PAPP A Human

Pregnancy-Associated Plasma Protein-1 Human Recombinant
Cat. No.
BT26160
Source
Escherichia Coli.
Synonyms

Pappalysin-1, Pregnancy-associated plasma protein A, PAPP-A, IGF-dependent IGFBP-4 protease, IGFBP-4ase, PAPPA, PAPA, DIPLA1, PAPPA1, ASBABP2.

Appearance
Sterile Filtered clear solution.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Usage
Prospec'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

PAPP-A Human Recombinant produced in E.Coli is single, a non-glycosylated, Polypeptide chain containing 191 amino acids fragment (81-271) corresponding to the PAPP-A “Jelly-Roll” domain fragment, having a total molecular mass of 25.75kDa and fused with an amino-terminal hexahistidine tag.

The PAPP-A is purified by proprietary chromatographic techniques.

Product Specs

Introduction
Pregnancy-associated plasma protein A (PAPP-A) is a large zinc-dependent metalloproteinase that plays a role in regulating insulin-like growth factor (IGF) bioavailability. PAPP-A cleaves IGF binding proteins (IGFBPs), particularly IGFBP-4 and IGFBP-5, releasing bound IGFs and enhancing their activity. This process is crucial in various biological systems, including the ovaries, cardiovascular system, wound healing, and bone remodeling. Elevated PAPP-A levels are linked to conditions like unstable angina and myocardial infarction, while low levels are associated with fetal chromosomal abnormalities, pre-eclampsia, and stillbirth. During pregnancy, PAPP-A is produced in high concentrations by the placenta, and its levels rise throughout gestation. The protein's proteolytic activity can be inhibited by targeting specific binding sites.
Description

This product consists of the recombinant PAPP-A 'Jelly-Roll' domain (amino acids 81-271) produced in E. coli. It is a non-glycosylated polypeptide chain with an amino-terminal hexahistidine tag, resulting in a molecular mass of 25.75 kDa. The protein is purified using proprietary chromatographic techniques.

Physical Appearance
A clear, sterile-filtered solution.
Formulation

The PAPP-A protein is supplied in a buffer consisting of 20mM Tris-HCl (pH 8.0), 4M Urea, and 50% Glycerol.

Stability
For short-term storage (up to 4 weeks), the product can be stored at 4°C. For extended periods, store frozen at -20°C. Avoid repeated freeze-thaw cycles.
Purity
The purity of this product is greater than 95%, as determined by SDS-PAGE analysis.
Synonyms

Pappalysin-1, Pregnancy-associated plasma protein A, PAPP-A, IGF-dependent IGFBP-4 protease, IGFBP-4ase, PAPPA, PAPA, DIPLA1, PAPPA1, ASBABP2.

Source
Escherichia Coli.

Product Science Overview

Function and Mechanism

PAPP-A’s proteolytic activity is activated upon binding to collagen . It plays a crucial role in local proliferative processes such as wound healing and bone remodeling . The enzyme catalyzes the cleavage of the Met135-Lys bond in IGFBP-4 and the Ser143-Lys bond in IGFBP-5 .

Clinical Significance

PAPP-A is widely used in prenatal screening tests for Down syndrome . Low levels of PAPP-A in maternal serum during the first trimester are associated with an increased risk of chromosomal abnormalities, including Down syndrome . Additionally, low PAPP-A levels can indicate potential complications with the placenta, such as intrauterine growth restriction, preeclampsia, placental abruption, premature birth, or fetal death .

Recombinant PAPP-A

Recombinant PAPP-A is produced using recombinant DNA technology, which allows for the expression of the human PAPP-A protein in various host cells. This recombinant form is used in research and clinical applications to study its function and potential therapeutic uses .

Research and Applications

Studies have shown that PAPP-A interacts with major basic protein and is involved in various physiological processes . Research continues to explore its role in different conditions and its potential as a biomarker for various diseases .

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