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Recombinant Human E3 SUMO-protein ligase PIAS1 (PIAS1)

  • 货号:
    CSB-YP017957HU
  • 规格:
  • 来源:
    Yeast
  • 其他:
  • 货号:
    CSB-EP017957HU
  • 规格:
  • 来源:
    E.coli
  • 其他:
  • 货号:
    CSB-EP017957HU-B
  • 规格:
  • 来源:
    E.coli
  • 共轭:
    Avi-tag Biotinylated

    E. coli biotin ligase (BirA) is highly specific in covalently attaching biotin to the 15 amino acid AviTag peptide. This recombinant protein was biotinylated in vivo by AviTag-BirA technology, which method is BriA catalyzes amide linkage between the biotin and the specific lysine of the AviTag.

  • 其他:
  • 货号:
    CSB-BP017957HU
  • 规格:
  • 来源:
    Baculovirus
  • 其他:
  • 货号:
    CSB-MP017957HU
  • 规格:
  • 来源:
    Mammalian cell
  • 其他:

产品详情

  • 纯度:
    >85% (SDS-PAGE)
  • 基因名:
  • Uniprot No.:
  • 别名:
    AR interacting protein; DDXBP1; DEAD/H (Asp-Glu-Ala-Asp/His) box binding protein 1; DEAD/H box binding protein 1 ; DEAD/H box-binding protein 1; E3 SUMO-protein ligase PIAS1; GBP; Gu binding protein; Gu-binding protein; GU/RH-II; Pias1; PIAS1_HUMAN; Protein inhibitor of activated STAT protein 1; Protein inhibitor of activated STAT; 1; RNA helicase II binding protein; RNA helicase II-binding protein; Zinc finger; MIZ-type containing 3; ZMIZ3
  • 种属:
    Homo sapiens (Human)
  • 蛋白长度:
    Full Length of Mature Protein
  • 表达区域:
    2-651
  • 氨基酸序列
    ADSAELKQM VMSLRVSELQ VLLGYAGRNK HGRKHELLTK ALHLLKAGCS PAVQMKIKEL YRRRFPQKIM TPADLSIPNV HSSPMPATLS PSTIPQLTYD GHPASSPLLP VSLLGPKHEL ELPHLTSALH PVHPDIKLQK LPFYDLLDEL IKPTSLASDN SQRFRETCFA FALTPQQVQQ ISSSMDISGT KCDFTVQVQL RFCLSETSCP QEDHFPPNLC VKVNTKPCSL PGYLPPTKNG VEPKRPSRPI NITSLVRLST TVPNTIVVSW TAEIGRNYSM AVYLVKQLSS TVLLQRLRAK GIRNPDHSRA LIKEKLTADP DSEIATTSLR VSLLCPLGKM RLTIPCRALT CSHLQCFDAT LYIQMNEKKP TWVCPVCDKK APYEHLIIDG LFMEILKYCT DCDEIQFKED GTWAPMRSKK EVQEVSASYN GVDGCLSSTL EHQVASHHQS SNKNKKVEVI DLTIDSSSDE EEEEPSAKRT CPSLSPTSPL NNKGILSLPH QASPVSRTPS LPAVDTSYIN TSLIQDYRHP FHMTPMPYDL QGLDFFPFLS GDNQHYNTSL LAAAAAAVSD DQDLLHSSRF FPYTSSQMFL DQLSAGGSTS LPTTNGSSSG SNSSLVSSNS LRESHSHTVT NRSSTDTASI FGIIPDIISL D
  • 蛋白标签:
    Tag type will be determined during the manufacturing process.
    The tag type will be determined during production process. If you have specified tag type, please tell us and we will develop the specified tag preferentially.
  • 产品提供形式:
    Lyophilized powder
    Note: We will preferentially ship the format that we have in stock, however, if you have any special requirement for the format, please remark your requirement when placing the order, we will prepare according to your demand.
  • 复溶:
    We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Please reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL.We recommend to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20℃/-80℃. Our default final concentration of glycerol is 50%. Customers could use it as reference.
  • 储存条件:
    Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. Avoid repeated freeze-thaw cycles.
  • 保质期:
    The shelf life is related to many factors, storage state, buffer ingredients, storage temperature and the stability of the protein itself.
    Generally, the shelf life of liquid form is 6 months at -20°C/-80°C. The shelf life of lyophilized form is 12 months at -20°C/-80°C.
  • 货期:
    Delivery time may differ from different purchasing way or location, please kindly consult your local distributors for specific delivery time.
    Note: All of our proteins are default shipped with normal blue ice packs, if you request to ship with dry ice, please communicate with us in advance and extra fees will be charged.
  • 注意事项:
    Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.
  • Datasheet :
    Please contact us to get it.

