Text Article
      21738699 21738699
      Mammal-specific, ERK-dependent, caldesmon phosphorylation in smooth muscle. Quantitation using novel anti-phosphopeptide antibodies.
      D'Angelo, G, et al.
      J. Biol. Chem., 274: 30115-21 (1999)  1999

      Show Abstract
      10514499 10514499

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      Life Science Research > Antibodies and Assays > Primary Antibodies