Recombinant Human Polypyrimidine Tract-Binding Protein 1 (PTBP1) Protein (hFc-Myc)

Name: Recombinant Human Polypyrimidine Tract-Binding Protein 1 (PTBP1) Protein (hFc-Myc)
Brand: Beta LifeScience
SKU: BLC-06498P
Availability: InStock

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Product Overview

Description	Recombinant Human Polypyrimidine Tract-Binding Protein 1 (PTBP1) Protein (hFc-Myc) is produced by our Mammalian cell expression system. This is a full length protein.
Purity	Greater than 85% as determined by SDS-PAGE.
Uniprotkb	P26599
Target Symbol	PTBP1
Species	Homo sapiens (Human)
Expression System	Mammalian cell
Tag	C-hFc-Myc
Target Protein Sequence	MDGIVPDIAVGTKRGSDELFSTCVTNGPFIMSSNSASAANGNDSKKFKGDSRSAGVPSRVIHIRKLPIDVTEGEVISLGLPFGKVTNLLMLKGKNQAFIEMNTEEAANTMVNYYTSVTPVLRGQPIYIQFSNHKELKTDSSPNQARAQAALQAVNSVQSGNLALAASAAAVDAGMAMAGQSPVLRIIVENLFYPVTLDVLHQIFSKFGTVLKIITFTKNNQFQALLQYADPVSAQHAKLSLDGQNIYNACCTLRIDFSKLTSLNVKYNNDKSRDYTRPDLPSGDSQPSLDQTMAAAFGAPGIISASPYAGAGFPPTFAIPQAAGLSVPNVHGALAPLAIPSAAAAAAAAGRIAIPGLAGAGNSVLLVSNLNPERVTPQSLFILFGVYGDVQRVKILFNKKENALVQMADGNQAQLAMSHLNGHKLHGKPIRITLSKHQNVQLPREGQEDQGLTKDYGNSPLHRFKKPGSKNFQNIFPPSATLHLSNIPPSVSEEDLKVLFSSNGGVVKGFKFFQKDRKMALIQMGSVEEAVQALIDLHNHDLGENHHLRVSFSKSTI
Expression Range	1-557aa
Protein Length	Full Length
Mol. Weight	89.7 kDa
Research Area	Others
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	Plays a role in pre-mRNA splicing and in the regulation of alternative splicing events. Activates exon skipping of its own pre-mRNA during muscle cell differentiation. Binds to the polypyrimidine tract of introns. May promote RNA looping when bound to two separate polypyrimidine tracts in the same pre-mRNA. May promote the binding of U2 snRNP to pre-mRNA. Cooperates with RAVER1 to modulate switching between mutually exclusive exons during maturation of the TPM1 pre-mRNA. Represses the splicing of MAPT/Tau exon 10. In case of infection by picornaviruses, binds to the viral internal ribosome entry site (IRES) and stimulates the IRES-mediated translation.
Subcellular Location	Nucleus.
Database References	HGNC: 9583 OMIM: 600693 KEGG: hsa:5725 STRING: 9606.ENSP00000349428 UniGene: PMID: 28024117 study provides evidence for the role of PTB in keloid pathophysiology and offers a novel therapeutic target for keloids. Most importantly, the role TGF-beta1 regulation of PTB may provide new insights into the mechanisms underlying inflammatory cytokine-induced fibrosis. PMID: 27897224 the study revealed that PTBP1 facilitates colorectal cancer migration and invasion activities by inclusion of cortactin exon 11 PMID: 28404950 Results showed the expression level of PTBP1 were increased in bladder cancer (BC) patients and that its expression is negatively regulated by MIR-145. PMID: 28380435 PTBP1 is a novel regulator of MCL1 mRNA by which it controls apoptotic response to antitubulin chemotherapeutics. PMID: 27367564 PTB interacts specifically with 3'UTR of p53 mRNA and positively regulates expression of p53 isoforms. PTB showed some overlapping binding regions in the p53 3'UTR with miR-1285. Knockdown of miR-1285 as well as expression of p53 3'UTR with mutated miR-1285 binding sites resulted in enhanced association of PTB with the 3'UTR, which provides mechanistic insights of this interplay. PMID: 28973454 It has been established that PTBP1 and PTBP2 are members of a family of cryptic exon repressors. PMID: 27681424 These results demonstrate that during early stages of splicing, exon RNP complexes are highly dynamic with many proteins failing to bind during PTBP1 arrest. PMID: 27882870 Studied interactions of polypyrimidine tract-binding protein (PTBP1), pyruvate kinase M2 (PKM2), and STAT3 (signal transducer and activator of transcription 3) in oncogenesis of anaplastic large cell lymphoma (ALCL). Results