产品评价

靶点详情

  • 功能:
    Functions as an E3-type small ubiquitin-like modifier (SUMO) ligase, stabilizing the interaction between UBE2I and the substrate, and as a SUMO-tethering factor. Plays a crucial role as a transcriptional coregulation in various cellular pathways, including the STAT pathway, the p53 pathway and the steroid hormone signaling pathway. In vitro, binds A/T-rich DNA. The effects of this transcriptional coregulation, transactivation or silencing, may vary depending upon the biological context. Sumoylates PML (at'Lys-65' and 'Lys-160') and PML-RAR and promotes their ubiquitin-mediated degradation. PIAS1-mediated sumoylation of PML promotes its interaction with CSNK2A1/CK2 which in turn promotes PML phosphorylation and degradation. Enhances the sumoylation of MTA1 and may participate in its paralog-selective sumoylation. Plays a dynamic role in adipogenesis by promoting the SUMOylation and degradation of CEBPB.
  • 基因功能参考文献:
    1. Rad18, independently of its ubiquitin ligase activity, promotes DNA polymerase eta SUMOylation by facilitating its interaction with its SUMO ligase PIAS1 and is required for DNA polymerase eta function at difficult to replicate loci. PMID: 27811911
    2. PIAS1 as a key regulator of Epstein-Barr Virus lytic replication. PIAS1 acts as an inhibitor for transcription factors involved in lytic gene expression. PMID: 29262325
    3. these results indicate that PIAS1 is a positive regulator of MYC. PMID: 27239040
    4. PIAS1 is a prognostic biomarker in breast cancer PMID: 28493978
    5. PIAS1 is a determinant of poor survival and acts as a positive feedback regulator of AR signaling through enhanced AR stabilization in prostate cancer PMID: 26257066
    6. PIAS1 overexpression exacerbated mutant Huntingtin-associated phenotypes and aberrant protein accumulation PMID: 27146268
    7. HBs protein-induced hPIAS1 transcription requires TAL1, E47, MYOG, NFI, and MAPK signal pathways PMID: 27276529
    8. identified the SUMO ligase PIAS1 as a constituent PML-NB antiviral protein. This finding distinguishes a SUMO ligase that may mediate signaling events important in promyelocytic leukemia nuclear body mediated intrinsic immunity. PMID: 27099310
    9. PIAS1 enhances p300 recruitment to c-Myb-bound sites through interaction with both proteins. In addition, the E3 activity of PIAS1 enhances further its coactivation PMID: 27032383
    10. Results show that apocrine breast cancer and prostate cancer cells share a core AR cistrome and target gene signature linked to cancer cell growth, and PIAS1 plays a similar coregulatory role for AR in both cancer cell types. PMID: 26219822
    11. c-Myc is targeted to the proteasome for degradation in a SUMOylation-dependent manner, regulated by PIAS1, SENP7 and RNF4 PMID: 25895136
    12. Data demonstrate that PIAS1 interacts with TRF2 and mediates its sumoylation serving as a molecular switch that controls the level of TRF2 at telomeres. PMID: 26450775
    13. the expression of SENP8, SAE1, PIAS1, PIAS2 and ZMIZ1 is deregulated in the majority of PTC tissues, likely contributing to the PTC phenotype. PMID: 26403403
    14. Our data suggest that necdin suppresses PIAS1 both by inhibiting SUMO E3 ligase activity and by promoting ubiquitin-dependent degradation. PMID: 24911587
    15. the presented data indicate that PIAS1 is crucial for parental and docetaxel resistant prostate cancer cell survival PMID: 25474038
    16. Elevated PIAS1 expression was observed in breast tumor samples. PMID: 24586797
    17. PIAS1 is the E3 ligase responsible for SUMOylation of HMGN2. PMID: 24872413
    18. Further study indicated that PIAS1 interacted with IRF3 and inhibited the DNA binding activity of IRF3. PMID: 24036127
    19. Levels of STAT1 andor the protein expression of its negative regulators, PIAS1 and SOCS3, may be a good predictor of hepatitis C virus response to therapy PMID: 23472246
    20. Smad2 and PIAS1 proteins were significantly upregulated resulting in dramatically increased interactions between Smad2/4 and PIAS1 in the presence of zinc. PMID: 24052079
    21. Phosphorylation of serine residues adjacent to the PIAS1 SUMO-interacting motif favors formation of the non covalent PIAS1.SUMO.UBC9 ternary complex PMID: 24174529
    22. Data suggest that the pro-apoptotic protein Daxx specifically interacts with one or more substrates SUMOylated by PIAS1 and this interaction leads to apoptosis following UV irradiation. PMID: 22976298
    23. data suggest that PIAS1 may function as a tumor suppressor to regulate gastric cancer cell metastasis by targeting the MAPK signaling pathway PMID: 22972521
