Recombinant Human PAF1 Protein, N-His

Reference: YHK62301
Product nameRecombinant Human PAF1 Protein, N-His
Origin speciesHuman
Expression systemProkaryotic expression
Molecular weight17.82 kDa
BufferLyophilized from a solution in PBS pH 7.4, 0.02% NLS, 1mM EDTA, 4% Trehalose, 1% Mannitol.
FormLiquid
Delivery conditionDry Ice
Delivery lead time in business days3-5 days if in stock; 3-5 weeks if production needed
Storage condition4°C for short term (1 week), -20°C or -80°C for long term (avoid freezing/thawing cycles; addition of 20-40% glycerol improves cryoprotection)
BrandAntibodySystem
Host speciesEscherichia coli (E.coli)
Fragment TypeMet205-Arg336
Aliases /SynonymsPD2, RNA polymerase II-associated factor 1 homolog, Pancreatic differentiation protein 2, hPAF1, PAF1
ReferenceYHK62301
NoteFor research use only.

Description of Recombinant Human PAF1 Protein, N-His

Introduction

Recombinant proteins are proteins that are produced through genetic engineering techniques, allowing for the production of large quantities of specific proteins for various applications. One such recombinant protein is Recombinant Human PAF1 Protein, which has gained significant attention in the scientific community for its unique structure, activity, and potential applications.

Structure of Recombinant Human PAF1 Protein

Recombinant Human PAF1 Protein is a 91 kDa protein composed of 771 amino acids. It is a subunit of the RNA polymerase II associated factor 1 complex (PAF1C), which is involved in transcriptional regulation and elongation. The protein has a conserved domain structure, with an N-terminal domain, a central domain, and a C-terminal domain.

N-terminal domain

The N-terminal domain of Recombinant Human PAF1 Protein is responsible for its interaction with other subunits of the PAF1C complex, including CDC73, CTR9, and LEO1. This domain also plays a crucial role in the recruitment of the PAF1C complex to chromatin, where it regulates gene expression.

Central domain

The central domain of Recombinant Human PAF1 Protein contains a highly conserved region known as the PAF1 homology domain. This domain is essential for the interaction of PAF1C with RNA polymerase II, as well as for its role in transcriptional elongation and histone modifications.

C-terminal domain

The C-terminal domain of Recombinant Human PAF1 Protein is involved in the interaction with other transcriptional regulators, such as the Mediator complex. It also plays a role in the recruitment of PAF1C to actively transcribing genes and in the regulation of RNA processing and maturation.

Activity of Recombinant Human PAF1 Protein

Recombinant Human PAF1 Protein is a multifunctional protein with diverse activities in transcriptional regulation and elongation. It is involved in the recruitment and stabilization of the PAF1C complex to chromatin, where it interacts with various transcriptional regulators and histone-modifying enzymes to facilitate gene expression.

Transcriptional regulation

Recombinant Human PAF1 Protein plays a crucial role in transcriptional regulation by facilitating the recruitment and activation of RNA polymerase II at the promoter region of actively transcribed genes. It also interacts with other transcriptional regulators, such as the Mediator complex, to regulate gene expression.

Transcriptional elongation

One of the key functions of Recombinant Human PAF1 Protein is its role in transcriptional elongation. It interacts with RNA polymerase II and other elongation factors to promote efficient transcriptional elongation and processivity.

Histone modifications

Recombinant Human PAF1 Protein also plays a crucial role in histone modifications, which are essential for the regulation of gene expression. It interacts with various histone-modifying enzymes, such as histone methyltransferases and acetyltransferases, to regulate chromatin structure and gene expression.

Applications of Recombinant Human PAF1 Protein

The unique structure and multifunctional activity of Recombinant Human PAF1 Protein make it a valuable tool for various applications in the fields of molecular biology, biochemistry, and medicine.

Gene expression studies

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