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PDIA2

This gene encodes a member of the disulfide isomerase (PDI) family of endoplasmic reticulum (ER) proteins that catalyze protein folding and thiol-disulfide interchange reactions. The encoded protein has an N-terminal ER-signal sequence, two catalytically active thioredoxin (TRX) domains, two TRX-like domains and a C-terminal ER-retention sequence. The protein plays a role in the folding of nascent proteins in the endoplasmic reticulum by forming disulfide bonds through its thiol isomerase, oxidase, and reductase activity. The encoded protein also possesses estradiol-binding activity and can modulate intracellular estradiol levels.
Protein class

Enzymes, Metabolic proteins

Predicted location

Intracellular

Single cell type specificity

Cell type enriched (Exocrine glandular cells)

Immune cell specificity

Not detected in immune cells

Cell line specificity

Cell line enhanced (HAP1, HEK93, Hep G2, Karpas-707, MCF7, SH-SY5Y)

Interaction

Monomer; predominantly as monomer under reducing conditions. Homodimer; disulfide-linked. Part of a large chaperone multiprotein complex comprising DNAJB11, HSP90B1, HSPA5, HYOU, PDIA2, PDIA4, PDIA6, PPIB, SDF2L1, UGGT1 and very small amounts of ERP29, but not, or at very low levels, CALR nor CANX.

Molecular function

Chaperone, Isomerase

More Types Infomation

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For Research Use Only. Not For Clinical Use.

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