Recombinant Human P4HB Protein (C-6His)

Name: Recombinant Human P4HB Protein (C-6His)
Brand: Beta LifeScience
SKU: BL-1518NP
Availability: InStock

BL-1518NP: Greater than 95% as determined by reducing SDS-PAGE. (QC verified)

Collections: All products, High-quality recombinant proteins, Other recombinant proteins

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Product Overview

Description	Recombinant Human Prolyl 4-Hydroxylase Subunit Beta is produced by our Mammalian expression system and the target gene encoding Asp18-Lys505 is expressed with a 6His tag at the C-terminus.
Accession	P07237
Synonym	Protein Disulfide-Isomerase; PDI; Cellular Thyroid Hormone-Binding Protein; Prolyl 4-Hydroxylase Subunit Beta; p55; P4HB; ERBA2L; PDI; PDIA1; PO4DB
Gene Background	Protein Disulfide-Isomerase (P4HB) is an endoplasmic reticulum lumen protein that belongs to the protein disulfide isomerase family. P4HB contains two thioredoxin domains and catalyzes the formation, breakage, and rearrangement of -S-S- bonds in proteins. P4HB is involved in hydroxylation of prolyl residues in preprocollagen. P4HB has the ability to act as a chaperone that inhibits aggregation of misfolded proteins in a concentration-dependent manner. P4HB plays a role in both the influx and efflux of S-nitrosothiol-bound nitric oxide.
Molecular Mass	55.9 KDa
Apmol Mass	65 KDa, reducing conditions
Formulation	Supplied as a 0.2 μm filtered solution of PBS, pH 7.4.
Endotoxin	Less than 0.1 ng/µg (1 EU/µg) as determined by LAL test.
Purity	Greater than 95% as determined by reducing SDS-PAGE. (QC verified)
Biological Activity	Not tested
Reconstitution
Storage	Store at ≤-70°C, stable for 6 months after receipt. Store at ≤-70°C, stable for 3 months under sterile conditions after opening. Please minimize freeze-thaw cycles.
Shipping	The product is shipped on dry ice/polar packs. Upon receipt, store it immediately at the temperature listed below.
Usage	For Research Use Only

