Recombinant Human Polyadenylate-Binding Protein 2 (PABPN1) Protein (His)

Name: Recombinant Human Polyadenylate-Binding Protein 2 (PABPN1) Protein (His)
Brand: Beta LifeScience
SKU: BLC-07515P
Availability: InStock

Greater than 85% as determined by SDS-PAGE.

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

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Product Overview

Description	Recombinant Human Polyadenylate-Binding Protein 2 (PABPN1) Protein (His) is produced by our Baculovirus expression system. This is a full length protein.
Purity	Greater than 85% as determined by SDS-PAGE.
Uniprotkb	Q86U42
Target Symbol	PABPN1
Synonyms	(PABP-2)(Poly(A)-binding protein 2)(Nuclear poly(A)-binding protein 1)(Poly(A)-binding protein II)(PABII)(Polyadenylate-binding nuclear protein 1)
Species	Homo sapiens (Human)
Expression System	Baculovirus
Tag	N-10His
Target Protein Sequence	AAAAAAAAAAGAAGGRGSGPGRRRHLVPGAGGEAGEGAPGGAGDYGNGLESEELEPEELLLEPEPEPEPEEEPPRPRAPPGAPGPGPGSGAPGSQEEEEEPGLVEGDPGDGAIEDPELEAIKARVREMEEEAEKLKELQNEVEKQMNMSPPPGNAGPVIMSIEEKMEADARSIYVGNVDYGATAEELEAHFHGCGSVNRVTILCDKFSGHPKGFAYIEFSDKESVRTSLALDESLFRGRQIKVIPKRTNRPGISTTDRGFPRARYRARTTNYNSSRSRFYSGFNSRPRGRVYRGRARATSWYSPY
Expression Range	2-306aa
Protein Length	Full Length of Mature Protein
Mol. Weight	35.1 kDa
Research Area	Epigenetics And Nuclear Signaling
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	Involved in the 3'-end formation of mRNA precursors (pre-mRNA) by the addition of a poly(A) tail of 200-250 nt to the upstream cleavage product. Stimulates poly(A) polymerase (PAPOLA) conferring processivity on the poly(A) tail elongation reaction and controls also the poly(A) tail length. Increases the affinity of poly(A) polymerase for RNA. Is also present at various stages of mRNA metabolism including nucleocytoplasmic trafficking and nonsense-mediated decay (NMD) of mRNA. Cooperates with SKIP to synergistically activate E-box-mediated transcription through MYOD1 and may regulate the expression of muscle-specific genes. Binds to poly(A) and to poly(G) with high affinity. May protect the poly(A) tail from degradation. Subunit of the trimeric poly(A) tail exosome targeting (PAXT) complex, a complex that directs a subset of long and polyadenylated poly(A) RNAs for exosomal degradation. The RNA exosome is fundamental for the degradation of RNA in eukaryotic nuclei. Substrate targeting is facilitated by its cofactor MTREX, which links to RNA-binding protein adapters.
Subcellular Location	Nucleus. Cytoplasm. Nucleus speckle.
Database References	HGNC: 8565 OMIM: 164300 KEGG: hsa:8106 STRING: 9606.ENSP00000216727 UniGene: PMID: 27854203 The purpose of this study was to characterize the type of PABPN1 expanded alleles in a large cohort of Oculopharyngeal muscular dystrophy individuals from Mexico. PMID: 27980005 We propose that the extensive binding of CircPABPN1 to HuR prevents HuR binding to PABPN1 mRNA and lowers PABPN1 translation, providing the first example of competition between a circRNA and its cognate mRNA for an RBP that affects translation. PMID: 28080204 Whereas PABPN1 strongly increases the activity of its cognate poly(A) polymerase in vitro, Pab2 was unable to stimulate Pla1 to any significant extent. PMID: 28096519 The described is the mRNA degradation poly(A) tail exosome targeting (PAXT) connection, which comprises the ZFC3H1 Zn-knuckle protein as a central link between MTR4 and the nuclear poly(A)-binding protein PABPN1. PMID: 27871484 PABPN1 aggregates are able to trap TNNT3 pre-mRNA, driving it outside nuclear speckles, leading to an altered SC35-mediated splicing. PMID: 27507886 The levels of these 6 cytokines were not altered in expPABPN1 carriers at a pre-symptomatic stage, suggesting that this group of cytokines is a