show that in ALCL cells, PTBP1 is crucial for PKM2 phosphorylation of STAT3 in the nucleus. PMID: 28414323 Expression of ATG10 negatively regulated by PTBP1 and is associated with metastasis of colorectal cancer cells. PMID: 27836735 Polypyrimidine tract binding protein (PTBP1) is a heterogeneous nuclear ribonucleoprotein (hnRNP) that plays roles in most stages of the life-cycle of pre-mRNA and mRNAs in the nucleus and cytoplasm. PMID: 27528752 follow-up molecular analyses of one splicing factor PTBP1 revealed its impact on disease-associated splicing patterns in Huntington's disease (HD). Collectively, our data provide genomic evidence for widespread splicing dysregulation in HD brains, and suggest the role of aberrant alternative splicing in the pathogenesis of HD PMID: 27378699 CD5 transcription is increased, leading to the production of three mRNA isoforms by APA, all contributing for protein production, at different levels. PTBP1 binds in the vicinity of pA1, leading to an increase in mRNA levels and miR-204 targets the longer CD5 mRNA. PMID: 27005442 Increased expression of microRNA miR-145 combined with knockdown of PTBP1 protein contributed to the greater and longer growth suppression compared with each single treatment. PMID: 28106737 MiR-133b switched the PKM isoform expression from PKM2 to PKM1 through the silencing of PTBP1, which is an alternative splicer of PKM, leading to growth suppression through the induction of autophagy in part by the metabolic switching from glycolysis to oxidative phosphorylation for a short period of time. PMID: 27696637 Results suggested that PTBP1 and PTBP1-associated miR-1 and -133b are crucial molecules for the maintenance of the Warburg effect in colorectal tumors. PMID: 26980745 The polypyrimidine tract binding protein 1 (PTBP1) shields specific retroviral and cellular transcripts from nonsense-mediated mRNA decay. PMID: 26744779 findings point to PKM2 and PTBP1 as new potential therapeutic targets to improve response of PDAC to chemotherapy PMID: 26234680 PTBP1 and PTBP2 impaired autoregulation of SRSF3 in oral squamous cell carcinoma cancer cells. PMID: 26416554 Results suggest that the role of polypyrimidine tract binding protein 1 (PTBP1) in tumorigenesis may be partly mediated by its regulation of cdc42 GTP-binding protein (CDC42) alternative splicing and CDC42-v2 might function as a tumor suppressor. PMID: 26336992 Data indicate that polypyrimidine tract-binding protein (PTBP1) is preferentially overexpressed in clinical colorectal cancers PMID: 25904505 PTB/hnRNP1 binds to the 3'UTR of Human Astrovirus-8 and is required or participates in viral replication. PMID: 25406089 Data show that the protein levels of polypyrimidine tract binding protein 1 (PTBP1) and adenosine deaminase RNA-specific binding protein ADAR1 were cooperatively expressed in glioma tissues and cells. PMID: 26047657 Organ-specific PTB1-associated microRNAs determine expression of pyruvate kinase isoforms PMID: 25721733 HUR competes with the host protein PTB, which is a negative regulator of hepatitis C virus replication. PMID: 26339049 protein knockdown enhances neurogenesis PMID: 25800779 RBFOX proteins can facilitate the splicing of micro-exons. We also found that PTBP1 likely regulates the inclusion of micro-exons, possibly by repressing the inclusion of micro-exons that are enhanced by RBFOX proteins and other splicing factors. PMID: 25524026 ABLIM1 splicing is regulated by several splice factors, including MBNL family proteins, CELF1, 2 and 6, and PTBP1, using a cellular splicing assay. PMID: 25403273 Suggest that miR-124 acts as a tumor-suppressor and a modulator of energy metabolism through a PTB1/PKM1/PKM2 feedback cascade in human colorectal tumor cells. PMID: 25818238 impact of PTBP1 rs11085226 on glucose-stimulated