ASPA Human

Aspartoacylase Human Recombinant
Cat. No.
BT22638
Source
E.coli.
Synonyms

Aspartoacylase, Aminoacylase-2, ACY-2, ASPA, ACY2, ASP

Appearance
Sterile Filtered colorless solution.
Purity

Greater than 90.0% 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

ASPA Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 313 amino acids (1-313) and having a molecular mass of 35.7 kDa.
ASPA is purified by proprietary chromatographic techniques.

Product Specs

Introduction
Aspartoacylase, also known as ASPA, is a protein present in various tissues, including skeletal muscle, cerebral white matter, kidney, liver, and lungs. It functions as a homodimer, catalyzing the deacetylation of N-acetylaspartic acid (NAA) to produce L-aspartate and acetate.
Description
Recombinant human ASPA, expressed in E. coli, is a single, non-glycosylated polypeptide chain consisting of 313 amino acids (1-313) with a molecular weight of 35.7 kDa. The protein is purified using proprietary chromatographic methods.
Physical Appearance
Clear, colorless solution, sterile-filtered.
Formulation
The ASPA solution is provided at a concentration of 1 mg/ml in a buffer containing 10% glycerol and phosphate-buffered saline (pH 7.4).
Stability
For short-term storage (2-4 weeks), the solution should be kept at 4°C. For extended storage, it is recommended to freeze the solution at -20°C. Adding a carrier protein like 0.1% HSA or BSA is advisable for long-term storage. Repeated freezing and thawing should be avoided.
Purity
The purity of ASPA is greater than 90.0% as determined by SDS-PAGE analysis.
Synonyms

Aspartoacylase, Aminoacylase-2, ACY-2, ASPA, ACY2, ASP

Source
E.coli.
Amino Acid Sequence

MTSCHIAEEH IQKVAIFGGT HGNELTGVFL VKHWLENGAE IQRTGLEVKP FITNPRAVKK CTRYIDCDLN RIFDLENLGK KMSEDLPYEV RRAQEINHLF GPKDSEDSYD IIFDLHNTTS NMGCTLILED SRNNFLIQMF HYIKTSLAPL PCYVYLIEHP SLKYATTRSI AKYPVGIEVG PQPQGVLRAD ILDQMRKMIK HALDFIHHFN EGKEFPPCAI EVYKIIEKVD YPRDENGEIA AIIHPNLQDQ DWKPLHPGDP MFLTLDGKTI PLGGDCTVYP VFVNEAAYYE KKEAFAKTTK LTLNAKSIRC CLH

Product Science Overview

Introduction

Aspartoacylase, also known as ASPA, is a hydrolytic enzyme that plays a crucial role in the metabolism of N-acetyl-L-aspartic acid (NAA). This enzyme is encoded by the ASPA gene in humans and is primarily found in the brain. Aspartoacylase catalyzes the deacylation of NAA to produce aspartate and acetate .

Structure and Function

Aspartoacylase is a zinc-dependent hydrolase that promotes the deprotonation of water to use as a nucleophile, a mechanism similar to many other zinc-dependent hydrolases . The enzyme is a dimer composed of two identical monomers, each consisting of 313 amino acids. Each monomer has two distinct domains: the N-terminal domain (residues 1-212) and the C-terminal domain (residues 213-313) .

The primary function of aspartoacylase is to regulate the levels of NAA in the brain. NAA is abundant in the brain and is involved in maintaining white matter integrity. The hydrolysis of NAA by aspartoacylase is essential for the proper functioning of the central nervous system .

Clinical Significance

Mutations in the ASPA gene can lead to a rare autosomal recessive neurodegenerative disorder known as Canavan disease. This condition is characterized by the accumulation of NAA in the brain, leading to spongy degeneration of the white matter. Canavan disease results in severe developmental delays, motor dysfunction, and early mortality .

Recombinant Aspartoacylase

Human recombinant aspartoacylase is produced using recombinant DNA technology, which involves inserting the ASPA gene into a suitable expression system, such as bacteria or yeast. This allows for the large-scale production of the enzyme for research and therapeutic purposes. Recombinant aspartoacylase is used in studies to understand the enzyme’s structure, function, and role in diseases like Canavan disease .

Research and Applications

Research on aspartoacylase has provided valuable insights into its role in the brain and its involvement in neurological disorders. Studies have shown that aspartoacylase activity is crucial for the maintenance of white matter and the proper functioning of oligodendrocytes, the cells responsible for myelination in the central nervous system .

In addition to its role in the brain, aspartoacylase has been implicated in the metabolic reprogramming of cancer cells. Recent studies suggest that ASPA may play a role in tumor development and progression, making it a potential target for cancer therapy .

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