Recombinant Human Dynamin-1 (DNM1) Protein (His)

Name: Recombinant Human Dynamin-1 (DNM1) Protein (His)
Brand: Beta LifeScience
SKU: BLC-03408P
Availability: InStock

Greater than 85% as determined by SDS-PAGE.

Our products are highly customizable to meet your specific needs. You can choose options such as endotoxin removal, liquid or lyophilized forms, preferred tags, and the desired functional sequence range for proteins. Submitting a written inquiry expedites the quoting process.

Product Overview

Description	Recombinant Human Dynamin-1 (DNM1) Protein (His) is produced by our E.coli expression system. This is a protein fragment.
Purity	Greater than 85% as determined by SDS-PAGE.
Uniprotkb	Q05193
Target Symbol	DNM1
Synonyms	B dynamin; D100; DNM 1; DNM; DNM1; DYN1_HUMAN; Dynamin; Dynamin-1; Dynamin1
Species	Homo sapiens (Human)
Expression System	E.coli
Tag	N-6His
Target Protein Sequence	GNRGMEDLIPLVNRLQDAFSAIGQNADLDLPQIAVVGGQSAGKSSVLENFVGRDFLPRGSGIVTRRPLVLQLVNATTEYAEFLHCKGKKFTDFEEVRLEIEAETDRVTGTNKGISPVPINLRVYSPHVLNLTLVDLPGMTKVPVGDQPPDIEFQIRDMLMQFVTKENCLILAVSPANSDLANSDALKVAKEVDPQGQRTIGVITKLDLMDEGTDARDVLENKLLPLRRGYIGVVNRSQKDIDGK
Expression Range	2-245aa
Protein Length	Partial
Mol. Weight	32.2 kDa
Research Area	Neuroscience
Form	Liquid or Lyophilized powder
Buffer	Liquid form: default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol. Lyophilized powder form: the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, pH 8.0.
Reconstitution	Briefly centrifuged the vial prior to opening to bring the contents to the bottom. Reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL. It is recommended to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20°C/-80°C. The default final concentration of glycerol is 50%.
Storage	1. Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. 2. Avoid repeated freeze-thaw cycles. 3. Store working aliquots at 4°C for up to one week. 4. In general, protein in liquid form is stable for up to 6 months at -20°C/-80°C. Protein in lyophilized powder form is stable for up to 12 months at -20°C/-80°C.
Notes	Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.

Target Details

Target 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.
Subcellular Location	Cytoplasm. Cytoplasm, cytoskeleton. Note=Microtubule-associated.
Protein Families	TRAFAC class dynamin-like GTPase superfamily, Dynamin/Fzo/YdjA family
Database References	HGNC: 2972 OMIM: 602377 KEGG: hsa:1759 STRING: 9606.ENSP00000362014 UniGene: Hs.522413
Associated Diseases	Epileptic encephalopathy, early infantile, 31 (EIEE31)

Gene Functions References

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
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
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
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
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
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
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
CLCb/Dyn1-dependent adaptive clathrin-mediated endocytosis selectively altered EGF receptor trafficking. PMID: 28171750
Down-regulation of Dyn1 activity enhances extracellular Nme1 in human colon tumor cell lines. PMID: 27449069
Hypoxic down-regulation of constitutive endocytosis is HIF-independent, and involves caveolin-1-mediated inhibition of dynamin-dependent, membrane raft endocytosis. PMID: 27094744
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
The rare variants in DNM1 were significantly associated with smoking status. PMID: 25450229
Data indicate that stimulation of the dynamin GTPase activity by SH3 domains is determined by its middle domain. PMID: 26659814
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
Data indicate the dynamics of a dynamin 1-catalysed GTP hydrolysis and tube-severing reaction in real time using fluorescence microscopy. PMID: 26479317
This study identified and confirmed DNM1 protein changes within the postsynaptic density in schizophrenia. PMID: 25048004
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
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
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
Dynamin 1 and dynamin 2 activity are not essential for Chlamydia trachomatis internalization but is required for normal development. PMID: 25116793
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
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
De novo mutations in synaptic transmission genes including DNM1 cause epileptic encephalopathies. PMID: 25262651
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
Alternate pleckstrin homology domain orientations regulate dynamin-catalyzed membrane fission. PMID: 24478459
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
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
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
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
analysis of how the membrane interactions of disease-related dynorphin A variants cause differences in cell toxicity PMID: 23705820
dyn1 affects amyloid generation through regulation of BACE-1 subcellular localization and therefore its enzymatic activities. PMID: 23024787
Herpes simplex virus type 1 can enter human keratinocytes by alternative entry pathways that require dynamin and host cholesterol. PMID: 22022400
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
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
A new role for the dynamin-1 GTPase in the regulation of fusion pore expansion PMID: 21460182
In conclusion, Clostridium botulinum C2 toxin is endocytosed by dynamin-dependent mechanisms and we provide evidence for involvement of clathrin and Rho. PMID: 20690924
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
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
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
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
These findings suggest that dynamin is part of a protein network that controls nucleation of actin from membranes. PMID: 11782545
dynamin-dependent endocytosis is inhibited by syntaphilin PMID: 12896979
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
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
dynamin-1 interacts with Sumo-1, Ubc9, and PIAS-1, all of which are members of the sumoylation machinery PMID: 15123615
Dynamin GTPase domain is important for GTP binding, GTP hydrolysis, and clathrin-mediated endocytosis PMID: 15262989
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
S-nitrosylation of dynamin regulates endocytosis through nitric oxide PMID: 16432212
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
Data show that swapping the highly homologous GTPase domain of dynamin-2 into dynamin-1 is sufficient to confer caspase-3 activation. PMID: 16938290

FAQs

Please fill out the Online Inquiry form located on the product page. Key product information has been pre-populated. You may also email your questions and inquiry requests to sales1@betalifesci.com. We will do our best to get back to you within 4 business hours.

Feel free to use the Chat function to initiate a live chat. Our customer representative can provide you with a quote immediately.

Proteins are sensitive to heat, and freeze-drying can preserve the activity of the majority of proteins. It improves protein stability, extends storage time, and reduces shipping costs. However, freeze-drying can also lead to the loss of the active portion of the protein and cause aggregation and denaturation issues. Nonetheless, these adverse effects can be minimized by incorporating protective agents such as stabilizers, additives, and excipients, and by carefully controlling various lyophilization conditions.

Commonly used protectant include saccharides, polyols, polymers, surfactants, some proteins and amino acids etc. We usually add 8% (mass ratio by volume) of trehalose and mannitol as lyoprotectant. Trehalose can significantly prevent the alter of the protein secondary structure, the extension and aggregation of proteins during freeze-drying process; mannitol is also a universal applied protectant and fillers, which can reduce the aggregation of certain proteins after lyophilization.

Our protein products do not contain carrier protein or other additives (such as bovine serum albumin (BSA), human serum albumin (HSA) and sucrose, etc., and when lyophilized with the solution with the lowest salt content, they often cannot form A white grid structure, but a small amount of protein is deposited in the tube during the freeze-drying process, forming a thin or invisible transparent protein layer.

Reminder: Before opening the tube cap, we recommend that you quickly centrifuge for 20-30 seconds in a small centrifuge, so that the protein attached to the tube cap or the tube wall can be aggregated at the bottom of the tube. Our quality control procedures ensure that each tube contains the correct amount of protein, and although sometimes you can't see the protein powder, the amount of protein in the tube is still very precise.

To learn more about how to properly dissolve the lyophilized recombinant protein, please visit Lyophilization FAQs.