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P4HB Antibody (C-term)
Purified Rabbit Polyclonal Antibody (Pab)
- SPECIFICATION
- CITATIONS: 1
- PROTOCOLS
- BACKGROUND
Application 
| FC, IHC-P, WB, E |
|---|---|
| Primary Accession | P07237 |
| Other Accession | P04785, P09103, Q8R4U2, P05307 |
| Reactivity | Human |
| Predicted | Bovine, Hamster, Mouse, Rat |
| Host | Rabbit |
| Clonality | Polyclonal |
| Isotype | Rabbit IgG |
| Calculated MW | 57116 Da |
| Antigen Region | 436-464 aa |
| Gene ID | 5034 |
|---|---|
| Other Names | Protein disulfide-isomerase, PDI, Cellular thyroid hormone-binding protein, Prolyl 4-hydroxylase subunit beta, p55, P4HB, ERBA2L, PDI, PDIA1, PO4DB |
| Target/Specificity | This P4HB antibody is generated from rabbits immunized with a KLH conjugated synthetic peptide between 436-464 amino acids from the C-terminal region of human P4HB. |
| Dilution | WB~~1:1000 IHC-P~~1:50~100 FC~~1:10~50 |
| Format | Purified polyclonal antibody supplied in PBS with 0.09% (W/V) sodium azide. This antibody is prepared by Saturated Ammonium Sulfate (SAS) precipitation followed by dialysis against PBS. |
| Storage | Maintain refrigerated at 2-8°C for up to 2 weeks. For long term storage store at -20°C in small aliquots to prevent freeze-thaw cycles. |
| Precautions | P4HB Antibody (C-term) is for research use only and not for use in diagnostic or therapeutic procedures. |
| Name | P4HB |
|---|---|
| Synonyms | ERBA2L, PDI, PDIA1, PO4DB |
| Function | 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 and following phosphorylation by FAM20C, functions as a chaperone that inhibits aggregation of misfolded proteins (PubMed:32149426). 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 as 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 (PubMed:21670307). |
| Cellular Location | Endoplasmic reticulum. Endoplasmic reticulum lumen. Melanosome. Cell membrane; Peripheral membrane protein. Note=Highly abundant. In some cell types, seems to be also secreted or associated with the plasma membrane, where it undergoes constant shedding and replacement from intracellular sources (Probable). Localizes near CD4-enriched regions on lymphoid cell surfaces (PubMed:11181151). Identified by mass spectrometry in melanosome fractions from stage I to stage IV (PubMed:10636893) Colocalizes with MTTP in the endoplasmic reticulum (PubMed:23475612) {ECO:0000269|PubMed:10636893, ECO:0000269|PubMed:11181151, ECO:0000269|PubMed:23475612, ECO:0000305} |
Provided below are standard protocols that you may find useful for product applications.
Background
P4HB is 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.
References
Ewing,R.M., et.al., Mol. Syst. Biol. 3, 89 (2007)
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