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SUMO1 Antibody

  • 货号：
    CSB-PA042567
  • 规格：
    ￥2024
  • 图片：
    • Western blot analysis of extracts from 293 cells, using Sumo1 antibody.
    • Immunohistochemistry analysis of paraffin-embedded human breast carcinoma tissue using Sumo1 antibody.
    • Immunofluorescence analysis of NIH/3T3 cells, using Sumo1 antibody.
  • 其他：

产品详情

  • 产品名称：
    Rabbit anti-Homo sapiens (Human) SUMO1 Polyclonal antibody
  • Uniprot No.：
    P63165
  • 基因名：
    SUMO1
  • 宿主：
    Rabbit
  • 反应种属：
    Human,Mouse,Rat
  • 免疫原：
    Synthesized peptide derived from N-terminal of Human SUMO-1.
  • 免疫原种属：
    Homo sapiens (Human)
  • 克隆类型：
    Polyclonal
  • 纯化方式：
    The antibody was affinity-purified from rabbit antiserum by affinity-chromatography using epitope-specific immunogen.
  • 浓度：
    It differs from different batches. Please contact us to confirm it.
  • 产品提供形式：
    Liquid
  • 应用范围：
    ELISA,WB,IHC,IF
  • 推荐稀释比：
    Application Recommended Dilution
    WB 1:500-1:3000
    IHC 1:50-1:100
    IF 1:100-1:500
  • Protocols：
  • 储存条件：
    Upon receipt, store at -20°C or -80°C. Avoid repeated freeze.
  • 货期：
    Basically, we can dispatch the products out in 1-3 working days after receiving your orders. Delivery time maybe differs from different purchasing way or location, please kindly consult your local distributors for specific delivery time.

