pdi

P4HB Protein, Human, Recombinant (His) is expressed in HEK293 mammalian cells with His tag. The predicted molecular weight is 56.4 kDa and the accession number is A0A024R8S5.

P4HB Protein, Mouse, Recombinant (His) is expressed in HEK293 mammalian cells with His tag. The predicted molecular weight is 56.2 kDa and the accession number is P09103.

IL-11 Protein, Rat, Recombinant (His & PDI) is expressed in yeast with N-6xHis-PDI tag. The predicted molecular weight is 78.0 kDa and the accession number is Q99MF5.

Protein Disulfide-Isomerase A6 (PDIA6) is a 48.5kDa protein that belongs to the protein disulfide isomerase family (PDI). PDIA6 is an enzyme in the endoplasmic reticulum in eukaryotes which catalyzes the formation and breakage of disulfide bonds between cysteine residues within proteins as they fold. The PDIA6 expressed in platelets, its functions as a chaperone that inhibits aggregation of misfolded proteins. PDIA6 is part a large chaperone multiprotein complex comprising DNAJB11, HSP90B1, HSPA5, HYOU, PDIA2, PDIA4, PDIA6, PPIB, SDF2L1, UGT1A1. PDIA6 also plays a role in platelet aggregation and activation by agonists such as convulxin, collagen and thrombin.

PDIA3 protein is also known as Protein disulfide-isomerase A3. It is a protein that in humans is encoded by the PDIA3 gene.PDIA3 is an enzyme that belongs to the endoplasmic reticulum and interacts with lectin chaperones calreticulin and calnexin to modulate folding of newly synthesized glycoproteins. PDIA3 interacts with thiazide-sensitive sodium-chloride cotransporter in the kidney and is induced by glucose deprivation. PDIA3 is part of the major histocompatibility complex (MHC) class I peptide-loading complex (TAP1), which is important for formation of the final antigen conformation and export from the endoplasmic reticulum to the cell surface.

Protein disulfide-isomerase A5 is a 519 amino acids protein that belongs to the protein disulfide isomerase family.It contains 3 thioredoxin domains.It can catalyze the rearrangement of -S-S- bonds in proteins.

Protein Disulfide-Isomerase-Like Protein of the Testis (PDILT) is a protein that belongs to the protein disulfide isomerase family. Human PDILT is synthesized as a 584 amino acid precursor that contains an 20 amino acid signal sequence and a 564 amino acid mature chain. PDILT contains 1 thioredoxin domain lacks the conserved redox-active Cys at position 417 which is replaced by a Ser residue, suggesting that it lacks thioredoxin activity. PDILT is an enzyme in the endoplasmic reticulum in eukaryotes. It is not a disulfide-linked homodimer. The PDILT protein can interacts with ERO1L and CLGN. PDILT probable redox-inactive chaperone involved in spermatogenesis.

Acts as an intracellular estrogen-binding protein. May be involved in modulating cellular levels and biological functions of estrogens in the pancreas. May act as a chaperone that inhibits aggregation of misfolded proteins.

Anterior Gradient 2 (AGR2) is an 18-21 kDa member of the PDI family of enzymes. AGR2 is widely expressed in secretory cells, such as small intestine goblet, prostate epithelium, enteroendocrine cells, and multiple carcinoma cell types. AGR2 forms transient disulfide linkages with molecules destined for secretion, possibly aiding protein folding. Expression of AGR2 shows a positive correlation with expression of estrogen receptor in breast carcinoma and a negative correlation with expression of EGF receptor. Mature human AGR2 is 155 amino acids (aa) in length (aa 21 - 175). Cys81 is presumed to participate in intermolecular bond formation. Over aa 21 - 175, human AGR2 shares 94% aa identity with mouse AGR2.

ERO1-Like Protein α (ERO1L) is an enzyme that belongs to the EROs family. ERO1L is expressed at high level in esophagus and upper digestive tract. ERO1L is an essential oxidoreductase that oxidizes proteins in the endoplasmic reticulum to produce disulfide bonds. ERO1L acts by oxidizing directly P4HB PDI isomerase through a direct disulfide exchange. It associates with ERP44, demonstrating that it does not oxidize all PDI related proteins and can discriminate between PDI and related proteins. Its reoxidation probably involves electron transfer to molecular oxygen via FAD. ERO1L may be responsible for a significant proportion of reactive oxygen species (ROS) in the cell. ERO1L responses to temperature stimulus, protein thiol-disulfide exchange, protein folding with or without chaperone cofactor and transport.

Peptidylarginine deiminase type4 (PADI4) was firstly identified as a non-MHC RA genetic risk factor. Furthermore, PADI4 risk allele possessed the association with bone damage regardless of anti citrullinated peptide antibody (ACPA) positivity in Asian RA patients. PADI4 gene codes PAD4 protein which has post-translational modification activity (citrullination). Padi4 is mainly expressed in myeloid cells and granulocytes. PADI4 Protein (Primary Amine Labeling), Human, Recombinant (His), Biotinylated is expressed in E. coli expression system with N-His tag. The predicted molecular weight is 76.6 kDa and the accession number is Q9UM07.

