O-GlcNAcase/OGA Protein, B. thetaiotaomicron (His)

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Based on 1 Customer Validation

O-GlcNAcase (OGA) is an enzyme responsible for the hydrolysis of glycosidic bonds in O-GlcNA acylated proteins. It exhibits its enzymatic activity in vitro by efficiently utilizing substrates such as p-nitrophenyl-β-GlcNAc and 4-methylumbelliferone-GlcNAc. O-GlcNAcase/OGA Protein, B. thetaiotaomicron (His) is the recombinant O-GlcNAcase/OGA protein, expressed by E. coli , with N-6*His labeled tag.

For research use only. We do not sell to patients.
  • Species: Others
  • Source: E. coli
  • Storage:
    Stored at -20°C for 2 years from date of receipt. After reconstitution, it is stable at 4°C for 1 week or -20°C for longer (with carrier protein). It is recommended to freeze aliquots at -20°C or -80°C for extended storage.
  • Biological Activity
  • Technical Parameters
  • Product Properties
  • Documentation
  • Help & FAQs

Biological Activity

Description

O-GlcNAcase (OGA) is an enzyme responsible for the hydrolysis of glycosidic bonds in O-GlcNA acylated proteins. It exhibits its enzymatic activity in vitro by efficiently utilizing substrates such as p-nitrophenyl-β-GlcNAc and 4-methylumbelliferone-GlcNAc. O-GlcNAcase/OGA Protein, B. thetaiotaomicron (His) is the recombinant O-GlcNAcase/OGA protein, expressed by E. coli , with N-6*His labeled tag.

Background

O-GlcNAcase (OGA) is an enzyme responsible for the hydrolysis of the glycosidic link in O-GlcNAcylated proteins. It exhibits its enzymatic activity in vitro by efficiently utilizing substrates like p-nitrophenyl-beta-GlcNAc and 4-methylumbelliferone-GlcNAc. OGA plays a crucial role in regulating O-GlcNAcylation, a post-translational modification that involves the attachment of N-acetylglucosamine (GlcNAc) to serine or threonine residues of proteins. By catalyzing the removal of O-GlcNAc groups, OGA contributes to the dynamic control of O-GlcNAcylation levels, thereby influencing various cellular processes such as signal transduction, gene expression, and protein stability. Further investigation is necessary to fully comprehend the complex regulatory mechanisms and physiological significance of OGA in cellular functions and disease pathways.

Verified Bioactivity

Measured by its ability to cleave a peptide substrate, 4-methylumbelliferyl-N-acetyl-beta-D-glucosaminide. Read at excitation and emission wavelengths of 365 nm and 445 nm. The specific activity is 3120.1541 pmol/min/µg, as measured under the described conditions.

MCE Validation Data

  • Purity - SDS-PAGE

    Purity - SDS-PAGE

    ≥ 95%, as determined by reducing SDS-PAGE.

Technical Parameters

  • Species Others
  • Source E. coli
  • Tag N-6*His
  • Accession
  • Gene ID
  • Molecular Construction
    • N-term
    • 6*His
    • OGA (Q22-K737)
      Accession # Q89ZI2
    • C-term
  • Protein Length

    Full Length of Mature Protein

  • Synonyms

    O-GlcNAcase BT_4395; EC:3.2.1.169; Beta-N-acetylglucosaminidase; Beta-N-acetylhexosaminidase; Beta-hexosaminidase; Hexosaminidase B; N-acetyl-beta-glucosaminidase; BT_4395

  • AA Sequence

    QNVSLQPPPQQLIVQNKTIDLPAVYQLNGGEEANPHAVKVLKELLSGKQSSKKGMLISIGEKGDKSVRKYSRQIPDHKEGYYLSVNEKEIVLAGNDERGTYYALQTFAQLLKDGKLPEVEIKDYPSVRYRGVVEGFYGTPWSHQARLSQLKFYGKNKMNTYIYGPKDDPYHSAPNWRLPYPDKEAAQLQELVAVANENEVDFVWAIHPGQDIKWNKEDRDLLLAKFEKMYQLGVRSFAVFFDDISGEGTNPQKQAELLNYIDEKFAQVKPDINQLVMCPTEYNKSWSNPNGNYLTTLGDKLNPSIQIMWTGDRVISDITRDGISWINERIKRPAYIWWNFPVSDYVRDHLLLGPVYGNDTTIAKEMSGFVTNPMEHAESSKIAIYSVASYAWNPAKYDTWQTWKDAIRTILPSAAEELECFAMHNSDLGPNGHGYRREESMDIQPAAERFLKAFKEGKNYDKADFETLQYTFERMKESADILLMNTENKPLIVEITPWVHQFKLTAEMGEEVLKMVEGRNESYFLRKYNHVKALQQQMFYIDQTSNQNPYQPGVKTATRVIKPLIDRTFATVVKFFNQKFNAHLDATTDYMPHKMISNVEQIKNLPLQVKANRVLISPANEVVKWAAGNSVEIELDAIYPGENIQINFGKDAPCTWGRLEISTDGKEWKTVDLKQKESRLSAGLQKAPVKFVRFTNVSDEEQQVYLRQFVLTIEKK

  • Molecular Weight

    Approximately 66-76 kDa, based on SDS-PAGE under reducing conditions.

  • Purity

    ≥ 95%, as determined by reducing SDS-PAGE.

Product Properties

Appearance

Lyophilized powder.

Formulation

Lyophilized from a 0.22 μm filtered solution of 50 mM Tris-HCl, 300 mM NaCl, pH 7.4.
Note: For SPR assay, please replace the buffer. Primary amine components (e.g., Tris, imidazole) can affect protein-coupled chips.

Endotoxin Level

<1 EU/μg, determined by LAL method.

Reconstitution

It is not recommended to reconstitute to a concentration less than 100 μg/mL in ddH2O. For long term storage it is recommended to add a carrier protein (0.1% BSA, 5% HSA, 10% FBS or 5% Trehalose).

Storage & Stability

Stored at -20°C for 2 years from date of receipt. After reconstitution, it is stable at 4°C for 1 week or -20°C for longer (with carrier protein). It is recommended to freeze aliquots at -20°C or -80°C for extended storage.

Shipping

Room temperature in continental US; may vary elsewhere.

Calculators

Reconstitution Calculator

Volume (to add to vial) = Mass (in vial) ÷ Desired Reconstitution Concentration

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=
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Desired Reconstitution Concentration Desired Reconstitution Concentration
Dilution Calculator

Concentration (start) × Volume (start) = Concentration (final) × Volume (final)

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The Specific Activity Calculator Equation
  • Specific Activity (Unit/mg)
  • Biological Activity (ED50)

Specific Activity (Unit/mg) = 106 ÷ Biological Activity (ED50)

Specific Activity (Unit/mg) Specific Activity (Unit/mg)
Unit/mg
= 106 ÷
Biological Activity (ED50) Biological Activity (ED50)
106 ÷
ng/mL
MOQ
Minimum order quantity
100 mg

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