Recombinant Human Dynamin-1(DNM1) ,partial

In Stock
Code CSB-EP007062HU
Size US$1726
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  • (Tris-Glycine gel) Discontinuous SDS-PAGE (reduced) with 5% enrichment gel and 15% separation gel.

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Product Details

Purity Greater than 90% as determined by SDS-PAGE.
Target Names DNM1
Uniprot No. Q05193
Research Area Neuroscience
Alternative Names B dynamin; D100; DNM 1; DNM; DNM1; DYN1_HUMAN; Dynamin; Dynamin-1; Dynamin1
Species Homo sapiens (Human)
Source E.coli
Expression Region 2-245aa
Target Protein Sequence GNRGMEDLIPLVNRLQDAFSAIGQNADLDLPQIAVVGGQSAGKSSVLENFVGRDFLPRGSGIVTRRPLVLQLVNATTEYAEFLHCKGKKFTDFEEVRLEIEAETDRVTGTNKGISPVPINLRVYSPHVLNLTLVDLPGMTKVPVGDQPPDIEFQIRDMLMQFVTKENCLILAVSPANSDLANSDALKVAKEVDPQGQRTIGVITKLDLMDEGTDARDVLENKLLPLRRGYIGVVNRSQKDIDGK
Note: The complete sequence including tag sequence, target protein sequence and linker sequence could be provided upon request.
Mol. Weight 42.7kDa
Protein Length Partial
Tag Info N-terminal 6xHis-SUMO-tagged
Form Liquid or Lyophilized powder
Note: We will preferentially ship the format that we have in stock, however, if you have any special requirement for the format, please remark your requirement when placing the order, we will prepare according to your demand.
Buffer If the delivery form is liquid, the default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol.
Note: If you have any special requirement for the glycerol content, please remark when you place the order.
If the delivery form is lyophilized powder, the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, pH 8.0.
Reconstitution We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Please reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL.We recommend to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20°C/-80°C. Our default final concentration of glycerol is 50%. Customers could use it as reference.
Troubleshooting
and FAQs
Protein FAQs
Storage Condition Store at -20°C upon receipt, aliquoting is necessary for mutiple use. Avoid repeated freeze-thaw cycles.
Shelf Life The shelf life is related to many factors, storage state, buffer ingredients, storage temperature and the stability of the protein itself.
Generally, the shelf life of liquid form is 6 months at -20°C/-80°C. The shelf life of lyophilized form is 12 months at -20°C/-80°C.
Lead Time Delivery time may differ from different purchasing way or location, please kindly consult your local distributors for specific delivery time.
Notes Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.
Datasheet & COA Please contact us to get it.

Q&A and Customer Reviews

 Q&A
Q:

I would like to know if this protein has been reported to be active or if it is expected to be active based on its sequence. Has the tag been successfully removed from this protein?
I would prefer a full length protein with GTPase activity, do you have a human full length human dynamin-1 protein? If yes please provide the catalog number and pricing information and let me know if the tag has ever been successfully removed.

A:
Here is a literature about the activity for your reference: http://europepmc.org/articles/PMC2719574/
Please remark your requirement for tag removal if you need the untagged protein or tag removal when placing the order.
Sorry, we haven't tried to remove the tag before. We can try enzyme digestion, but we can't guarantee 100% successfully.
The overall success rate of enzyme digestion data analysis is 75%-86%.
Not all protein tags can be removed as some proteins will be very unstable after tag removal.
If we succeed in removing the tag, we will charge for extra cost.
If we fail in removing the tag, we won’t charge for tag removal and provide the fusion protein, and remark this information in datasheet as follows
“Note: The laboratory determined that the Tag on your protein could not be removed with standard laboratory procedures. Your protein is being supplied with the Tag intact.”
Generally, the delivery time will be extended for 3 days.
We can provide the custom service for this full length protein if you need, pls check the details as follows:
Product Name:Recombinant Human Dynamin-1(DNM1)
Expression Region:1-864aa; Full length.
Tag information: Tag type will be determined during the manufacturing process. (Such as His-tagged, etc)
We can try to express your desired tag first if you have special request for the tag, but as we can't guarantte, if it's failed, we can provide protein with other tag.
Sequence:

