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However, the speeds of individual ENCCs were variable, and some ENCCs migrating within thick strands migrated at approximately 130 μm/h for over four hours.
The amplicon migrating at approximately 610 nucleotide corresponded to Kirrel3 B while the amplicon that migrated at approximately 590 nucleotides lacked the 13th exon of Kirrel3 B which contains 37 nucleotides (see Table 2 for raw sequence data obtained).
On denaturing and native gels, cgd8_2530 migrated at approximately 150 and 1000 kDa, respectively, suggesting an involvement in a multi-subunit protein complex.
Here, we detected one clear band that migrated at approximately 5 kb.
The bands which were the second most intensely staining migrated at approximately 48 kD, corresponding to the molecular weight of MMP-13.
We observed a single PstI-digested band that migrated at approximately 9 kbp (lane 5) and a predominant MunI-digested band at approximately 2.3 kbp as well as a very faint larger band probably due to incomplete digestion (lane 6), consistent with integration of the transposon approximately 1 kbp from an MunI site in the rickettsial chromosome.
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Intact ribosomal RNA migrated as bands at approximately 1.6 and 3.8 kb relative to RNA markers (Fig. 5A, lane 1) in RNA extracts of untransformed R. montanensis (lanes 2 and 5) and Rmontanensis700 (lanes 3 and 6).
The antibody specifically recognized a single protein band, in both HeLa and mouse testis extracts, that migrated at a same position representing approximately 90 kDa (Supplementary Fig. S1), which corresponds to the previously reported molecular weight of this protein in human cells ([30]).
5 µl of each sample was mixed with 1 µl loading dye and loaded onto a roti-safe (Carl Roth GmbH, Karlsruhe, Germany) stained 1 % agarose gel in tris base boric acid EDTA buffer (TBE; containing per liter 10.8 g tris base, 5.5 g boric acid, 20 mM EDTA) and migrated for approximately 1 h at 90 V.
At 2 years, their cemented components migrated (MTPM) approximately 0.6 mm and their HA components migrated approximately 1.0 mm.
L-DNase II was originally identified in a commercial preparation of DNase 2 [21], possibly indicating that it can be easily co-purified with DNase 2 or that it might even physically interact with DNase 2. It is tempting to speculate that serpinB1 bound to DNase 2 in a putative multi-protein complex that migrated at the apparent molecular weight of approximately 130 kD in zymography.
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