TOP
Enquiry
×
*
*
*
相談
Enzyme Materials

Polymerase

 

Code

Product Name

MD031H

Phi29 DNA Polymerase(High Concentration)

MD033

T4 DNA Polymerase

MD063

HiFi Seq DNA Polymerase

MD037

Klenow Fragment

MD038L

Klenow (3′→ 5′ exo-)

FPZ-14

T7 RNA Polymerase

FPZ-26

DNA Polymerase I

FPZ-29

Poly(A) Polymerase


MD031H--- Phi29 DNA Polymerase (High Concentration)

Phi29 DNA polymerase is a highly processive polymerase (up to 70KB) featuring strong strand displacement activity, which allows for highly efficient isothermal DNA amplification. Phi29 DNA Polymerase also possesses a 3'→5' exonuclease (proofreading) activity acting preferentially on single-stranded DNA or RNA. Therefore 3'-modified primers are highly recommended.


MD033--- T4 DNA Polymerase

T4 DNA Polymerase catalyzes the extension of a primed DNA template in the 5′→3′ direction. This enzyme exhibits a powerful 3′→5′ exonuclease activity, while lacking any inherent 5′→3′ exonuclease or strand displacement functions.


MD063--- HiFi Seq DNA Polymerase

High-Fidelity DNA polymerase is an engineered, ultra-thermostable polymerase designed to maximize the speed, accuracy, and length of DNA synthesis during sequencing template preparation. The result is a novel enzyme that can extend a kilobase of sequence in 15 seconds and with accuracy 50 times higher than Taq DNA Polymerase.


MD037--- Klenow Fragment

Klenow Fragment is a DNA-dependent Polymerase I enzyme derived from the mesophilic E.coli. The enzyme exhibits DNA synthesis and proofreading (3′→5′) activities. A holoenzymes (5′→3′) nuclease lost Klenow Fragment domain displays a moderate strand displacement activity during DNA synthesis. The protein is expressed as a product of truncated E.coli. PolA gene.


MD038L--- Klenow (3′→5′ exo-)

Klenow (3′→5′ exo-) is a mesophilic DNA polymerase deficient in both proofreading (3→5′) and nick-translation (5′→3′) nuclease activities, and that displays a moderate strand displacement activity during DNA synthesis. The protein is expressed as a truncated product of the E.coli. PolA gene with the D355A and E357A mutations.


FPZ-14--- T7 RNA Polymerase

T7 RNA Polymerase is a DNA-dependent RNA polymerase having high specificity for the T7 promoter. After promoter initiation, it catalyzes the Mg dependent synthesis of RNA from rNTPs.


FPZ-26---DNA Polymerase I

DNA Polymerase I is a mesophilic DNA polymerase that exhibits 5'→3' DNA synthesis in addition to both 3′→5′ and 5′→3′ exonuclease activities. The combination of DNA synthesis and 5′→3′ nuclease characteristics enable nick-translation during DNA synthesis.


FPZ-29---Poly(A) Polymerase

Poly(A) Polymerase catalyzes the addition of AMP from ATP to the 3'-hydroxyl of RNA. The reaction requires Mg and is template independent. 


Ligase

Code

Product Name

MD035

Fast T4 DNA Ligase

FPZ-16

T3 DNA Ligase

FPZ-17

T4 DNA Ligase

FPZ-20

Taq DNA Ligase

FPZ-21

T4 RNA Ligase 1

FPZ-22

T4 RNA Ligase 2

FPZ-24

T4 Gene 32 Protein

FPZ-38

E.coli DNA Ligase


MD035--- Fast T4 DNA Ligase

T4 DNA Ligase catalyzes the formation of a phosphodiester bond between the terminal 5′-phosphate and 3′-hydroxyl groups of duplex DNA or RNA. The enzyme efficiently joins blunt and cohesive ends and repairs single-stranded nicks in duplex DNA, RNA or DNA/RNA hybrids.


FPZ-16---T3 DNA Ligase

T3 DNA Ligase catalyzes the formation of a phosphodiester bond between 5-phosphate and 3′-hydroxyl termini in duplex DNA. The enzyme will join blunt end and cohesive end termini as well as repair single stranded nicks in duplex DNA. In the absence of 20-30% PEG 6000, T3 DNA Ligase displays a very low efficiency for blunt-ended ligation. T3 DNA Ligase displays a higher efficiency for joining A/T overhangs than C/G matched ends. T3 DNA Ligase retains 95% of its activity in 1.0 M NaCl or KCl, with an optimal concentration of 300 mM.


FPZ-17---T4 DNA Ligase

T4 DNA Ligase catalyzes the formation of a phosphodiester bond between the terminal 5′-phosphate and 3′-hydroxyl groups of duplex DNA or RNA. The enzyme efficiently joins blunt and cohesive ends and repairs single-stranded nicks in duplex DNA, RNA or DNA/RNA hybrids.


FPZ-20---Taq DNA Ligase

Taq DNA Ligase catalyzes the formation of a phosphodiester bond in duplex DNA containing adjacent 5'-phosphoryl and 3'-hydroxyl termini, using NAD+ as a cofactor.


