Recombinant Human Tar Dna-Binding Protein 43 (TARDBP)

Name: Recombinant Human Tar Dna-Binding Protein 43 (TARDBP)
Brand: Beta LifeScience
SKU: BLC-00967P
Availability: InStock

Greater than 85% as determined by SDS-PAGE.

Collections: High-quality recombinant proteins, Other recombinant proteins

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Product Overview

Description	Recombinant Human Tar Dna-Binding Protein 43 (TARDBP) is produced by our E.coli expression system. This is a full length protein.
Purity	Greater than 85% as determined by SDS-PAGE.
Uniprotkb	Q13148
Target Symbol	TARDBP
Species	Homo sapiens (Human)
Expression System	E.coli
Tag	Tag-Free
Target Protein Sequence	MSEYIRVTEDENDEPIEIPSEDDGTVLLSTVTAQFPGACGLRYRNPVSQCMRGVRLVEGILHAPDAGWGNLVYVVNYPKDNKRKMDETDASSAVKVKRAVQKTSDLIVLGLPWKTTEQDLKEYFSTFGEVLMVQVKKDLKTGHSKGFGFVRFTEYETQVKVMSQRHMIDGRWCDCKLPNSKQSQDEPLRSRKVFVGRCTEDMTEDELREFFSQYGDVMDVFIPKPFRAFAFVTFADDQIAQSLCGEDLIIKGISVHISNAEPKHNSNRQLERSGRFGGNPGGFGNQGGFGNSRGGGAGLGNNQGSNMGGGMNFGAFSINPAMMAAAQAALQSSWGMMGMLASQQNQSGPSGNNQNQGNMQREPNQAFGSGNNSYSGSNSGAAIGWGSASNAGSGSGFNGGFGSSMDSKSSGWGM
Expression Range	1-414aa
Protein Length	Full Length
Mol. Weight	44.9 kDa
Research Area	Microbiology
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	RNA-binding protein that is involved in various steps of RNA biogenesis and processing. Preferentially binds, via its two RNA recognition motifs RRM1 and RRM2, to GU-repeats on RNA molecules predominantly localized within long introns and in the 3'UTR of mRNAs. In turn, regulates the splicing of many non-coding and protein-coding RNAs including proteins involved in neuronal survival, as well as mRNAs that encode proteins relevant for neurodegenerative diseases. Plays a role in maintaining mitochondrial homeostasis by regulating the processing of mitochondrial transcripts. Regulates also mRNA stability by recruiting CNOT7/CAF1 deadenylase on mRNA 3'UTR leading to poly(A) tail deadenylation and thus shortening. In response to oxidative insult, associates with stalled ribosomes localized to stress granules (SGs) and contributes to cell survival. Participates also in the normal skeletal muscle formation and regeneration, forming cytoplasmic myo-granules and binding mRNAs that encode sarcomeric proteins. Plays a role in the maintenance of the circadian clock periodicity via stabilization of the CRY1 and CRY2 proteins in a FBXL3-dependent manner. Negatively regulates the expression of CDK6. Regulates the expression of HDAC6, ATG7 and VCP in a PPIA/CYPA-dependent manner.
Subcellular Location	Nucleus. Cytoplasm. Cytoplasm, Stress granule.
Database References	HGNC: 11571 OMIM: 605078 KEGG: hsa:23435 STRING: 9606.ENSP00000240185 UniGene: PMID: 30030424 CHCHD10 mutations have a role in cytoplasmic TDP-43 accumulation and synaptic integrity PMID: 28585542 Study confirms the high expression of hTDP-43 in the CNS, increased microgliosis and motor deficits, exhibiting further prominent ALS/FTLD pathologies, such as cytoplasmic and insoluble TDP-43 in TAR6/6 mice. This model represents not only pathological TDP-43 expression but also disease-relevant posttranslational changes. PMID: 29787578 The relevance of contact-independent cell-to-cell transfer of TDP-43 and SOD1 in amyotrophic lateral sclerosis. PMID: 28711596 Findings highlight that the phosphatase regulator, GADD34, also functions as a kinase scaffold in response to chronic oxidative stress and recruits CK1 and oxidized TDP-43 to facilitate its phosphorylation, as seen in TDP-43 proteinopathies. PMID: 29109149 We identified impaired RNA metabolism, secondary to TDP-43 loss of function, as a possible pathological mechanism of HSPB8 toxicity, leading to muscle and nerve degeneration PMID: 29029362 the introduction of SOD1(G93A) and TDP43(A315T), established Amyotrophic lateral sclerosis (ALS)-related mutations, changed the subcellular expression and localization of RNAs within the neurons, showing a spatial specificity to either the soma or the axon. Altogether, we provide here the first combined inclusive profile of mRNA and miRNA expression in two ALS models at the subcellular level PMID: 28300211 These data provide structural detail for the established mechanistic role of the well-folded TDP-43 NTD in splicing and link this function to liquid-liquid phase separation. PMID: 29438978 TDP43 alters most splicing events with splicing factor SRSF3 in triple-negative breast cancer. PMID: 29581274 Of the whole cohort of patients with Motor Neuron Disease and Frontotemporal Dementia, 1 patient harboured a mutation in the TAR DNA-binding protein (TARDBP) gene. PMID: 29886477 Study demonstrated TDP-43/pTDP-43 deposition in skin nerves in ALS patients. Although the mechanisms underlying TDP-43 in ALS are currently unknown, its detection