Recombinant Human Polyadenylate-Binding Protein 1 (PABPC1) Protein (His-SUMO)

Name: Recombinant Human Polyadenylate-Binding Protein 1 (PABPC1) Protein (His-SUMO)
Brand: Beta LifeScience
SKU: BLC-03083P
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 Polyadenylate-Binding Protein 1 (PABPC1) Protein (His-SUMO) is produced by our E.coli expression system. This is a protein fragment.
Purity	Greater than 90% as determined by SDS-PAGE.
Uniprotkb	P11940
Target Symbol	PABPC1
Synonyms	PABPC1; PAB1; PABP1; PABPC2; Polyadenylate-binding protein 1; PABP-1; Poly(A)-binding protein 1
Species	Homo sapiens (Human)
Expression System	E.coli
Tag	N-6His-SUMO
Target Protein Sequence	MNPSAPSYPMASLYVGDLHPDVTEAMLYEKFSPAGPILSIRVCRDMITRRSLGYAYVNFQQPADAERALDTMNFDVIKGKPVRIMWSQRDPSLRKSGVGNIFIKNLDKSIDNKALYDTFSAFGNILSCKVVCDENGSKGYGFVHFETQEAAERAIEKMNGMLLNDRKVFVGRFKSRKEREAELGARAKEFTNVYIKNFGEDMDDERLKDLFGKFGPALSVKVMTDESGKSKGFGFVSFERHEDAQKAVDEMNGKELNGKQIYVGRAQKKVERQTELKRKFEQMKQDRITRYQGVNLYVKNLDDGIDDERLRKEFSPFGTITSAKVMMEGGRSKGFGFVCFSSPEEATKAVTEMNGRIVATKPLYVALAQR
Expression Range	1-370aa
Protein Length	Partial
Mol. Weight	57.8kDa
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	Binds the poly(A) tail of mRNA, including that of its own transcript, and regulates processes of mRNA metabolism such as pre-mRNA splicing and mRNA stability. Its function in translational initiation regulation can either be enhanced by PAIP1 or repressed by PAIP2. Can probably bind to cytoplasmic RNA sequences other than poly(A) in vivo. Involved in translationally coupled mRNA turnover. Implicated with other RNA-binding proteins in the cytoplasmic deadenylation/translational and decay interplay of the FOS mRNA mediated by the major coding-region determinant of instability (mCRD) domain. Involved in regulation of nonsense-mediated decay (NMD) of mRNAs containing premature stop codons; for the recognition of premature termination codons (PTC) and initiation of NMD a competitive interaction between UPF1 and PABPC1 with the ribosome-bound release factors is proposed. By binding to long poly(A) tails, may protect them from uridylation by ZCCHC6/ZCCHC11 and hence contribute to mRNA stability.; (Microbial infection) Positively regulates the replication of dengue virus (DENV).
Subcellular Location	Cytoplasm. Cytoplasm, Stress granule. Nucleus. Cell projection, lamellipodium.