Target Details

Target Function	This multifunctional protein catalyzes the formation, breakage and rearrangement of disulfide bonds. At the cell surface, seems to act as a reductase that cleaves disulfide bonds of proteins attached to the cell. May therefore cause structural modifications of exofacial proteins. Inside the cell, seems to form/rearrange disulfide bonds of nascent proteins. At high concentrations, functions as a chaperone that inhibits aggregation of misfolded proteins. At low concentrations, facilitates aggregation (anti-chaperone activity). May be involved with other chaperones in the structural modification of the TG precursor in hormone biogenesis. Also acts a structural subunit of various enzymes such as prolyl 4-hydroxylase and microsomal triacylglycerol transfer protein MTTP. Receptor for LGALS9; the interaction retains P4HB at the cell surface of Th2 T helper cells, increasing disulfide reductase activity at the plasma membrane, altering the plasma membrane redox state and enhancing cell migration.
Subcellular Location	Endoplasmic reticulum. Endoplasmic reticulum lumen. Melanosome. Cell membrane; Peripheral membrane protein.
Protein Families	Protein disulfide isomerase family
Database References	HGNC: 8548 OMIM: 112240 KEGG: hsa:5034 STRING: 9606.ENSP00000327801 UniGene: PMID: 29191937 Overexpression of HIF-1alpha and P4HB is associated with poor prognosis in patients with gastric cancer. PMID: 29904245 Study demonstrated that the expression of P4HB is frequently upregulated at the mRNA and protein levels in diffuse gliomas. Its high expression was significantly correlated with high Ki-67, more TP53 mutations and poor survival outcome. These findings imply that high expression of P4HB plays an important role in diffuse glioma progression. PMID: 29207176 identify a potent and selective PDIA1 inhibitor, KSC-34, with 30-fold selectivity for the a site over the a' site. KSC-34 displays time-dependent inhibition of PDIA1 reductase activity in vitro with a kinact/ KI of 9.66 x 10(3) M(-1) s(-1) and is selective for PDIA1 over other members of the PDI family, and other cellular cysteine-containing proteins. PMID: 29521097 P4HB promotes hepatocellular carcinoma progression by down-regulating GRP78 expression and subsequently promoting epithelial-to-mesenchymal transition. PMID: 28052026 analysis of antiplatelet activity of CxxC through binding to Cys400 in the PDI a0 domain, which can be further exploited as a model for sitedriven antithrombotic agent development PMID: 28109047 Current findings indicate that thiol isomerase-mediated disulfide bond modification in receptors and plasma proteins is an important layer of control of thrombosis and vascular function more generally. PMID: 28598864 DIA1 was robustly secreted by physiological levels of arterial laminar shear in endothelial cells and supported alpha 5 integrin thiol oxidation. PMID: 28034831 Kinetic-based trapping by intervening sequence variants of the active sites of protein-disulfide isomerase identifies platelet protein substrates. PMID: 28364042 a mechanism of dual Ero1alpha regulation by dynamic redox interactions between PDI and the two Ero1alpha flexible loops that harbor the regulatory cysteines. PMID: 27703014 analysis of how redox affects human protein disulfide isomerase regulate binding affinity of 17 beta-estradiol PMID: 28257787 These findings improve our understanding of PDI-protected aggregation of wild-type alpha-Syn and its H50Q familial mutant. PMID: 27142583 Association of P4HB polymorphisms with sporadic amyotrophic lateral sclerosis susceptibility in the Chinese Han population. PMID: 26000911 the effect of the endoplasmic reticulum chaperone protein disulfide isomerase (PDI) on beta-cell dysfunction, was examined. PMID: 26607804 Amyotrophic lateral sclerosis-linked PDIA1 mutations disrupt motor neuron connectivity. PMID: 26869642 direct binding of PDIA1 to VWF, is reported. PMID: 26670633 Selective sequestration of PDI1A in a calcium depletion-mediated complex with the abundant chaperone calreticulin attenuates the effective concentration of this major lumenal thiol oxidant. PMID: 25575667 Cole-Carpenter syndrome is caused by a specific de novo mutation in P4HB that impairs the disulfide isomerase activity of protein disulfide isomerase. PMID: 25683117 PDI has a role as a competent regulator and a specific substrate of Ero1alpha govern efficient and faithful oxidative protein folding and maintain the ER redox homeostasis PMID: 25258311 The crystal structure of the dimeric form of noncatalytic bb' domains of human PDIA1 determined to 2.3 A resolution revealed that the formation of dimers occludes the substrate binding site. PMID: 24549644 Elevated P4HB expression is associated with temozolomide resistance in malignant glioma. PMID: 23444257 ). The results suggest that P4HB is a modifier gene inamyotrophic lateral sclerosis susceptibility and may represent a potential therapeutic target for amyotrophic lateral sclerosis . PMID: 23337974 A mixed disulfide complex was formed with the catalytic domain A1 from human PDI consistent with a model for cotranslational oxidative protein folding wherein PDI acts as a placeholder that is relieved by the pairing of cysteines caused by substrate folding. PMID: 23141538 TPM4, PDIA and SRC8 were also localized to the trophoblast cells, further highlighting the importance of these cytoskeletal remodelling proteins in early pregnancy PMID: 21373848 these data revealed a redox-regulated chaperone function of PDI in delivering antigenic peptides from TAP to MHC-I. PMID: 21299467 Functional PDI is rapidly secreted from human umbilical vein endothelial cells in culture upon activation with thrombin or after laser-induced stimulation. PMID: 20668226 domain c is required for the stabilization and maintenance of the chaperone function of PDI under extreme conditions PMID: 15358778 data indicate that binding sites in three PDI domains, a, b', and a', contribute to efficient C-P4H tetramer assembly PMID: 15590633 PDI can be S-nitrosated and PDI-SNO can be denitrosated by PDI suggesting that this enzyme could be intimately involved in the transport of intracellular NO equivalents to the cell surface. PMID: 15611098 Data show that protein disulfide isomerase can switch its conformation from dimer to tetramer in its functions as a foldase. PMID: 15695804

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Proteins are sensitive to heat, and freeze-drying can preserve the activity of the majority of proteins. It improves protein stability, extends storage time, and reduces shipping costs. However, freeze-drying can also lead to the loss of the active portion of the protein and cause aggregation and denaturation issues. Nonetheless, these adverse effects can be minimized by incorporating protective agents such as stabilizers, additives, and excipients, and by carefully controlling various lyophilization conditions.

Commonly used protectant include saccharides, polyols, polymers, surfactants, some proteins and amino acids etc. We usually add 8% (mass ratio by volume) of trehalose and mannitol as lyoprotectant. Trehalose can significantly prevent the alter of the protein secondary structure, the extension and aggregation of proteins during freeze-drying process; mannitol is also a universal applied protectant and fillers, which can reduce the aggregation of certain proteins after lyophilization.

Our protein products do not contain carrier protein or other additives (such as bovine serum albumin (BSA), human serum albumin (HSA) and sucrose, etc., and when lyophilized with the solution with the lowest salt content, they often cannot form A white grid structure, but a small amount of protein is deposited in the tube during the freeze-drying process, forming a thin or invisible transparent protein layer.

Reminder: Before opening the tube cap, we recommend that you quickly centrifuge for 20-30 seconds in a small centrifuge, so that the protein attached to the tube cap or the tube wall can be aggregated at the bottom of the tube. Our quality control procedures ensure that each tube contains the correct amount of protein, and although sometimes you can't see the protein powder, the amount of protein in the tube is still very precise.

To learn more about how to properly dissolve the lyophilized recombinant protein, please visit Lyophilization FAQs.