产品评价

靶点详情

  • 功能：
    Ubiquitin-like protein that can be covalently attached to proteins as a monomer or a lysine-linked polymer. Covalent attachment via an isopeptide bond to its substrates requires prior activation by the E1 complex SAE1-SAE2 and linkage to the E2 enzyme UBE2I, and can be promoted by E3 ligases such as PIAS1-4, RANBP2 or CBX4. This post-translational modification on lysine residues of proteins plays a crucial role in a number of cellular processes such as nuclear transport, DNA replication and repair, mitosis and signal transduction. Involved for instance in targeting RANGAP1 to the nuclear pore complex protein RANBP2. Covalently attached to the voltage-gated potassium channel KCNB1; this modulates the gating characteristics of KCNB1. Polymeric SUMO1 chains are also susceptible to polyubiquitination which functions as a signal for proteasomal degradation of modified proteins. May also regulate a network of genes involved in palate development. Covalently attached to ZFHX3.
  • 基因功能参考文献：
    1. SUMO1 expression results in a gain of PKR activity by increasing its activation. SUMO1 was able to activate PKR and eIF-2alpha in the absence of viral infection. PMID: 29352251
    2. SPOP inhibits hepatocellular carcinoma (HCC) cell metastasis via ubiquitin-dependent SUMO1/SENP7 proteolysis and may thus serve as a new opinion for the prevention of HCC metastasis. PMID: 29777712
    3. Study found a significant difference in the expression of Cx43 and SUMO1 between cancer stem cells and non-cancer stem cells in liver cancer. By the co-expression of Cx43 and SUMO1 in cancer stem cells, the gap junction intercellular communication of liver cancer stem cells was obviously improved. PMID: 29393359
    4. Two SUMO modification sites existed in dopamine receptor D1, the phosphorylation of which, due to SUMO modification, can interact with PP2A, leading to the inhibition of D1 de-phosphorylation and normal function. PMID: 28770955
    5. These results suggest that SUMO1 contributes to hepatocellular carcinoma progression by promoting p65 nuclear translocation PMID: 26993772
    6. In summary, our study revealed a negative regulation of the UPR transducer ATF6 through post-translational SUMOylation. The information from this study will not only increase our understanding of the fine-tuning regulation of the UPR signaling but will also be informative to the modulation of the UPR for therapeutic benefits. PMID: 29061306
    7. Molecular dynamics simulations showed that binding of the beta-grasp domain of SUMO1 induces significant conformational and dynamic changes in SENP1, including widening of the exosite cleft and quenching of nanosecond dynamics in all but a distal region. PMID: 27576863
    8. Mutational analysis of functional sites showed that both peroxidase and PLA2 active sites were necessary for mutant Prdx6 function, and that Prdx6 phosphorylation (at T177 residue) was essential for optimum PLA2 activity.Mutant Prdx6 at its Sumo1 sites escapes and abates this adverse process by maintaining its integrity and gaining function PMID: 28055018
    9. SUMO and p21Cip1 regulate the transit of proteins through the nucleolus; disruption of nucleolar export by DNA damage induces SUMO and p21Cip1 to act as hub proteins to form a multiprotein complex in the nucleolus. PMID: 28582471
    10. This study reveals an essential role of SUMOylated FADD in Drp1- and caspase-10-dependent necrosis. PMID: 27799292
    11. SUMO-1 gene silencing inhibits proliferation and promotes apoptosis of human gastric cancer cells. PMID: 28222440
    12. the critical role of Cys52 in maintaining SUMO-1 conformation and function PMID: 27195426
    13. Findings suggest SUMO-1 protein and PGE2 receptor subtype 4 (EP4) as two potential targets for new therapeutic or prevention strategies for endometrial cancers. PMID: 27230680
    14. This study demonstrated that the rs12472035 polymorphism of SUMO1 was significantly associated with an increased risk of AD in male group. PMID: 27084229
    15. FOXP2 can be modified with all three human SUMO proteins and that PIAS1 promotes this process. PMID: 26867680
    16. Ang II-induced upregulation of ATF3 and SUMO1 in vitro and in vivo was blocked by Ang II type I receptor antagonist olmesartan. Moreover, Ang II induced ATF3 SUMOylation at lysine 42, which is SUMO1 dependent. PMID: 26850942
    17. Data show that mutation of key residues in the binding site abolishes binding and that small ubiquitin-like modifier 1 (SUMO1) can simultaneously and non-cooperatively bind both the ZZ domain and a canonical SIM motif of CREB-binding protein (CBP/p300). PMID: 27129204
    18. Roles for SUMO in pre-mRNA processing PMID: 26563097
    19. SUMOylation at specific sites on PXR protein are involved in enhancement of transcription function of this receptor. PMID: 26549688
    20. High DAP1 expression is associated with a 4-fold increase in the risk of lymph node metastases in squamous cell carcinoma of the oral cavity. PMID: 26400283
