RBKS Human

Ribokinase Human Recombinant
Cat. No.
BT14569
Source
Escherichia Coli.
Synonyms
Ribokinase, RBKS, RBSK, DKFZp686G13268.
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.
Shipped with Ice Packs
In Stock

Description

RBKS Human Recombinant fused with a 20 amino acid His tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 342 amino acids (1-322 a.a.) and having a molecular mass of 36.3kDa. The RBKS is purified by proprietary chromatographic techniques.

Product Specs

Introduction
Ribokinase (RBKS) plays a crucial role in ribose metabolism by catalyzing the phosphorylation of ribose into ribose-5-phosphate. This enzymatic reaction requires the presence of ATP and magnesium. RBKS belongs to the pfkB family of carbohydrate kinases.
Description
Recombinant human RBKS, expressed in E. coli, is a purified protein with a His tag attached to its N-terminus. This non-glycosylated polypeptide consists of 342 amino acids (with the first 322 amino acids representing the RBKS sequence) and has a molecular weight of 36.3 kDa. Purification is achieved using proprietary chromatographic techniques.
Physical Appearance
Clear, colorless solution, sterile-filtered.
Formulation
The RBKS protein is supplied in a solution at a concentration of 1 mg/ml. The solution contains 20mM Tris-HCl buffer at pH 8.0 and 10% glycerol.
Stability
For optimal storage, the entire vial should be stored at 4°C if it will be used within 2 to 4 weeks. For longer storage, it is recommended to store the protein frozen at -20°C. To further enhance long-term stability during frozen storage, adding a carrier protein such as 0.1% HSA or BSA is advised. Repeated freezing and thawing cycles should be avoided.
Purity
The purity of RBKS is greater than 95% as determined by SDS-PAGE analysis.
Synonyms
Ribokinase, RBKS, RBSK, DKFZp686G13268.
Source
Escherichia Coli.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MAASGEPQRQ WQEEVAAVVV VGSCMTDLVS LTSRLPKTGE TIHGHKFFIG FGGKGANQCV QAARLGAMTS MVCKVGKDSF GNDYIENLKQ NDISTEFTYQ TKDAATGTAS IIVNNEGQNI IVIVAGANLL LNTEDLRAAA NVISRAKVMV CQLEITPATS LEALTMARRS GVKTLFNPAP AIADLDPQFY TLSDVFCCNE SEAEILTGLT VGSAADAGEA ALVLLKRGCQ VVIITLGAEG CVVLSQTEPE PKHIPTEKVK AVDTTGAGDS FVGALAFYLA YYPNLSLEDM LNRSNFIAAV SVQAAGTQSS YPYKKDLPLT LF.

Product Science Overview

Introduction

Ribokinase is a carbohydrate kinase enzyme that plays a crucial role in the metabolism of ribose, a five-carbon sugar. This enzyme catalyzes the phosphorylation of ribose to ribose-5-phosphate, a key intermediate in the pentose phosphate pathway. The human recombinant form of ribokinase is produced through recombinant DNA technology, allowing for the study and utilization of this enzyme in various research and therapeutic applications.

Discovery and Identification

The gene responsible for ribokinase in human cells was identified through comparative studies with the ribokinase from Escherichia coli. Researchers used BLAST searches to find a human protein with significant similarity to the bacterial ribokinase . The cDNA for this human protein was expressed in E. coli, and the recombinant protein was found to efficiently phosphorylate ribose to ribose-5-phosphate using ATP, confirming its identity as ribokinase .

Structure and Function

Ribokinase belongs to the PfkB family of carbohydrate kinases, which includes enzymes such as adenosine kinase, inosine-guanosine kinase, fructokinase, and phosphofructokinase . Despite the low sequence identity among PfkB family members, they exhibit remarkably high structural similarity. The catalytic activity of ribokinase is dependent on the presence of inorganic phosphate, similar to other kinases in this family .

The enzyme specifically phosphorylates ribose and shows very little to no activity towards other sugars such as D-arabinose, D-xylose, D-fructose, and D-galactose . This specificity is crucial for its role in ribose metabolism.

Biological Significance

Ribokinase plays a vital role in the pentose phosphate pathway, which is essential for the production of nucleotides and nucleic acids. Ribose-5-phosphate, the product of the ribokinase-catalyzed reaction, is a precursor for the synthesis of nucleotides, which are the building blocks of DNA and RNA .

Exogenous ribose has been shown to have beneficial effects in various studies. It enhances cardiac and muscular performance and accelerates the repletion of ATP in myocardial and endothelial cells . Ribose supplementation has also been reported to improve neurological symptoms in patients with adenylosuccinase deficiency .

Applications

The human recombinant form of ribokinase is used in research to study its structure, function, and role in metabolism. It is also utilized in therapeutic applications, particularly in conditions where ribose metabolism is impaired. The production of human recombinant ribokinase through recombinant DNA technology allows for the large-scale production of this enzyme, facilitating its use in various scientific and medical fields.

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