is of interest, and the deposition may occur not only in ALS but also during the aging process which is based on observations of the present study. PMID: 29804146 Both ALS and FTD patients presented with higher TDP-43 and tauT levels compared to the control group. The combination of biomarkers in the form of the TDP-43 x tauT / tauP-181 formula achieved the best discrimination between ALS or FTD and controls, with sensitivities and specificities >0.8. PMID: 28848086 TDP-43 turnover and toxicity depend in part upon the endocytosis pathway. TDP-43 inhibits endocytosis, and co-localizes strongly with endocytic proteins, including in amyotrophic lateral sclerosis patient tissue. PMID: 29233983 more selective group of neurons appears to be affected in frontotemporal lobar degeneration (FTLD)-TDP and FTLD-FUS than in FTLD-tau PMID: 28984110 study found a high frequency of the TARDBP p.M337 V mutation in familial amyotrophic lateral sclerosis (ALS) in south-eastern China; the TARDBP-linked ALS patients showed a benign disease course and prolonged survival PMID: 29621978 describe here two cases of apparently sporadic amyotrophic lateral sclerosis associated with mutations, respectively, in SOD1 and TARDP genes PMID: 27494151 Study indicates that there are at least two common patterns of TDP-43 and tau protein misfolding in human brain aging. In patients lacking substantial Alzheimer's disease pathology, cerebral age-related TDP-43 with sclerosis (CARTS) cases tend to have tau neurofibrillary tangles in the hippocampal dentate granule neurons, providing a potential proxy indicator of CARTS. PMID: 28281308 Depletion of TAF15, FUS and TDP-43 in human-induced pluripotent stem cell-derived motor neurons affects different genes. PMID: 27378374 TDP-43 mislocalisation into axons precedes cell death in cortical neurons, and that cytoskeletal structure and function is impaired by expression of either TDP-43 wild-type or mutant constructs in vitro. PMID: 29787572 TDP-43 impairs the induction of multiple key stress genes required to protect from disease by reducing the recruitment of the chromatin remodeler Chd1 to chromatin. PMID: 29153328 The mutation of TARDBP caused amyotrophic lateral sclerosis PMID: 29478603 Cytoplasmic TDP-43 mislocalization and aggregation is a pathological hallmark of amyotrophic lateral sclerosis and frontotemporal lobar degeneration. TDP-43 is an RNA-binding protein with a prion-like domain that promotes TDP-43 misfolding. [review] PMID: 27920024 SOD1 mutations were present in 20% of familial amyotrophic lateral sclerosis (ALS) patients and 1.9% of sporadic ALS patients, while FUS mutations were responsible for 13.3% of familial ALS cases, and TARDBP mutations were rare in either familial or sporadic ALS cases. PMID: 27604643 an alpha-helical component in the centre (residues 320-340) of the C-terminal domain is related to the protein's self-association and LLPS. Systematically analysing ALS-related TDP-43 mutants (G298S, M337V, and Q331K) in different buffer conditions at different temperatures, we prove that this phase separation is driven by hydrophobic interactions but is inhibited by electrostatic repulsion. PMID: 28988034 the present study did not demonstrate oxidative phosphorylation defects in TDP-43 mutants PMID: 28482850 both FUS and TDP43 colocalize with active RNA polymerase II at sites of DNA damage along with the DNA damage repair protein, BRCA1, and FUS and TDP43 participate in the prevention or repair of R loop-associated DNA damage, a manifestation of aberrant transcription and/or RNA processing PMID: 27849576 The data of this study suggest that TDP-43 pathology is associated with age and exacerbated by the presence of concomitant Alzheimer's disease pathology. PMID: 27495267 The A382T mutation in TARDBP caused a reduction in the ability of cells to respond to stress through loss of TDP-43 function in stress granule nucleation. The pathogenetic action revealed in study model does not seem to be mediated by changes in the localization of the TDP-43 protein. PMID: 28172957 TDP-43 competes with other splicing factors for binding to cryptic exons and can repress cryptic exon inclusion. PMID: 28549443 Study shows that TDP-43 is deposited in the olfactory bulb in Alzheimer's disease, albeit of low frequency. The deposition appears to be a late occurrence compared to TDP-43 deposition in other brain regions. PMID: 26810591 ALS-mutant linked TDP-43 mutations expressed at moderate levels in a pattern mimicking endogenous TDP-43 also cause toxicity in a non-cell autonomous manner. Eliminating mutant TDP-43Q331K synthesis in a proportion of motor neurons delayed disease onset, reduced aberrant nuclear morphology in those neurons at early disease stages, and almost eliminated age-dependent