RBBP4 Human

Retinoblastoma Binding Protein 4 Human Recombinant
Cat. No.
BT14247
Source
E.coli.
Synonyms
Histone-binding protein RBBP4, Chromatin assembly factor 1 subunit C, CAF-1 subunit C, Chromatin assembly factor I p48 subunit, CAF-I 48 kDa subunit, CAF-I p48, Nucleosome-remodeling factor subunit RBAP48, Retinoblastoma-binding protein 4, RBBP-4, Retinoblastoma-binding protein p48, RBBP4, RBAP48, NURF55.
Appearance
Sterile Filtered colorless solution.
Purity
Greater than 90% 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.
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Description

RBBP4 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 449 amino acids (1-425 a.a) and having a molecular mass of 50.2kDa.
RBBP4 is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Product Specs

Introduction
Retinoblastoma binding protein 4 (RBBP4), also known as RbAp48, is a ubiquitously expressed nuclear protein that belongs to a highly conserved family of WD-repeat proteins. It plays a crucial role in various cellular processes, including histone acetylation, chromatin assembly, and transcriptional regulation. RBBP4 is found in protein complexes involved in histone acetylation and chromatin assembly, contributing to the regulation of gene expression. Moreover, it is an integral component of co-repressor complexes, which are essential for transcriptional silencing. RBBP4 interacts directly with retinoblastoma protein (pRb), a tumor suppressor protein, to modulate cell proliferation. Furthermore, it is associated with the Mi-2 complex, involved in chromatin remodeling and transcriptional repression linked to histone deacetylation.
Description
Recombinant human RBBP4, expressed in E. coli, is a single, non-glycosylated polypeptide chain. This protein consists of 449 amino acids, encompassing residues 1 to 425, and has a molecular weight of 50.2 kDa. The recombinant protein includes a 24-amino acid His-tag fused at the N-terminus to facilitate purification. The purification process employs proprietary chromatographic techniques, ensuring high purity.
Physical Appearance
Clear, colorless solution, sterile-filtered.
Formulation
The RBBP4 protein solution is provided at a concentration of 0.5 mg/ml in a buffer consisting of 20 mM Tris-HCl (pH 8.0), 0.1 M NaCl, 10% glycerol, and 1 mM EDTA.
Stability
For short-term storage (up to 2-4 weeks), the protein solution should be stored at 4°C. For long-term storage, it is recommended to store the solution at -20°C. To enhance stability during long-term storage, the addition of a carrier protein like HSA or BSA (0.1%) is advised. It's important to avoid repeated freeze-thaw cycles to maintain protein integrity.
Purity
The purity of RBBP4 is determined by SDS-PAGE analysis and is consistently greater than 90%.
Synonyms
Histone-binding protein RBBP4, Chromatin assembly factor 1 subunit C, CAF-1 subunit C, Chromatin assembly factor I p48 subunit, CAF-I 48 kDa subunit, CAF-I p48, Nucleosome-remodeling factor subunit RBAP48, Retinoblastoma-binding protein 4, RBBP-4, Retinoblastoma-binding protein p48, RBBP4, RBAP48, NURF55.
Source
E.coli.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSHMADKEA AFDDAVEERV INEEYKIWKK NTPFLYDLVM THALEWPSLT AQWLPDVTRP EGKDFSIHRL VLGTHTSDEQ NHLVIASVQL PNDDAQFDAS HYDSEKGEFG GFGSVSGKIE IEIKINHEGE VNRARYMPQN PCIIATKTPS SDVLVFDYTK HPSKPDPSGE CNPDLRLRGH QKEGYGLSWN PNLSGHLLSA SDDHTICLWD ISAVPKEGKV VDAKTIFTGH TAVVEDVSWH LLHESLFGSV ADDQKLMIWD TRSNNTSKPS HSVDAHTAEV NCLSFNPYSE FILATGSADK TVALWDLRNL KLKLHSFESH KDEIFQVQWS PHNETILASS GTDRRLNVWD LSKIGEEQSP EDAEDGPPEL LFIHGGHTAK ISDFSWNPNE PWVICSVSED NIMQVWQMAE NIYNDEDPEG SVDPEGQGS.

Product Science Overview

Introduction

Retinoblastoma Binding Protein 4 (RBBP4), also known as histone-binding protein RBBP4, is a nuclear protein that plays a crucial role in chromatin remodeling and gene expression regulation. It is a member of the WD40 repeat protein family and is involved in various cellular processes, including cell cycle regulation, DNA replication, and repair. RBBP4 is highly conserved across species and is implicated in several human cancers.

Structure and Function

RBBP4 is a 425 amino acid protein that contains six WD40 repeats, which are structural motifs involved in protein-protein interactions . These repeats form a beta-propeller structure that allows RBBP4 to interact with multiple proteins within diverse complexes such as the nucleosome remodeling and deacetylase (NuRD) complex, polycomb repressive complex 2 (PRC2), and SIN3A . These interactions are essential for its role in chromatin remodeling and histone modification.

Role in Cancer

RBBP4 is widely implicated in various cancers, including breast cancer, hepatocellular carcinoma, acute myeloid leukemia, glioblastoma, and colon and lung cancers . It functions as a nuclear factor involved in chromatin remodeling and histone assistance within multiple epigenetic complexes. High expression of RBBP4 is associated with aggressive cancer subtypes and poor prognosis. For instance, in breast cancer, RBBP4 shows a negative correlation with estrogen receptor (ER) and progesterone receptor (PR) but not with HER-2. Its high expression indicates poor prognosis, correlating significantly with lymph node metastasis and shorter overall survival .

Mechanisms of Action

RBBP4 interacts with multiple proteins through two distinct binding sites. The top of the donut-shaped seven-bladed beta-propeller fold of RBBP4 binds to proteins such as B-cell lymphoma/leukemia 11A (BCL11A) and histone H3, while a pocket on the side of the WD40 repeats binds to suppressor of zeste 12 (SUZ12), metastasis-associated protein 1 (MTA1), and histone H4 . These interactions are crucial for its role in chromatin remodeling and gene expression regulation.

Therapeutic Potential

Given its significant role in cancer, RBBP4 is considered a potential drug target. Recent studies have identified small molecule antagonists that can inhibit the interaction of RBBP4 with its binding partners. For example, the discovery of the small molecule OICR17251, which competes with interacting peptides from proteins such as BCL11A and histone H3, has paved the way for the development of more potent antagonists . These findings highlight the therapeutic potential of targeting RBBP4 in cancer treatment.

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