Antibodies to Dynamins

Introduction

Membrane transport between compartments in eukaryotic cells requires proteins that allow the budding and scission of nascent cargo vesicles from one compartment and their targeting and fusion with another. Dynamins are involved in the scission of a wide range of vesicles and organelles as well as in many processes including budding of transport vesicles, division of organelles, cytokinesis and pathogen resistance.

The Dynamins are a family of 100 kDa GTPases transcribed from at least three separate genes. They contain several conserved regions; an amino-terminal GTPase domain, a centrally located membrane-binding plekstrin homology domain (PHD), and a region located in front of the proline-rich domain (PRD). This PRD region is thought to mediate interactions between Dynamin and other cellular proteins.

There are also at least three isoforms of this protein. Dynamin 1 is exclusively neuronal and is phosphorylated by PKC and dephosphorylated by calcineurin during an action potential in the nerve terminal. Dynamin 2 is ubiquitous. Dynamin 3 is expressed in the brain, testis, heart and lung. The dynamins participate in the cellular process of clathrin-mediated and fluidphase endocytosis.

Antibody Panel to Dynamins

Acris Antibodies offers a range of monoclonal and polyclonal antibodies to Dynamins isoforms 1-3 suitable for Western blotting, Immunohistochemistry/ Immunofluorescence.and / or other immunological detection methods.

Fig. 1: Western blot of Dynamin 1 on rat brain homogenate using antibody Cat.No. SP5239P.

Fig. 2: Western blot of Dynamin 2 on mouse testes homogenate using antibody Cat.No. SP5240P.

Fig. 3: Western blot using antibody Cat.No. NB300-209 specific for Dynamin phosphorylated at Ser 774. A band representing Dynamin is seen at ~ 97 kD. The labeling of the Dynamin bands in Western Blots of rat brain is blocked by the phosphopeptide.

Antibody Panel to Dynamins

Dynamins (DNM1, DNM2 and DNM3) antibody.

Literature

Wells RC, Picton LK, Williams SC, Tan FJ, Hill RB. Direct binding of the dynamin-like GTPase, Dnm1, to mitochondrial dynamics protein Fis1 is negatively regulated by the Fis1 N-terminal arm. J Biol Chem. 2007 Nov 16;282(46):33769-75. Epub 2007 Sep 20

Naylor K, Ingerman E, Okreglak V, Marino M, Hinshaw JE, Nunnari J. Mdv1 interacts with assembled dnm1 to promote mitochondrial division. J Biol Chem. 2006 Jan 27;281(4):2177-83. Epub 2005 Nov 4.

Ingerman E, Perkins EM, Marino M, Mears JA, McCaffery JM, Hinshaw JE, Nunnari J. Dnm1 forms spirals that are structurally tailored to fit mitochondria. J Cell Biol. 2005 Sep 26;170(7):1021-7.

Reubold TF, Eschenburg S, Becker A, Leonard M, Schmid SL, Vallee RB, Kull FJ, Manstein DJ. Crystal structure of the GTPase domain of rat dynamin 1. Proc Natl Acad Sci U S A. 2005 Sep 13;102(37):13093-8.

Carey RM, Balcz BA, Lopez-Coviella I, Slack BE. Inhibition of dynamin-dependent endocytosis increases shedding of the amyloid precursor protein ectodomain and reduces generation of amyloid beta protein. BMC Cell Biol. 2005 Aug 11;6:30.