DHPS Human

Deoxyhypusine Synthase Human Recombinant
Cat. No.
BT23777
Source
Escherichia Coli.
Synonyms
MIG13, EC 2.5.1.46, Deoxyhypusine synthase, DHS, DHPS, DS.
Appearance
Sterile Filtered clear colorless solution.
Purity
Greater than 95% 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

DHPS Human Recombinant fused to 20 amino acid His Tag at N-terminal produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 389 amino acids (1-369 a.a.) and having a molecular mass of 43.1 kDa. The DHPS is purified by proprietary chromatographic techniques.

Product Specs

Introduction
Deoxyhypusine synthase (DHPS) is an enzyme that plays a crucial role in the first step of hypusine biosynthesis, a unique post-translational modification essential for the eukaryotic translation initiation factor 5A (eIF5A) activity. DHPS catalyzes the NAD-dependent transfer of the butylamine moiety from spermidine to a specific lysine residue on the eIF5A precursor protein, resulting in the formation of the deoxyhypusine intermediate.
Description
Recombinant human DHPS, expressed in E. coli, is a single, non-glycosylated polypeptide chain. This protein, with a molecular weight of 43.1 kDa, comprises 389 amino acids, including a 20 amino acid His tag at the N-terminus (1-369 a.a. of the DHPS sequence). Purification is achieved through proprietary chromatographic techniques, ensuring high purity.
Physical Appearance
The product is a clear, colorless solution that has been sterilized by filtration.
Formulation
The DHPS protein is supplied in a solution containing 20mM Tris-HCl (pH 8), 0.1M NaCl, and 20% glycerol.
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. To ensure stability during long-term storage, consider adding a carrier protein (0.1% HSA or BSA). Avoid repeated freeze-thaw cycles.
Purity
The purity of the DHPS protein is greater than 95%, as determined by SDS-PAGE analysis.
Synonyms
MIG13, EC 2.5.1.46, Deoxyhypusine synthase, DHS, DHPS, DS.
Source
Escherichia Coli.
Amino Acid Sequence

MGSSHHHHHH SSGLVPRGSH MEGSLEREAP AGALAAVLKH SSTLPPESTQ VRGYDFNRGV NYRALLEAFG TTGFQATNFG RAVQQVNAMI EKKLEPLSQD EDQHADLTQS RRPLTSCTIF LGYTSNLISS GIRETIRYLV QHNMVDVLVT TAGGVEEDLI KCLAPTYLGE FSLRGKELRE NGINRIGNLL VPNENYCKFE DWLMPILDQM VMEQNTEGVK WTPSKMIARL GKEINNPESV YYWAQKNHIP VFSPALTDGS LGDMIFFHSY KNPGLVLDIV EDLRLINTQA IFAKCTGMII LGGGVVKHHI ANANLMRNGA DYAVYINTAQ EFDGSDSGAR PDEAVSWGKI RVDAQPVKVY ADASLVFPLL VAETFAQKMD AFMHEKNED.

Product Science Overview

Enzymatic Function and Mechanism

DHS catalyzes the first step in the biosynthesis of hypusine, a unique amino acid. The reaction involves the transfer of a 4-aminobutyl moiety from spermidine to a specific lysine residue on the eIF5A precursor, forming deoxyhypusine. This reaction can be summarized as follows :

[ \text{[eIF5A-precursor]-lysine} + \text{spermidine} \rightleftharpoons \text{[eIF5A-precursor]-deoxyhypusine} + \text{propane-1,3-diamine} ]

The enzyme uses NAD+ as a cofactor, which is reduced to NADH during the reaction .

Genetic and Structural Information

In humans, DHS is encoded by the DHPS gene, located on chromosome 19 . The human DHS protein consists of 369 amino acids and has a molecular mass of approximately 41 kDa . The enzyme’s structure includes a binding site for NAD+ and spermidine, which are essential for its catalytic activity.

Recombinant Expression

Recombinant DHS can be expressed in various systems, including Escherichia coli. The recombinant protein is often tagged with histidine to facilitate purification through nickel-chelate affinity chromatography . This method allows for the isolation of DHS under denaturing conditions, ensuring high purity and activity.

Biological Significance

The hypusine modification catalyzed by DHS is critical for the function of eIF5A, which is involved in multiple cellular processes, including mRNA translation, cell proliferation, and apoptosis . Dysregulation of DHS activity has been linked to various diseases, including cancer and neurodegenerative disorders.

Research and Therapeutic Potential

Due to its essential role in cell proliferation, DHS is a potential target for therapeutic intervention. Inhibitors of DHS, such as N-guanyl-1,7-diaminoheptane (GC7), have been shown to suppress its activity significantly . These inhibitors are being explored for their potential in treating diseases characterized by uncontrolled cell growth, such as cancer .

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