ABclonal Technology

application (WB, IHC-P, FC (intra), ELISA) & cross reactivity (Human)

application (WB, IHC-P, IP, ELISA) & cross reactivity (Human, Mouse, Rat)

application (WB, IHC-P, IP, ELISA) & cross reactivity (Human, Mouse, Rat)

application (WB, IF/ICC, ELISA) & cross reactivity (Human, Mouse, Rat)

application (WB, IF/ICC, ELISA) & cross reactivity (Human, Mouse, Rat)

T3 DNA Ligase is an ATP-dependent ds DNA ligase from bacteriophage T3. It can catalyze the formation of a phosphodiester bond between juxtaposed 5′ phosphate and 3′ hydroxyl termini in duplex DNA or RNA. T3 DNA Ligase will join blunt end and cohesive end termini. It and can also repair single-stranded nicks in duplex DNA, RNA or DNA/RNA hybrids and close the gaps in these DNA substrates. In addition, T3 DNA Ligase is more tolerant to NaCl than T4 DNA Ligase (2-fold).
As with T4 DNA Ligase , addition of PEG 6000 to the T3 DNA Ligase reaction system can improve the ligation efficiency of the blunt end. 1X T4 DNA Ligase Reaction Buffer can be used in some experiments where PEG 6000 is not available, but the activity of T3 DNA Ligase is reduced to 1/10. In applications where high concentrations of NaCl need to be maintained, we recommend the use of reaction buffers without PEG 6000.

T3 DNA Ligase is an ATP-dependent ds DNA ligase from bacteriophage T3. It can catalyze the formation of a phosphodiester bond between juxtaposed 5′ phosphate and 3′ hydroxyl termini in duplex DNA or RNA. T3 DNA Ligase will join blunt end and cohesive end termini. It and can also repair single-stranded nicks in duplex DNA, RNA or DNA/RNA hybrids and close the gaps in these DNA substrates. In addition, T3 DNA Ligase is more tolerant to NaCl than T4 DNA Ligase (2-fold).
As with T4 DNA Ligase , addition of PEG 6000 to the T3 DNA Ligase reaction system can improve the ligation efficiency of the blunt end. 1X T4 DNA Ligase Reaction Buffer can be used in some experiments where PEG 6000 is not available, but the activity of T3 DNA Ligase is reduced to 1/10. In applications where high concentrations of NaCl need to be maintained, we recommend the use of reaction buffers without PEG 6000.

T4 DNA Ligase catalyzes the formation of a phosphodiester bond between juxtaposed 5′ phosphate and 3′ hydroxyl termini in duplex DNA or RNA. This enzyme will join blunt end and cohesive end termini as well as repair single stranded nicks in duplex DNA and some DNA/RNA hybrids. T4 DNA ligase will seal nicks for these DNA substrates. T4 DNA Ligase is applicable to cloning of restriction fragments and to joining linkers and adapters to blunt-ended DNA.

T4 DNA Ligase catalyzes the formation of a phosphodiester bond between juxtaposed 5′ phosphate and 3′ hydroxyl termini in duplex DNA or RNA. This enzyme will join blunt end and cohesive end termini as well as repair single stranded nicks in duplex DNA and some DNA/RNA hybrids. T4 DNA ligase will seal nicks for these DNA substrates. T4 DNA Ligase is applicable to cloning of restriction fragments and to joining linkers and adapters to blunt-ended DNA.

T4 DNA Ligase catalyzes the formation of a phosphodiester bond between juxtaposed 5′ phosphate and 3′ hydroxyl termini in duplex DNA or RNA. This enzyme will join blunt end and cohesive end termini as well as repair single stranded nicks in duplex DNA and some DNA/RNA hybrids. T4 DNA ligase will seal nicks for these DNA substrates. T4 DNA Ligase is applicable to cloning of restriction fragments and to joining linkers and adapters to blunt-ended DNA.

