PRAP1 Human

Proline-Rich Acidic Protein 1 Human Recombinant
Cat. No.
BT8556
Source
Escherichia Coli.
Synonyms
Proline-rich acidic protein 1, Epididymis tissue protein Li 178, Uterine-specific proline-rich acidic protein, PRAP1, UPA, PRO1195.
Appearance
Filtered White lyophilized (freeze-dried) powder.
Purity
Greater than 85.0% as determined by SDS-PAGE.
Usage
Prospec's products are furnished for LABORATORY RESEARCH USE ONLY. They may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
Shipped with Ice Packs
In Stock

Description

PRAP1 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain (a.a 21-151) containing 141 amino acids including a 10 a.a N-terminal His tag. The total molecular mass is 16.2kDa (calculated).

Product Specs

Introduction
Proline-rich acidic protein 1 (PRAP1) plays a crucial role in maintaining the balance and function of epithelial cells, particularly in the liver and gastrointestinal tract. This protein is found in high concentrations within the epithelial cells of various organs, including the liver, kidney, gastrointestinal tract, and cervix. Studies have shown a significant decrease in PRAP1 levels in hepatocellular carcinoma (liver cancer) and right colon adenocarcinoma (colon cancer) compared to healthy tissues in the respective organs.
Description
Recombinant human PRAP1, produced in E. coli, is a single, non-glycosylated polypeptide chain consisting of 141 amino acids (amino acids 21-151). It includes a 10 amino acid N-terminal His tag and has a calculated molecular weight of 16.2 kDa.
Physical Appearance
White powder, lyophilized (freeze-dried), and filtered.
Formulation
PRAP1 is supplied as a lyophilized powder, filtered through a 0.4 μm filter. The protein was initially prepared in a 0.05 M phosphate buffer with 0.075 M NaCl at pH 7.4, at a concentration of 0.5 mg/ml, before lyophilization.
Solubility
To create a working stock solution, add deionized water to the lyophilized pellet to achieve an approximate concentration of 0.5 mg/ml. Allow sufficient time for the pellet to dissolve completely. Please note that PRAP1 is not sterile. Before using it in cell culture, filter the solution through an appropriate sterile filter.
Stability
Store the lyophilized protein at -20°C. After reconstituting the protein, aliquot and store it to prevent repeated freeze-thaw cycles. The reconstituted protein remains stable at 4°C for a limited period and shows no significant changes for up to two weeks when stored at this temperature.
Purity
The purity of PRAP1 is determined to be greater than 85.0% by SDS-PAGE analysis.
Synonyms
Proline-rich acidic protein 1, Epididymis tissue protein Li 178, Uterine-specific proline-rich acidic protein, PRAP1, UPA, PRO1195.
Source
Escherichia Coli.
Amino Acid Sequence
MKHHHHHHASVPAPKVPIKM QVKHWPSEQD PEKAWGARVV EPPEKDDQLV VLFPVQKPKL LTTEEKPRGQ GRGPILPGTK AWMETEDTLG HVLSPEPDHD SLYHPPPEED QGEERPRLWV MPNHQVLLGP EEDQDHIYHP Q.

Product Science Overview

Introduction

Proline-Rich Acidic Protein 1 (PRAP1) is a protein encoded by the PRAP1 gene in humans. This protein is known for its significant role in various physiological processes, particularly in epithelial cells. The recombinant form of this protein is produced through biotechnological methods to study its functions and potential therapeutic applications.

Gene and Protein Structure

The PRAP1 gene is located on chromosome 10 and encodes a protein that is rich in proline and acidic amino acids. The protein is characterized by its ability to bind lipids, which is crucial for its role in lipid absorption and metabolism . The gene is also known by several aliases, including Uterine-Specific Proline-Rich Acidic Protein and Epididymis Secretory Sperm Binding Protein .

Functions and Mechanisms

PRAP1 is involved in several critical biological processes:

  1. Lipid Metabolism: PRAP1 facilitates the transfer of lipids, particularly triglycerides and phospholipids, by interacting with microsomal triglyceride transfer protein (MTTP). This interaction is essential for the assembly and secretion of apoB lipoproteins .
  2. Cell Protection: The protein plays a protective role in the gastrointestinal epithelium, safeguarding it from irradiation-induced apoptosis. This function is particularly important in maintaining the integrity of the gastrointestinal barrier .
  3. DNA Damage Response: PRAP1 is involved in the p53-mediated DNA damage response, which leads to cell cycle arrest and the prevention of apoptosis. This mechanism is crucial for maintaining cellular homeostasis and preventing the development of cancer .
Expression and Localization

PRAP1 is abundantly expressed in the epithelial cells of various organs, including the liver, kidney, gastrointestinal tract, and cervix . Its expression is regulated by several factors, including hormonal signals and environmental stressors.

Clinical Significance

The role of PRAP1 in lipid metabolism and cell protection makes it a potential target for therapeutic interventions. For instance, enhancing PRAP1 expression could be a strategy to protect the gastrointestinal tract from damage during cancer treatments involving radiation . Additionally, its involvement in lipid metabolism suggests that it could be a target for treating metabolic disorders.

Research and Applications

Recombinant PRAP1 is used in various research applications to study its functions and potential therapeutic uses. By producing the protein in a controlled environment, researchers can investigate its interactions, mechanisms, and effects in detail. This research is crucial for developing new treatments for diseases related to lipid metabolism and epithelial cell protection.

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