PIH1D1 Human

PIH1 Domain Containing 1 Human Recombinant
Cat. No.
BT4228
Source
Escherichia Coli.
Synonyms
NOP17, Nucleolar Protein 17 Homolog, PIH1 Domain-Containing Protein 1, PIH1 Domain-Containing 1, PIH1D1.
Appearance
Sterile Filtered clear solution.
Purity
Greater than 85% 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

PIH1D1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 313 amino acids (1-290a.a) and having a molecular mass of 34.8kDa. PIH1D1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Product Specs

Introduction
PIH1 domain-containing protein 1 (PIH1D1), a member of the PIH1 family, is a phylogenetically conserved protein. It plays a crucial role in the efficient processing of pre-rRNA during ribosomal biogenesis by associating with small nucleolar RNAs (snoRNAs). These snoRNAs are found within ribonucleoprotein particles located in the nucleolus. Additionally, PIH1D1 might function as a regulator of the apoptosis pathway.
Description
Recombinant PIH1D1, produced in E. coli, is a single, non-glycosylated polypeptide chain consisting of 313 amino acids (1-290a.a.). With a molecular weight of 34.8 kDa, PIH1D1 is fused to a 23 amino acid His-tag at its N-terminus and purified using proprietary chromatographic techniques.
Physical Appearance
A clear, sterile-filtered solution.
Formulation
The PIH1D1 protein solution is provided at a concentration of 0.25 mg/ml in a buffer consisting of 20 mM Tris-HCl (pH 8.0), 0.4 M Urea, and 10% glycerol.
Stability
For short-term storage (2-4 weeks), the product should be kept at 4°C. For extended storage, it is recommended to freeze the product at -20°C. The addition of a carrier protein (0.1% HSA or BSA) is advised for long-term storage. Avoid repeated freeze-thaw cycles.
Purity
The purity of the PIH1D1 protein is greater than 85%, as determined by SDS-PAGE analysis.
Synonyms
NOP17, Nucleolar Protein 17 Homolog, PIH1 Domain-Containing Protein 1, PIH1 Domain-Containing 1, PIH1D1.
Source
Escherichia Coli.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSMANPKLL GMGLSEAEAI GADSARFEEL LLQASKELQQ AQTTRPESTQ IQPQPGFCIK TNSSEGKVFI NICHSPSIPP PADVTEEELL QMLEEDQAGF RIPMSLGEPH AELDAKGQGC TAYDVAVNSD FYRRMQNSDF LRELVITIAR EGLEDKYNLQ LNPEWRMMKN RPFMGSISQQ NIRSEQRPRI QELGDLYTPA PGRAESGPEK PHLNLWLEAP DLLLAEVDLP KLDGALGLSL EIGENRLVMG GPQQLYHLDA YIPLQINSHE SKAAFHRKRK QLMVAMPLLP VPS

Product Science Overview

Structure and Function

PIH1D1 is characterized by the presence of a PIH1 domain, which is essential for its function. The protein plays a crucial role in the assembly of C/D box snoRNP particles, which are involved in the processing of pre-rRNA during ribosomal biogenesis . Additionally, PIH1D1 is known to recruit the SWI/SNF complex to the core promoter of rRNA genes, thereby enhancing pre-rRNA transcription .

PIH1D1 also mediates the interaction of TELO2 with the R2TP complex, which is necessary for the stability of key proteins such as MTOR and SMG1. This interaction positively regulates the assembly and activity of the mTORC1 complex, which is crucial for cellular growth and metabolism .

Biological Significance

The biological significance of PIH1D1 extends to its role as a modulator of the apoptosis pathway . It is involved in the regulation of cellular protein metabolic processes and positive regulation of signal transduction . The protein is located in both the cytoplasm and nucleolus, indicating its involvement in various cellular processes .

Clinical Relevance

Mutations or dysregulation of the PIH1D1 gene have been associated with certain diseases, including Psoriasis 4 and 3-Methylglutaconic Aciduria, Type IX . Understanding the function and regulation of PIH1D1 is therefore important for developing potential therapeutic strategies for these conditions.

Recombinant PIH1D1

Recombinant human PIH1D1 protein is often used in research to study its function and interactions. The recombinant protein is typically expressed in E. coli and purified for use in various assays . It is available with an N-terminal His-tag, which facilitates its purification and detection in experimental setups .

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