POLB Human

Polymerase (DNA directed), Beta Human Recombinant
Cat. No.
BT15534
Source
Escherichia Coli.
Synonyms

DNA polymerase beta, DNA directed DNA polymerase beta, DNA pol beta, DNA polymerase beta, DNA polymerase beta subunit, MGC125976, Pol B, Pol beta, PolB, Polymerase (DNA directed) beta.

Appearance
Sterile filtered colorless solution.
Purity

Greater than 95.0% as determined by SDS-PAGE.

Usage
Prospec's 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.
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Description

POLB Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 355 amino acids (1-335 a.a) and having a molecular mass of 40.3kDa.
POLB is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Product Specs

Introduction
DNA polymerase beta (POLB) is a crucial enzyme involved in DNA repair, replication, recombination, and drug resistance in eukaryotic cells. As a member of the DNA polymerase type-X family, it plays a vital role in base excision repair, a critical pathway for maintaining DNA integrity. POLB consists of two distinct domains: a larger polymerase domain responsible for its primary function and a smaller N-terminal domain with AP lyase activity. This lyase activity is essential for removing damaged sugar-phosphate residues during the repair process. Specifically, POLB fills single nucleotide gaps generated during base excision repair in mammalian cells. Notably, the overexpression of POLB, observed in certain human tumors, can lead to increased spontaneous mutagenesis.
Description
Recombinant Human POLB, expressed in E. coli, is available as a single, non-glycosylated polypeptide chain. This protein comprises 355 amino acids, with amino acids 1-335 representing the POLB sequence, and has a molecular weight of 40.3 kDa. A 20 amino acid His-tag is fused to the N-terminus to facilitate purification, which is achieved through proprietary chromatographic techniques.
Physical Appearance
The product is a clear and colorless solution that has been sterilized by filtration.
Formulation
The POLB protein solution is provided at a concentration of 0.5 mg/ml in a buffer consisting of 20mM Tris-HCl (pH 8.0), 1mM DTT, 30% glycerol, and 0.1M NaCl.
Stability
For short-term storage (up to 2-4 weeks), the product can be stored at 4°C. For extended storage, it is recommended to freeze the product at -20°C. Adding a carrier protein such as HSA or BSA (0.1%) is advisable for long-term storage. To maintain product quality, avoid repeated freeze-thaw cycles.
Purity
The purity of the protein is greater than 95%, as determined by SDS-PAGE analysis.
Synonyms

DNA polymerase beta, DNA directed DNA polymerase beta, DNA pol beta, DNA polymerase beta, DNA polymerase beta subunit, MGC125976, Pol B, Pol beta, PolB, Polymerase (DNA directed) beta.

Source
Escherichia Coli.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MSKRKAPQET LNGGITDMLT ELANFEKNVS QAIHKYNAYR KAASVIAKYP HKIKSGAEAK KLPGVGTKIA EKIDEFLATG KLRKLEKIRQ DDTSSSINFL TRVSGIGPSA ARKFVDEGIK TLEDLRKNED KLNHHQRIGL KYFGDFEKRI PREEMLQMQD
IVLNEVKKVD SEYIATVCGS FRRGAESSGD MDVLLTHPSF TSESTKQPKL LHQVVEQLQK VHFITDTLSK GETKFMGVCQ LPSKNDEKEY PHRRIDIRLI PKDQYYCGVL YFTGSDIFNK NMRAHALEKG FTINEYTIRP LGVTGVAGEP LPVDSEKDIF DYIQWKYREP KDRSE.

Product Science Overview

Structure and Function

DNA polymerase beta is a small, monomeric enzyme with a molecular weight of approximately 39 kDa . It consists of two distinct domains:

  1. Polymerase Domain: This larger domain is responsible for the polymerase activity, which adds nucleotides to the 3’ end of a DNA strand during DNA synthesis.
  2. N-terminal Domain: This smaller, basic domain contains an apurinic/apyrimidinic (AP) lyase activity that excises the abasic sugar-phosphate residue at the strand break .
Role in Base Excision Repair

DNA polymerase beta plays a pivotal role in the BER pathway, which is essential for repairing small base lesions resulting from oxidation, alkylation, deamination, or spontaneous loss of a base. The enzyme operates in two BER sub-pathways:

  • Single-Nucleotide BER: In this pathway, DNA polymerase beta fills in a single nucleotide gap created after the removal of a damaged base.
  • Long-Patch BER: Here, the enzyme synthesizes a short stretch of DNA to replace a longer damaged segment .

During the BER process, DNA polymerase beta is recruited by the AP endonuclease 1 (APE1) and interacts with other proteins such as XRCC1, DNA ligase III, and poly (ADP-ribose) polymerase .

Recombinant Production

Recombinant human DNA polymerase beta is produced using genetic engineering techniques. The POLB gene is inserted into the genetic material of Escherichia coli (E. coli) bacteria, which then express the enzyme. The recombinant enzyme is purified to a high degree of purity (≥98%) and is used for various research purposes .

Clinical Significance

Overexpression of DNA polymerase beta has been observed in certain human tumors, which may lead to an increase in spontaneous mutagenesis . This enzyme’s role in DNA repair makes it a potential target for cancer therapy, as inhibiting its activity could enhance the effectiveness of DNA-damaging agents used in cancer treatment.

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