MGNRGMEDLIPLVNRLQDAFSAIGQNADLDLPQIAVVGGQSAGKSSVLENFVGRDFLPRGSGIVTRRPLVLQLVNATTEYAEFLHCKGKKFTDFEEVRLEIEAETDRVTGTNKGISPVPINLRVYSPHVLNLTLVDLPGMTKVPVGDQPPDIEFQIRDMLMQFVTKENCLILAVSPANSDLANSDALKVAKEVDPQGQRTIGVITKLDLMDEGTDARDVLENKLLPLRRGYIGVVNRSQKDIDGKKDITAALAAERKFFLSHPSYRHLADRMGTPYLQKVLNQQLTNHIRDTLPGLRNKLQSQLLSIEKEVEEYKNFRPDDPARKTKALLQMVQQFAVDFEKRIEGSGDQIDTYELSGGARINRIFHERFPFELVKMEFDEKELRREISYAIKNIHGIRTGLFTPDMAFETIVKKQVKKIREPCLKCVDMVISELISTVRQCTKKLQQYPRLREEMERIVTTHIREREGRTKEQVMLLIDIELAYMNTNHEDFIGFANAQQRSNQMNKKKTSGNQDEILVIRKGWLTINNIGIMKGGSKEYWFVLTAENLSWYKDDEEKEKKYMLSVDNLKLRDVEKGFMSSKHIFALFNTEQRNVYKDYRQLELACETQEEVDSWKASFLRAGVYPERVGDKEKASETEENGSDSFMHSMDPQLERQVETIRNLVDSYMAIVNKTVRDLMPKTIMHLMINNTKEFIFSELLANLYSCGDQNTLMEESAEQAQRRDEMLRMYHALKEALSIIGDINTTTVSTPMPPPVDDSWLQVQSVPAGRRSPTSSPTPQRRAPAVPPARPGSRGPAPGPPPAGSALGGAPPVPSRPGASPDPFGPPPQVPSRPNRAPPGVPSRSGQASPSRPESPRPPFDL


Reference:http://www.uniprot.org/uniprot/Q05193
Lead time:50-65 working days
As the full length of this protein is over 800aa, so we will charge step by step, if we can successfully express this protein,
the total charges of each epression system is list as below:
CSB-YP007062HU(A4) >> Yeast
CSB-EP007062HU(A4) >> E.coli
CSB-BP007062HU(A4) >> Baculovirus
CSB-MP007062HU(A4) >> Mammalian cell
If we fail in expressing this full length protein, you need to pay, we will provide the constructed plasmid and strains of the corresponding expression system.

