NANP Human

N-Acetylneuraminic Acid Phosphatase Human Recombinant

Cat. No.

BT29507

Source

Escherichia Coli.

Synonyms

N-acylneuraminate-9-phosphatase, Haloacid dehalogenase-like hydrolase domain-containing protein 4, Neu5Ac-9-Pase, NANP, HDHD4, MGC26833, C20orf147, dJ694B14.3.

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.

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Description

NANP Human Recombinant fused with a 36 amino acid His tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 284 amino acids (1-248 a.a.) and having a molecular mass of 31.9kDa. The NANP is purified by proprietary chromatographic techniques.

Product Specs

Introduction

N-acylneuraminate-9-phosphatase (NANP) is an enzyme within the haloacid dehalogenase (HAD) family. It catalyzes the dephosphorylation of N-acylneuraminate 9-phosphate, resulting in the formation of N-acylneuraminate. This reaction can be represented as: N-acylneuraminate 9-phosphate + H2O = N-acylneuraminate + phosphate. NANP requires magnesium for its catalytic activity, and its activity is inhibited by vanadate and calcium, which is characteristic of HAD phosphatases.

Description

Recombinant human NANP, expressed in E. coli, is a purified protein with a 36 amino acid His tag added to the N-terminus. This single, non-glycosylated polypeptide chain contains 284 amino acids (residues 1-248) and has a molecular weight of 31.9 kDa. The purification process utilizes proprietary chromatographic methods.

Physical Appearance

A clear, colorless solution that has been sterilized by filtration.

Formulation

This solution contains NANP at a concentration of 0.5 mg/ml in a 20mM Tris-HCl buffer (pH 8.0) with 10% glycerol, 2mM DTT, and 100mM NaCl.

Stability

For optimal storage, the product should be kept at 4°C if it will be used within 2-4 weeks. For longer storage periods, it is recommended to store the product frozen at -20°C. To further enhance long-term stability, adding a carrier protein such as HSA or BSA to a final concentration of 0.1% is advised. Repeated freezing and thawing of the product should be avoided.

Purity

Purity is determined by SDS-PAGE analysis and is guaranteed to be greater than 90.0%.

Synonyms

N-acylneuraminate-9-phosphatase, Haloacid dehalogenase-like hydrolase domain-containing protein 4, Neu5Ac-9-Pase, NANP, HDHD4, MGC26833, C20orf147, dJ694B14.3.

Source

Escherichia Coli.

Amino Acid Sequence

MRGSHHHHHH GMASMTGGQQ MGRDLYDDDD KDRWGSMGLS RVRAVFFDLD NTLIDTAGAS RRGMLEVIKL LQSKYHYKEE AEIICDKVQV KLSKECFHPY NTCITDLRTS HWEEAIQETK GGAANRKLAE ECYFLWKSTR LQHMTLAEDV KAMLTELRKE VRLLLLTNGD RQTQREKIEA CACQSYFDAV VVGGEQREEK PAPSIFYYCC NLLGVQPGDC VMVGDTLETD IQGGLNAGLK ATVWINKNGI VPLKSSPVPH YMVSSVLELP ALLQSIDCKV SMST.

Product Science Overview

Enzymatic Function

NANP catalyzes the dephosphorylation of N-acetylneuraminic acid 9-phosphate (Neu5Ac-9-P) to produce free Neu5Ac and phosphate . This reaction is essential in the biosynthesis pathway of sialic acids, as Neu5Ac-9-P is an intermediate product formed by the condensation of N-acetylmannosamine 6-phosphate (ManNAc-6-P) with phosphoenolpyruvate (PEP), catalyzed by Neu5Ac-9-P synthase (NANS).

Biological Importance

Sialic acids, including Neu5Ac, are critical for various biological functions, such as protein-protein and cell-cell recognition. They are found on the surface of cells and are involved in numerous physiological and pathological processes, including immune response, microbial pathogenesis, and cancer metastasis.

Gene and Protein Structure

The human NANP gene is located on chromosome 20 at position 20p11.21 and consists of two exons. The gene encodes a protein of 248 amino acids with a predicted molecular mass of approximately 27.8 kDa . The protein belongs to the haloacid dehalogenase (HAD) superfamily of hydrolases, characterized by three conserved motifs essential for its phosphatase activity.

Expression and Regulation

NANP expression is tissue-specific and regulated by various factors, including the availability of substrates and cofactors. The enzyme’s activity is dependent on the presence of magnesium ions (Mg²⁺) and is inhibited by vanadate and calcium ions (Ca²⁺), which is typical for members of the HAD family.

Clinical Relevance

Alterations in NANP activity or expression can have significant implications for human health. For instance, dysregulation of sialic acid metabolism has been associated with various diseases, including cancer and infectious diseases. Understanding the function and regulation of NANP can provide insights into potential therapeutic targets for these conditions.

Recombinant Production

Human recombinant NANP is produced using recombinant DNA technology, which involves cloning the NANP gene into an expression vector, transforming it into a suitable host cell (such as E. coli), and purifying the expressed protein. This recombinant enzyme is used in research to study its biochemical properties and potential applications in biotechnology and medicine.

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NANP Human

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