Recombinant Human Nuclear Distribution Protein Nude-Like 1 (NDEL1) Protein (GST)

Name: Recombinant Human Nuclear Distribution Protein Nude-Like 1 (NDEL1) Protein (GST)
Brand: Beta LifeScience
SKU: BLC-08704P
Availability: InStock

Greater than 90% as determined by SDS-PAGE.

Collections: All products, High-quality recombinant proteins, Other recombinant proteins

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Product Overview

Description	Recombinant Human Nuclear Distribution Protein Nude-Like 1 (NDEL1) Protein (GST) is produced by our E.coli expression system. This is a full length protein.
Purity	Greater than 90% as determined by SDS-PAGE.
Uniprotkb	Q9GZM8
Target Symbol	NDEL1
Synonyms	A. nidulans; DKFZp451M0318; ENDOOLIGOPEPTIDASE A; EOPA; MITAP 1; MITAP1; Mitosin associated protein 1; Mitosin associated protein MITAP1; Mitosin-associated protein 1; Ndel 1; NDEL1; NDEL1_HUMAN; Nuclear distribution gene E like homolog 1; Nuclear distribution protein nudE like 1; Nuclear distribution protein nudE-like 1; NUDE like protein; NudE nuclear distribution gene E homolog like 1 A. nidulans; NudE nuclear distribution gene E homolog like 1; NUDEL; Protein Nudel
Species	Homo sapiens (Human)
Expression System	E.coli
Tag	N-GST
Target Protein Sequence	MDGEDIPDFSSLKEETAYWKELSLKYKQSFQEARDELVEFQEGSRELEAELEAQLVQAEQRNRDLQADNQRLKYEVEALKEKLEHQYAQSYKQVSVLEDDLSQTRAIKEQLHKYVRELEQANDDLERAKRATIVSLEDFEQRLNQAIERNAFLESELDEKESLLVSVQRLKDEARDLRQELAVRERQQEVTRKSAPSSPTLDCEKMDSAVQASLSLPATPVGKGTENTFPSPKAIPNGFGTSPLTPSARISALNIVGDLLRKVGALESKLAACRNFAKDQASRKSYISGNVNCGVLNGNGTKFSRSGHTSFFDKGAVNGFDTAPPPPGLGSSRPSSAPGMLPLSV
Expression Range	1-345aa
Protein Length	Full Length of BC026101
Mol. Weight	65.4kDa
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	Required for organization of the cellular microtubule array and microtubule anchoring at the centrosome. May regulate microtubule organization at least in part by targeting the microtubule severing protein KATNA1 to the centrosome. Also positively regulates the activity of the minus-end directed microtubule motor protein dynein. May enhance dynein-mediated microtubule sliding by targeting dynein to the microtubule plus ends. Required for several dynein- and microtubule-dependent processes such as the maintenance of Golgi integrity, the centripetal motion of secretory vesicles and the coupling of the nucleus and centrosome. Also required during brain development for the migration of newly formed neurons from the ventricular/subventricular zone toward the cortical plate. Plays a role, together with DISC1, in the regulation of neurite outgrowth. Required for mitosis in some cell types but appears to be dispensible for mitosis in cortical neuronal progenitors, which instead requires NDE1. Facilitates the polymerization of neurofilaments from the individual subunits NEFH and NEFL. Positively regulates lysosome peripheral distribution and ruffled border formation in osteoclasts.
Subcellular Location	Cytoplasm, cytoskeleton. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome. Chromosome, centromere, kinetochore. Cytoplasm, cytoskeleton, spindle.
Protein Families	NudE family
Database References	HGNC: 17620 OMIM: 607538 KEGG: hsa:81565 STRING: 9606.ENSP00000333982 UniGene: PMID: 27546710 results highlight S-Nitrosylation as a key activity-dependent mechanism underlying neonatal brain maturation and suggest that reduction of S-Nitrosylation of NDEL1 acts as a pathological factor mediating neurodevelopmental abnormalities caused by maternal alcohol exposure PMID: 27371763 disrupting DISC1/Ndel1 complex formation prolongs mitotic length and interferes with cell-cycle progression in human cells, and it causes cell-cycle deficits of radial glial cells in the embryonic mouse cortex and human forebrain organoids PMID: 29103808 Study showed that Ndel1 enzyme activity is a complex trait influenced by many different genetic variants that may contribute to schizophrenia physiopathology PMID: 26851141 This study observed a significantly increased myelin basic protein (MBP) and nuclear distribution protein nudE-like 1 (NDEL1) mRNA levels in FEP patients compared with controls. PMID: 26476704 The Plasma Ndel1 enzyme activity is reduced in patients with schizophrenia. PMID: 23388542 Short (DISC)1 splice variants show reduced or no binding to nudE nuclear distribution E homolog (NDEL)1 and phosphodiesterase (PDE)4B proteins, but fully interact with FEZ1 and glycogen synthase kinase 3 (GSK3)beta. PMID: 22832604 Nudel markedly promotes the HSPC300-WAVE2 interaction. PMID: 22453242 Cytosolic mfGbeta is recruited to dynein by Nudel and transported to the centrosome for rapid sequestration and degradation. PMID: 22430153 