potential biomarker for muscle weakness in OPMD. Correlation pattern of expression levels could be a novel measurer for disease state PMID: 27506982 Large cohort study demonstrated that in heterozygous and homozygous patients with oculopharyngeal muscular dystrophy, the mean age at diagnosis and the severity of the clinical symptoms correlate to the number of PABPN1 (GCN) repeats. Homozygous patients showed the worse phenotype, suggesting a gene-dose effect in addition to the repeat number expansion. PMID: 28011929 we found a polyadenylation-dependent 3' end maturation pathway for the human telomerase RNA that relies on the nuclear poly(A)-binding protein PABPN1 and the poly(A)-specific RNase PARN. PMID: 26628368 Many ribozymes were assayed and validated, including four ribozymes targeting the transcript of a disease-causing gene (a mutant version of PABPN1). PMID: 26527730 Studied if the stability of the RNP domain of PABPN1 or domain swapping within the RNP domain may add to fibril formation. PMID: 26267866 This function is mediated by the concerted actions of the nuclear poly(A) binding protein PABPN1, poly(A) polymerase (PAP), and the nuclear exosome complex, a pathway we have named PABPN1 and PAP-mediated RNA decay (PPD) PMID: 26484760 These findings demonstrate a role for PABPN1 in rescuing several cytopathological features of TDP-43 proteinopathy by increasing the turnover of pathologic proteins. PMID: 26130692 PABPN1 inhibits expression of transcripts with pAs near the transcription start site (TSS), a property possibly related to its role in RNA degradation PMID: 25906188 this study provided a systematic phosphorylation analysis of the Fanconi anemia protein PALB2, and have revealed important roles of PALB2 Ser-157 and Ser-376 in driving cellular responses to genotoxic stress. PMID: 26420486 the first step of the cleavage and polyadenylation reaction, mRNA cleavage, is affected in muscles expressing alanine-expanded PABPN1. We propose that impaired cleavage is an early defect in Oculopharyngeal muscular dystrophy. PMID: 25816335 Data indicate that intron 6 of the poly(A)-binding protein nuclear 1 (PABPN1) gene is required for autoregulation. PMID: 25963658 The ability of PABPN1 to promote splicing requires its RNA binding and, to a lesser extent, poly(A)polymerase (PAP) - stimulatory functions. PMID: 25896913 We show that ARIH2 E3-ligase regulates PABPN1 protein accumulation and aggregation PMID: 24486325 Loss of PABPN1, a suppressor of APA, might promote tumor aggressiveness by releasing the cancer cells from microRNA-mediated gene regulation. PMID: 24975429 These results suggest that PABPN1 levels regulate muscle cell aging and oculopharyngeal muscular dystrophy represents an accelerated muscle aging disorder. PMID: 23793615 although function of PABPN1 may be compensated by nuclear translocation of PABP4 and perhaps by increase the cytoplasmic abundance of PABP5, these were not sufficient to prevent apoptosis of cells. PABPN1 may have an anti apoptotic role in mammalian cells PMID: 23300856 Concerning the frequency of the expanded (GCN)11 polymorphism in PABPN1, all 34 patients have the normal allele, correlating genotypic and phenotypic features. PMID: 22231868 we show that PABPN1 promotes lncRNA turnover via a polyadenylation-dependent mechanism PMID: 23166521 Time-lapse experiments in cultured myoblasts confirm nuclear speckles as biogenesis sites of PABPN1 inclusions in oculopharyngeal muscular dystrophy. PMID: 22249111 PABPN1 with a 17 alanine expansion generates stress that initiates apoptosis through a p53-dependent mechanism. PMID: 22519734 Taken together, the present data suggest that heterozygote OPMD patients may show some cognitive impairments and psychological disorders PMID: 