    21. Knockdown of SUMO1 using specific siRNA influenced the accumulation of lipid droplets and reduced HCV replication. PMID: 26449956
    22. The LKB1 K178R SUMO mutant had defective AMPK signaling and mitochondrial function, inducing death in energy-deprived cells. PMID: 26212320
    23. Data suggest that small ubiquitin-related modifier protein SUMO1 modification of the promyelocytic leukemia protein (PML) RING domain promotes SUMO2 conjugation to Lys160. PMID: 26060329
    24. Data identify PDGFRbeta as the hub gene in both inflammatory (IBC) and non-inflammatory breast neoplasm (non-IBC) and SUMO1 and COL1A1 the respective key genes for IBC and non-IBC suggesting they might play important role in the pathogenesis of the neoplasm. PMID: 26403314
    25. PML IV/ARF interaction enhances p53 SUMO-1 conjugation, activation, and senescence. PMID: 26578773
    26. Data indicate that small ubiquitin-like modifiers SUMO1, SUMO2, or SUMO3 were found in nuclear speckles. PMID: 26223657
    27. These results confirm that the SUMO machinery is involved in TRIM5alpha-mediated retroviral restriction, and demonstrate that TRIM5alpha is a SUMO 1 and SUMO 2 substrate. PMID: 25880753
    28. Under cell-free in vitro conditions, p35 is covalently modified by SUMO1. Sumoylation is a likely candidate mechanism for the rapid modulation of p35/Cdk5 activity in physiological situations as well as in disease. PMID: 25391294
    29. SUMO1 modification stabilizes CDK6 protein and drives the cell cycle and glioblastoma progression. PMID: 24953629
    30. SUMO1 accelerates the accumulation of autophagic vacuoles and promotes Abeta production. PMID: 25484073
    31. Expression of SUMO1/2/3 is dramatically enhanced by interferons through an miRNA-based mechanism involving the Lin28/let-7. PMID: 24942926
    32. SUMO-1 modification may affect the transcriptional activity of EGFR PMID: 26244656
    33. The crystal structures of SUMO1 bound to unphosphorylated and tetraphosphorylated PML-SUMO-interacting motifs peptides indicate that three phosphoserines directly contact specific positively charged residues of SUMO1. PMID: 25497731
    34. The expression of SUMO-1 in OLP was similar to normal mucosa and inflammatory fibrous hyperplasia, suggesting that alterations of this protein occur at later stages of carcinogenesis PMID: 23350884
    35. reveals an unexpected role of SUMO-1 and SAFB in the stimulatory coupling of promoter binding, transcription initiation and RNA processing PMID: 25800734
    36. MDM2 and SUMO-1 proteins are up-regulated in actinic cheilitis and lip cancer. PMID: 25241153
    37. Identify DRP1, RanGAP1 and topoisomerase IIa as targets of SUMO1 in human ejaculated sperm, giving more insights on the role of SUMO1-ylation in sperm morphology and motility. PMID: 25118297
    38. findings provide empirical evidence that SUMO1 genetic polymorphisms might be strongly involved in the etiology of NSCL/P, especially for rs12470401 T>C, rs16838917 A>G, rs12470529 A>G, and rs7572505 A>G polymorphisms. PMID: 25111678
    39. Overexpression of SUMO-1 decreased phosphorylated GSK-3beta at Ser-9. Mutagenesis of tau at K340R or inhibition of tau SUMOylation by ginkgolic acid abolishes the effect of SUMO-1. PMID: 25378699
    40. The mutation of the sumoylation site (Lys137) of PTBP2 markedly inhibited its modification by SUMO1. PMID: 24286314
    41. SUMO potentiates the inhibition of protein synthesis induced by PKR in response to dsRNA. PMID: 25074923
    42. These results show that DAP1 is a key regulator, of the induction of apoptosis and reduction of autophagy by subtilase cytotoxin (SubAB). PMID: 25183729
    43. identified 295 SUMO1 and 167 SUMO2 sites on endogenous substrates of HeLa cells PMID: 25114211
    44. Modification of TDG by small ubiquitin-like modifier (SUMO) proteins weakens its binding to abasic DNA. PMID: 24753249
    45. SUMO-1 modification of RARA is a potent mechanism for balancing proliferation and differentiation by controlling the stability of RARA in cancer cells. PMID: 24819975
    46. SUMO1P3 was significantly up-regulated in gastric cancer tissues. PMID: 23996296
    47. SUMO chain-induced dimerization activates RNF4. PMID: 24656128
    48. The mitosis-dependent dynamic SUMO-1 modification of NuMA might contribute to NuMA-mediated formation and maintenance of mitotic spindle poles during mitosis. PMID: 24309115
    49. PIASxalpha is a novel SUMO E3 ligase for PTEN, and it positively regulates PTEN protein level in tumor suppression. PMID: 24344134
    50. SUMO participates in transcriptional repression as both a covalent modification and through non-covalent interactions with E2 and E3 enzymes. PMID: 24174529

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  • 相关疾病：
    Non-syndromic orofacial cleft 10 (OFC10)
  • 亚细胞定位：
    Nucleus membrane. Nucleus speckle. Cytoplasm. Nucleus, PML body. Cell membrane. Nucleus.
  • 蛋白家族：
    Ubiquitin family, SUMO subfamily
  • 数据库链接：

    HGNC: 12502

    OMIM: 601912

    KEGG: hsa:7341

    STRING: 9606.ENSP00000376076

    UniGene: Hs.81424