- Name
- Description
- Cat#
- Pricings
- Quantity
Catalogue number
ENZ-164
Synonyms
Ribonuclease HI, RNase HI, Ribonuclease H, RNase H, rnhA, dasF, herA, rnh, sdrA, b0214, JW0204.
Introduction
RNHA is an endonuclease which specifically degrades the RNA of RNA-DNA hybrids. Localized to the nucleus, the RNHA protein mediates the removal of Okazaki fragment RNA primers which are present on the lagging strand during DNA replication. RNHA catalyzes the endonucleolytic cleavage of RNA to a 5'-phosphomonoester and is capable of binding magnesium or manganese as cofactors.
Description
RNASEH1 E.coli Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 178 amino acids (1-155 a.a.) and having a molecular mass of 20kDa.
RNASEH1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
RNASEH1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Physical Appearance
Sterile Filtered clear solution.
Formulation
RNASEH1 protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 10% glycerol and 2mM DTT.
Stability
Store at 4°C if entire vial will be used within 2-4 weeks.
Store, frozen at -20°C for longer periods of time.
For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).
Avoid multiple freeze-thaw cycles.
Store, frozen at -20°C for longer periods of time.
For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).
Avoid multiple freeze-thaw cycles.
Purity
Greater than 95% as determined by SDS-PAGE.
Amino acid sequence
MGSSHHHHHH SSGLVPRGSH MGSMLKQVEI FTDGSCLGNP GPGGYGAILR YRGREKTFSA GYTRTTNNRM ELMAAIVALE ALKEHCEVIL STDSQYVRQG ITQWIHNWKK RGWKTADKKP VKNVDLWQRL DAALGQHQIK WEWVKGHAGH PENERCDELA RAAAMNPTLE DTGYQVEV.
Safety Data Sheet
Usage
ProSpecs products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.