Anti-Yeast Pdi1p Monoclonal antibody (DMAB8408)

Mouse Anti-Yeast Pdi1p Monoclonal antibody for IF, WB Datasheet

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Specifications


Host Species
Mouse
Clone
Y50M50
Species Reactivity
Yeast
Immunogen
Pdi1p is a yeast protein disulfide isomerase. It is a major endoplasmic reticulum protein with chaperone and co-chaperone activity, involved in retention of resident ER proteins. It also has a role in recognizing proteins targeted for ER-associated degrad
Conjugate
Unconjugated

Target


Alternative Names
MFP1; PDI1; Pdi1p; Protein disulfide isomerase; Thioredoxin related glycoprotein 1; TRG1

Product Background


Antigen Description
PDI1 is a protein disulfide isomerase, multifunctional protein resident in the endoplasmic reticulum lumen, essential for the formation of disulfide bonds in secretory and cell-surface proteins, unscrambles non-native disulfide bonds. Yeasts are eukaryotic micro-organisms classified in the kingdom Fungi, with 1,500 species currently described estimated to be only 1% of all fungal species. Most reproduce asexually by mitosis, and many do so by an asymmetric division process called budding. Yeasts are unicellular, although some species with yeast forms may become multicellular through the formation of a string of connected budding cells known as pseudohyphae, or false hyphae, as seen in most molds. Yeast size can vary greatly depending on the species, typically measuring 3–4 µm in diameter, although some yeasts can reach over 40 µm.

Citations


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References


KELLOKUMPU, S; SORMUNEN, R; et al. LYSYL HYDROXYLASE, A COLLAGEN PROCESSING ENZYME, EXEMPLIFIES A NOVEL CLASS OF LUMINALLY-ORIENTED PERIPHERAL MEMBRANE-PROTEINS IN THE ENDOPLASMIC-RETICULUM. JOURNAL OF BIOLOGICAL CHEMISTRY 269:30524-30529(1994).
Smathers, RL; Galligan, JJ; et al. Overview of lipid peroxidation products and hepatic protein modification in alcoholic liver disease. CHEMICO-BIOLOGICAL INTERACTIONS 192:107-112(2011).

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