MGEA5 Recombinant Monoclonal Antibody

Code CSB-RA833565A0HU
Size US$210
Order now
Image
  • Western Blot
    Positive WB detected in: Hela whole cell lysate, L02 whole cell lysate, HepG2 whole cell lysate
    All lanes: MGEA5 antibody at 1:1000
    Secondary
    Goat polyclonal to rabbit IgG at 1/50000 dilution
    Predicted band size: 103, 96, 77, 97 kDa
    Observed band size: 130 kDa
Have Questions? Leave a Message or Start an on-line Chat

Product Details

Uniprot No.
Target Names
MGEA5
Alternative Names
Protein O-GlcNAcase (OGA) (EC 3.2.1.169) (Beta-N-acetylglucosaminidase) (Beta-N-acetylhexosaminidase) (Beta-hexosaminidase) (Meningioma-expressed antigen 5) (N-acetyl-beta-D-glucosaminidase) (N-acetyl-beta-glucosaminidase) (Nuclear cytoplasmic O-GlcNAcase and acetyltransferase) (NCOAT), MGEA5, HEXC KIAA0679 MEA5
Species Reactivity
Human
Immunogen
A synthesized peptide derived from human MGEA5
Immunogen Species
Homo sapiens (Human)
Conjugate
Non-conjugated
Clonality
Monoclonal
Isotype
Rabbit IgG
Clone No.
8D12
Purification Method
Affinity-chromatography
Concentration
It differs from different batches. Please contact us to confirm it.
Buffer
Rabbit IgG in phosphate buffered saline, pH 7.4, 150mM NaCl, 0.02% sodium azide and 50% glycerol.
Form
Liquid
Tested Applications
ELISA, WB
Recommended Dilution
Application Recommended Dilution
WB 1:500-1:5000
Troubleshooting and FAQs
Storage
Upon receipt, store at -20°C or -80°C. Avoid repeated freeze.
Lead Time
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.
Description

The MGEA5 gene encodes protein O-GlcNAcase (OGA), which is responsible for the hydrolysis of the O-linked β-N-acetyl glucosamine (O-GlcNAc) modification, an essential protein glycosylation event that modulates the function of numerous cellular proteins in response to nutrients and stress. OGA is a member of the family of hexosaminidases and is mainly localized in the cytosol. However, unlike lysosomal hexosaminidases, OGA activity is the highest at neutral pH (approximately 7). Nicholas B. Hastings et al. has demonstrated that inhibition of O-GlcNAcase leads to elevation of O-GlcNAc tau and reduction of tauopathy and cerebrospinal fluid tau in rTg4510 mice.

Compared with the polyclonal and monoclonal antibodies of MGEA5, this MGEA5 recombinant antibody has the features of increased reproducibility and control, animal-free technology, high degree of monovalency, high batch-to-batch consistency, easier isotype conversion, etc. And it has been validated in ELISA, WB.

Customer Reviews and Q&A

 Customer Reviews

There are currently no reviews for this product.

Submit a Review here

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

Show More

Hide All

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

icon of phone
Call us
301-363-4651 (Available 9 a.m. to 5 p.m. CST from Monday to Friday)
icon of address
Address
7505 Fannin St., Ste 610, Room 7 (CUBIO Innovation Center), Houston, TX 77054, USA
icon of social media
Join us with

Subscribe newsletter

Leave a message

* To protect against spam, please pass the CAPTCHA test below.
CAPTCHA verification
© 2007-2024 CUSABIO TECHNOLOGY LLC All rights reserved. 鄂ICP备15011166号-1
Place an order now

I. Product details

*
*
*
*

II. Contact details

*
*

III. Ship To

*
*
*
*
*
*
*

IV. Bill To

*
*
*
*
*
*
*
*