Protein Families	Polyadenylate-binding protein type-1 family
Database References	HGNC: 8554 OMIM: 604679 KEGG: hsa:26986 STRING: 9606.ENSP00000313007 UniGene: PMID: 29362417 Epstein-Barr Virus protein EB2 first is recruited to the mRNA cap structure in the nucleus and then interacts with the proteins eIF4G and PABP to enhance the initiation step of translation. PMID: 29142127 These findings identify PABPC1 as a direct regulator of cardiac hypertrophy and define a new paradigm of gene regulation in the heart, where controlled changes in poly(A) tail length influence mRNA translation. PMID: 28653618 Data suggest that DEAD-box helicase 3 (DDX3X) physically interacts and co-localizes with poly(A)-binding cytoplasmic protein 1 (PABPC1) and caprin-1 in lamellipodia at the leading edge of spreading cells; these interactions are dependent on mRNA; depletion of DDX3X (via gene silencing with the CRISPR-Cas system) leads to decreased cell motility. These studies were conducted using MRC5 lung fibroblast cell line. PMID: 28733330 Data suggest that hnRNPLL specifically associates with cytoplasmic PABPC1 in both T-lymphocytes and plasma cells; PABPC1 promotes binding of hnRNPLL to immunoglobulin H (IgH, heavy chain) mRNA and regulates switching from mIgH (membrane isoform) to sIgH (secreted isoform) in plasma cells. (hnRNPLL = heterogeneous nuclear ribonucleoprotein L-like protein; PABPC1 = cytoplasmic poly[A]-binding protein 1) PMID: 28611064 PABP enhances the productive binding of the eRF1-eRF3 complex to the ribosome, via interactions with the N-terminal domain of eRF3a which itself has an active role in translation termination. PMID: 27418677 Unr stimulated the binding of PABP1 to mRNA, and that Unr was required for the stable interaction of PABP1 and eIF4G in cells. PMID: 26936655 PABPC1 decreased expression in in infertile men with non-obstructive azoospermia PMID: 26843391 BTG2 stimulates mRNA deadenylation via CAF1 activation through interaction with PABPC1. Interaction of BTG2 with the first RRM domain of PABPC1 is required for BTG2 to control cell proliferation. PMID: 26912148 PABPC1 is a novel co-regulator of the AR PMID: 26176602 PABPC1 is upregulated in gastric carcinoma tissues, and high PABPC1 expression predicts poor survival. PABPC1 regulates proliferation and transformation of gastric cancer cells in vitro and in vivo. PABPC1 knockdown induces apoptosis. PMID: 26097561 PABPC1 interacts with AGO2 and is responsible for the microRNA mediated gene silencing in high grade hepatocellular carcinoma. PMID: 26188282 Poly(A) binding protein 1 enhances cap-independent translation initiation of neurovirulence factor from avian herpesvirus PMID: 25503397 Metastatic duodenal cancer cells do not tolerate intracellular PABP1 accumulation and are thus exported into the extracellular milieu by the exosome-mediated pathway. In addition, PABP1 has a potential use as a biomarker for metastatic duodenal cancer. PMID: 25065644 This study highlights PABP-1 as a protein that is important to the pathology of ALS and indicates that the proteomic profile of TDP-43 inclusions in ALS may differ depending on the causative genetic mutation. PMID: 25111021 PABPC1 is mislocalized in spinal cord motor neurons in amyotrophic lateral sclerosis. PMID: 24336168 Study shows that PABP specifically regulates iNOS mRNA stability in human DLD-1 cells by binding to different sites in the 50- and 30-UTR of the iNOS mRNA. . PMID: 23711718 These results suggest that production of the NSs protein during rift valley fever virus infection leads to sequestration of PABP1 in the nuclear speckles, creating a state within the cell that favors viral protein production. PMID: 23966414 These data indicate that PABPC1 is an important cellular target of human herpesvirus 8 ORF57 to directly upregulate polyadenylated nuclear RNA accumulation during viral lytic infection. PMID: 23077296 Data show that eIF4G interacts with the RRM2 domain of polyadenylate-binding protein-1 (PABP). PMID: 23041282 data suggest that PABPC1 is essential for the formation of L1 RNA-protein complexes and may play a role in L1 RNP translocation in the host cell PMID: 22907758 EMCV 3C proteinase mediates site-specific PABP cleavage and demonstrate that PABP cleavage by 3C regulates EMCV replication PMID: 22837200 This finding demonstrates that viruses can increase host translation initiation factor concentration to foster