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UBC Antibody

  • 货号：
    CSB-PA03742A0Rb
  • 规格：
    ￥440
  • 促销：
    小规格抗体限时一口价
  • 图片：
    • Western Blot
      Positive WB detected in: HepG2 whole cell lysate, 293T whole cell lysate, Hela whole cell lysate, MCF-7 whole cell lysate, K562 whole cell lysate, LO2 whole cell lysate, Jurkat whole cell lysate
      All lanes: UBC antibody at 1:2000
      Secondary
      Goat polyclonal to rabbit IgG at 1/50000 dilution
      Predicted band size: 78 kDa
      Observed band size: 78 kDa
  • 其他：

产品详情

  • 产品名称：
    Rabbit anti-Homo sapiens (Human) UBC Polyclonal antibody
  • Uniprot No.：
    P0CG48
  • 基因名：
  • 别名：
    UBC antibody; Polyubiquitin-C [Cleaved into: Ubiquitin] antibody
  • 宿主：
    Rabbit
  • 反应种属：
    Human
  • 免疫原：
    Peptide sequence from Human Polyubiquitin-C protein (19-36AA)
  • 免疫原种属：
    Homo sapiens (Human)
  • 标记方式：
    Non-conjugated

    本页面中的产品，UBC Antibody (CSB-PA03742A0Rb)，的标记方式是Non-conjugated。对于UBC Antibody，我们还提供其他标记。见下表：