    24. MAPK-activated protein kinase-2 limits endothelial inflammation via the PIAS1 S522 phosphorylation-mediated increase in PIAS1 transrepression and SUMO ligase activity. PMID: 23202365
    25. PIAS1 is a SUMO ligase for GATA4 that differentially regulates GATA4 transcriptional activity independent of SUMO ligase activity and GATA4 sumoylation. PMID: 22539995
    26. The data reveal an important new role for PIAS1 in the regulation of cell proliferation in prostate cancer. PMID: 22449952
    27. PIAS1 negatively regulates ubiquitination of Msx1 homeoprotein independent of its SUMO ligase activity. PMID: 21717107
    28. There are differences in the PIAS3 expression from different stages of gastric precancerous conditions/lesions to GC, which may reveal a close relationship between expression reduction or loss of PIAS3 and gastric tumorigenesis. PMID: 21925039
    29. PIAS1 determines the level of JNK activity in human endometrial stromal cells , couples ROS signaling to the SUMO pathway, and promotes oxidative cell death. PMID: 21676946
    30. PIAS1 is a common partner for two cancer-related nuclear factors, c-Myb and FLASH. PMID: 21338522
    31. Data show that regulation of SATB1 sumoylation and caspase cleavage is controlled by SATB1 phosphorylation; specifically, PIAS1 interaction with SATB1 is inhibited by phosphorylation. PMID: 20351170
    32. protein inhibitor of activated Stat1 (PIAS1) interacts with the tetramerization and C-terminal regulatory domains of p53 in yeast two-hybrid analyses PMID: 11788578
    33. Protein inhibitors of activated STAT resemble scaffold attachment factors and function as interacting nuclear receptor coregulators. PMID: 11877418
    34. PIAS1 and PIASxalpha modulate the AR-dependent transactivation, which, at least in part, can be attributed to their SUMO-E3 activity toward AR. PMID: 12177000
    35. PIAS1 has a role in sumoylation of MDM2 in the cell nucleus PMID: 12393906
    36. found to strongly stimulate sumoylation of STAT1 at Lys703; results suggest a negative regulatory function for sumoylation. PMID: 12855578
    37. PIAS1 interacts with the N-terminal domain of human mineralocorticoid receptor and represses its ligand-dependent transcription. PMID: 14500761
    38. three-dimensional structure and its binding duality are discussed in conjunction with the biological functions of PIAS1 as a SUMO ligase PMID: 15133049
    39. PIAS1 is a checkpoint regulator which affects exit from G1 and G2 by sumoylation of p73. PMID: 15572666
    40. PIAS1 interacts with DNA cross-link repair SNM1A in nuclear focus formation. PMID: 15572677
    41. Results suggest that recombinant human interleukin-12 upregulates STAT-1 expression and that increased expression may be dose dependent. PMID: 15901746
    42. PIAS1 modulates transcriptional activation of smooth muscle cells marker genes through cooperative interactions with both serum response factor and class I basic helix-loop-helix proteins proteins. PMID: 16135793
    43. Pias1 binds to and sumoylates metabotropic glutamate receptor 8 PMID: 16144832
    44. In this study, we demonstrate that MEF2A undergoes sumoylation primarily at a single lysine residue (K395) both in vitro and in vivo. We also show that the nuclear E3 ligase, PIAS1, promotes sumoylation of MEF2A. PMID: 16563226
    45. PIAS1 is required for the appropriate localization and retention of Msx1 at the nuclear periphery in myoblast cells. PMID: 16600910
    46. TGF-beta rapidly suppresses IFN-gamma-driven STAT1 signaling by reducing DNA binding via promotion of STAT1--PIAS1 interactions and not inhibition of STAT1 activation. PMID: 17371985
    47. PIASy cooperates with PIAS1 to down-regulate the specificity and magnitude of NF-kappa B/STAT1-mediated gene activation. PMID: 17606919
    48. The data show that HCV NS3/4a is able to block the Jak-Stat signaling pathway at the stage of Stat-1 serine 727 phosphorylation. PMID: 18190974
    49. PIAS1 staining of the colon cancer tissue microarrays indicated a strong correlation of normal colon cells, and adenomas, with high expression of both PIAS1 and IRF-1 PMID: 19288270
    50. novel function of PIAS1 in the induction of JNK-dependent apoptosis, independent of the previously known inhibitory activity of PIAS1 in STAT-mediated gene activation. PMID: 11451946

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  • 亚细胞定位:
    Nucleus speckle. Nucleus, PML body. Note=Interaction with CSRP2 may induce a partial redistribution along the cytoskeleton.
  • 蛋白家族:
    PIAS family
  • 组织特异性:
    Expressed in numerous tissues with highest level in testis.
  • 数据库链接:

    HGNC: 2752

    OMIM: 603566

    KEGG: hsa:8554

    STRING: 9606.ENSP00000249636

    UniGene: Hs.162458