MBP – Maltose Binding Protein > MBP - ¹⁵N

Description
MW = 40.3 kDa calculated. Recombinant Maltose binding protein from E. coli, expressed in E. coli. The protein consists of the residues 27-392 with a mutation the T28I (UniProtKB accession P0AEX9).

Sequence

                              30         40         50
                          M-KIEE GKLVIWINGD KGYNGLAEVG 
        60         70         80         90        100
KKFEKDTGIK VTVEHPDKLE EKFPQVAATG DGPDIIFWAH DRFGGYAQSG 
       110        120        130        140        150
LLAEITPDKA FQDKLYPFTW DAVRYNGKLI AYPIAVEALS LIYNKDLLPN 
       160        170        180        190        200
PPKTWEEIPA LDKELKAKGK SALMFNLQEP YFTWPLIAAD GGYAFKYENG 
       210        220        230        240        250
KYDIKDVGVD NAGAKAGLTF LVDLIKNKHM NADTDYSIAE AAFNKGETAM 
       260        270        280        290        300
TINGPWAWSN IDTSKVNYGV TVLPTFKGQP SKPFVGVLSA GINAASPNKE 
       310        320        330        340        350
LAKEFLENYL LTDEGLEAVN KDKPLGAVAL KSYEEELAKD PRIAATMENA 
       360        370        380        390 
QKGEIMPNIP QMSAFWYAVR TAVINAASGR QTVDEALKDA QT

Purity
> 95% by SDS-PAGE. The protein is observed, in denaturing conditions, as a single band migrating between 35.0 and 45.0 kDa.

Supplied as
1.0 mg/mL solution in phosphate buffer 20 mM pH 7.2, EDTA 0.1 mM, NaN₃ 3 mM, Maltotriose 3 mM, Pefabloc® (AEBSF) 50 uM. The concentration is calculated by the analysis of the absorbance at 280 nm (ε₂₈₀ = 66350 M^-1cm^-1 calculated).
(unless otherwise specified, NMR tubes will be sold at a concentration of 1mM)

Characteristics
Under the above described conditions, to avoid precipitation or protein dimerization, the product can be concentrated up to 1.5 mM.

Storage
-20°C. The protein is stable at 4°C for months.
Avoid repeated freeze/thaw cycles.

Evenäs, J. et al. J. Mol. Biol. 309 (4), 961-974 (2001).
Gardner, K.H. et al. J. Am. Chem. Soc. 120 (45), 11738-11748 (1998).