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Proteins and peptidesAnti-Ly6g antibody [1A8] - mouse IgG2c (Chimeric)
Low endotoxin, Azide free.
Our first-to-market chimera with mouse IgG2c backbone, this functional antibody specifically depletes neutrophils in vivo for up to 72h.
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MW 408.6 Da, Purity >99%. Potent, cell-permeable dynamin I and dynamin II inhibitor (IC50 values are 1.3 and 14.2 μM for inhibition of dynamin I and II GTPase, respectively). Targets the GTPase domain at an allosteric site. Potently inhibits receptor-mediated and synaptic vesicle endocytosis (IC50 values are 5 and 41.1 μM, respectively). 15-fold more active than Dynasore (ab120192) against dynamin I.
1128165-88-7
> 99%
Solid
408.6 Da
C25H36N4O
44157463
Synthetic
B dynamin, CMT2M, CMTDI1, CMTDIB, DI CMTB, DNM, DNM 1, DYN II, DYN1_HUMAN, DYN2_HUMAN, Dynamin, Dynamin II, Dynamin-1, Dynamin-2
MW 408.6 Da, Purity >99%. Potent, cell-permeable dynamin I and dynamin II inhibitor (IC50 values are 1.3 and 14.2 μM for inhibition of dynamin I and II GTPase, respectively). Targets the GTPase domain at an allosteric site. Potently inhibits receptor-mediated and synaptic vesicle endocytosis (IC50 values are 5 and 41.1 μM, respectively). 15-fold more active than Dynasore (ab120192) against dynamin I.
B dynamin, CMT2M, CMTDI1, CMTDIB, DI CMTB, DNM, DNM 1, DYN II, DYN1_HUMAN, DYN2_HUMAN, Dynamin, Dynamin II, Dynamin-1, Dynamin-2
1128165-88-7
> 99%
Solid
408.6 Da
C25H36N4O
44157463
Synthetic
Dynole 34-2
Potent, cell-permeable dynamin I and dynamin II inhibitor (IC50 values are 1.3 and 14.2 μM for inhibition of dynamin I and II GTPase, respectively). Targets the GTPase domain at an allosteric site. Potently inhibits receptor-mediated and synaptic vesicle endocytosis (IC50 values are 5 and 41.1 μM, respectively). 15-fold more active than Dynasore (ab120192) against dynamin I.
CCCCCCCCNC(=O)C(=CC1=CN(C2=CC=CC=C21)CCCN(C)C)C#N
CCCCCCCCNC(=O)/C(=C/C1=CN(C2=CC=CC=C21)CCCN(C)C)/C#N
InChI=1S/C25H36N4O/c1-4-5-6-7-8-11-15-27-25(30)21(19-26)18-22-20-29(17-12-16-28(2)3)24-14-10-9-13-23(22)24/h9-10,13-14,18,20H,4-8,11-12,15-17H2,1-3H3,(H,27,30)/b21-18+
MYIMRONQBLZJFI-DYTRJAOYSA-N
(E)-2-cyano-3-[1-[3-(dimethylamino)propyl]indol-3-yl]-N-octylprop-2-enamide
Ambient - Can Ship with Ice
+4°C
Store under desiccating conditions, The product can be stored for up to 12 months
Sold under exclusive licence from Children's Medical Research Institute and Newcastle Innovation Ltd. Dynole® is a trademark of Children's Medical Research Institute and Newcastle Innovation Ltd.
Dynamins are involved in essential tasks within cells specifically mediating membrane scission. Dynamin 1 along with Dynamin 2 forms helical structures around the neck of budding vesicles contributing to their detachment from the plasma membrane. These proteins work closely with actin and microtubule networks ensuring proper cytoskeleton-dependent trafficking. Dynamins can also interact with a complex of proteins including amphiphysin and endophilin enhancing their function.
Dynamin 1 and Dynamin 2 are important proteins playing an important mechanical role in cellular processes. Dynamin proteins are large with masses of about 96 kDa for Dynamin 1 and 100 kDa for Dynamin 2. They function as GTPases driving membrane constriction and fission. These processes help in membrane trafficking such as endocytosis. Both types of Dynamin are present in various tissues with Dynamin 1 being expressed mainly in the brain and neurons while Dynamin 2 is expressed in non-neuronal cells.
Dynamins play significant roles in synaptic vesicle recycling and receptor-mediated endocytosis. These pathways are important for neurotransmitter release and nutrient uptake. In these contexts Dynamins interact with proteins like clathrin and sorting nexin. The GTPase activity of Dynamins is fundamental to their action in these pathways facilitating vesicle budding and fusion events.
Disruptions in Dynamin function are linked to cancer and neurological diseases. Mutations in Dynamin 2 can cause Charcot-Marie-Tooth disease a hereditary neuropathy affecting peripheral nerves. Additionally altered expression or function of Dynamins relates to cancer types like glioblastoma often through interactions with proteins such as EGFR which can exacerbate tumor progression and chemoresistance.
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2D chemical structure image of ab120463, Dynole® 34-2, dynamin I and dynamin II inhibitor
ab66705 staining PAI1 in HeLa cells treated with dynole-34-2™; (ab120463), by ICC/IF. Increase in PAI1 expression correlates with increased concentration of dynole-34-2™, as described in literature.
The cells were incubated at 37°C for 24h in media containing different concentrations of ab120463 (dynole-34-2™) in DMSO, fixed with 100% methanol for 5 minutes at -20°C and blocked with PBS containing 10% goat serum, 0.3 M glycine, 1% BSA and 0.1% tween for 2h at room temperature. Staining of the treated cells with ab66705 (5 μg/ml) was performed overnight at 4°C in PBS containing 1% BSA and 0.1% tween. A DyLight 488 goat anti-rabbit polyclonal antibody (ab96899) at 1/250 dilution was used as the secondary antibody. Nuclei were counterstained with DAPI and are shown in blue.
Primary human monocyte-derived macrophages (HMDM) were incubated with 30 μM of ab120463 for indicated time periods to determine if Dynamin inhibition decreases apoE secretion from primary human macrophages. Dynole-34-2 both dose- and time-dependently decreased apoE secretion without affecting HMDM viability (botton line on the graph as appose to the control, top line).
Kockx et al., PLOS One., 9(10): e111186. Fig 1F.; doi: https://doi.org/10.1371/journal.pone.0111186.
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