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The antibody against P4HB was raised in rabbit using the Human PDIA1 as the immunogen. This antibody exists as a non-conjugated isotype IgG, Antigen affinity purified. This antibody has been validated on ELISA, WB, IHC, IF.
The antibody against P4HB was raised in rabbit using the Human PDIA1 as the immunogen. This antibody exists as a non-conjugated isotype IgG, Antigen affinity purified. This antibody has been validated on ELISA, WB, IHC, IF.
$600.00
| Cat.No | ADC-51187A | Clonality | Polyclonal |
|---|---|---|---|
| Host Species | Rabbit | Target Name | P4HB |
| Target Synonyms | family A | Form | Liquid |
| Species Reactivity | Human, Mouse, Rat | Isotype | IgG |
| Storage Buffer | 50% Glycerol, Avoid freeze / thaw cycles., PBS with 0.1% Sodium Azide | Purification Method | Antigen affinity purified |
| Conjugate | Non-conjugated | Application | ELISA, IF, IHC, WB |
| Storage | Upon receipt |
| Immunogen Description | Human PDIA1 | Target Species | Human |
|---|---|---|---|
| Immunogen Sequence | Complete sequences for the immunogen, target protein, and peptides are available upon request. | Uniprot ID | P07237 |
Uniprot Id
P07237
Target Species
Human
Target Name
P4HB
Target Full Name
Protein disulfide-isomerase
Target 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, 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.
Target Involvement
Cole-Carpenter syndrome 1 (CLCRP1)
Target Subcellular Location
Endoplasmic reticulum. Endoplasmic reticulum lumen. Melanosome. Cell membrane; Peripheral membrane protein.
Target Protein Families
Protein disulfide isomerase family
Target Research Area
Metabolism, Cancer
Target Synonyms
Cellular thyroid hormone binding protein; Cellular thyroid hormone-binding protein; Collagen prolyl 4 hydroxylase beta; Disulphide Isomerase; DSI; EC 5.3.4.1; Endoplasmic reticulum resident protein 59; ER protein 59; ERBA2L; ERp59; GIT; Gltathione insulin transhydrogenase; Glutathione insulin transhydrogenase; P4HB; P4Hbeta; p55; PDI; PDIA1; PDIA1_HUMAN; PDIR; PHDB; PO4DB; PO4HB; Procollagen proline 2 oxoglutarate 4 dioxygenase (proline 4 hydroxylase) beta polypeptide (protein disulfide isomerase associated 1); Procollagen proline 2 oxoglutarate 4 dioxygenase beta subunit; PROHB; Prolyl 4 hydroxylase beta polypeptide; Prolyl 4 hydroxylase beta subunit; Prolyl 4 hydroxylase subunit beta; Prolyl 4-hydroxylase subunit beta; Protein disulfide isomerase associated 1; Protein disulfide isomerase, family A, member 1; Protein disulfide isomerase/oxidoreductase; Protein disulfide-isomerase; Protocollagen hydroxylase; Thbp; Thyroid hormone binding protein p55 ; Thyroid hormone binding protein p55 cellular; V erb a avian erythroblastic leukemia viral oncogene homolog 2 like
Target Background
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.
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