RPAIN Human

RPA Interacting Protein Human Recombinant
Cat. No.
BT12780
Source
Escherichia Coli.
Synonyms
HRIP, RIP, RPA-interacting protein, hRIP, RPAIN.
Appearance
Sterile Filtered clear solution.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Usage

THE BioTek'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

RPAIN Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 129 amino acids (1-106 a.a.) and having a molecular mass of 14.7kDa.RPAIN is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Product Specs

Introduction
RPA-interacting protein isoform d (RPAIN), also known as RPA-associated protein 32, is a single-stranded DNA (ssDNA) binding protein involved in essential DNA processes like replication, repair, and recombination. It acts as an adapter protein, facilitating the transport of Replication Protein A (RPA) into the nucleus, a role typically carried out by importin proteins. RPAIN exhibits broad expression, with notable presence in pancreas, kidney, muscle, liver, lung, placenta, brain, heart, leukocytes, colon, intestine, ovary, testis, prostate, thymus, and spleen.
Description
Recombinant human RPAIN, produced in E. coli, is a single, non-glycosylated polypeptide chain consisting of 129 amino acids. This includes amino acids 1 to 106 of the RPAIN sequence and a 23 amino acid His-tag fused at the N-terminus. The protein has a molecular weight of 14.7 kDa and is purified using proprietary chromatographic techniques.
Physical Appearance
A clear solution, sterile-filtered for purity.
Formulation
The RPAIN protein solution is provided at a concentration of 0.25 mg/ml in a buffer consisting of 20mM Tris-HCl (pH 8.0), 0.2M NaCl, 40% glycerol, and 2mM DTT.
Stability
For short-term storage (up to 2-4 weeks), the protein should be kept at 4°C. For extended storage, it's recommended to freeze the protein at -20°C. Adding a carrier protein like HSA or BSA (0.1%) is advisable for long-term storage. To maintain protein integrity, avoid repeated cycles of freezing and thawing.
Purity
Analysis by SDS-PAGE confirms a purity greater than 95.0%.
Synonyms
HRIP, RIP, RPA-interacting protein, hRIP, RPAIN.
Source
Escherichia Coli.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSMAESLRS PRRSLYKLVG SPPWKEAFRQ RCLERMRNSR DRLLNRYRQA GSSGPGNSQN SFLVQEVMEE EWNALQSVEN CPEDLAQLEE LIDMAVLEEI QQELINQGL.

Product Science Overview

Structure and Function of RPA

RPA binds to ssDNA with high affinity, protecting it from nucleolytic degradation and preventing the formation of secondary structures that could impede DNA metabolism . The binding of RPA to ssDNA is essential for maintaining genome stability and facilitating the recruitment of other proteins involved in DNA transactions .

The RPA complex consists of several oligonucleotide/oligosaccharide binding (OB) domains, which are classified as either DNA-binding domains (DBDs) or protein-interaction domains. These domains enable RPA to interact with a variety of proteins and coordinate different DNA metabolic processes .

RPA Interacting Protein

RPA interacts with numerous proteins to regulate DNA metabolism. One such protein is the RPA Interacting Protein (RPA-IP), which plays a critical role in modulating the function of RPA. RPA-IP can access the ssDNA buried under RPA by remodeling one or more domains without displacing RPA . This interaction is crucial for the proper functioning of RPA in DNA replication and repair.

Human Recombinant RPA Interacting Protein

The human recombinant form of RPA Interacting Protein is produced using recombinant DNA technology. This involves cloning the gene encoding RPA-IP into an expression vector, which is then introduced into a host cell (such as E. coli or yeast) to produce the protein. The recombinant protein is subsequently purified for research and therapeutic applications.

Recombinant RPA-IP is used in various studies to understand its role in DNA metabolism and its potential as a therapeutic target. By studying the recombinant form, researchers can gain insights into the molecular mechanisms underlying the interaction between RPA and RPA-IP and develop strategies to modulate this interaction for therapeutic purposes.

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.