UBC Recombinant Monoclonal Antibody

說明書

中文名稱：

UBC重組抗體
貨號：

CSB-RA316735MA1HU
規(guī)格：

￥1320
圖片：
Overlay Peak curve showing MCF7 cells stained with CSB-RA316735MA1HU (red line) at 1:50. The cells were fixed in 4% formaldehyde (15min) and permeated by 0.2% TritonX-100 for 10min. Then 10% normal goat serum to block non-specific protein-protein interactions followed by the antibody (1ug/1*10⁶cells) for 45min at 4℃. The secondary antibody used was FITC-conjugated Goat Anti-Mouse IgG(H+L) at 1/200 dilution for 35 min at 4°C. Isotype control antibody (green line) was mouse IgG1 (1μg/1*10⁶cells) used under the same conditions. Acquisition of >10, 022 events was performed.
其他：

產(chǎn)品詳情
產(chǎn)品評價(jià)
相關(guān)產(chǎn)品
靶點(diǎn)詳情

產(chǎn)品詳情

產(chǎn)品描述：

CSB-RA316735MA1HU UBC重組單克隆抗體是經(jīng)哺乳動(dòng)物細(xì)胞表達(dá)系統(tǒng)制備的高特異性抗體，靶向泛素C（Ubiquitin C）蛋白。UBC作為泛素-蛋白酶體系統(tǒng)的核心組分，通過介導(dǎo)蛋白質(zhì)泛素化修飾參與細(xì)胞周期調(diào)控、DNA損傷修復(fù)及異常蛋白降解等關(guān)鍵生物學(xué)過程，其表達(dá)異常與腫瘤發(fā)生、神經(jīng)退行性疾病密切相關(guān)。本產(chǎn)品經(jīng)ELISA和流式細(xì)胞術(shù)（FC）雙重驗(yàn)證，在推薦稀釋度（FC 1:20-1:500）范圍內(nèi)展現(xiàn)優(yōu)異的抗原結(jié)合能力與信號穩(wěn)定性，不同批次間具有高度一致性，確保實(shí)驗(yàn)可重復(fù)性。適用于泛素化通路機(jī)制研究、疾病模型中蛋白質(zhì)穩(wěn)態(tài)失衡分析，以及通過流式細(xì)胞技術(shù)定量檢測細(xì)胞內(nèi)UBC表達(dá)水平等科研場景，為探索蛋白質(zhì)翻譯后修飾調(diào)控網(wǎng)絡(luò)提供可靠工具。
Uniprot No.：

P0CG48
基因名：

UBC
別名：

UBC antibody; Polyubiquitin-C [Cleaved into: Ubiquitin] antibody
反應(yīng)種屬：

Human
免疫原：

Recombinant Human UBC protein
免疫原種屬：

Homo sapiens (Human)
標(biāo)記方式：

Non-conjugated
克隆類型：

Monoclonal
抗體亞型：

Mouse IgG
純化方式：

Affinity-chromatography
克隆號：

6G8
濃度：

It differs from different batches. Please contact us to confirm it.
保存緩沖液：

Preservative: 0.03% Proclin 300
Constituents: 50% Glycerol, 0.01M PBS, PH 7.4
產(chǎn)品提供形式：

Liquid
應(yīng)用范圍：

ELISA, FC

推薦稀釋比：

Application	Recommended Dilution
FC	1:20-1:500

Protocols：

ELISA Protocol
Flow cytometry (FC) Protocol
儲(chǔ)存條件：

Upon receipt, store at -20°C or -80°C. Avoid repeated freeze.
貨期：

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.
用途：

For Research Use Only. Not for use in diagnostic or therapeutic procedures.

產(chǎn)品評價(jià)

靶點(diǎn)詳情

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.
基因功能參考文獻(xiàn)：
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 authors 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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亞細(xì)胞定位：

[Ubiquitin]: Cytoplasm. Nucleus.
蛋白家族：

Ubiquitin family
數(shù)據(jù)庫鏈接：

HGNC: 12468

OMIM: 191340

KEGG: hsa:7316

STRING: 9606.ENSP00000344818

UniGene: Hs.520348

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