Target Data

Function 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.
Gene References into Functions
  1. The twin siblings exhibit mild to moderate intellectual disability and autistic symptoms but no epileptic encephalopathy. Exome sequencing revealed a genetic variant, c.1603A>G (p.Lys535Glu), in the PH domain of dynamin 1. The twin sisters studied here share the de novo variant, c.1603A>G (p.Lys535Glu) in exon 15 of DNM1, classified as likely pathogenic. PMID: 29397573
  2. The data show that the dynamin-amphiphysin helices are rearranged to form clusters upon GTP hydrolysis and membrane constriction occurs at protein-uncoated regions flanking the clusters. PMID: 29357276
  3. Together, these observations suggest that while endophilin helps shape endocytic tubules and recruit dynamin to endocytic sites, it can also block membrane fission when present in excess by inhibiting inter-dynamin interactions. PMID: 28933693
  4. The authors show that in fibroblasts, dynamin GTP hydrolysis occurs as stochastic bursts, which are randomly distributed relatively to the peak of dynamin assembly. Thus, dynamin disassembly is not coupled to GTPase activity, supporting that the GTP energy is primarily spent in constriction. PMID: 29022874
  5. Dynamin isoforms differentially regulate the endocytosis and apoptotic signaling downstream of TRAIL-death receptor (TRAIL-DR) complexes in cancer cells. TRAIL stimulation activates ryanodine receptor-mediated calcium release from endoplasmic reticulum stores, leading to calcineurin-mediated dephosphorylation and activation of Dyn1, TRAIL-DR endocytosis, and increased resistance to TRAIL-induced apoptosis. PMID: 28049841
  6. Three genes in our epilepsy cohort (COQ4, DNM1, and PURA), accounting for 14% (3/21) of all novel genetic etiologies identified in patients with epilepsy, were subsequently confirmed in independent publications. PMID: 26795593
  7. Study delineates the phenotypic spectrum of DNM1 encephalopathy, an emerging disease of synaptic vesicle fission characterized by severe to profound developmental delay, infantile-onset epilepsy beginning with infantile spasms, and movement disorder. The genetic landscape of DNM1 encephalopathy is notable for the recurrent c.709C>T (p.Arg237Trp) variant and localization of mutations to specific domains of the protein. PMID: 28667181
  8. CLCb/Dyn1-dependent adaptive clathrin-mediated endocytosis selectively altered EGF receptor trafficking. PMID: 28171750
  9. Down-regulation of Dyn1 activity enhances extracellular Nme1 in human colon tumor cell lines. PMID: 27449069
  10. Hypoxic down-regulation of constitutive endocytosis is HIF-independent, and involves caveolin-1-mediated inhibition of dynamin-dependent, membrane raft endocytosis. PMID: 27094744
  11. study reports 2 patients with early onset epileptic encephalopathy possessing de novo DNM1 mutations; detected the novel mutation c.127G>A (p.Gly43Ser) in a patient with Lennox-Gastaut syndrome, and a recurrent mutation c.709C>T (p.Arg237Trp) in a patient with West syndrome PMID: 26611353
  12. The rare variants in DNM1 were significantly associated with smoking status. PMID: 25450229
  13. Data indicate that stimulation of the dynamin GTPase activity by SH3 domains is determined by its middle domain. PMID: 26659814
  14. molecular simulations corroborate the bimodal character of dynamin action and indicate radial and axial forces as dominant, although not independent, drivers of hemi-fission and fission membrane- transformations, respectively PMID: 26123023
  15. Data indicate the dynamics of a dynamin 1-catalysed GTP hydrolysis and tube-severing reaction in real time using fluorescence microscopy. PMID: 26479317
  16. This study identified and confirmed DNM1 protein changes within the postsynaptic density in schizophrenia. PMID: 25048004
  17. findings support a role for HTT on dynamin 1 function and ER homoeostasis. Proteolysis-induced alteration of this function may be relevant to disease. PMID: 26165689
  18. CRISPR-Cas9n-mediated knockout and reconstitution studies establish that dynamin-1 is activated by Akt/GSK3beta signaling in H1299 non-small lung cancer cells. PMID: 26139537
  19. Data suggest that by binding to both clathrin and F-actin, mammalian actin-binding protein 1 (mAbp1; HIP-55 or SH3P7) is specifically recruited at a late stage of clathrin-coated pits (CCPs) formation, which subsequently recruits dynamin to CCPs. PMID: 25690657
  20. Dynamin 1 and dynamin 2 activity are not essential for Chlamydia trachomatis internalization but is required for normal development. PMID: 25116793
  21. activity-dependent acceleration is only prominent at physiological temperature and that the mechanism of this modulation is based on the dephosphorylation of dynamin 1 PMID: 23908769
  22. determined the alpha-synuclein-binding domain of beta-III tubulin and demonstrated that a short fragment containing this domain can suppress alpha-synuclein accumulation in the primary cultured cells PMID: 25031323
  23. De novo mutations in synaptic transmission genes including DNM1 cause epileptic encephalopathies. PMID: 25262651
  24. Data show that the classical dynamin DNM1 and DNM3 genes reach their maximum expression levels (100% of maximal expression) in all normal central nervous system tissues studied. PMID: 24673776
  25. Alternate pleckstrin homology domain orientations regulate dynamin-catalyzed membrane fission. PMID: 24478459
  26. Dynamin1 is associated with both preserved cognition and regenerative responses in older people with cerebrovascular disease and may represent a novel treatment target. PMID: 24486840
