Technical Data
Maltose Phosphorylase (Biotin)
In enzymology, a maltose phosphorylase (EC is an enzyme that catalyzes the chemical reaction
maltose + phosphate D-glucose + beta-D-glucose 1-phosphate
Thus, the two substrates of this enzyme are maltose and phosphate, whereas its two products are D-glucose and beta-D-glucose 1-phosphate.
This enzyme belongs to the family of glycosyltransferases, specifically the hexosyltransferases. The systematic name of this enzyme class is maltose:phosphate 1-beta-D-glucosyltransferase. This enzyme participates in starch and sucrose metabolism.

Suitable for Immunoblot (Western or Dot Blot), ELISA, Immunomicroscopy and Immunohistochemistry as well as other antibody based assays using streptavidin or avidin conjugates. Other applications not tested.

Recommended Dilution:
ELISA: 1:4000-1:20,000; 1ug of Maltose Phosphorylase was used in a standard capture ELISA with Streptavidin (HRP) S7973-97A and ABTS (2,2'-azino-bis-[3-ethylbenthiazoline-6-sulfonic acid]), A0030, as a substrate for 30 minutes at RT.
Optimal dilutions to be determined by the researcher.

Biotinamidocaproate N-Hydroxysuccinimide Ester (BAC)

Biotin/Protein Ratio:
10-20 BAC molecules per Goat IgG molecule

Storage and Stability:
May be stored at 4C for short-term only. For long-term storage, store at -20C. Aliquots are stable for at least 6 months at -20C. For maximum recovery of product, centrifuge the original vial after thawing and prior to removing the cap. Further dilutions can be made in assay buffer.
PabIgGHighly Purified
100ug-20CBlue IceGoat
Maltose Phosphorylase (E. coli)
Purified by delipidation, salt fractionation and ion exchange chromatography.
Supplied as a liquid in PBS, pH 7.2, 10mg/ml BSA, 0.01% sodium azide, 40% glycerol. Labeled with Biotin.
Assay by IEP resulted in a single precipitin arc against anti-Biotin, anti-Goat Serum as well as purified and partially purified Maltose Phosphorylase (E. coli).
Intended for research use only. Not for use in human, therapeutic, or diagnostic applications.
Bayer & Wilchek Methods in Enzymology 184; 138-160, 1990.