OGT Antibody, FITC conjugated

說明書

中文名稱：

OGT兔多克隆抗體, FITC偶聯
貨號：

CSB-PA016315LC01HU
規格：

￥880
其他：

產品詳情
產品評價
相關產品
靶點詳情

產品詳情

產品名稱：

Rabbit anti-Homo sapiens (Human) OGT Polyclonal antibody
Uniprot No.：

O15294
基因名：

OGT
別名：

FLJ23071 antibody; GlcNAc transferase antibody; HRNT1 antibody; MGC22921 antibody; O GlcNAc antibody; O GlcNAc transferase p110 subunit antibody; O GlcNAc transferase subunit p110 antibody; O linked N acetylglucosamine (GlcNAc) transferase (UDP N acetylglucosamine:polypeptide N acetylglucosaminyl transferase) antibody; O linked N acetylglucosamine (GlcNAc) transferase antibody; O linked N acetylglucosamine transferase 110 kDa subunit antibody; O-GlcNAc transferase subunit p110 antibody; O-linked N-acetylglucosamine transferase 110 kDa subunit antibody; ogt antibody; OGT1_HUMAN antibody; UDP N acetylglucosamine peptide N acetylglucosaminyltransferase 110 kDa subunit antibody; UDP N acetylglucosamine peptide N acetylglucosaminyltransferase GlcNAc transferase antibody; UDP-N-acetylglucosamine--peptide N-acetylglucosaminyltransferase 110 kDa subunit antibody; UDP-N-acetylglucosamine:polypeptide-N-acetylglucosaminyl transferase antibody; Uridinediphospho N acetylglucosamine:polypeptide beta N acetylglucosaminyl transferase antibody
宿主：

Rabbit
反應種屬：

Human
免疫原：

Recombinant Human UDP-N-acetylglucosamine--peptide N-acetylglucosaminyltransferase 110 kDa subunit protein (606-1022AA)
免疫原種屬：

Homo sapiens (Human)
標記方式：

FITC
克隆類型：

Polyclonal
抗體亞型：

IgG
純化方式：

>95%, Protein G purified
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
產品提供形式：

Liquid
儲存條件：

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.

