HNRNPAB Human

Heterogeneous Nuclear Ribonucleoprotein A/B Human Recombinant
Cat. No.
BT20674
Source
Escherichia Coli.
Synonyms
Heterogeneous Nuclear Ribonucleoprotein A/B, ABBP-1, ABBP1, APOBEC1-Binding Protein 1, HnRNP A/B, Apobec-1 Binding Protein 1, Apolipoprotein B MRNA Editing Enzyme, Catalytic Polypeptide 1-Binding Protein 1, HnRNP Type A/B Protein.
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. They may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
Shipped with Ice Packs
In Stock

Description

HNRNPAB Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 308 amino acids (1-285 a.a) and having a molecular mass of 33kDa.
HNRNPAB is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Product Specs

Introduction
Heterogeneous Nuclear Ribonucleoprotein A/B (HNRNPAB) belongs to a family of proteins known as heterogeneous nuclear ribonucleoproteins (hnRNPs), which are found in all tissues. These proteins are made using instructions from RNA polymerase II and are integral parts of heterogeneous nuclear RNA (hnRNA) complexes. They interact with pre-mRNAs within the cell nucleus and appear to influence the processing of pre-mRNAs, as well as other aspects of mRNA metabolism and movement. While all hnRNPs are located in the nucleus, some shuttle between the nucleus and the cytoplasm. HNRNPAB is noteworthy because it binds to a part of the multiprotein complex called the editosome. HNRNPAB possesses two repeating quasi-RRM (RNA recognition motif) domains that allow it to bind to RNAs. The protein's significance is further highlighted by its association with diseases like Wells syndrome and cystic fibrosis.
Description
Recombinant human HNRNPAB, produced in E. coli bacteria, is a single polypeptide chain that does not have any sugar molecules attached (non-glycosylated). It contains 308 amino acids, specifically amino acids 1 to 285, and has a molecular weight of 33kDa. For purification and detection purposes, a 23 amino acid His-tag is attached to the N-terminus of the HNRNPAB protein. Purification is achieved using specialized chromatographic methods.
Physical Appearance
A clear solution that has been sterilized by filtration.
Formulation
The HNRNPAB protein is supplied in a solution with a concentration of 0.25mg/ml. The solution also contains 30% glycerol and 1mM DTT to help stabilize the protein.
Stability
For short-term storage (2-4 weeks), keep the vial at 4°C. For longer storage, freeze the protein at -20°C. Adding a carrier protein like HSA or BSA to a final concentration of 0.1% is recommended for long-term storage. It is important to avoid repeatedly freezing and thawing the protein.
Purity
The purity of the HNRNPAB protein is greater than 95%, as determined by SDS-PAGE analysis.
Synonyms
Heterogeneous Nuclear Ribonucleoprotein A/B, ABBP-1, ABBP1, APOBEC1-Binding Protein 1, HnRNP A/B, Apobec-1 Binding Protein 1, Apolipoprotein B MRNA Editing Enzyme, Catalytic Polypeptide 1-Binding Protein 1, HnRNP Type A/B Protein.
Source
Escherichia Coli.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSMSEAGEE QPMETTGATE NGHEAVPEGE SPAGAGTGAA AGAGGATAAP PSGNQNGAEG DQINASKNEE DAGKMFVGGL SWDTSKKDLK DYFTKFGEVV DCTIKMDPNT GRSRGFGFIL FKDAASVEKV LDQKEHRLDG RVIDPKKAMA MKKDPVKKIF VGGLNPEATE EKIREYFGEF GEIEAIELPM DPKLNKRRGF VFITFKEEEP VKKVLEKKFH TVSGSKCEIK VAQPKEVYQQ QQYGSGGRGN RNRGNRGSGG GGGGGGQGST NYGKSQRRGG HQNNYKPY

Product Science Overview

Introduction

Heterogeneous Nuclear Ribonucleoproteins (hnRNPs) are a group of RNA-binding proteins that play crucial roles in the processing, metabolism, and transport of pre-mRNA in the nucleus. Among these, the hnRNP A/B family is particularly significant due to its involvement in various cellular processes and its association with several diseases, including cancer .

Structure and Classification

The hnRNP A/B family consists of four main subtypes: hnRNPA0, hnRNPA1, hnRNPA2/B1, and hnRNPA3. These proteins share a similar structure, typically comprising two RNA recognition motifs (RRMs) and a glycine-rich domain . The RRMs are responsible for binding to RNA, while the glycine-rich domain is involved in protein-protein interactions .

Biological Properties and Functions

HnRNP A/B proteins are produced by RNA polymerase II and are components of the heterogeneous nuclear RNA (hnRNA) complexes . They associate with nascent pre-mRNAs, packaging them into hnRNP particles. This arrangement is non-random and sequence-dependent, serving to condense and stabilize the transcripts and minimize tangling and knotting .

These proteins influence various aspects of mRNA metabolism, including splicing, transport, and translation . They are also involved in the regulation of gene expression and the maintenance of genomic stability .

Modes of Action

HnRNP A/B proteins function by recognizing specific nucleic acid sequences and guiding the hnRNPs to interact with target genes or other proteins . They play a critical role in almost every step of the RNA life cycle, from transcription to translation .

Regulatory Mechanisms

The expression and activity of hnRNP A/B proteins are tightly regulated at multiple levels, including transcriptional, post-transcriptional, and post-translational modifications . Aberrant expression or mutations in these proteins can lead to various diseases, particularly cancer .

Clinical Significance

HnRNP A/B proteins have been identified as promising biomarkers and therapeutic targets for cancer . Their dynamic changes in expression are closely associated with cancer initiation and progression . Inhibitors targeting hnRNP A/B are being explored for clinical use, with several compounds showing potential in cancer therapy .

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.