Studies indicate that binding of dynactin, LIS1 and NudEL regulate cytoplasmic dynein motor activity. PMID: 22373868 DISC1 forms octamers via dimers as building blocks. S704C forms higher-order oligomers, without affecting its affinity with NDEL1 PMID: 21998303 Nuclear distribution element-like 1 (Ndel1 or Nudel) was firstly described as a regulator of the cytoskeleton in microtubule and intermediate filament dynamics and microtubule-based transport. PMID: 21948775 Evidence of statistical epistasis between DISC1, CIT and NDEL1 impacting risk for schizophrenia: biological validation with functional neuroimaging. PMID: 20084519 The truncated monomeric form of LIS1 had little effect on dynein motility, but an artificial dimer of truncated LIS1 suppressed dynein motility, which was restored by the N-terminal fragment of NDEL1. PMID: 21036906 NDEL1 is essential for a specific late step of neuronal migration: entry into the target lamina. PMID: 21092859 This data supports a physiological role for the endooligopeptidase activity of Ndel1 and suggests it plays a key role during neurite outgrowth. PMID: 20462516 Findings suggest that physiological functions of LIS1 and NDEL1 in neurons have been ascribed for proteins fundamentally required for cell cycle progression and control. PMID: 20168084 palmitoylated Ndel1 reduced cytoplasmic dynein activity as judged by Golgi distribution, VSVG and short microtubule trafficking, transport of endogenous Ndel1 and LIS1 from neurite tips to the cell body and neuronal migration PMID: 19927128 disease mutant form of Disrupted-in-Schizophrenia-1 fails to bind NUDEL PMID: 12506198 results point to the importance of Nudel-Lis1 interaction for the dynein activity in M phase and to a possible role of Nudel phosphorylation as facilitating such interaction. PMID: 12556484 DISC1 inhibits NUDEL-oligopeptidase activity in a competitive fashion. PMID: 15728732 NDEL1 is essential for mitotic cell division and neuronal migration not only via regulation of cytoplasmic dynein function but also by modulation of katanin p60 localization and function. PMID: 16203747 Aurora-A-mediated phosphorylation of NDEL1 is essential for centrosomal separation and centrosomal maturation and for mitotic entry PMID: 17060449 These results suggest a dual role of kinetochore Nudel: it activates dynein-mediated protein transport and, when interacting with both mitosin and dynein, stabilizes kinetochore dynein/dynactin. PMID: 17494871 Ndel1-deficient cells enter anaphase in a timely manner but lagging chromosomes then manifest. PMID: 17600710 crystallographic study of two fragments of the coiled-coil domain of Ndel1, one of which reveals contiguous high-quality electron density for residues 10-166, the longest such structure reported by X-ray diffraction at high resolution PMID: 17997972 Our work uncovers a unique regulatory mechanism of MT organization by PP4c through its targets Cdk1 and NDEL1 via regulation of katanin p60 distribution. PMID: 18347064 For DISC1-related sporadic psychiatric disease, impaired cellular control over self-association of DISC1 leads to excessive multimerization and subsequent formation of detergent-resistant aggregates, with loss of ligand binding, exemplified by NDEL1. PMID: 18400883 NDEL1 regulates cytoplasmic dynein and involved in the regulation of microtubule organization, and becomes the target of various kinases and phosphatases. PMID: 18421979 NDEL1 significantly influences risk for schizophrenia via an interaction with DISC1. PMID: 18469341 Data show that LIS1 suppresses the motility of cytoplasmic dynein on microtubules, whereas NDEL1 releases the blocking effect of LIS1 on cytoplasmic dynein. PMID: 18784752 NDEL1 protein interacts directly with Cyclic Nucleotide Phosphodiesterases, Type 4 and its isoforms and interaction of NDEL1 protein with phosphodiesterase isoform is uniquely disrupted by elevation of intracellular cyclic AMP levels. PMID: 18845247 Nudel regulates microtubule organization in part by facilitating assembly of the lamin B spindle matrix in a dynein-dependent manner. PMID: 19198602 These results suggest a novel mechanism for selective reinforcement of nascent adhesions via interplays of Nudel and FAK with paxillin to facilitate cell migration. PMID: 19492042 These results indicate an antagonistic effect of alpha1, alpha2 and Ndel1 for Lis1 binding, probably to modulate dynein functions in vivo. PMID: 19622634 There was no strong evidence for association with NUDEL in schizophrenia. PMID: 19632097

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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.

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