T4 DNA Ligase catalyzes the formation of a phosphodiester bond between juxtaposed 5′ phosphate and 3′ hydroxyl termini in duplex DNA or RNA. This enzyme will join blunt end and cohesive end termini as well as repair single stranded nicks in duplex DNA and some DNA/RNA hybrids. T4 DNA ligase will seal nicks for these DNA substrates. T4 DNA Ligase is applicable to cloning of restriction fragments and to joining linkers and adapters to blunt-ended DNA.

T4 DNA Polymerase catalyzes the synthesis of DNA in the 5’→3′ direction and requires the presence of template and primer. This enzyme has a 3’→5′ exonuclease activity which is much more active than that found in DNA Polymerase I (E. coli). Unlike E. coli DNA Polymerase I, T4 DNA Polymerase does not have a 5’→3′ exonuclease function.
It is applicable to 3′ overhang removal to form blunt ends, 5′ overhang fill-in to form blunt ends, single strand deletion subcloning, second strand synthesis in site-directed mutagenesis and probe labeling using replacement synthesis.

T4 DNA Polymerase catalyzes the synthesis of DNA in the 5’→3′ direction and requires the presence of template and primer. This enzyme has a 3’→5′ exonuclease activity which is much more active than that found in DNA Polymerase I (E. coli). Unlike E. coli DNA Polymerase I, T4 DNA Polymerase does not have a 5’→3′ exonuclease function.
It is applicable to 3′ overhang removal to form blunt ends, 5′ overhang fill-in to form blunt ends, single strand deletion subcloning, second strand synthesis in site-directed mutagenesis and probe labeling using replacement synthesis.

T4 Gene 32 Protein (10 mg/mL), also known as T4 gp32 protein, is a single stranded specific DNA binding protein. The native Gene 32 Protein from bacteriophage T4 (T4gp32) is a single-stranded DNA binding protein that is required for T4 DNA replication, recombination and repair. T4 Gene 32 protein can increase the yield of long PCR products when the reaction contains proteins ranging from 0.5 to 1.0 nmol. The T4 Gene 32 protein can increase the production of PCR products，reducing the inhibitor influence of humic acid. Meanwhile, the protein can promote the digestion reaction of restriction endonucleases, reverse transcription efficiency in RT-PCR, and enhance the activity of T4 DNA polymerase.

T4 Gene 32 Protein (10 mg/mL), also known as T4 gp32 protein, is a single stranded specific DNA binding protein. The native Gene 32 Protein from bacteriophage T4 (T4gp32) is a single-stranded DNA binding protein that is required for T4 DNA replication, recombination and repair. T4 Gene 32 protein can increase the yield of long PCR products when the reaction contains proteins ranging from 0.5 to 1.0 nmol. The T4 Gene 32 protein can increase the production of PCR products，reducing the inhibitor influence of humic acid. Meanwhile, the protein can promote the digestion reaction of restriction endonucleases, reverse transcription efficiency in RT-PCR, and enhance the activity of T4 DNA polymerase.

T4 Polynucleotide Kinase (T4 PNK) catalyzes the transfer and exchange of Pi from the γ position of ATP to the 5´ -hydroxyl terminus of polynucleotides (double-and single-stranded DNA and RNA) and nucleoside 3´-monophosphates. T4 Polynucleotide Kinase also catalyzes the removal of 3´-phosphoryl groups from 3´-phosphoryl polynucleotides, deoxynucleoside 3´-monophosphates and deoxynucleoside 3´-diphosphates.
T4 PNK is applicable to end-labeling DNA or RNA for probes and DNA sequencing, addition of 5´-phosphates to oligonucleotides to allow subsequent ligation and removal of 3´-phosphoryl groups.

