ADPRH Human

ADP-Ribosylarginine Hydrolase Human Recombinant
Cat. No.
BT26700
Source
E.coli.
Synonyms
[Protein ADP-ribosylarginine] hydrolase, ADP-ribosylarginine hydrolase, ADP-ribose-L-arginine cleaving enzyme, ADPRH, ARH1.
Appearance
Sterile Filtered colorless solution.
Purity
Greater than 90% 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

ADPRH Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 381 amino acids (1-357) and having a molecular mass of 42.1kDa.
ADPRH is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Product Specs

Introduction
ADP-ribosylarginine hydrolase (ADPRH) is an enzyme that plays a crucial role in the ADP-ribosylation cycle by removing mono-ADP-ribose from arginine residues in proteins. This process is essential for regulating protein function. Unlike rat and mouse ADPRH, the human enzyme does not require DTT for optimal activity.
Description
This product consists of the recombinant human ADPRH enzyme, produced in E.coli. It is a single, non-glycosylated polypeptide chain with 381 amino acids (residues 1-357) and a molecular weight of 42.1 kDa. The enzyme has a His-tag fused to its N-terminus for purification purposes. Purification is achieved through proprietary chromatographic techniques.
Physical Appearance
A clear, colorless solution that has been sterilized by filtration.
Formulation
This ADPRH solution is provided at a concentration of 0.5mg/ml in a buffer containing 20mM Tris-HCl (pH 8.0), 10% glycerol, 1mM DTT, and 100mM NaCl.
Stability
For short-term storage (up to 4 weeks), the product can be kept at 4°C. For longer storage, freezing at -20°C is recommended. Adding a carrier protein (0.1% HSA or BSA) is advisable for long-term storage. Avoid repeated freeze-thaw cycles to maintain product integrity.
Purity
The purity of this product is greater than 90%, as determined by SDS-PAGE analysis.
Synonyms
[Protein ADP-ribosylarginine] hydrolase, ADP-ribosylarginine hydrolase, ADP-ribose-L-arginine cleaving enzyme, ADPRH, ARH1.
Source
E.coli.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSHMEKYVA AMVLSAAGDA LGYYNGKWEF LQDGEKIHRQ LAQLGGLDAL DVGRWRVSDD TVMHLATAEA LVEAGKAPKL TQLYYLLAKH YQDCMEDMDG RAPGGASVHN AMQLKPGKPN GWRIPFNSHE GGCGAAMRAM CIGLRFPHHS QLDTLIQVSI ESGRMTHHHP TGYLGALASA LFTAYAVNSR PPLQWGKGLM ELLPEAKKYI VQSGYFVEEN LQHWSYFQTK WENYLKLRGI LDGESAPTFP ESFGVKERDQ FYTSLSYSGW GGSSGHDAPM IAYDAVLAAG DSWKELAHRA FFHGGDSDST AAIAGCWWGV MYGFKGVSPS NYEKLEYRNR
LEETARALYS LGSKEDTVIS L.

Product Science Overview

Gene and Protein Information

The ADPRH gene encodes the ADP-Ribosylarginine Hydrolase enzyme. This gene is located on chromosome 3 in humans and is a protein-coding gene . The enzyme is also known by several other names, including ARH1 and ADP-ribosylhydrolase .

Function and Mechanism

ADPRH functions by hydrolyzing the ADP-ribosyl-arginine bond, thereby reversing the ADP-ribosylation modification. This activity is crucial for the regulation of protein function and cellular processes. Unlike the rat and mouse enzymes that require dithiothreitol (DTT) for maximal activity, the human enzyme is DTT-independent .

Biological Significance

ADP-ribosylation is involved in various cellular processes, including DNA repair, gene expression, and signal transduction. The removal of ADP-ribose by ADPRH is essential for maintaining the balance of these modifications and ensuring proper cellular function .

Clinical Relevance

Mutations or dysregulation of the ADPRH gene have been associated with certain diseases, such as Glycine N-Methyltransferase Deficiency and Tyrosinemia . Understanding the function and regulation of ADPRH can provide insights into these conditions and potential therapeutic targets.

Recombinant ADPRH

Recombinant ADP-Ribosylarginine Hydrolase is produced using recombinant DNA technology, which involves inserting the human ADPRH gene into a suitable expression system, such as bacteria or yeast. This allows for the production of large quantities of the enzyme for research and therapeutic purposes.

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