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DNM1 / Dynamin Antibody (C-Terminus)

Rabbit Polyclonal Antibody

     
  • IHC - DNM1 / Dynamin Antibody (C-Terminus) ALS11954
    Anti-DNM1 / Dynamin antibody IHC of human brain, cortex.
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Product Information
Application
  • Applications Legend:
  • WB=Western Blot
  • IHC=Immunohistochemistry
  • IHC-P=Immunohistochemistry (Paraffin-embedded Sections)
  • IHC-F=Immunohistochemistry (Frozen Sections)
  • IF=Immunofluorescence
  • FC=Flow Cytopmetry
  • IC=Immunochemistry
  • ICC=Immunocytochemistry
  • E=ELISA
  • IP=Immunoprecipitation
  • DB=Dot Blot
  • CHIP=Chromatin Immunoprecipitation
  • FA=Fluorescence Assay
  • IEM=Immunoelectronmicroscopy
  • EIA=Enzyme Immunoassay
WB, IHC-P, E
Primary Accession Q05193
Reactivity Human
Host Rabbit
Clonality Polyclonal
Calculated MW 97kDa
Dilution ELISA (1 µg/ml), IHC-P (10 µg/ml), WB (1 µg/ml)
Additional Information
Gene ID 1759
Other Names Dynamin-1, 3.6.5.5, DNM1, DNM
Target/Specificity synthetic peptide corresponding to C-terminal residues of human DNM1(Dynamin-1)
Reconstitution & Storage +4°C or -20°C, Avoid repeated freezing and thawing.
PrecautionsDNM1 / Dynamin Antibody (C-Terminus) is for research use only and not for use in diagnostic or therapeutic procedures.
Protein Information
Name DNM1 (HGNC:2972)
Synonyms DNM
Function Catalyzes the hydrolysis of GTP and utilizes this energy to mediate vesicle scission and participates in many forms of endocytosis, such as clathrin-mediated endocytosis or synaptic vesicle endocytosis as well as rapid endocytosis (RE) (PubMed:8910402, PubMed:20428113, PubMed:15703209, PubMed:9362482, PubMed:29668686, PubMed:8101525). Associates to the membrane, through lipid binding, and self-assembles into rings and stacks of interconnected rings through oligomerization to form a helical polymer around the vesicle membrane leading to constriction of invaginated coated pits around their necks (PubMed:7877694, PubMed:9922133, PubMed:30069048). Self-assembly of the helical polymer induces membrane tubules narrowing until the polymer reaches a length sufficient to trigger GTP hydrolysis (PubMed:19084269). Depending on the curvature imposed on the tubules, membrane detachment from the helical polymer upon GTP hydrolysis can cause spontaneous hemifission followed by complete fission (PubMed:19084269). May play a role in regulating early stages of clathrin-mediated endocytosis in non-neuronal cells through its activation by dephosphorylation via the signaling downstream of EGFR (PubMed:29668686). Controls vesicle size at a step before fission, during formation of membrane pits, at hippocampal synapses (By similarity). Controls plastic adaptation of the synaptic vesicle recycling machinery to high levels of activity (By similarity). Mediates rapid endocytosis (RE), a Ca(2+)-dependent and clathrin- and K(+)-independent process in chromaffin cells (By similarity). Microtubule-associated force-producing protein involved in producing microtubule bundles and able to bind and hydrolyze GTP (By similarity). Through its interaction with DNAJC6, acts during the early steps of clathrin-coated vesicle (CCV) formation (PubMed:12791276).
Cellular Location Cell membrane. Membrane, clathrin-coated pit. Cytoplasmic vesicle {ECO:0000250|UniProtKB:P21575, ECO:0000250|UniProtKB:P39053} Presynapse {ECO:0000250|UniProtKB:P21575}. Cytoplasmic vesicle, secretory vesicle, chromaffin granule {ECO:0000250|UniProtKB:Q08DF4} Note=Associated to the membrane in an helical polymer shape in a GTP bound state (PubMed:30069048). Transiently recruited to endocytic clathrin-coated pits (CCPs) at a late stage of clathrin-coated vesicle (CCV) formation (PubMed:15703209).
Research Areas
Citations (0)
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Background

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.

References

van der Bliek A.M.,et al.J. Cell Biol. 122:553-563(1993).
Humphray S.J.,et al.Nature 429:369-374(2004).
Soulet F.,et al.Mol. Biol. Cell 16:2058-2067(2005).
Olsen J.V.,et al.Cell 127:635-648(2006).
Krendel M.,et al.FEBS Lett. 581:644-650(2007).

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Discontinued
Cat# ALS11954
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