Anterior gradient protein (AGR) 3 is a highly related homologue of pro-oncogenic AGR2 and belongs to the family of protein disulfide isomerases. AGR3 was found in breast, ovary, prostate, and liver cancer, it is associated with the level of differentiation, slowly proliferating tumors, and more favorable prognosis of breast cancer patients. AGR3 is a specialized member of the PDI family that plays an unexpected role in the regulation of CBF and mucociliary clearance in the airway. AGR3 had been characterised as a novel potential biomarker both for breast cancer prognosis and early breast cancer detection from blood.

Peptidylarginine deiminase type4 (PADI4) was firstly identified as a non-MHC RA genetic risk factor. Furthermore, PADI4 risk allele possessed the association with bone damage regardless of anti citrullinated peptide antibody (ACPA) positivity in Asian RA patients. PADI4 gene codes PAD4 protein which has post-translational modification activity (citrullination). Padi4 is mainly expressed in myeloid cells and granulocytes. PADI4 Protein (Primary Amine Labeling), Cynomolgus, Recombinant (His), Biotinylated is expressed in E. coli expression system with N-His tag. The predicted molecular weight is 76.6 kDa and the accession number is A0A2K5USI5.

ERP27 contains 1 thioredoxin domain and is a noncatalytic member of the protein disulfide isomerase family. Protein disulfide isomerases (PDIs) constitute a family of structurally related enzymes which catalyze disulfide bonds formation, reduction, or isomerization of newly synthesized proteins in the lumen of the endoplasmic reticulum (ER). They act also as chaperones, and are, therefore, part of a quality-control system for the correct folding of the proteins in the same subcellular compartment. PDI has been found to have moderate effects (25-fold) on the rate of oxidative folding of proteins in vitro. Recombinant Human Protein Disulfide Isomerase is involved in disulphide-bond formation and isomerization, as well as the reduction of disulphide bonds in proteins. Recombinant PDI has been found to have moderate effects (25-fold) on the rate of oxidative folding of proteins in vitro. ERP27 is a widely expressed protein which localizes to the ER and may act as a protease, protein disulfide isomerase, thiol-disulfide oxidase or phospholipase. ERP27 doesn't contain a CXXC active site motif indicating that it is a catalytically redox-inactive member of the protein disulfide isomerase family.

Protein-arginine deiminase type-4, also known as HL-6 PAD, Peptidylarginine deiminase IV, Protein-arginine deiminase type I V and PADI4, is a cytoplasm and nucleus protein that belongs to the protein arginine deiminase family. PADI4 is expressed in CD34+stem cells in normal tissues, and many more CD34+ cells expressing PADI4 are present in tumour tissues. PADI4 post-translationally converts peptidylarginine to citrulline, a process called citrullination. Studies have demonstrated the high expression of PADI4 in various malignant tumor tissues. PADI4 is also expressed at high levels in the blood of patients with some malignant tumors. Citrullination of histone, cytokeratin, antithrombin and fibronectin have been confirmed to be involved in abnormal apoptosis, high coagulation, and disordered cell proliferation and differentiation, all of which are main features of malignant tumors. PADI4 may play an important role in tumorigenesis. Genetic variations in PADI4 are a cause of susceptibility to rheumatoid arthritis (RA). It is a systemic inflammatory disease with autoimmune features and a complex genetic component. It primarily affects the joints and is characterized by inflammatory changes in the synovial membranes and articular structures, widespread fibrinoid degeneration of the collagen fibers in mesenchymal tissues, and by atrophy and rarefaction of bony structures.

Peptidylarginine deiminase type4 (PADI4) was firstly identified as a non-MHC RA genetic risk factor. Furthermore, PADI4 risk allele possessed the association with bone damage regardless of anti citrullinated peptide antibody (ACPA) positivity in Asian RA patients. PADI4 gene codes PAD4 protein which has post-translational modification activity (citrullination). Padi4 is mainly expressed in myeloid cells and granulocytes. PADI4 Protein, Cynomolgus, Recombinant (His) is expressed in E. coli expression system with N-His tag. The predicted molecular weight is 76.6 kDa and the accession number is A0A2K5USI5.

Protein-Arginine Deiminase Type-4 (PADI4) belongs to the Protein Arginine Deiminase family. PADI4 is expressed in eosinophils and neutrophils, but it is not expressed in peripheral monocytes or lymphocytes. PADI4 catalyzes the citrullination deimination of arginine residues of proteins. In addition, PADI4 may play an important role in tumourigenesis. Genetic variations in PADI4 are a cause of susceptibility to rheumatoid arthritis (RA), which is a systemic inflammatory disease with autoimmune features and a complex genetic component.