    可提供标记
    标记方式 货号 产品名称 应用
    HRP CSB-PA03742B0Rb UBC Antibody, HRP conjugated ELISA
    FITC CSB-PA03742C0Rb UBC Antibody, FITC conjugated
    Biotin CSB-PA03742D0Rb UBC Antibody, Biotin conjugated ELISA
  • 克隆类型：
    Polyclonal
  • 抗体亚型：
    IgG
  • 纯化方式：
    Antigen Affinity Purified
  • 浓度：
    It differs from different batches. Please contact us to confirm it.
  • 保存缓冲液：
    Preservative: 0.03% Proclin 300
    Constituents: 50% Glycerol, 0.01M PBS, pH 7.4
  • 产品提供形式：
    Liquid
  • 应用范围：
    ELISA, WB
  • 推荐稀释比：
    Application Recommended Dilution
    WB 1:1000-1:5000
  • 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：
    Exists either covalently attached to another protein, or free (unanchored). When covalently bound, it is conjugated to target proteins via an isopeptide bond either as a monomer (monoubiquitin), a polymer linked via different Lys residues of the ubiquitin (polyubiquitin chains) or a linear polymer linked via the initiator Met of the ubiquitin (linear polyubiquitin chains). Polyubiquitin chains, when attached to a target protein, have different functions depending on the Lys residue of the ubiquitin that is linked: Lys-6-linked may be involved in DNA repair; Lys-11-linked is involved in ERAD (endoplasmic reticulum-associated degradation) and in cell-cycle regulation; Lys-29-linked is involved in lysosomal degradation; Lys-33-linked is involved in kinase modification; Lys-48-linked is involved in protein degradation via the proteasome; Lys-63-linked is involved in endocytosis, DNA-damage responses as well as in signaling processes leading to activation of the transcription factor NF-kappa-B. Linear polymer chains formed via attachment by the initiator Met lead to cell signaling. Ubiquitin is usually conjugated to Lys residues of target proteins, however, in rare cases, conjugation to Cys or Ser residues has been observed. When polyubiquitin is free (unanchored-polyubiquitin), it also has distinct roles, such as in activation of protein kinases, and in signaling.
  • 基因功能参考文献：
    1. Regulation of transcriptional activators by DNA-binding domain (DBD) ubiquitination has shown that, when attached to the DBD of either p53 or IRF-1, ubiquitin is orientated towards, and makes contact with, the DNA. PMID: 28362432
    2. Data show that ubiquitin variants (Ubvs) that bind to USP2 or USP21 contain a similar core functional epitope, or "hot spot," consisting mainly of positions that are conserved as the wild type sequence, but also some positions that prefer mutant sequences. PMID: 27436899
    3. Data show that the packing of ubiquitin can significantly alter the thermodynamics and kinetics of local conformational exchange. PMID: 28747759
    4. Model of ASB9 in complex with its substrate, creatine kinase, reveals a mechanism for dynamic ubiquitin transfer. PMID: 27396830
    5. The lysine48-lysine63 branched ubiquitin chain regulates NF-kappaB signaling. PMID: 27746020
    6. Noncovalent ubiquitin interactions regulate the catalytic activity of ubiquitin writers. (Review) PMID: 27614784
    7. The s now report the crystal structure of a human Parkin-phosphoubiquitin complex, which shows that phosphoubiquitin binding induces movement in the 'in-between RING' (IBR) domain to reveal a cryptic ubiquitin-binding site. PMID: 28414322
    8. Studies indicate a role for the ubiquitin-proteasome system (UPS) as a key regulator of ciliogenesis. PMID: 27911708
    9. Chicago Sky Blue 6B (CSB6B) binds directly to the beta-groove of ubiquitin and could inhibit the binding of ubiquitin to chemokine (C-X-C motif) receptor 4 (CXCR4), a cell surface ubiquitin receptor. PMID: 27613091
    10. Studies suggest that ubiquitin signals for the proteasome involved more that Lys48 (K48). PMID: 28069863
    11. Data show that the stereospecific complex of ubiquitin and the ubiquitin-associated domain (UBA) is minimally perturbed by the crowding agent Ficoll. PMID: 28267209
    12. Studies indicate complex ubiquitin architectures function as important signals including post-translational modification (PTM) of ubiquitin itself, such as acetylated ubiquitin and phospho-ubiquitin.. PMID: 28011818
    13. Upon stabilization of the protein's core, the long loop converges on the core in the final step of the folding process. PMID: 27111887
    14. Our study predicted that UBC and RPA had potential as target genes for the diagnosis and treatment of osteosarcoma PMID: 26782416
    15. Data show that at least three heat shock elements with different configurations, exist in the UBC promoter. All of them are bound by transcription factors belonging to the heat shock factor family clarifying the mechanisms regulating UBC expression. PMID: 26317694
    16. Data show that discoidin domain receptor 2 (DDR2) is linked to a polyubiquitin (Ub) chain predominantly through lysine K27 conjugation and slightly through K33. PMID: 26271983
    17. USP4 requires its N-terminal DUSP-Ubl domain to achieve full catalytic turnover by promoting ubiquitin exchange. PMID: 25404403
    18. Data suggest that ubiquitin-conjugating enzyme E2 variant 2 (Ube2V2) and ring finger protein 4 (RNF4) together induce an active conformation of the ubiquitin-conjugating enzyme Ubc13-ubiquitin (Ubc13~Ub) thioester. PMID: 26148049
    19. noncovalent ubiquitin:ubiquitin interactions are nearly identical to those reported for Lys11-linked ubiquitin and seem to play a significant role in stabilizing the crystal structure without the isopeptide bond. PMID: 26171660
