ACP2 Human

Acid Phosphatase-2 Human Recombinant
Cat. No.
BT26368
Source
Escherichia Coli.
Synonyms
Acid Phosphatase 2, Lysosoma, EC 3.1.3.2 LAP, Lysosomal Acid Phosphatase, ACP2.
Appearance
Sterile filtered colorless solution.
Purity
Greater than 85.0% 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

ACP2 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 373 amino acids (31-380 a.a.) and having a molecular mass of 42.9kDa.

ACP2 is fused to a 23 amino acid His-Tag at N-Terminus and purified by conventional chromatography techniques.

Product Specs

Introduction
Acid Phosphatase-2, also known as ACP2, is composed of two subunits, Alpha and beta. It is chemically and genetically distinct from red cell acid phosphatase. ACP2 belongs to a family of isoenzymes that hydrolyze orthophosphoric monoesters to alcohol and phosphate. Acid phosphatase deficiency is caused by mutations in the genes encoding the ACP2-beta and ACP3-alpha subunits.
Description
ACP2 Human Recombinant protein is produced in E. coli. It is a single, non-glycosylated polypeptide chain containing 373 amino acids (residues 31-380) with a molecular mass of 42.9 kDa. The protein is fused to a 23 amino acid His-Tag at the N-terminus and purified using conventional chromatography techniques.
Physical Appearance
Sterile, colorless solution.
Formulation
The ACP2 protein solution (1 mg/ml) is supplied in 20 mM Tris-HCl (pH 8.0) and 10% glycerol.
Stability
For short-term storage (2-4 weeks), store at 4°C. For long-term storage, freeze at -20°C. Adding a carrier protein (0.1% HSA or BSA) is recommended for long-term storage. Avoid repeated freeze-thaw cycles.
Purity
Greater than 85.0% purity as determined by SDS-PAGE.
Synonyms
Acid Phosphatase 2, Lysosoma, EC 3.1.3.2 LAP, Lysosomal Acid Phosphatase, ACP2.
Source
Escherichia Coli.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSRSLRFVT LLYRHGDRSP VKTYPKDPYQ EEEWPQGFGQ LTKEGMLQHW ELGQALRQRY HGFLNTSYHR QEVYVRSTDF DRTLMSAEAN LAGLFPPNGM QRFNPNISWQ PIPVHTVPIT EDRLLKFPLG PCPRYEQLQN ETRQTPEYQN ESSRNAQFLD MVANETGLTD LTLETVWNVY DTLFCEQTHG LRLPPWASPQ TMQRLSRLKD FSFRFLFGIY QQAEKARLQG GVLLAQIRKN LTLMATTSQL PKLLVYSAHD TTLVALQMAL DVYNGEQAPY ASCHIFELYQ EDSGNFSVEM YFRNESDKAP WPLSLPGCPH RCPLQDFLRL TEPVVPKDWQ QECQLASGPA DTE

Product Science Overview

Structure and Function

ACP2 is localized to the lysosomal membrane and is chemically and genetically distinct from red cell acid phosphatase . It plays a crucial role in the lysosomal degradation pathway, where it functions optimally at an acidic pH. The enzyme catalyzes the hydrolysis of phosphate monoesters, releasing phosphate and alcohol .

Genetic Information

The ACP2 gene is located on chromosome 11 and has several aliases, including LAP and EC 3.1.3.2 . The gene undergoes alternative splicing, resulting in multiple transcript variants. Additionally, a C-terminally extended isoform is predicted to be produced by the use of an alternative in-frame translation termination codon via a stop codon readthrough mechanism .

Biological Significance

ACP2 is essential for normal cellular function. Mice lacking this gene exhibit multiple defects, including bone structure alterations, lysosomal storage defects, and an increased tendency towards seizures . An enzymatically inactive allele of this gene in mice showed severe growth retardation, hair-follicle abnormalities, and an ataxia-like phenotype .

Clinical Relevance

The enzyme’s activity is used as a biochemical marker in various clinical settings. For instance, different forms of acid phosphatase are found in different organs, and their serum levels are used to evaluate the success of surgical treatment for prostate cancer . In the past, acid phosphatase levels were also used to diagnose prostate cancer .

Recombinant Production

Recombinant human ACP2 is produced using Escherichia coli expression systems. The recombinant protein is typically purified to a high degree, making it suitable for various biochemical assays and research applications .

Quick Inquiry

Personal Email Detected
Please use an institutional or corporate email address for inquiries. Personal email accounts ( such as Gmail, Yahoo, and Outlook) are not accepted. *
© Copyright 2024 Thebiotek. All Rights Reserved.