FPZ-21---T4 RNA Ligase1

T4 RNA Ligase catalyzes the ATP-dependent ligation of single-stranded nucleic acids (RNA or DNA).


FPZ-22---T4 RNA Ligase2

T4 RNA Ligase 2 truncated catalyzes phosphodiester bond formation between a pre-adenylated 5'-phosphate (DNA or RNA) and the 3'-hydroxyl of RNA. The truncated enzyme contains the first 249 amino acids which make the enzyme requires a pre-adenylated 5'-terminal donor and eliminates the need for ATP. Because T4 RNA ligase 2 truncated cannot use the 5'-phosphate of RNA or DNA as a donor in the ligation reaction, it is useful for certain applications such as linker ligations with pre-adenylated 5'-DNA to 3'-hydroxyl RNA. The desired specific ligation products are enhanced dramatically over unwanted background ligation products, making the truncated enzyme superior to the full-length enzyme for this use.


FPZ-24---T4 Gene 32 Protein

T4 Gene 32 Protein is a single-stranded DNA binding protein which is required for T4 DNA replication, recombination and repair. The protein has exhibited an ability to enhance the performance of several DNA synthesis-related activities, including DNA sequencing in secondary-structure rich regions and PCR amplification. T4 Gene 32 also greatly stimulates the rate of synthesis of T4 DNA Polymerase on primed-single-stranded substrates (5-10 folds increase in synthesis rate).


FPZ-38--- E.coli DNA Ligase

E.coli DNA ligase catalyzes the phosphodiester bond formation between an adjacent 5'-phosphate and a 3'-hydroxyl of DNA ends, requiring NAD+ and Mg as cofactors. Ligation of blunt-ended DNA is extremely inefficient relative to cohesive DNA end ligation and nick sealing.



Endonuclease

Code

Product Name

FPZ-31

Exonuclease I

FPZ-32

Exonuclease III


FPZ-31---Exonuclease I

Exonuclease I cleaves single-stranded DNA in the 3′→5′ direction, releasing 5′-mono/di-nucleotides and leaving double-stranded DNA molecules and the 5'-terminus intact. The enzyme is processive though digestion and is inhibited by the presence of a 3′-terminal phosphate. Exonuclease I is tolerant of a wide range of buffer conditions and can typically be added to reactions containing magnesium.


FPZ-32---Exonuclease III

Exonuclease III is a 3′→5′ exonuclease which acts by digesting one strand of a dsDNA duplex at a time or digesting the RNA strand of an RNA-DNA heteroduplex. Exonuclease III breaks phosphodiester bonds on the 5′-side of AP sites in both dsDNA and ssDNA, removes 3′-terminal groups on dsDNA, increases MutY turnover, and efficiently degrades 3′-recessed but not 3′-protruding DNA ends (creating 5′-overhangs). Exo III removes a limited number of nucleotides per binding event, resulting in coordinated progressive deletions within the population of DNA molecules.




Code

Product Name

Others

MD034

T4 Polynucleotide Kinase

MD025

Proteinase K

MD056

RNase H

FPZ-42

Terminal Deoxynucleotidy Transferase


MD034---T4 Polynucleotide Kinase (T4 PNK)

T4 Polynucleotide Kinase (PNK) catalyzes the transfer and exchange of the terminal gamma position phosphate of ATP to the 5′-hydroxyl terminus of double-and single-stranded DNA, RNA and nucleoside 3′-monophosphate molecules. T4 PNK also exhibits 3′-phosphatase and 2′, 3′-cyclic phosphodiesterase activities.


MD025---Proteinase K

Proteinase K is a broad-spectrum serine protease, coming from Tritirachium album limber. It belongs to Peptidase family S8, which enzyme activity is the highest in proteinase. The site of cleave is the peptide bond adjacent to the carboxyl group of aliphatic and aromatic amino acids with blocked alpha amino groups, which is used to digest protein in biological samples


Fapon Proteinase K is recombinant protein from Yeast. The enzyme activity theoretically was enhanced 50 times through six site directed mutagenesis. RNA and DNA were eliminated by decoloration and chromatogram. There is no other enzyme in our proteinase K. It is stable and could work perfectly from pH4 to pH12 even with SDS, urea or EDTA. Proteinase K could be applied widely in molecular diagnostic test kit, genome DNA extraction kit, RNA extraction kit to digest the nuclease in DNA/RNA extraction or protein impurity during extraction of nonprotein component from tissue.


MD056---RNase H

RNase H (rnh) is an endoribonuclease which degrades the RNA strand of RNA/DNA hybrid molecules. RNase H digestion produces ribonucleotide molecules with 5′-phosphate and 3′-hydroxyl termini. RNase H is nearly inactive against single or double-stranded RNA molecules.


FPZ-42---Terminal deoxynucleotidyl Transferase (TdT)

Terminal deoxynucleotidyl transferase (TdT) is a template-independent DNA polymerase that catalyzes the addition of deoxynucleotides to the 3'-hydroxyl terminus of single or double-stranded DNA molecules. The presence of 1 mM Co stimulates the tailing of the 3'-ends of DNA fragments. This construct is sold as an N-terminal truncation of the terminal transferase gene attached to an N-terminal fusion tag.