PHF5A Human

PHD Finger Protein 5A Human Recombinant
Cat. No.
BT6836
Source
Escherichia Coli.
Synonyms
PHD finger protein 5A, bK223H9.2, INI, Rds3, SAP14b, SF3b14b, PHD finger-like domain-containing protein 5A, PHD finger-like domain protein 5A, Splicing factor 3B-associated 14 kDa protein, PHF5A.
Appearance
Sterile Filtered clear solution.
Purity
Greater than 85% 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

PHF5A Human Recombinant produced in E. coli is a single polypeptide chain containing 133 amino acids (1-110) and having a molecular mass of 14.8kDa. PHF5A is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Product Specs

Introduction
PHD Finger Protein 5A, also called PHF5A, belongs to the PHD-finger protein family and functions as a chromatin-associated protein. It is a component of the splicing factor 3b protein complex, which, together with splicing factor 3a and a 12S RNA unit, forms the U2 small nuclear ribonucleoproteins complex (U2 snRNP). The splicing factor 3b/3a complex interacts with pre-mRNA upstream of the intron's branch site in a sequence-independent manner and anchors the U2 snRNP to the pre-mRNA. PHF5A possesses a PHD-finger-like domain located between highly basic N- and C-termini.
Description
Recombinant human PHF5A, expressed in E. coli, is a single polypeptide chain with a molecular weight of 14.8kDa. This protein comprises 133 amino acids, including the 110 amino acids of PHF5A and a 23 amino acid His-tag fused at the N-terminus. Purification is achieved through proprietary chromatographic techniques.
Physical Appearance
A clear, sterile-filtered solution.
Formulation
The PHF5A solution is provided at a concentration of 0.25mg/ml in a buffer consisting of 20mM Tris-HCl (pH 7.5), 0.15M NaCl, 10% glycerol, and 1mM DTT.
Stability
For short-term storage (up to 4 weeks), the solution should be kept at 4°C. For extended storage, it is recommended to freeze the solution at -20°C. The addition of a carrier protein (0.1% HSA or BSA) is advised for long-term storage. Repeated freezing and thawing should be avoided.
Purity
The purity of PHF5A is determined to be greater than 85% using SDS-PAGE analysis.
Synonyms
PHD finger protein 5A, bK223H9.2, INI, Rds3, SAP14b, SF3b14b, PHD finger-like domain-containing protein 5A, PHD finger-like domain protein 5A, Splicing factor 3B-associated 14 kDa protein, PHF5A.
Source
Escherichia Coli.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSMAKHHPD LIFCRKQAGV AIGRLCEKCD GKCVICDSYV RPCTLVRICD ECNYGSYQGR CVICGGPGVS DAYYCKECTI QEKDRDGCPK IVNLGSSKTD LFYERKKYGF KKR.

Product Science Overview

Introduction

PHD Finger Protein 5A (PHF5A) is a highly conserved protein that plays a crucial role in the regulation of gene expression. It is a member of the plant homeodomain (PHD) finger protein family, which is known for its involvement in chromatin remodeling and transcriptional regulation. The PHD finger domain is a specialized zinc finger motif that can bind to specific histone modifications, acting as an “epigenome reader” to mediate the activation or repression of underlying genes .

Structure and Function

PHF5A contains a PHD-finger-like domain flanked by highly basic N- and C-termini. This domain is essential for its function as a chromatin-associated protein. PHF5A is a component of the 17S U2 small nuclear ribonucleoprotein (snRNP) complex of the spliceosome, a large ribonucleoprotein complex that removes introns from transcribed pre-mRNAs . Within this complex, PHF5A is part of the SF3B subcomplex, which is required for the assembly of the ‘A’ complex formed by the stable binding of U2 snRNP to the branchpoint sequence in pre-mRNA .

Biological Significance

PHF5A is involved in pre-mRNA splicing, a critical process in gene expression. It directly participates in early spliceosome assembly and mediates the recognition of the intron branch site during pre-mRNA splicing by promoting the selection of the pre-mRNA branch-site adenosine, the nucleophile for the first step of splicing . This function is vital for the accurate and efficient removal of introns from pre-mRNA, ensuring the proper expression of genes.

Role in Cancer

Recent studies have highlighted the role of PHF5A as an oncoprotein in various cancers, including non-small cell lung cancer (NSCLC). PHF5A has been found to be highly upregulated in lung adenocarcinoma (LAC) tissues compared to adjacent non-tumor tissues . Its expression is closely associated with tumor progression and poor patient prognosis . Functional studies have demonstrated that PHF5A knockdown results in reduced cell proliferation, increased cell apoptosis, cell cycle arrest, and suppressed migration and invasion in LAC cells . These findings suggest that PHF5A contributes to LAC progression by regulating multiple signaling pathways and may serve as a potential therapeutic target in NSCLC .

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