The P4HB Polyclonal Antibody (PAC046850) is a valuable tool for researchers studying P4HB, also known as protein disulfide isomerase, a multifunctional enzyme involved in protein folding and redox regulation. This antibody, generated in rabbits, is highly specific for human samples and has been validated for Western blot applications. It binds to the P4HB protein, allowing for precise detection and analysis in a variety of cell types, making it ideal for investigations in fields such as biochemistry and cell biology.P4HB is essential for maintaining protein structure and function in cells, playing a critical role in processes such as protein disulfide bond formation and redox signaling.
Its involvement in various cellular functions makes it a key target for research on diseases like cancer, neurodegenerative disorders, and cardiovascular diseases. Understanding the functions of P4HB can provide insights into potential therapeutic strategies for these conditions by targeting its enzymatic activities or redox regulatory functions.
Antibody Name:
P4HB Antibody (PACO46850)
Antibody SKU:
PACO46850
Size:
50ug
Host Species:
Rabbit
Tested Applications:
ELISA
Recommended Dilutions:
Species Reactivity:
Cricetulus griseus
Immunogen:
Recombinant Cricetulus griseus Protein disulfide-isomerase protein (20-509AA)
This multifunctional protein catalyzes the formation, breakage and rearrangement of disulfide bonds. At the cell surface, seems to act as a reductase that cleaves disulfide bonds of proteins attached to the cell. May therefore cause structural modifications of exofacial proteins. Inside the cell, seems to form/rearrange disulfide bonds of nascent proteins. At high concentrations, functions as a chaperone that inhibits aggregation of misfolded proteins. At low concentrations, facilitates aggregation (anti-chaperone activity). May be involved with other chaperones in the structural modification of the TG precursor in hormone biogenesis. Also acts a structural subunit of various enzymes such as prolyl 4-hydroxylase and microsomal triacylglycerol transfer protein MTTP. Receptor for LGALS9; the interaction retains P4HB at the cell surface of Th2 T helper cells, increasing disulfide reductase activity at the plasma membrane, altering the plasma membrane redox state and enhancing cell migration.
PDIA1: This multifunctional protein catalyzes the formation, breakage and rearrangement of disulfide bonds. At the cell surface, seems to act as a reductase that cleaves disulfide bonds of proteins attached to the cell. May therefore cause structural modifications of exofacial proteins. Inside the cell, seems to form/rearrange disulfide bonds of nascent proteins. At high concentrations, functions as a chaperone that inhibits aggregation of misfolded proteins. At low concentrations, facilitates aggregation (anti-chaperone activity). May be involved with other chaperones in the structural modification of the TG precursor in hormone biogenesis. Also acts a structural subunit of various enzymes such as prolyl 4-hydroxylase and microsomal triacylglycerol transfer protein MTTP. Homodimer. Monomers and homotetramers may also occur. Also constitutes the structural subunit of prolyl 4-hydroxylase and of the microsomal triacylglycerol transfer protein MTTP in mammalian cells. Stabilizes both enzymes and retain them in the ER without contributing to the catalytic activity. Binds UBQLN1. Binds to CD4, and upon HIV-1 binding to the cell membrane, is part of a P4HB/PDI-CD4-CXCR4-gp120 complex. Belongs to the protein disulfide isomerase family.Protein type: Isomerase; Oxidoreductase; Nuclear receptor co-regulator; EC 5.3.4.1; Endoplasmic reticulumChromosomal Location of Human Ortholog: 17q25Cellular Component: focal adhesion; endoplasmic reticulum; endoplasmic reticulum lumen; melanosome; plasma membrane; ER-Golgi intermediate compartment; extracellular regionMolecular Function: protein binding; enzyme binding; procollagen-proline 4-dioxygenase activity; protein heterodimerization activity; endopeptidase activity; protein disulfide isomerase activityBiological Process: extracellular matrix organization and biogenesis; response to reactive oxygen species; protein folding; cell redox homeostasis; lipoprotein metabolic process; peptidyl-proline hydroxylation to 4-hydroxy-L-proline; proteolysisDisease: Cole-carpenter Syndrome 1
UniProt Protein Details:
NCBI Summary:
This gene encodes the beta subunit of prolyl 4-hydroxylase, a highly abundant multifunctional enzyme that belongs to the protein disulfide isomerase family. When present as a tetramer consisting of two alpha and two beta subunits, this enzyme is involved in hydroxylation of prolyl residues in preprocollagen. This enzyme is also a disulfide isomerase containing two thioredoxin domains that catalyze the formation, breakage and rearrangement of disulfide bonds. Other known functions include its ability to act as a chaperone that inhibits aggregation of misfolded proteins in a concentration-dependent manner, its ability to bind thyroid hormone, its role in both the influx and efflux of S-nitrosothiol-bound nitric oxide, and its function as a subunit of the microsomal triglyceride transfer protein complex. [provided by RefSeq, Jul 2008]