產品評價

靶點詳情

功能：

Catalyzes the transfer of a single N-acetylglucosamine from UDP-GlcNAc to a serine or threonine residue in cytoplasmic and nuclear proteins resulting in their modification with a beta-linked N-acetylglucosamine (O-GlcNAc). Glycosylates a large and diverse number of proteins including histone H2B, AKT1, EZH2, PFKL, KMT2E/MLL5, MAPT/TAU and HCFC1. Can regulate their cellular processes via cross-talk between glycosylation and phosphorylation or by affecting proteolytic processing. Probably by glycosylating KMT2E/MLL5, stabilizes KMT2E/MLL5 by preventing its ubiquitination. Involved in insulin resistance in muscle and adipocyte cells via glycosylating insulin signaling components and inhibiting the 'Thr-308' phosphorylation of AKT1, enhancing IRS1 phosphorylation and attenuating insulin signaling. Involved in glycolysis regulation by mediating glycosylation of 6-phosphofructokinase PFKL, inhibiting its activity. Component of a THAP1/THAP3-HCFC1-OGT complex that is required for the regulation of the transcriptional activity of RRM1. Plays a key role in chromatin structure by mediating O-GlcNAcylation of 'Ser-112' of histone H2B: recruited to CpG-rich transcription start sites of active genes via its interaction with TET proteins (TET1, TET2 or TET3). As part of the NSL complex indirectly involved in acetylation of nucleosomal histone H4 on several lysine residues. O-GlcNAcylation of 'Ser-75' of EZH2 increases its stability, and facilitating the formation of H3K27me3 by the PRC2/EED-EZH2 complex. Regulates circadian oscillation of the clock genes and glucose homeostasis in the liver. Stabilizes clock proteins ARNTL/BMAL1 and CLOCK through O-glycosylation, which prevents their ubiquitination and subsequent degradation. Promotes the CLOCK-ARNTL/BMAL1-mediated transcription of genes in the negative loop of the circadian clock such as PER1/2 and CRY1/2. O-glycosylates HCFC1 and regulates its proteolytic processing and transcriptional activity. Regulates mitochondrial motility in neurons by mediating glycosylation of TRAK1. Glycosylates HOXA1. O-glycosylates FNIP1.; the mitochondrial isoform (mOGT) is cytotoxic and triggers apoptosis in several cell types including INS1, an insulinoma cell line.
基因功能參考文獻：
1. High OGT expression is associated with breast cancer. PMID: 30106436
2. O-GlcNAc transferase (OGT) is a partner of the MCM2-7 complex and O-GlcNAcylation might regulate MCM2-7 complex by regulating the chromatin loading of MCM6 and MCM7 and stabilizing MCM/MCM interactions. PMID: 30069701
3. LXRalpha interacts with OGT in its N-terminal domain and ligand-binding domain (LBD) in a ligand-independent fashion. PMID: 29577901
4. Findings demonstrate a novel role of Poleta O-GlcNAcylation by OGT in translesion DNA synthesis regulation and genome stability maintenance. PMID: 29208956
5. OGT, a unique glycosyltransferase enzyme, was identified to be upregulated in non-alcoholic fatty liver disease-associated hepatocellular carcinoma tissues by transcriptome sequencing. Here, we found that OGT plays a role in cancer by promoting tumor growth and metastasis in cell models. This effect is mediated by the induction of palmitic acid. PMID: 28347804
6. Nrf1 is regulated by O-GlcNAc transferase. PMID: 28625484
7. Findings indicate O-linked N-acetylglucosamine transferase (OGT) as a cellular factor involved in human papillomaviruses type 16/18 E6 and E7 expressions and cervical cancer tumorigenesis, suggesting that targeting OGT in cervical cancer may have potential therapeutic benefit. PMID: 27331873
8. The findings suggest that OGT promotes the O-GlcNAc modification of HDAC1 in the development of progression hepatocellular carcinoma. PMID: 27060025
9. Tax interacts with the host OGT/OGA complex and inhibits the activity of OGT-bound OGA. PMID: 28742148
10. We identified two human PRC2 complexes and two PR-DUB deubiquitination complexes, which contain the O-linked N-acetylglucosamine transferase OGT1 and several transcription factors. PMID: 27705803
11. Mutations in N-acetylglucosamine (O-GlcNAc) transferase in patients with X-linked intellectual disability PMID: 28584052
12. This work uncovers that URI-regulated OGT confers c-MYC-dependent survival functions in response to glucose fluctuations. PMID: 27505673
13. The results of this study showed that the OGT is essential for sensory neuron survival and target innervation. PMID: 28115479
14. The authors show that O-GlcNAcylation of KEAP1 by OGT at serine 104 is required for the efficient ubiquitination and degradation of NRF2. PMID: 28663241
15. Data suggest that O-GlcNAc transferase 1 (OGT1) specifically binds to, O-GlcNAcylates, and stabilizes nonspecific lethal protein3 (NSL3); stabilization of NSL3 by OGT1 up-regulates global acetylation levels of histone 4 at Lys-5, Lys-8, and Lys-16. PMID: 28450392
16. conclusion, our results demonstrated that miR24 inhibits breast cancer cells invasion by targeting OGT and reducing FOXA1 stability. These results also indicated that OGT might be a potential target for the diagnosis and therapy of breast cancer metastasis. PMID: 28455227
17. Fatty acid synthase fine-tunes the cell's response to stress and injury by remodeling cellular O-GlcNAcylation PMID: 28232487
18. OGT functions in metastatic spread of HPV E6/E7-positive HeLa cells to xenografted lungs through E6/E7, HCF-1 and CXCR4 PMID: 27845045
19. Reducing endogenous mitochondrial OGT expression leads to alterations in mitochondrial structure and function, including Drp1-dependent mitochondrial fragmentation, reduction in mitochondrial membrane potential, and a significant loss of mitochondrial content in the absence of mitochondrial reactive oxygen species. PMID: 28100784
20. Thus, a single amino acid substitution in the regulatory domain (the tetratricopeptide repeat domain) of OGT, which catalyzes the O-GlcNAc post-translational modification of nuclear and cytosolic proteins, appears causal for X-linked intellectual disability. PMID: 28302723
