Recombinant Human Protein O-GlcNAcase (MGEA5), partial

Code CSB-YP013786HU
MSDS
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Source Yeast
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Code CSB-EP013786HU
MSDS
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Source E.coli
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Code CSB-EP013786HU-B
MSDS
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Source E.coli
Conjugate 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.
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Code CSB-BP013786HU
MSDS
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Source Baculovirus
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Code CSB-MP013786HU
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Source Mammalian cell
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Product Details

Purity
>85% (SDS-PAGE)
Target Names
MGEA5
Uniprot No.
Alternative Names
Beta-hexosaminidase; Beta-N-acetylglucosaminidase; Beta-N-acetylhexosaminidase; Bifunctional protein NCOAT; HEXC; Hyaluronidase in meningioma; KIAA0679; MEA5; Meningioma expressed antigen 5; Meningioma-expressed antigen 5; MGEA 5; Mgea5; N-acetyl-beta-D-glucosaminidase; N-acetyl-beta-glucosaminidase; NCOAT; Nuclear cytoplasmic O GlcNAcase and acetyltransferase; Nuclear cytoplasmic O-GlcNAcase and acetyltransferase; OGA; OGA_HUMAN; Protein O-GlcNAcase
Species
Homo sapiens (Human)
Protein Length
Partial
Tag Info
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.
Form
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.
Buffer before Lyophilization
Tris/PBS-based buffer, 6% Trehalose, pH 8.0
Reconstitution
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.
Troubleshooting and FAQs
Storage Condition
Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. Avoid repeated freeze-thaw cycles.
Shelf Life
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.
Lead Time
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.
Notes
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.

Customer Reviews and Q&A

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Target Background

Function
Cleaves GlcNAc but not GalNAc from O-glycosylated proteins. Can use p-nitrophenyl-beta-GlcNAc and 4-methylumbelliferone-GlcNAc as substrates but not p-nitrophenyl-beta-GalNAc or p-nitrophenyl-alpha-GlcNAc (in vitro). Does not bind acetyl-CoA and does not have histone acetyltransferase activity.; Cleaves GlcNAc but not GalNAc from O-glycosylated proteins. Can use p-nitrophenyl-beta-GlcNAc as substrate but not p-nitrophenyl-beta-GalNAc or p-nitrophenyl-alpha-GlcNAc (in vitro), but has about six times lower specific activity than isoform 1.
Gene References into Functions
  1. Beta-N-acetylhexosaminidase substrate recognition and specificity PMID: 28939839
  2. Tax interacts with the host OGT/OGA complex and inhibits the activity of OGT-bound OGA. PMID: 28742148
  3. TGFBR3 and/or MGEA5 rearrangements are much more common in hybrid hemosiderotic fibrolipomatous tumor-myxoinflammatory fibroblastic sarcomas than in classical myxoinflammatory fibroblastic sarcomas. PMID: 26980036
  4. Data suggest that the substrate specificity of O-GlcNAcase/OGA does not extend to proteins/peptides modified with S-GlcNAc (an analog of O-GlcNAc); proteins modified with S-GlcNAc appear to be stable against O-GlcNAcase/OGA hydrolysis. PMID: 28627871
  5. hOGA forms an unusual arm-in-arm homodimer in which the catalytic domain of one monomer is covered by the stalk domain of the sister monomer to create a substrate-binding cleft. PMID: 28319083
  6. 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
  7. E2F1 negatively regulates both Ogt and Mgea5 expression in an Rb1 protein-dependent manner. PMID: 26527687
  8. OGA overexpression in endothelial cells improves endothelial function and may have a beneficial effect on coronary vascular complications in diabetes. PMID: 26269457
  9. Amino acid composition of splice variants, post-translational modifications, and stable associations with regulatory proteins influence subcellular distribution/substrate specificity of OGA and OGT (O-linked N-acetylglucosamine transferase). [REVIEW] PMID: 25173736
  10. This work identifies the first target of miR-539 in the heart and the first miRNA that regulates OGA. PMID: 25183011
  11. Report the presence of TGFBR3 and/or MGEA5 rearrangements in pleomorphic hyalinizing angiectatic tumors and the spectrum of related neoplasms. PMID: 24705316
  12. 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
  13. O-linked beta-N-acetylglucosaminylation (O-GlcNAcylation) in primary and metastatic colorectal cancer clones and effect of N-acetyl-beta-D-glucosaminidase silencing on cell phenotype and transcriptome. PMID: 22730328
  14. Data show that the interplay between O-GlcNAc and phosphorylation on proteins and indicate that these effects can be mediated by changes in hOGT and hOGA kinetic activity. PMID: 22311971
  15. Analysis of urinary content of MGEA5 and OGT may be useful for bladder cancer diagnostics. PMID: 22783592
  16. Decrease in MGEA5 and increase in O-GlcNAc transferease expression in higher grade tumors suggests that increased O-GlcNAc modification may be implicated in breast tumor progression and metastasis. PMID: 21567137
  17. Chromosomal translocation t(1;10) is consistent with rearrangements of TGFBR3 and MGEA5 in both myxoinflammatory fibroblastic sarcoma and hemosiderotic fibrolipomatous tumor. PMID: 21717526
  18. Reducing ChREBP(OG) levels via OGA overexpression decreased lipogenic protein content (ACC, FAS), prevented hepatic steatosis, and improved the lipidic profile of OGA-treated db/db mice. PMID: 21471514
  19. Direct evidence links muscle atrophy and the disruption of O-GlcNAcase activity in male bitransgenic mice. PMID: 21178104
  20. Results provide evidence that OGA may possess a substrate-recognition mechanism tinvolving interactions with O-GlcNAcylated proteins beyond the GlcNAc-binding site. PMID: 20863279
  21. N-terminal region of OGA contains the catalytic site and the C-terminal region stabilizes the protein structure and affects substrate affinity. PMID: 20673219
  22. This study analyzes the activity of the enzyme involved in the removal of these sugar residues, i.e. beta-N-acetylglucosaminidase (O-GlcNAcase) as well as the level of N-acetylglucosamine in benign and malignant thyroid lesions. PMID: 20198314
  23. Investigated this locus in Pima Indians who have the world's highest prevalence of NIDDM. Concluded that mutations in MGEA5 are unlikely to contribute to NIDDM in this population PMID: 12359146
  24. In type 2 Diabetes patients in Mexico City, the frequency of the T allele of MGEAT5 was higher (2.6%) in the cases than in controls (1.8%), but not a significant deviation from Hardy_Weinberg proportions. PMID: 17546623
  25. review of modifications, phosphorylation and a specific form of glycosylation, O-linked -N-acetylglucosaminylation by O-GlcNAc, relevant to pathological tau phosphorylation PMID: 18641620
  26. the short nuclear variant of O-GlcNAcase, which has the identical catalytic domain as the full-length enzyme, has similar trends in a pH-rate profile and Taft linear free energy analysis as the full-length enzyme PMID: 19423084
  27. characterization of O-GlcNAcase transition states using several series of substrates to generate multiple simultaneous free-energy relationships PMID: 19715310
  28. This protein is a cytosolic, neutral, O-GlcNAc specific hexosaminidase termed O-GlcNAcase. PMID: 11148210

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Subcellular Location
[Isoform 3]: Nucleus.; [Isoform 1]: Cytoplasm.
Protein Families
Glycosyl hydrolase 84 family
Tissue Specificity
Ubiquitous. Shows highest expression in the brain, placenta and pancreas.
Database Links

HGNC: 7056

OMIM: 604039

KEGG: hsa:10724

STRING: 9606.ENSP00000354850

UniGene: Hs.500842

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