T4 Polynucleotide Kinase (T4 PNK) catalyzes the transfer and exchange of Pi from the γ position of ATP to the 5´ -hydroxyl terminus of polynucleotides (double-and single-stranded DNA and RNA) and nucleoside 3´-monophosphates. T4 Polynucleotide Kinase also catalyzes the removal of 3´-phosphoryl groups from 3´-phosphoryl polynucleotides, deoxynucleoside 3´-monophosphates and deoxynucleoside 3´-diphosphates.
T4 PNK is applicable to end-labeling DNA or RNA for probes and DNA sequencing, addition of 5´-phosphates to oligonucleotides to allow subsequent ligation and removal of 3´-phosphoryl groups.

T4 RNA ligase 1 catalyzes the formation of a 3´ → 5´ phosphodiester bond by joining the 5´ phosphate end of a nucleotide to the 3´ hydroxyl end, accompanied by the hydrolysis of ATP to AMP and PPi. Substrates include single-stranded RNA, DNA, and dinucleoside pyrophosphates.

T4 RNA ligase 1 catalyzes the formation of a 3´ → 5´ phosphodiester bond by joining the 5´ phosphate end of a nucleotide to the 3´ hydroxyl end, accompanied by the hydrolysis of ATP to AMP and PPi. Substrates include single-stranded RNA, DNA, and dinucleoside pyrophosphates.

T4 RNA Ligase 2, is an ATP-dependent double-stranded RNA ligase (dsRNA ligase), also known as T4 Rnl2 (gp24.1), which can be used for intramolecular circularization and intermolecular linear ligation of double-stranded RNA. Unlike T4 RNA Ligase 1, T4 RNA Ligase 2 exhibits significantly higher activity in connecting gaps (nicks) in double-stranded RNA compared to connecting ends of single-stranded RNA. T4 RNA Ligase 2 is also applicable for intra- or inter-molecular ligation of the 3′ hydroxyl of RNA chains and the 5′ phosphate of DNA chains within double-stranded nucleic acids (such as RNA double strands, RNA/DNA hybrids, and/or DNA double strands). The enzyme requires an adjacent 5´ phosphate and 3´ OH for ligation. The enzyme can also ligate the 3´ OH of RNA to the 5´ phosphate of DNA in a double stranded structure.

T4 RNA Ligase 2, is an ATP-dependent double-stranded RNA ligase (dsRNA ligase), also known as T4 Rnl2 (gp24.1), which can be used for intramolecular circularization and intermolecular linear ligation of double-stranded RNA. Unlike T4 RNA Ligase 1, T4 RNA Ligase 2 exhibits significantly higher activity in connecting gaps (nicks) in double-stranded RNA compared to connecting ends of single-stranded RNA. T4 RNA Ligase 2 is also applicable for intra- or inter-molecular ligation of the 3′ hydroxyl of RNA chains and the 5′ phosphate of DNA chains within double-stranded nucleic acids (such as RNA double strands, RNA/DNA hybrids, and/or DNA double strands). The enzyme requires an adjacent 5´ phosphate and 3´ OH for ligation. The enzyme can also ligate the 3´ OH of RNA to the 5´ phosphate of DNA in a double stranded structure.

T4 RNA Ligase 2, truncated (T4 Rnl2 truncated) specifically ligates the pre-adenylated 5´ end of DNA or RNA to the 3´ end of RNA. The enzyme does not require ATP for ligation but does need the pre-adenylated substrate. T4 Rnl2 truncated is expressed from a plasmid in E. coli which encodes the first 249 amino acids of the full length T4 RNA Ligase 2. Unlike the full length ligase, T4 Rnl2 truncated is unable to adenylate the 5´ end of the substrate, and as a result it cannot ligate the phosphorylated 5´ end of RNA or DNA to the 3´ end of RNA. This enzyme, also known as Rnl2 (1-249) has been used for optimized linker ligation for the cloning of microRNAs. This enzyme reduces background ligation because it can only use adenylated primers.

