Protein Disulfide Isomerase/P4HB Overexpression Lysate (Denatured) Summary
| Description |
Pasmid: pCMV-P4HB full-length
|
| Gene |
P4HB
|
Packaging, Storage & Formulations
| Storage |
Store at -80C. Avoid freeze-thaw cycles.
|
| Buffer |
Sample Buffer (50 mM Tris-HCl, 2% SDS, 10% glycerol, 300 mM 2-mercaptoethanol, and 0.01% Bromophenol blue).
|
Lysate Details for Protein Disulfide Isomerase/P4HB
| Type |
Overexpression
|
| Protein State |
Denatured
|
Notes
Quality control test: Transient overexpression cell lysate was tested with Anti-P4HB antibody by Western Blots.
This product is produced by and distributed for Abnova, a company based in Taiwan.
Alternate Names for Protein Disulfide Isomerase/P4HB Overexpression Lysate (Denatured)
- Cellular thyroid hormone-binding protein
- collagen prolyl 4-hydroxylase beta
- DSI
- ERBA2L
- GIT
- glutathione-insulin transhydrogenase
- P4HB
- P4Hbeta
- p55
- PDI
- PDIA1
- PDIA1procollagen-proline, 2-oxoglutarate 4-dioxygenase (proline 4-hydroxylase), betapolypeptide (protein disulfide isomerase-associated 1)
- PDIEC 5.3.4.1
- PHDB
- PO4DB
- PO4HB
- procollagen-proline, 2-oxoglutarate 4-dioxygenase (proline 4-hydroxylase), betapolypeptide
- PROHB
- PROHBprocollagen-proline, 2-oxoglutarate 4-dioxygenase (proline 4-hydroxylase), betapolypeptide (protein disulfide isomerase; thyroid hormone binding protein p55)
- Prolyl 4-hydroxylase subunit beta
- prolyl 4-hydroxylase, beta polypeptide
- protein disulfide isomerase family A, member 1
- protein disulfide isomerase/oxidoreductase
- protein disulfide isomerase-associated 1
- protein disulfide-isomerase
- protocollagen hydroxylase
- Thbp
- thyroid hormone-binding protein p55
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. [provided by RefSeq]