    20. Studies indicate that ubiquitin proteasome system (UPS) controls all aspects of cholesterol metabolism including its synthesis, uptake, and efflux. PMID: 25220377
    21. Studies suggest that quantitative proteomic approaches would set a standard for elucidating biochemical mechanisms of Ubiquitin (UB)-driven signaling systems. PMID: 26000850
    22. In testicular germ cell tumors, the ubiquitin expression is decreased indicating disturbances of ubiquitin-proteolysis system components at the initial stages of testicular tissue carcinogenesis. PMID: 26118027
    23. Data indicate that TRAF interacting protein TRIP negatively regulates the TNFR-associated factor 2 (TRAF2) ubiquitin-dependent pathway by modulating the TRAF2-sphingosine 1-phosphate (S1P) interaction. PMID: 25716317
    24. Data indicate that heat shock protein 90kDa (Hsp90) inhibition suppresses 26S proteasome remodeling, unanchored ubiquitin chain production, and aggresome clearance. PMID: 25713068
    25. Static HMG-20 structure is derived from high precision residual dipolar couplings measured in a drug-based liquid crystalline phase using NMR spectroscopy. PMID: 24568736
    26. This study identifies altered proteolysis as a feature of persistent podocyte injury. In the future, specific UPS proteins may serve as new biomarkers or therapeutic targets in persistent nephrotic syndrome. PMID: 24722446
    27. Data indicate that conditional replacement of endogenous ubiquitin (Ub) by Ub(R54A/Y59A) or Ub(K48R) yielded profound apoptosis at a similar extent. PMID: 24912152
    28. Data indicate that a single point deletion (DeltaE81) in RAP80 abrogates multivalent interactions with polyubiquitin. PMID: 24627472
    29. UbcH5c~Ubiqitin binding stabilizes an active conformation of the Shigella flexneri OspG kinase, greatly enhancing its activity. PMID: 24446487
    30. These results reveal an unanticipated mode of Ube2g2 self-association that allows Ube2g2 to effectively engage two ubiquitins to specifically synthesize Lys48-linked ubiquitin chains. PMID: 24366945
    31. Yin Yang 1 intronic binding sequences and splicing elicit intron-mediated enhancement of ubiquitin C gene expression. PMID: 23776572
    32. This article reviews the recent advances in proteomics of HMG20 and reveals novel networks and associations with human disease.[review] PMID: 23339974
    33. The donor ubiquitin, transferred from the E2, is bound to the Nedd4 C lobe with its C-terminal tail locked in an extended conformation, primed for catalysis. PMID: 23644597
    34. Ubiquitin's regulatory mechanisms of expression in heart failure patients' cardiomyocytes. (review) PMID: 23180530
    35. The GP78 CUE domain functions to both facilitate substrate binding and enable switching between adjacent ubiquitin molecules of a growing chain to enable processivity in ubiquitination. PMID: 23123110
    36. Data suggest that ubiquitin (Ub) binding provides a negative feedback loop upon NOD1 and NOD2 (nucleotide-binding oligomerization domain-containing proteins)-dependent activation of receptor-interacting protein kinase 2 (RIP2). PMID: 23300079
    37. Data indicate that pressure induced ubiquitin unfolding in methanol. PMID: 23284170
    38. Regulation of ubiquitin transfer by XIAP, a dimeric RING E3 ligase. PMID: 23259674
    39. The human ubiquitin C promoter transgene might be useful to selectively target projections of brain neurons. PMID: 21802467
    40. analysis of cold-induced changes in the protein ubiquitin PMID: 22737208
    41. Ubiquitin targeting of tau protein occurs at neurofibrillary tangles in the early and intermediate maturation stages. PMID: 21919991
    42. Data indicate that modification of NEMO with linear di-ubiquitin is sufficient for full NF-kappaB activation. PMID: 22605335
    43. the ubiquitin independent degradation pathway utilized by a hepatitis B virus envelope protein limits antigen presentation PMID: 21969857
    44. Studies indicate that signaling controlled by ubiquitin or ubiquitin-like proteins has recently emerged as key regulator of the cellular DNA damage response, and viruses can reveal key convergence points in this important cellular pathway. PMID: 21549706
    45. Studies indicate that Ku80 is removed from DNA through a ubiquitin-mediated process. PMID: 21640108
    46. Studies indicate that Non-proteolytic ubiquitylation of chromatin surrounding DSBs, mediated by the RNF8/RNF168 ubiquitin ligase cascade, has emerged as a key mechanism for restoration of genome integrity. PMID: 21664912
    47. Studies suggest that DNA damage-induced ubiquitination or sumoylation of PCNA prevents CRL4Cdt2-dependent degradation by inhibiting binding of Cdt1 to PCNA. PMID: 21846465
    48. Studies indicate that monoubiquitylation of PCNA allows mutagenic translesion synthesis by damage-tolerant DNA polymerases, polyubiquitylation is required mainly for an error-free pathway that likely involves template switching. PMID: 21605556
    49. Studies indicate that All the Y-family polymerases have ubiquitin binding domains that bind to mono-ubiquitinated PCNA to effect the switching from replicative to Y-family polymerase. PMID: 21704031
    50. Studies indicate that the involvement of the degradation-linked K48-ubiquitin signal and the proteasome at the sites of DSBs. PMID: 21536036

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  • 亚细胞定位：
    [Ubiquitin]: Cytoplasm. Nucleus.
  • 蛋白家族：
    Ubiquitin family
  • 数据库链接：

    HGNC: 12468

    OMIM: 191340

    KEGG: hsa:7316

    STRING: 9606.ENSP00000344818

    UniGene: Hs.520348