T4 RNA Ligase 2, truncated (T4 Rnl2 truncated) specifically ligates the pre-adenylated 5´ end of DNA or RNA to the 3´ end of RNA. The enzyme does not require ATP for ligation but does need the pre-adenylated substrate. T4 Rnl2 truncated is expressed from a plasmid in E. coli which encodes the first 249 amino acids of the full length T4 RNA Ligase 2. Unlike the full length ligase, T4 Rnl2 truncated is unable to adenylate the 5´ end of the substrate, and as a result it cannot ligate the phosphorylated 5´ end of RNA or DNA to the 3´ end of RNA. This enzyme, also known as Rnl2 (1-249) has been used for optimized linker ligation for the cloning of microRNAs. This enzyme reduces background ligation because it can only use adenylated primers.

T4 RNA Ligase 2, truncated KQ (T4 Rnl2tr R55K, K227Q), specifically catalyzes the ligation of a 5´-adenylated DNA or RNA to the 3´ OH end of an RNA molecule. This enzyme-mediated ligation does not require ATP but necessitates a pre-adenylated adapter. T4 RNA Ligase 2, truncated KQ, a double-point mutant of T4 RNA Ligase 2 with R55K and K227Q substitutions, significantly reduces the non-specific ligation of RNA (such as concatenation or self-circularization) compared to T4 RNA Ligase 2, truncated, while maintaining enzyme activity similar to that of T4 RNA Ligase 2, truncated.

T4 RNA Ligase 2, truncated KQ (T4 Rnl2tr R55K, K227Q), specifically catalyzes the ligation of a 5´-adenylated DNA or RNA to the 3´ OH end of an RNA molecule. This enzyme-mediated ligation does not require ATP but necessitates a pre-adenylated adapter. T4 RNA Ligase 2, truncated KQ, a double-point mutant of T4 RNA Ligase 2 with R55K and K227Q substitutions, significantly reduces the non-specific ligation of RNA (such as concatenation or self-circularization) compared to T4 RNA Ligase 2, truncated, while maintaining enzyme activity similar to that of T4 RNA Ligase 2, truncated.

T4 UvsX Recombinase is homologous to the RecA/Rad51 family. The RecA/Rad51 family of recombinases plays an important role in gene recombination, DNA repair, and replication, with pairing and strand replacement activities. T4 UvsX Recombinase can bind with primers to form a complex to search for homologous sequences in double stranded DNA and perform strand displacement reactions. It can work together with T4 UvsY protein, single stranded DNA binding protein, Bsu polymerase, etc. to complete isothermal amplification (RPA) of recombinase polymerase.

T4 UvsX Recombinase is homologous to the RecA/Rad51 family. The RecA/Rad51 family of recombinases plays an important role in gene recombination, DNA repair, and replication, with pairing and strand replacement activities. T4 UvsX Recombinase can bind with primers to form a complex to search for homologous sequences in double stranded DNA and perform strand displacement reactions. It can work together with T4 UvsY protein, single stranded DNA binding protein, Bsu polymerase, etc. to complete isothermal amplification (RPA) of recombinase polymerase.

T4 UvsY Protein can help T4 UvsX Recombinase compete for primers that pre bind to single stranded DNA binding proteins. It promotes the binding of T4 UvsX Recombinase with primers to form a complex, searching for homologous sequences in double stranded DNA for strand displacement reactions. It is mainly used in recombinase polymerase amplification (RPA).

T4-BGT

T5 Exonuclease is a double-stranded DNA-specific exonuclease and single-stranded DNA endonuclease that degrades DNA in the 5′ ́to 3′ ́direction. T5 Exonuclease can digest nucleotides starting from the 5′ end or at gaps and nicks in linear or circular dsDNA. The enzyme does not digest supercoiled dsDNA and exhibits endonuclease activity on ssDNA

T5 Exonuclease is a double-stranded DNA-specific exonuclease and single-stranded DNA endonuclease that degrades DNA in the 5′ ́to 3′ ́direction. T5 Exonuclease can digest nucleotides starting from the 5′ end or at gaps and nicks in linear or circular dsDNA. The enzyme does not digest supercoiled dsDNA and exhibits endonuclease activity on ssDNA

T7 DNA Ligase is an ATP-dependent ds DNA ligase from bacteriophage T7. It can catalyze the formation of a phosphodiester bond between adjacent 5′ phosphate and 3′ hydroxyl termini in double-stranded DNA. T7 DNA ligase can catalyze ligation of cohesive ends and repair nicks, but not blunt end ligation. This makes a good choice for applications in which blunt and cohesive ends of DNA are present but only the cohesive ends are to be joined .

