Recombinant T. maritima alpha-L-Fucosidase Protein, CF

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Product Details

Summary
Reactivity TmSpecies Glossary
Applications Enzyme Activity
Format
Carrier-Free

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Recombinant T. maritima alpha-L-Fucosidase Protein, CF Summary

Details of Functionality
Measured by its ability to cleave a fluorogenic substrate 4-methylumbelliferyl-alpha -L-fucopyranoside. The specific activity is >1,600 pmol/min/μg, as measured under the described conditions.
Source
E. coli-derived t. maritima alpha-L-Fucosidase protein
Ile2-Glu449, with an N-terminal Met and 6-His tag
Accession #
N-terminal Sequence
Met
Protein/Peptide Type
Recombinant Enzymes
Gene
TM0306
Purity
>95%, by SDS-PAGE under reducing conditions and visualized by Colloidal Coomassie® Blue stain at 5 μg per lane
Endotoxin Note
<1.0 EU per 1 μg of the protein by the LAL method.

Applications/Dilutions

Theoretical MW
53 kDa.
Disclaimer note: The observed molecular weight of the protein may vary from the listed predicted molecular weight due to post translational modifications, post translation cleavages, relative charges, and other experimental factors.
SDS-PAGE
43-50 kDa, reducing conditions

Packaging, Storage & Formulations

Storage
Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
  • 6 months from date of receipt, -20 to -70 °C as supplied.
  • 3 months, -20 to -70 °C under sterile conditions after opening.
Buffer
Supplied as a 0.2 μm filtered solution in Tris and NaCl.
Purity
>95%, by SDS-PAGE under reducing conditions and visualized by Colloidal Coomassie® Blue stain at 5 μg per lane
Assay Procedure
  • Assay Buffer: 50 mM MES, 200 mM NaCl, pH 5.5
  • Recombinant T. maritima alpha ‑L‑Fucosidase (rT. maritima alpha -L-Fucosidase) (Catalog # 6556-GH)
  • Substrate: 4-Methylumbelliferyl-alpha -L-fucopyranoside (Research Products International Corp, Catalog # M65200), 50 mM stock in DMSO
  • F16 Black Maxisorp Plate (Nunc, Catalog # 475515)
  • Fluorescent Plate Reader (Model: SpectraMax Gemini EM by Molecular Devices) or equivalent
  1. Dilute rT. maritima alpha -L-Fucosidase to 2 ng/μL in Assay Buffer.
  2. Dilute Substrate to 400 μM in Assay Buffer.
  3. Load into a plate 50 μL of 2 ng/μL rT. maritima alpha -L-Fucosidase, and start the reaction by adding 50 μL of 400 μM Substrate. For Substrate Blanks, load 50 μL of Assay Buffer and 50 μL of 400 μM Substrate.
  4. Read plate at excitation and emission wavelengths of 365 nm and 445 nm, respectively, in kinetic mode for 5 minutes.
  5. Calculate specific activity:

     Specific Activity (pmol/min/µg) =

Adjusted Vmax* (RFU/min) x Conversion Factor** (pmol/RFU)
amount of enzyme (µg)

     *Adjusted for Substrate Blank
     **Derived using calibration standard 4-Methylumbelliferone (Sigma, Catalog # M1381).

Per Well:
  • rT. maritima alpha -L-Fucosidase: 0.100 μg
  • Substrate: 200 μM

Notes

This product is produced by and ships from R&D Systems, Inc., a Bio-Techne brand.

Alternate Names for Recombinant T. maritima alpha-L-Fucosidase Protein, CF

  • alphaLFucosidase
  • alpha-L-Fucosidase

Background

Fucosylated glycoconjugates play numerous roles in biological events, including development and apoptosis (1, 2), and are involved in the pathology of inflammation, cancer, and cystic fibrosis (3, 4). Fucosidases are generally used for studying fucosylated glycans. With a Kcat/Km value of 160,000 M-1s-1, the alpha -L-fucosidases of Thermotoga maritima efficiently hydrolyzes 4-nitrophenyl fucoside (5). The enzyme is the closest bacterial relative of mammalian fucosidase with 38% identity to its human homologue. It is thought to remove alpha ‑1,2‑ and alpha -1,4-linked fucosyl side chains from algal fucoidan (5), while the activity on alpha -1,3- and alpha ‑1,6‑ linked fucose has not been tested. The enzyme assembles as a hexamer and displays a two-domain fold, with Asp224 and Glu266 being critical for enzyme activity (6).
  1. Hiraishi, K. et al. (1993) Glycobiology 3:381.
  2. Solter, D. and Knowles, B.B. (1978) Proc. Natl. Acad. Sci. USA 75:5565.
  3. Shah, M. et al. (2008) cancer 113:338.
  4. Becker, D.J. and Lowe, J.B. (2003) Glycobiology 13:41R.
  5. Tarling, C.A. et al. (2003) J. Biol. Chem. 278:47394.
  6. Sulzenbacher, G. et al. (2004) J. Biol. Chem. 279:13119.

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Bioinformatics

Gene Symbol TM0306
Uniprot