insulin release PMID: 25927630 IL-7 elevates miR-124 to decrease the expression of splicing regulator PTB and represses CD95 mRNA splicing. PMID: 25411246 PTBP1 and hnRNP C repress exon 3 inclusion, and that downregulation of PTBP1 inhibited BIM-mediated apoptosis. PMID: 24743263 Polypyrimidine tract-binding protein function is controlled by a set of co-recruited proteins and importantly provide further evidence that it is possible to dictate cell fate by modulating cytoplasmic gene expression pathways alone. PMID: 24141718 PCBP2 and PTB are differentially cleaved by human rhinovirus proteinase in infected cells. PMID: 24418535 PTBP1 regulates the alternative splicing of dopamine D2 receptor. PMID: 21054383 Study reports that repression of a single RNA binding polypyrimidine-tract-binding (PTB) protein, which occurs during normal brain development via the action of miR-124, is sufficient to induce trans-differentiation of fibroblasts into functional neurons. PMID: 23313552 conclude that common genetic variation in PTBP1 influences glucose-stimulated insulin secretion. This underlines the importance of PTBP1 for beta cell function in vivo PMID: 23077502 Production of the USP5 isoform 2 was strongly correlated with PTBP1 expression in glioblastoma tumor samples and cell lines. PMID: 21976412 Polypyrimidine tract binding protein (hnRNP I) is possibly a conserved modulator of miRNA-mediated gene regulation. PMID: 22427970 PTB depletion in the dorsal telencephalon is causally involved in the development of hydrocephalus. And PTB is important for the maintenance of Adherens Junctions in the neural stem cells of the dorsal telencephalon. PMID: 22705452 The defective splicing caused by the ISCU intron mutation in patients with myopathy with lactic acidosis is repressed by PTBP1 but can be derepressed by IGF2BP1. PMID: 22125086 PTB is shown to bind an exonic splicing silencer element and repress alternative splicing of FADS2 PMID: 21980057 RBM4 may synergize its effect on muscle cell-specific alternative splicing by down-regulating PTB expression and antagonizing the activity of PTB in exon selection PMID: 21518792 Silencing the expression of PTB with small interfering RNA in two cell lines (Huh7 and HEK 293T) led to a significant increase of up to 4-fold in mRNA levels and virus titer, indicating a negative effect of PTB on coronavirus RNA accumulation. PMID: 21411518 U1 snRNA directly interacts with polypyrimidine tract-binding protein during splicing repression PMID: 21362553 Differentially modified PTB regulates CD40L expression at multiple steps by retaining CD40L mRNA in the nucleus, directly regulating mRNA stability at late times of activation, and forming a ribonuclear complex. PMID: 21242519 The combined results suggest that 3C-mediated cleavage of PTB might be involved in down-regulation of viral translation to give way to subsequent viral genome replication. PMID: 19889140 a strong correlation between the expression of PTB-1, YB-1 and c-myc in multiple myeloma-derived cell lines PMID: 20190818 It appears that the polypyrimidine tract-binding protein might help in circularization of the coxsackievirus B3 RNA by bridging the ends necessary for efficient translation of the viral RNA. PMID: 20071487 The slow backbone dynamics of PTB1:34, induced by packing of (RNA recognition motifs) RRM3 and RRM4, could be essential for high-affinity binding to a flexible polypyrimidine tract RNA and also provide entropic compensation for its own formation. PMID: 20080103

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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 Polypyrimidine Tract-Binding Protein 1 (PTBP1) Protein (hFc-Myc)

Recombinant Human Polypyrimidine Tract-Binding Protein 1 (PTBP1) Protein (hFc-Myc)

Product Overview

Target Details

FAQs