Product: Reparixin (L-lysine salt)
Pdi1p Antibody (38H8) Summary
| Immunogen |
Yeast membrane preparations
|
| Localization |
endoplasmic reticulum and nuclear envelope
|
| Marker |
Endoplasmic Reticulum Marker
|
| Isotype |
IgG1 Kappa
|
| Clonality |
Monoclonal
|
| Host |
Mouse
|
| Purity |
Tissue culture supernatant
|
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|
Applications/Dilutions
| Dilutions |
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| Application Notes |
This Pdi1p (38H8) antibody is useful in Western blot and Immunocytochemistry/Immunofluorescence. In WB of yeast protein extracts a ~65 kDa band can be seen. In ICC/IF using yeast cells, endoplasmic reticulum staining can be seen.
The observed molecular weight of the protein may vary from the listed predicted molecular weight due to post translational modifications, post translation cleavages, relative charges, and other experimental factors. |
| Theoretical MW |
65 kDa.
Disclaimer note: The observed molecular weight of the protein may vary from the listed predicted molecular weight due to post translational modifications, post translation cleavages, relative charges, and other experimental factors. |
Reactivity Notes
Yeast.
Packaging, Storage & Formulations
| Storage |
Store at 4C short term. Aliquot and store at -20C long term. Avoid freeze-thaw cycles.
|
| Buffer |
PBS
|
| Preservative |
10mM Sodium Azide
|
| Purity |
Tissue culture supernatant
|
Alternate Names for Pdi1p Antibody (38H8)
- MFP 1
- MFP1
- PDI 1
- PDI
- PDI1
- Protein disulfide isomerase
- Thioredoxin related glycoprotein 1
- TRG 1
- TRG1
Background
One of the important aspects of secretory proteins folding process is the formation of native disulfide bonds which is catalyzed by enzyme protein disulfide isomerase (PDI) and yeast Saccharomyces cerevisiae has about 5 protein disulfide isomerase (PDI) family members (EUG1, MPD1, MPD2, EPS1 and PDI1/PDI1p). Pdi1p is a typical member of its family which is an essential gene and is considered homologus to human PDI with no significant differences; however, the two proteins are only 29% identical. It is a major ER protein with chaperon/co-chaperon activity and is involved in the retention of resident ER proteins as well as in recognizing proteins targeted for ER-associated degradation (ERAD). Yeast Pdi1p is a folding catalyst which introduces disulfide bonds into its substrates and rearranges or reduces pre-existing ones, and besides its oxidoreductase activity, Pdi1p acts as a molecular chaperone that also facilitates folding of proteins which do not contain disulfide bonds.