  27. findings show NDPKs (NM23-H1/H2/H4) interact with and provide GTP to dynamins, allowing these motor proteins to work with high thermodynamic efficiency for membrane remodeling PMID: 24970086
  28. Data suggest that dynorphin A (DynA) is ligand for opioid receptor kappa (KOR); upon DynA binding, only small chemical shifts observed in second extracellular loop of KOR; chemical shift changes of DynA show conclusively that DynA interacts with KOR. PMID: 24616919
  29. The discovery that the pre-mRNA sequence of dnm1 in humans has sequence features similar to that of the alternative splicing patterns observed in insects greatly expands the applicability of the docking site-selector sequence pairing model to bilaterian animals. PMID: 23793749
  30. analysis of how the membrane interactions of disease-related dynorphin A variants cause differences in cell toxicity PMID: 23705820
  31. dyn1 affects amyloid generation through regulation of BACE-1 subcellular localization and therefore its enzymatic activities. PMID: 23024787
  32. Herpes simplex virus type 1 can enter human keratinocytes by alternative entry pathways that require dynamin and host cholesterol. PMID: 22022400
  33. Study presents the GMPPCP-bound structures of the truncated human dynamin 1 helical polymer at 12.2 A and a fusion protein, GG, linking human dynamin 1's catalytic G domain to its GTPase effector domain (GED) at 2.2 A. PMID: 21962517
  34. crystal structure of human dynamin 1 in the nucleotide-free state with a four-domain architecture comprising the GTPase domain, the bundle signalling element, the stalk and the pleckstrin homology domain. PMID: 21927000
  35. A new role for the dynamin-1 GTPase in the regulation of fusion pore expansion PMID: 21460182
  36. In conclusion, Clostridium botulinum C2 toxin is endocytosed by dynamin-dependent mechanisms and we provide evidence for involvement of clathrin and Rho. PMID: 20690924
  37. 2.0 A resolution crystal structure of a human dynamin 1-derived minimal GTPase-GED fusion protein, which was dimeric in the presence of the transition state mimic GDP.AlF(4)(-) PMID: 20428113
  38. Endocytosis of FcalphaR is clathrin- and dynamin-dependent, but is not regulated by Rab5, and the endocytic motif is not located in the cytoplasmic domain of FcalphaR. PMID: 19859085
  39. Data suggest that the components of the GTPase-GED interface act as an intramolecular signaling module, which we term the bundle signaling element, that can modulate dynamin function in vitro and in vivo. PMID: 19515832
  40. Results demonstrate that, in concert with dynamin-1 self-assembly, pleckstrin homology domain membrane insertion is essential for fission and vesicle release in vitro and for clathrin-mediated endocytosis in vivo. PMID: 19776347
  41. These findings suggest that dynamin is part of a protein network that controls nucleation of actin from membranes. PMID: 11782545
  42. dynamin-dependent endocytosis is inhibited by syntaphilin PMID: 12896979
  43. serglycin-bound granzyme B in high-molecular-weight degranulate material from cytotoxic T lymphocytes predominantly followed a dynamin-dependent pathway to kill target cells PMID: 14739229
  44. Point mutations were made in the GTPase effector/assembly domain (GED)of dynamin 1 and tested for their effects on self-assembly and clathrin-mediated endocytosis. PMID: 15004222
  45. dynamin-1 interacts with Sumo-1, Ubc9, and PIAS-1, all of which are members of the sumoylation machinery PMID: 15123615
  46. Dynamin GTPase domain is important for GTP binding, GTP hydrolysis, and clathrin-mediated endocytosis PMID: 15262989
  47. dynamin, Cbl, and Src coordinately participate in signaling complexes that are important in the assembly and remodeling of the actin cytoskeleton, leading to changes in osteoclast adhesion, migration, and resorption PMID: 15872089
  48. S-nitrosylation of dynamin regulates endocytosis through nitric oxide PMID: 16432212
  49. PLD functions as a GTPase activating protein (GAP) through its phox homology domain (PX), which directly activates the GTPase domain of dynamin and increased epidermal growth factor receptor (EGFR) endocytosis at physiological EGF concentrations. PMID: 16622417
  50. Data show that swapping the highly homologous GTPase domain of dynamin-2 into dynamin-1 is sufficient to confer caspase-3 activation. PMID: 16938290
  51. Two mutations in middle domain, R361S and R399A, disrupt the tetrameric structure of dynamin in the unassembled state and impair its ability to stably bind to and nucleate higher-order self-assembly on membranes. PMID: 17170701
  52. Pockets of short-range transient order and restricted topological heterogeneity in the guanidine-denatured state ensemble of GED of DNM1. PMID: 17910478
  53. Data show that dynamin-1 is an inclusion body component in neuronal intranuclear inclusion disease identified by anti-SUMO-1-immunocapture. PMID: 18836734
  54. our findings indicate that DNM1 is likely involved in the etiology of nicotine dependence and represents a plausible candidate for further investigation in independent samples PMID: 18987626
  55. The ability of dynamin to alter the local distribution of PtdIns(4,5)P(2) could be crucial for the role of this GTPase in promoting membrane scission during clathrin-mediated endocytosis. PMID: 19666604

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Involvement in disease Epileptic encephalopathy, early infantile, 31 (EIEE31)
Subcellular Location Cytoplasm, Cytoplasm, cytoskeleton
Protein Families TRAFAC class dynamin-like GTPase superfamily, Dynamin/Fzo/YdjA family
Database Links

HGNC: 2972

OMIM: 602377

KEGG: hsa:1759

STRING: 9606.ENSP00000362014

UniGene: Hs.522413

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