their replication and defines a unique mechanism whereby control of PABP abundance regulates eIF4F assembly. PMID: 22431630 a role for PABPC1 and associated translation initiation factors in nonsense-mediated mRNA decay (NMD) evasion of AUG-proximal nonsense-mutated transcripts PMID: 21989405 study presents evidence that the function of KSHV polyadenylated nuclear (PAN) RNA is to bind poly(A) binding protein, which normally binds poly(A) tails of mRNAs in the cytoplasm but is re-localized into the nucleus during lytic KSHV infection PMID: 22022268 A direct link between PABP1 modification status and the formation of distinct mRNP (messenger ribonucleoprotein) complexes that regulate mRNA fate in the cytoplasm. PMID: 22004688 The present study has characterized DDX3 as a pivotal SG-nucleating factor and illustrates co-ordinative roles for DDX3, eIF4E and PABP1 in integrating environmental stress with translational regulation. PMID: 21883093 Nuclear relocalisation of cytoplasmic poly(A)-binding proteins PABP1 and PABP4 in response to UV irradiation reveals mRNA-dependent export PMID: 21940797 in the absence of PABP, the glycolytic enzyme GAPDH translocated to the cell nucleus and activated the GAPDH mediated apoptotic pathway by enhancing acetylation and serine 46 phosphorylation of p53. PMID: 21539808 these results suggest that depletion of PABP prevents protein synthesis and consequently leads to cell death through apoptosis. PMID: 21521633 LARP4 activity is integrated with other PAM2 protein activities by PABP as part of mRNA homeostasis. PMID: 21098120 Cytoplasmic PABP accumulation is translationally controlled in human cytomegalovirus-infected cells. PMID: 20980505 These findings reveal that despite species-specific differences in the relative strength of the PABPC1-binding sites, the interaction between GW182 proteins and PABPC1 is critical for miRNA-mediated silencing in animal cells. PMID: 21063388 Data show that in addition to PP2Ac, alpha4 interacts with EDD and PABP, suggesting its involvement in multiple steps in the mTOR pathway that leads to translation initiation and cell-cycle progression. PMID: 20544796 The cytoplasmic poly (A)-binding protein (PABP) plays a crucial role in regulating both translation and stability of eukaryotic mRNA. PMID: 20009508 PABP relocalization in infection was found to be independent of the viral protein ICP27. PMID: 20573819 Structural basis of binding of P-body-associated proteins GW182 and ataxin-2 by the Mlle domain of poly(A)-binding protein.( PMID: 20181956 HIV- 1 protease inhibits Cap- and poly(A)-dependent translation upon eIF4GI and PABP cleavage PMID: 19956697 The side chain of the invariant MLLE residue K580 of poly(A)-binding protein forms hydrogen bonds with the backbone of PAM2 residues 5 and 7. PMID: 20096703 The authors show that a conserved motif in the human GW182 paralog TNRC6C interacts with the C-terminal domain of polyadenylate binding protein 1 (PABC) and present the crystal structure of the complex. PMID: 20098421 Bunyamwera virus triggers nuclear retention of PABP in mammalian cells. PMID: 19193790 Poly(A)-binding protein modulates mRNA susceptibility to cap-dependent miRNA-mediated repression. PMID: 19934229 Methylated in vivo by CARM1. Methylated region is mapped. PMID: 11850402 PABP1 is a potential substrate in MAPKAP kinase 2-induced mRNA stabilization. PMID: 12565831 targeted degradation of PABP contributes to translation inhibition in apoptotic cells PMID: 14739600 PABP1 associates with paxillin in order to be efficiently transported from the nucleus to the cytoplasm; this event is necessary for cells to remodel their focal adhesions during cell migration. PMID: 15831480 a novel signaling pathway involving MKK-2 and ERK1/2 may down-regulate the activity of PABP and eIF4E by controlling their phosphorylation and compensates for the effect of excess cellular PABP PMID: 16332685 In esophageal cancer, reduced expression of PABPC1 was correlated with local tumor progression and poor prognosis after surgery. PMID: 16465428 PABP interacts with HHV-8 K10/10.1 protein in infected primary effusion lymphoma (PEL) cell lines. PMID: 16716377 poly(A)-binding protein 1 (PABP) as a novel BRCA1-interacting protein. PMID: 16782705

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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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