21956377 Fibrillar PABPN1 has a structure that differs from native PABPN1 and circumstantial evidence is presented that the C-terminal domain is involved in fibril formation. PMID: 22570486 Results elucidate a novel function for PABPN1 as a suppressor of alternative cleavage and polyadenylation. PMID: 22502866 In myotubes, the ratio of soluble/insoluble expPABPN1 is significantly lower compared with that of the WT protein. PMID: 21854744 Transportin binding might delay methylation of PABPN1 until after nuclear import. PMID: 21808065 A GCG expansion (GCG)11 in polyadenylate-binding protein nuclear 1 gene caused oculopharyngeal muscular dystrophy in a Chinese family. PMID: 21647273 no correlation was found between muscle weakness, the frequency of repeats in the polyadenine binding protein nuclear , and the frequency and size of nuclear inclusions PMID: 21545772 The autosomal dominant form of this disease is caused by short expansions of a (GCG)(6) repeat to (GCG)(8-13) in the PABPN1 gene. PMID: 11689481 In COS-7 cells, predominantly nuclear protein hnRNP A1 and A/B co-localize with mPABPN1 in insoluble intranuclear aggregates. PMID: 12945950 All families carrying the mutation (GCG)(11)(GCA)(3)(GCG) shared a common ancestral haplotype and the age of the mutation was estimated in 37-53 generations by a composite likelihood method. PMID: 15694141 a 64 year old Chinese-Malaysian woman who presented with progressive dysphagia and bilateral ptosis for about 6 years. and showed repeat expansion in one allele to (GCG)9 while normal in the other (GCG)6. PMID: 15725589 Expanded PABPN1, presumably via the toxic effects of its polyalanine tract, leads to inclusion formation and neurodegeneration in both the transgenic mouse and the human. PMID: 15755680 Cytoplasmic targeting of mutant PABPN1 suppresses protein aggregation and toxicity in oculopharyngeal muscular dystrophy. PMID: 16101680 Recruitment of HSP70 and HSC70 into the cell nucleus reduced mutant PABPN1 aggregation in a HeLa cell culture model. PMID: 16239242 PABPN1 has a role in myogenesis PMID: 16378590 Overexpression of either the wild type or mutant PABPN1 slowed down cell proliferation. The slowing down of proliferation together with the occasional occurrence of apoptosis could contribute in vivo to the late onset of this disease. PMID: 16860991 Mutation of the PABPN1 in oculopharyngeal muscular dystrophy (OPMD) provokes premature senescence in dividing myoblasts, that may be due to intranuclear toxic aggregates. PMID: 17005403 the N-terminal domain of PABPN1 has a role in oculopharyngeal muscular dystrophy PMID: 17229142 This is the first report directly indicating that nuclear aggregation in OPMD may reflect an active process by which cells sequester and inactivate the soluble toxic form of expPABPN1. PMID: 17418585 An Italy case of oculopharyngeal muscular dystrophy in PABNPN1 mutation. PMID: 18175083 Wild-type PABPN1 over-expression can reduce mutant PABPN1 toxicity in both cell and mouse models of Oculopharyngeal muscular dystrophy. PMID: 18178579 We report a unique PABPN1 gene mutation in a large Bulgarian family with OPMD. PMID: 18274805 Expression of additional HSPs including HSP27, HSP40, and HSP105 were induced in mutant PABPN1 expressing cells following exposure to the chemicals mentioned above. PMID: 18343218 PABPN1 transgenic nematodes show muscle cell degeneration and abnormal motility. PMID: 18397876

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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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Recombinant Human Polyadenylate-Binding Protein 2 (PABPN1) Protein (His)

Recombinant Human Polyadenylate-Binding Protein 2 (PABPN1) Protein (His)

Product Overview

Target Details

FAQs