Efficient cleavage requires at least two copies of the BpmI recognition sequence. Sticky ends from different BpmI sites may not be compatible. After cleavage, BpmI can remain bound to DNA and alter its electrophoretic mobility. BpmI quickly loses activity at 37°C. Sticky ends from different BsiHKAI sites may not be compatible.

CopGFP (ppluGFP2 in our scientific publications, Shagin et al., 2004) is a green fluorescent protein cloned from copepod Pontellina plumata (Arthropoda; Crustacea; Maxillopoda; Copepoda). CopGFP is characterized by superbright green fluorescence (excitation/ emission max = 482/ 502 nm) and fast maturation rate at a wide range of temperatures.

CopGFP is efficiently excited using an argon-ion laser or FITC filter set (absorption maximum at 482 nm) and produces green fluorescence at 502 nm with a brightness value approximately 30% higher than EGFP and much greater resistance to changes in pH.

CopGFP (ppluGFP2 in our scientific publications, Shagin et al., 2004) is a green fluorescent protein cloned from copepod Pontellina plumata (Arthropoda; Crustacea; Maxillopoda; Copepoda).

Through HDR, an exogenous fluorescent reporter DNA vector (also called “donor”), such as copepod green fluorescent protein (copGFP) or enhanced green fluorescent protein (EGFP), may be permanently introduced and placed under the control of …

CopGFP is efficiently excited using an argon-ion laser or FITC blue excitation filter set (absorption maximum at 482 nanometers) and produces green fluorescence at 502 nanometers with a brightness value approximately 30 percent higher than …

Plasmid pCDH-EF1-copGFP from Dr. Kazuhiro Oka's lab contains the insert copGFP and is published in Unpublished This plasmid is available through Addgene.

ppluGFP2 is a basic (constitutively fluorescent) green fluorescent protein published in 2004, derived from Pontellina plumata.

Jun 16, 2006 · We have determined the crystal structure of copGFP to 2.1 Å resolution, and compared it to the structures of GFP and DsRed. Presently, over 100 GFP-like proteins have been characterized from the Cnidaria, the vast majority of which arise from the class Anthozoa.

Feb 20, 2006 · We have determined to 2.1A resolution the crystal structure of copGFP, a representative GFP-like protein from a copepod, a member of the Bilateria.