Recombinant Proteins

p53
LBP
CEA
HLA
TCL
TTC
NPM
MAF
Bax
BID

PIH1D1 Human

PIH1 Domain Containing 1 Human Recombinant

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.
Shipped with Ice Packs
Cat. No.
BT4228
Source
Escherichia Coli.
Appearance
Sterile Filtered clear solution.

PIH1D2 Human

PIH1 Domain Containing 2 Human Recombinant

PIH1D2 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 338 amino acids (1-315 a.a) and having a molecular mass of 38.3kDa.
PIH1D2 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT4297
Source
Escherichia Coli.
Appearance
Sterile Filtered colorless solution.
Definition and Classification

PIH1 domain-containing proteins are a family of proteins characterized by the presence of the PIH1 (Protein Interacting with Hsp90) domain. This domain is known for its role in protein-protein interactions, particularly with molecular chaperones like Hsp90. These proteins are classified based on the presence of the PIH1 domain and are involved in various cellular processes, including protein folding, assembly, and stabilization.

Biological Properties

Key Biological Properties: PIH1 domain-containing proteins are essential for the proper functioning of molecular chaperones. They assist in the stabilization and assembly of protein complexes, ensuring proper protein folding and function.

Expression Patterns: The expression of PIH1 domain-containing proteins varies across different tissues and developmental stages. They are ubiquitously expressed but show higher expression levels in tissues with high protein turnover rates, such as the liver, brain, and reproductive organs.

Tissue Distribution: These proteins are found in various tissues, with significant expression in the liver, brain, testes, and ovaries. Their distribution is indicative of their role in supporting high levels of protein synthesis and turnover.

Biological Functions

Primary Biological Functions: PIH1 domain-containing proteins play a crucial role in the assembly and stabilization of protein complexes. They are involved in the maturation of ribonucleoprotein complexes and the regulation of protein degradation pathways.

Role in Immune Responses: These proteins are implicated in the regulation of immune responses by modulating the stability and function of key signaling proteins involved in pathogen recognition and immune activation.

Pathogen Recognition: PIH1 domain-containing proteins contribute to the recognition and response to pathogens by stabilizing proteins involved in pathogen detection and signaling pathways.

Modes of Action

Mechanisms with Other Molecules and Cells: PIH1 domain-containing proteins interact with molecular chaperones like Hsp90 and other co-chaperones to facilitate the proper folding and assembly of client proteins. They act as scaffolds, bringing together various components required for protein complex formation.

Binding Partners: These proteins bind to a variety of partners, including Hsp90, R2TP complex components, and other co-chaperones. These interactions are crucial for their function in protein stabilization and assembly.

Downstream Signaling Cascades: By stabilizing key signaling proteins, PIH1 domain-containing proteins influence downstream signaling pathways involved in cell growth, differentiation, and stress responses.

Regulatory Mechanisms

Regulatory Mechanisms Controlling Expression and Activity: The expression of PIH1 domain-containing proteins is regulated at the transcriptional level by various transcription factors. Post-transcriptional modifications, such as phosphorylation and ubiquitination, also play a role in modulating their activity and stability.

Transcriptional Regulation: Specific transcription factors bind to the promoter regions of PIH1 domain-containing genes, regulating their expression in response to cellular signals and stress conditions.

Post-Translational Modifications: Phosphorylation and ubiquitination are common post-translational modifications that regulate the activity, stability, and interactions of PIH1 domain-containing proteins.

Applications

Biomedical Research: PIH1 domain-containing proteins are studied for their role in protein homeostasis and their potential involvement in diseases related to protein misfolding and aggregation, such as neurodegenerative disorders.

Diagnostic Tools: These proteins can serve as biomarkers for diseases characterized by protein misfolding and aggregation. Their expression levels and modifications can provide insights into disease states and progression.

Therapeutic Strategies: Targeting PIH1 domain-containing proteins and their interactions with molecular chaperones offers potential therapeutic strategies for diseases involving protein misfolding and aggregation.

Role in the Life Cycle

Role Throughout the Life Cycle: PIH1 domain-containing proteins are essential throughout the life cycle, from development to aging. During development, they support the high demand for protein synthesis and assembly. In aging, they help maintain protein homeostasis and prevent the accumulation of misfolded proteins.

From Development to Aging and Disease: These proteins play a critical role in ensuring proper protein function during development, maintaining cellular homeostasis in adulthood, and preventing protein aggregation-related diseases in aging.

© Copyright 2024 Thebiotek. All Rights Reserved.