Protein Disulfide Isomerase / Streptavidin /

Product Details
Supplier Biorbyt
Catalog #: orb151400-100ul (View supplier product page)
Size 100 μl
Price $578.00
Antigen Protein Disulfide Isomerase
Clone
Host Rabbit
Isotype IgG
Conjugate Streptavidin
Target Species Canine, Guinea Pig, Hamster, Human, Monkey, Mouse, Porcine, Rat, Sheep
Applications WB, IHC-P, IF, ICC, IP
Description Rabbit polyclonal to PDI (Streptavidin). The three dimensional structure of many extracellular proteins is stabilized by the formation of disulphide bonds. Studies suggest that a microsomal enzyme known as Protein Disulphide Isomerase (PDI) is involved in disulphide-bond formation via its oxidase activity and isomerization via its isomerase activity, as well as the reduction of disulphide bonds in proteins. Studies suggest BiP and PDI work together sequentially to increase oxidation of these proteins. PDI has also been found to function as a chaperone to prevent the aggregation of unfolded substrates, and serves as a subunit of prolyl 4-hydroxylase and microsomal triglyceride transferase. PDI is an abundant 55kDa protein located primarily in the ER, however studies have also proved its presence in the cytosol. PDI has the ability to reside in the ER permanently due to the highly conserved KDEL sequence at its carboxy-terminus. It uses carboxy-terminal KDEL as a retention signal, and this appears to be sufficient to reduce the secretion of proteins from the ER. This retention is reported to be mediated by a KDEL receptor..
About Protein Disulfide Isomerase and Streptavidin
Protein Disulfide Isomerase 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]
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Streptavidin Excitation and Emission Spectra