T7 DNA Ligase is an ATP-dependent ds DNA ligase from bacteriophage T7. It can catalyze the formation of a phosphodiester bond between adjacent 5′ phosphate and 3′ hydroxyl termini in double-stranded DNA. T7 DNA ligase can catalyze ligation of cohesive ends and repair nicks, but not blunt end ligation. This makes a good choice for applications in which blunt and cohesive ends of DNA are present but only the cohesive ends are to be joined .

T7 Endonuclease I (T7 Endo I, T7EI)，can recognize and cleave non-perfectly mismatched DNA, cruciform DNA structures, holliday structures or junctions and Heteroduplex DNA. The cleavage site is at the first, second or third phosphodiester bond that is 5´ end to the mismatch.

T7 Endonuclease I (T7 Endo I, T7EI)，can recognize and cleave non-perfectly mismatched DNA, cruciform DNA structures, holliday structures or junctions and Heteroduplex DNA. The cleavage site is at the first, second or third phosphodiester bond that is 5´ end to the mismatch.

T7 Exonuclease is a double-stranded DNA-specific exonuclease that degrades linear or nicked double-stranded DNA in the 5′to 3′direction. The enzyme does not digest supercoiled dsDNA.

T7 Exonuclease is a double-stranded DNA-specific exonuclease that degrades linear or nicked double-stranded DNA in the 5′to 3′direction. The enzyme does not digest supercoiled dsDNA.

T7 High Yield RNA Synthesis Kit is an optimized RNA synthesis kit designed for high-yield in vitro transcription, as shown in Figure 1. The T7 RNA polymerase utilizes a DNA template with the T7 promoter to transcribe a large amount of RNA. The T7 Enzyme Mix in the kit contains RNase inhibitors and inorganic pyrophosphatase, enabling a yield of at least 150 μg of RNA from 1 μg of DNA template.
This kit is suitable for both long and short transcripts synthesis. The synthesized RNA can be used for downstream applications such as in vitro translation, RNA structure and function studies, RNase protection, probe hybridization, RNA interference, and more.

T7 RNA Polymerase is a DNA-dependent 5’→3′ RNA polymerase that highly specifically recognizes the T7 promoter sequence. T7 RNA Polymerase uses double-stranded DNA containing the T7 promoter sequence as a template and NTP as a substrate to synthesize RNA complementary to the single-stranded DNA downstream of the T7 promoter.

T7 RNA Polymerase is a DNA-dependent 5’→3′ RNA polymerase that highly specifically recognizes the T7 promoter sequence. T7 RNA Polymerase uses double-stranded DNA containing the T7 promoter sequence as a template and NTP as a substrate to synthesize RNA complementary to the single-stranded DNA downstream of the T7 promoter.

application (WB, ELISA) & cross reactivity (Human, Mouse, Rat)

application (WB, ELISA) & cross reactivity (Human, Mouse, Rat)

application (WB, IF/ICC, ELISA) & cross reactivity (Human, Mouse, Rat)

application (WB, IF/ICC, ELISA) & cross reactivity (Human, Mouse, Rat)

application (WB, IF/ICC, IP, ELISA) & cross reactivity (Human, Mouse)

application (WB, IF/ICC, IP, ELISA) & cross reactivity (Human, Mouse)

application (WB, ELISA) & cross reactivity (Human, Mouse, Rat)

application (WB, ELISA) & cross reactivity (Human, Mouse, Rat)

application (WB, ELISA) & cross reactivity (Human, Mouse)

application (WB, ELISA) & cross reactivity (Human, Mouse)