protein

Recombinant Human Dynamin-1

MBS968409

0.05 mg (E-Coli)

190 USD

Recombinant Protein

Recombinant Human Dynamin-1

Dynamin-1

dynamin-1 isoform 2; Dynamin-1; dynamin-1; dynamin 1

DNM1

DNM1; DNM1; DNM; EIEE31; DNM

DYN1_HUMAN

E Coli or Yeast or Baculovirus or Mammalian Cell

2-245

851

GNRGMEDLIPLVNRLQDAFSAIGQNADLDLPQIAVVGGQ
SAGKSSVLENFVGRDFLPRGSGIVTRRPLVLQLVNATTE
YAEFLHCKGKKFTDFEEVRLEIEAETDRVTGTNKGISPV
PINLRVYSPHVLNLTLVDLPGMTKVPVGDQPPDIEFQIR
DMLMQFVTKENCLILAVSPANSDLANSDALKVAKEVDPQ
GQRTIGVITKLDLMDEGTDARDVLENKLLPLRRGYIGVV
NRSQKDIDGK

Greater than 90% as determined by SDS-PAGE.

Liquid containing glycerol; lyophilization may be available upon request.

Store at -20 degree C, for extended storage, conserve at -20 degree C or -80 degree C.

Neuroscience

Microtubule-associated force-producing protein involved in producing microtubule bundles and able to bind and hydrolyze GTP. Most probably involved in vesicular trafficking processes. Involved in receptor-mediated endocytosis.

Mutations in human dynamin block an intermediate stage in coated vesicle formation.van der Bliek A.M., Redelmeier T.E., Tisdale E.J., Meyerowitz E.M., Schmid S.L.J. Cell Biol. 122:553-563(1993) DNA sequence and analysis of human chromosome 9.Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A., Frankland J.A., French L., Fricker D.G., Garner P., Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S., Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E., Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D., Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E., Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K., Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M., Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J., Dunham I.Nature 429:369-374(2004) SNX9 regulates dynamin assembly and is required for efficient clathrin-mediated endocytosis.Soulet F., Yarar D., Leonard M., Schmid S.L.Mol. Biol. Cell 16:2058-2067(2005) Global, in vivo, and site-specific phosphorylation dynamics in signaling networks.Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.Cell 127:635-648(2006) Myosin 1E interacts with synaptojanin-1 and dynamin and is involved in endocytosis.Krendel M., Osterweil E.K., Mooseker M.S.FEBS Lett. 581:644-650(2007) A novel sorting nexin modulates endocytic trafficking and alpha-secretase cleavage of the amyloid precursor protein.Schobel S., Neumann S., Hertweck M., Dislich B., Kuhn P.H., Kremmer E., Seed B., Baumeister R., Haass C., Lichtenthaler S.F.J. Biol. Chem. 283:14257-14268(2008) Phosphoproteome of resting human platelets.Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J., Schuetz C., Walter U., Gambaryan S., Sickmann A.J. Proteome Res. 7:526-534(2008) Initial characterization of the human central proteome.Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.BMC Syst. Biol. 5:17-17(2011) Three-dimensional solution structure of the pleckstrin homology domain from dynamin.Downing A.K., Driscoll P.C., Gout I., Salim K., Zvelebil M.J., Waterfield M.D.Curr. Biol. 4:884-891(1994) Crystal structure at 2.2-A resolution of the pleckstrin homology domain from human dynamin.Ferguson K.M., Lemmon M.A., Schlessinger J., Sigler P.B.Cell 79:199-209(1994) Crystal structure of the pleckstrin homology domain from dynamin.Timm D., Salim K., Gout I., Guruprasad L., Waterfield M., Blundell T.Nat. Struct. Biol. 1:782-788(1994)

56549117

NP_001005336.1

NM_001005336.2

Q05193

42.72kD

Adaptive Immune System Pathway (1269171); Axon Guidance Pathway (1270303); Bacterial Invasion Of Epithelial Cells Pathway (149807); Bacterial Invasion Of Epithelial Cells Pathway (148661); CXCR3-mediated Signaling Events Pathway (138011); CXCR4-mediated Signaling Events Pathway (137910); Developmental Biology Pathway (1270302); EGFR1 Signaling Pathway (198782); EPH-Ephrin Signaling Pathway (1270330); EPH-ephrin Mediated Repulsion Of Cells Pathway (1270334)

This gene encodes a member of the dynamin subfamily of GTP-binding proteins. The encoded protein possesses unique mechanochemical properties used to tubulate and sever membranes, and is involved in clathrin-mediated endocytosis and other vesicular trafficking processes. Actin and other cytoskeletal proteins act as binding partners for the encoded protein, which can also self-assemble leading to stimulation of GTPase activity. More than sixty highly conserved copies of the 3' region of this gene are found elsewhere in the genome, particularly on chromosomes Y and 15. Alternatively spliced transcript variants encoding different isoforms have been described. [provided by RefSeq, Jul 2008]

DYN1: a microtubule-associated force-producing protein involved in producing microtubule bundles and able to bind and hydrolyze GTP. Most probably involved in vesicular trafficking processes. Concentrates within the presynaptic compartment and may participate in specialized neuronal functions such as rapid synaptic vesicle recycling. Part of a protein network that controls nucleation of actin from membranes. Contains one PH domain. Protein type: Hydrolase; Motor; Microtubule-binding; EC 3.6.5.5; Vesicle; Motility/polarity/chemotaxis. Chromosomal Location of Human Ortholog: 9q34. Cellular Component: Golgi apparatus; membrane coat; microtubule; myelin sheath; photoreceptor inner segment; plasma membrane; synaptic vesicle. Molecular Function: D2 dopamine receptor binding; GTP binding; GTPase activity; identical protein binding; nitric-oxide synthase binding; protein binding; protein C-terminus binding; protein complex binding; protein dimerization activity; protein kinase binding. Biological Process: adult locomotory behavior; axon guidance; endocytosis; endosome organization and biogenesis; ephrin receptor signaling pathway; G-protein coupled receptor internalization; protein tetramerization; receptor-mediated endocytosis; sensory perception of sound; synaptic transmission, GABAergic. Disease: Epileptic Encephalopathy, Early Infantile, 31

0.05 mg (E-Coli)

190 USD

0.05 mg (Yeast)

190

0.2 mg (E-Coli)

460

0.2 mg (Yeast)

460

0.5 mg (E-Coli)

750