accelerated death of those motor neurons. PMID: 28357566 Study reports that cryptic exon incorporation occurred not only in Alzheimer' disease brains exhibiting TDP-43 pathology, but also in neurons lacking cytoplasmic inclusion but exhibiting nuclear clearance of TDP-43. PMID: 28332094 Acetylation of the protein triggers TDP-43 pathology in cultured cells and mouse skeletal muscle, which can be cleared through an HSF1-dependent chaperone mechanism that disaggregates the protein. PMID: 28724966 These studies showed that physiological oligomerization of TDP-43 is mediated through its N-terminal domain, which forms functional and dynamic oligomers antagonizing pathologic aggregation. PMID: 28663553 Expression of PFN1 mutants induces accumulation of TDP-43, and promotes conversion of normal TDP-43 into an abnormal form. These results provide new insight into the mechanisms of TDP-43 proteinopathies and other diseases associated with amyloid-like protein deposition. PMID: 27432186 Study reports the altered expression and/or mislocalization of the TAR-DNA binding protein 43 (TDP-43) in both niemann-pick disease type C mouse and in a human neuronal model of the disease. Results extend the importance of the role of TDP-43 in neurodegenerative disease and further highlight the need to prioritize the targeting of this protein to develop novel therapeutic strategies. PMID: 27193329 This study demonstrated that increased rates of TDP-43-associated hippocampal atrophy might occur at least 10 years before death in patient with Alzheimer disease. PMID: 28919059 Authors observed impaired levels of glutathione (downstream Nrf2 antioxidant) in TDP-43M337V patient fibroblasts and astrocyte cultures from TDP-43Q331K mice, indicative of elevated oxidative stress and failure of some upregulated antioxidant genes to be translated into protein. PMID: 28334913 removing the human orthologs of Hrb27c (DAZAP1) in human neuronal cell lines can correct several pre-mRNA splicing events altered by TDP-43 depletion PMID: 28575377 TDP-43 suppressed tau expression by promoting its mRNA instability through the UG repeats of its 3-UTR. The C-terminal region of TDP-43 was required for this function.The level of TDP-43, which is decreased in AD brains, was found to correlate negatively with the tau level in human brain. PMID: 28335005 Amyotrophic lateral sclerosis mutations disrupt phase separation mediated by alpha-helical structure in the TDP-43 low-complexity C-terminal domain. PMID: 27545621 we demonstrated cytoplasmic TDP-43 aggregate formation in neuronal and glial cells following adenoviral transduction of WT and CTF TDP-43 under MG-132 treatment. These TDP-43 aggregates were phosphorylated and ubiquitinated and consisted of electron-dense granules. PMID: 28599005 emphasize the importance of distinguishing cerebral age-related TDP-43 with sclerosis from late-onset frontotemporal lobar degeneration with TDP-43 pathology and from advanced Alzheimer disease with TDP-43 pathology PMID: 28467211 Mutant and wild type human TDP-43 replacing the endogenous Drosophila gene reveals phosphorylation and ubiquitination in mutant lines in the absence of viability or lifespan defects. PMID: 28686708 The study establishes a functional/physical partnership between FMRP and TDP-43 that mechanistically links several neurodevelopmental disorders and neurodegenerative diseases. PMID: 27518042 By silencing TDP-43, authors saw significant inhibition of cell proliferation and metastasis in A375 and WM451 cells. TDP-43 knockdown could suppress glucose transporter type-4 (GLUT4) expression and reduce glucose uptake. PMID: 27786596 The present study, based on 15 cases staged for pTDP-43 pathology, reports the finding that pathologically altered TDP-43 in Betz cells reacts differently than that in bulbar or spinal alpha-motoneurons. The major differences between the two types of histological profiles are discussed within the context of their possible consequences and implications for the potential further progression or spread of the pTDP-43 lesions. PMID: 27757524 This study have shown that TDP-43-positive cytoplasmic inclusions were frequently found in the amygdala of pathologically and genetically confirmed cases of Frontotemporal Lobar Degeneration and Motor Neuron Disease. PMID: 28859337 Results indicated that a range of disease specific TDP-43 variants are generated in amyotrophic lateral sclerosis patients with different variants being generated in sporadic and familial cases. PMID: 28122516 heterogeneous structural reorganization and decreased stability of the truncated RRM2 domain PMID: 28793209

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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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