PGK1 Human, Active

Phosphoglycerate Kinase 1 Human Recombinant, BioActive
Cat. No.
BT12906
Source
E.coli.
Synonyms

Phosphoglycerate kinase 1, MGC117307, MGC142128, MGC8947, MIG10, PGKA.

Appearance
Sterile Filtered colorless solution.
Purity

Greater than 95.0% as determined by SDS-PAGE.

Usage
THE BioTek'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

PGK1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 437 amino acids (1-417a.a.) and having a molecular mass of 46.8kDa.
PGK1 is fused to a 20 amino acid His tag at N-Terminus and purified by proprietary chromatographic techniques.

Product Specs

Introduction
Phosphoglycerate kinase 1, also known as PGK1, is an enzyme encoded by the PGK1 gene located on the X chromosome. This enzyme plays a crucial role in glycolysis, catalyzing the reversible conversion of 1,3-diphosphoglycerate to 3-phosphoglycerate, producing one molecule of ATP in the process. PGK1 is primarily known for its function in red blood cells, but evidence suggests it might also act as a cofactor for polymerase alpha, assisting in primer recognition during DNA replication.
Description
Recombinant human PGK1, expressed in E. coli, is a monomeric protein with a molecular weight of 46.8 kDa. It consists of a single polypeptide chain of 437 amino acids (residues 1-417) and lacks glycosylation. A 20-amino acid Histidine tag is fused to the N-terminus to facilitate purification, which is achieved through proprietary chromatographic methods.
Physical Appearance
Clear, colorless solution, sterilized by filtration.
Formulation
The PGK1 solution is supplied at a concentration of 1 mg/ml in a buffer consisting of 10% glycerol, 20 mM Tris-HCl (pH 8.0), and 1 mM DTT.
Stability
For short-term storage (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. Avoid repeated freeze-thaw cycles to maintain protein integrity.
Purity
The purity of PGK1 is determined by SDS-PAGE analysis and is greater than 95%.
Biological Activity
The specific activity of PGK1 is determined to be greater than 600 units per milligram of protein. One unit of activity is defined as the amount of enzyme required to convert 1 micromole of 1,3-bisphosphoglycerate to 3-phosphoglycerate per minute at a pH of 8.0 and a temperature of 37°C.
Synonyms

Phosphoglycerate kinase 1, MGC117307, MGC142128, MGC8947, MIG10, PGKA.

Source
E.coli.
Amino Acid Sequence

MGSSHHHHHH SSGLVPRGSH MSLSNKLTLD KLDVKGKRVV MRVDFNVPMK NNQITNNQRI KAAVPSIKFC LDNGAKSVVL MSHLGRPDGV PMPDKYSLEP VAVELKSLLG KDVLFLKDCV GPEVEKACAN PAAGSVILLE NLRFHVEEEG KGKDASGNKV KAEPAKIEAF RASLSKLGDV YVNDAFGTAH RAHSSMVGVN LPQKAGGFLM KKELNYFAKA LESPERPFLA ILGGAKVADK IQLINNMLDK VNEMIIGGGM AFTFLKVLNN MEIGTSLFDE EGAKIVKDLM SKAEKNGVKI TLPVDFVTAD KFDENAKTGQ ATVASGIPAG WMGLDCGPES SKKYAEAVTR AKQIVWNGPV GVFEWEAFAR GTKALMDEVV KATSRGCITI IGGGDTATCC AKWNTEDKVS HVSTGGGASL ELLEGKVLPG VDALSNI

Product Science Overview

Structure and Expression

PGK1 is a monomeric enzyme composed of 417 amino acids . The human recombinant form of PGK1 is typically expressed in Escherichia coli or Spodoptera frugiperda (Sf 21) cells using baculovirus expression systems . The recombinant protein is often tagged with a His-tag to facilitate purification and detection .

Biological Activity

The recombinant PGK1 protein is biologically active and retains its enzymatic function. It is used in various biochemical assays to study glycolysis and energy metabolism . The specific activity of recombinant PGK1 can be measured by NADH production in a reaction coupled with glyceraldehyde-3-phosphate dehydrogenase (GAPDH) .

Applications

Recombinant PGK1 is widely used in research to:

  • Study the glycolytic pathway and its regulation.
  • Investigate the role of PGK1 in various diseases, including cancer and metabolic disorders.
  • Develop high-throughput screening assays for drug discovery .
Industrial Production

The production of recombinant PGK1 involves several steps:

  1. Gene Cloning: The PGK1 gene is cloned into an expression vector, which is then introduced into the host cells (e.g., E. coli or Sf 21 cells).
  2. Protein Expression: The host cells are cultured under conditions that induce the expression of the recombinant PGK1 protein.
  3. Protein Purification: The recombinant protein is purified using affinity chromatography, typically exploiting the His-tag .
  4. Quality Control: The purity and activity of the recombinant PGK1 are assessed using SDS-PAGE and enzymatic assays .
Research and Clinical Implications

PGK1 is not only a key player in glycolysis but also acts as a cofactor for polymerase alpha, indicating its involvement in DNA replication . Its role in cancer metabolism has garnered significant interest, as cancer cells often exhibit altered glycolytic activity. Understanding the function and regulation of PGK1 can provide insights into cancer biology and potential therapeutic targets .

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