Recombinant Human PC4 Protein

Beta LifeScience SKU/CAT #: BLA-6706P

Recombinant Human PC4 Protein

Beta LifeScience SKU/CAT #: BLA-6706P
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Product Overview

Host Species Human
Accession P53999
Synonym Activated RNA polymerase II transcriptional coactivator p15 Interferon related developmental regulator 1 MGC102747 p14 P15 PC4 PC4 LSB Positive cofactor 4 RPO2TC1 Sub1 SUB1 homolog TCP4_HUMAN
Description Recombinant Human PC4 Protein was expressed in E.coli. It is a Full length protein
Source E.coli
Molecular Weight 17 kDa including tags
Purity >90% purity as determined by SDS-PAGE
Endotoxin < 1.0 EU per μg of the protein as determined by the LAL method
Formulation Liquid Solution
Stability The recombinant protein samples are stable for up to 12 months at -80°C
Reconstitution See related COA
Unit Definition For Research Use Only
Storage Buffer Shipped at 4°C. Upon delivery aliquot and store at -20°C or -80°C. Avoid repeated freeze / thaw cycle.

Target Details

Target Function General coactivator that functions cooperatively with TAFs and mediates functional interactions between upstream activators and the general transcriptional machinery. May be involved in stabilizing the multiprotein transcription complex. Binds single-stranded DNA. Also binds, in vitro, non-specifically to double-stranded DNA (ds DNA).
Subcellular Location Nucleus.
Protein Families Transcriptional coactivator PC4 family
Database References

Gene Functions References

  1. Study shows that PC4 might repress RNA pol II recruitment and transcription of replication-dependent histone genes in order to maintain the balance between histone gene expression and DNA synthesis. Moreover, PC4 might promote the interaction of cleavage and polyadenylation complex with histone pre-mRNAs, that might impede with the recruitment of histone cleavage complex. PMID: 30053800
  2. REVIEW: many evidences showed that Sub1 influences processes downstream during mRNA biogenesis, such as elongation, termination, and RNAPII phosphorylation. The recent discovery that Sub1 directly interacts with the RNAPII stalk adds new insights into how it achieves all these tasks. PMID: 28853990
  3. Evolutionarily conserved role for Sub1 and PC4 in the maintenance of yeast and human genome stability has been summarized. (Review) PMID: 28567479
  4. Yeast Sub1 and human PC4 are G-quadruplex binding proteins that suppress genome instability at co-transcriptionally formed G4 DNA. PMID: 28369605
  5. Results show elevated expression of SUB1 in aggressive prostate cancer. Knockdown of SUB1 in prostate cancer cells resulted in reduced cell proliferation, invasion and migration. PMID: 27270442
  6. these data provide a novel mode of PC4 binding to a DNA secondary structure that remains within the framework of the model for binding to ssDNA. Additionally, consideration of the PC4-G4DNA interaction could provide insight into the biological functions of PC4, which remain incompletely understood. PMID: 28416612
  7. PC4 associates with Aurora A and Aurora B and undergoes phosphorylation, following which PC4 activates both Aurora A and B to sustain optimal kinase activity to maintain the phosphorylation gradient for the proper functioning of the mitotic machinery. PMID: 26777301
  8. PC4 has similar functions to RPA in binding ssDNA to promote genome stability, especially at sites of replication-transcription collisions. PMID: 25961912
  9. SMYD3 interacts with the human positive coactivator 4 (PC4) and that such interaction potentiates a group of genes whose expression is linked to cell proliferation and invasion. PMID: 26350217
  10. Sub1, and its human homolog PC4, bind preferentially to G-quadruplexes PMID: 25813861
  11. expression of PC4 in astrocytoma was upregulated as assessed by western blot and immunohistochemical staining. Moreover, elevated PC4 expression was strongly correlated with the progression of astrocytoma and overall survival. PMID: 25262015
  12. PC4 protects esophageal squamous cell carcinoma cells from IR-induced death by enhancing the nonhomologous end joining-promoting activity of XLF. PMID: 25321468
  13. p38 MAP kinase mediated HNF4 Ser158 phosphorylation (P-HNF4-S158), binding of PC4 to P-HNF4-S158 and characterize the functional domain of PC4 required for P-HNF4-S158 binding. PMID: 17317687
  14. PC4 activates double-strand break (DSB) repair activity through stimulation of DSB rejoining in vivo PMID: 19038270
  15. acetylation of lysine 382/381 of p53 may play an important role in modulating p53-PC4 interaction and as a consequence PC4 mediated activation of p53 target genes. PMID: 21586571
  16. findings demonstrated a critical aspect of LHR modulation whereby PC4 acts as a coactivator of Sp1 to contribute to the human of LHR transcription PMID: 21193408
  17. Sub1/PC4 a chromatin associated protein with multiple functions in transcription. PMID: 20305379
  18. analysis of the interaction between the transactivation domain of p53 and PC4 PMID: 19525231
  19. PC4 interacts with the DNA binding and C-terminal domains of p53 through its DNA binding domain, which is essential for the stimulation of p53 DNA binding. PMID: 17785449
  20. PC4 interacts with heterochromatin protein 1alpha, REST/NRSF (RE1-silencing transcription factor/neuron-restrictive silencer factor) and CoREST to establish the repressed state of neural genes in nonneuronal cells. PMID: 20080105
  21. General transcription factor IIH protects promoters from PC4-mediated repression by relieving the topological constraint imposed by PC4 through the ERCC3 helicase activity rather than by reducing the repressive activity of PC4 via its phosphorylation. PMID: 12590132
  22. These results establish the first physiological role of PC4 as a transcriptional coactivator. PMID: 14966284
  23. structure explains high-affinity binding of PC4 to the complementary strands of unwinding duplex DNA. PMID: 16415882
  24. These results establish PC4 as a new member of chromatin-associated protein family, which plays an important role in chromatin organization. PMID: 16982701
  25. Report recruitment of RNA polymerase II cofactor PC4 to DNA damage sites. PMID: 19047459


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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.

To learn more about how to properly dissolve the lyophilized recombinant protein, please visit Lyophilization FAQs.

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