21. Beyond its well-known role in adding beta-O-GlcNAc to serine and threonine residues of nuclear and cytoplasmic proteins, OGT also acts as a protease in the maturation of the cell cycle regulator, HCF-1, and serves as an integral member of several protein complexes, many of them linked to gene expression. (Review) PMID: 27294441
22. the O-linked N-acetylglucosamine (O-GlcNAc) processing enzymes, O-GlcNAc-transferase (OGT) and O-GlcNAcase (OGA), interact with the (A)gamma-globin promoter at the -566 GATA repressor site PMID: 27231347
23. O-GlcNAcylation expression and its nuclear expression were associated with the carcinogenesis and progression of gastric carcinoma. PMID: 27131860
24. These results support a model in which OGT modifies HIRA to regulate HIRA-H3.3 complex formation and H3.3 nucleosome assembly and reveal the mechanism by which OGT functions in cellular senescence. PMID: 27217568
25. data indicate that O-GlcNAc-transferase activity is essential for RNA pol II promoter recruitment and that pol II goes through a cycling of O-GlcNAcylation at the promoter PMID: 27129214
26. OGT inhibited the formation of the Ecadherin/catenin complex through reducing the interaction between p120 and Ecadherin. PMID: 26707622
27. We concluded that OGT plays a key role in gastric cancer proliferation and survival, and could be a potential target for therapy. PMID: 26397041
28. Data suggest RNA polymerase II (POLR2A) is extensively modified on its unique C-terminal domain (CTD) by O-GlcNAc transferase (OGT); efficient O-GlcNAcylation requires a minimum of 20 heptad CTD repeats in POLR2A and more than half of NTD of OGT. PMID: 26807597
29. Together, these findings suggest that induction of SNO-OGT by Ab exposure is a pathogenic mechanism to cause cellular hypo-O-GlcNAcylation by which Ab neurotoxicity is executed PMID: 26854602
30. These results suggested roles of O-GlcNAcylation in modulating serine phosphorylation, as well as in regulating PKM2 activity and expression. PMID: 26252736
31. These results demonstrate that distinct OGT-binding sites in HCF-1 promote proteolysis, and provide novel insights into the mechanism of this unusual protease activity. PMID: 26305326
32. This work reveals that although the N-terminal TPR repeats of OGT may have roles in substrate recognition, the sequence restriction imposed by the peptide-binding site makes a substantial contribution to O-GlcNAc site specificity. PMID: 26237509
33. OGT expression is increased under hypoxic conditions. PMID: 26399441
34. E2F1 negatively regulates both Ogt and Mgea5 expression in an Rb1 protein-dependent manner. PMID: 26527687
35. a new function of histone O-GlcNAcylation in DNA damage response PMID: 26408091
36. Inhibition of O-Linked N-Acetylglucosamine Transferase Reduces Replication of Herpes Simplex Virus and Human Cytomegalovirus. PMID: 26041297
37. miR4235p was associated with congestive heart failure and the expression levels of proBNP; in addition, OGT was found to be a direct target of miR4235p. PMID: 25776937
38. Use of OGT(C917A) enhances O-GlcNDAz production, yielding improved cross-linking of O-GlcNDAz-modified molecules PMID: 26240142
39. Hexosamine biosynthetic pathway flux is increased in idiopathic pulmonary artery hypertension and drives OGT-facilitated pulmonary artery smooth muscle cell proliferation via specific proteolysis and direct activation of host cell factor-1. PMID: 25663381
40. Histone demethylase LSD2 acts as an E3 ubiquitin ligase and inhibits cancer cell growth through promoting proteasomal degradation of OGT. PMID: 25773598
41. Amino acid composition of splice variants, post-translational modifications, and stable associations with regulatory proteins influence subcellular distribution/substrate specificity of OGT and OGA (O-GlcNAcase beta-N-acetylglucosaminidase). [REVIEW] PMID: 25173736
42. Endogenous OTX2 from a medulloblastoma cell line is O-GlcNAcylated at several sites. PMID: 24580054
43. Phosphorylation of TET proteins is regulated via O-GlcNAcylation by the O-linked N-acetylglucosamine transferase (OGT). PMID: 25568311
44. O-linked beta-N-acetylglucosamine transferase mediates O-GlcNAcylation of the SNARE protein SNAP-29 and regulates autophagy in a nutrient-dependent manner. PMID: 25419848
45. Instead, an adipogenesis-dependent increase in O-linked beta-N-acetylglucosamine (O-GlcNAc) glycosylation of EWS was observed. PMID: 24928395
46. Estrogen replacement therapy and plyometric training influence muscle OGT and OGA gene expression, which may be one of the mechanisms by which HRT and PT prevent aging-related loss of muscle mass. PMID: 24365779
47. OGT catalyzes the O-GlcNAcylation of TET3, promotes TET3 nuclear export, and, consequently, inhibits the formation of 5-hydroxymethylcytosine catalyzed by TET3. PMID: 24394411
48. Data suggest that with multi-substrate enzymes, such as OGT, specific inhibition can rarely be achieved with ligands that compete solely with one of the substrates; OGT is inhibited by bisubstrate UDP-oligopeptide conjugates. PMID: 24256146
49. The backbone carbonyl oxygen of Leu653 and the hydroxyl group of Thr560 in OGT contribute to the recognition of sugar moieties via hydrogen bonds. PMID: 23700425
50. Expression of c-MYC and OGT was tightly correlated in human prostate cancer samples. PMID: 23720054
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相關疾病：

Mental retardation, X-linked 106 (MRX106)
亞細胞定位：

Nucleus. Cytoplasm.; [Isoform 2]: Mitochondrion. Membrane.; [Isoform 3]: Cytoplasm. Nucleus. Cell membrane. Mitochondrion membrane. Cell projection.; [Isoform 4]: Cytoplasm. Nucleus.
蛋白家族：

Glycosyltransferase 41 family, O-GlcNAc transferase subfamily
組織特異性：

Highly expressed in pancreas and to a lesser extent in skeletal muscle, heart, brain and placenta. Present in trace amounts in lung and liver.
數據庫鏈接：

HGNC: 8127

OMIM: 300255

KEGG: hsa:8473

STRING: 9606.ENSP00000362824

UniGene: Hs.405410

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