P4HB Recombinant Monoclonal Antibody

Code: CSB-RA923900A0HU

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Size:

50μl100μl

US$210

Quantity:

Species Reactivity: Human, Mouse

Application: ELISA, WB, IHC, IF, FC

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Product Details
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Target Background

Product Details

Uniprot NO.

P07237

Target Names

P4HB

Alternative Names

Protein disulfide-isomerase (PDI) (EC 5.3.4.1) (Cellular thyroid hormone-binding protein) (Prolyl 4-hydroxylase subunit beta) (p55), P4HB, ERBA2L PDI PDIA1 PO4DB

Species Reactivity

Human, Mouse

Immunogen

A synthesized peptide from human P4HB protein

Conjugate

Non-conjugated

Clonality

Monoclonal

Isotype

Rabbit IgG

Clone No.

3F11

Purification Method

Affinity-chromatography

Concentration

It differs from different batches. Please contact us to confirm it.

Buffer

Preservative: 0.03% Proclin 300
Constituents: 50% Glycerol, 0.01M PBS, PH 7.4

Form

Liquid
Note: We will preferentially ship the format that we have in stock, however, if you have any special requirement for the format, please remark your requirement when placing the order, we will prepare according to your demand.

Scope Application

ELISA Protocol Western Blotting(WB) Protocol Immunohistochemistry (IHC) Protocol Immunofluorescence (IF) Protocol Flow Cytometry (FC) Protocol

Recommended Dilution

Application	Recommended Dilution
WB	1:500-1:2000
IHC	1:50-1:200
IF	1:50-1:200
FC	1:50-1:200

Storage

Upon receipt, store at -20°C or -80°C. Avoid repeated freeze.

Lead Time

Basically, we can dispatch the products out in 1-3 working days after receiving your orders. Delivery time maybe differs from different purchasing way or location, please kindly consult your local distributors for specific delivery time.
Note: All of our proteins are default shipped with normal blue ice packs, if you request to ship with dry ice, please communicate with us in advance and extra fees will be charged.

Usage

For Research Use Only. Not for use in diagnostic or therapeutic procedures.

Datasheet & COA

Antibody FAQs

Images

Western Blot
Positive WB detected in: HepG2 whole cell lysate(30µg), COLO-205 whole cell lysate(30µg), Hela whole cell lysate(30µg), MCF-7 whole cell lysate(30µg), Mouse liver tissue lysate(30µg)
All lanes: PDI antibody at 1:1000
Secondary
Goat polyclonal to rabbit IgG at 1/40000 dilution
Predicted band size: 57 kDa
Observed band size: 60 kDa
Exposure time：3min
IHC image of CSB-RA923900A0HU diluted at 1:100 and staining in paraffin-embedded human pancreatic cancer performed on a Leica BondTM system. After dewaxing and hydration, antigen retrieval was mediated by high pressure in a citrate buffer (pH 6.0). Section was blocked with 10% normal goat serum 30min at RT. Then primary antibody (1% BSA) was incubated at 4°C overnight. The primary is detected by a Goat anti-rabbit polymer IgG labeled by HRP and visualized using 0.05% DAB.
Immunofluorescence staining of HepG2 cell with CSB-RA923900A0HU at 1:50, counter-stained with DAPI. The cells were fixed in 4% formaldehyde and blocked in 10% normal Goat Serum. The cells were then incubated with the antibody overnight at 4°C. The secondary antibody was Alexa Fluor 488-congugated AffiniPure Goat Anti-Rabbit IgG(H+L).
Overlay Peak curve showing Hela cells stained with CSB-RA923900A0HU (red line) at 1:100. The cells were fixed in 4% formaldehyde and permeated by 0.2% TritonX-100 for 10min. Then 10% normal goat serum to block non-specific protein-protein interactions followed by the antibody (1ug/1*10⁶cells) for 45min at 4℃. The secondary antibody used was FITC-conjugated goat anti-rabbit IgG (H+L) at 1/200 dilution for 35min at 4℃.Control antibody (green line) was Rabbit IgG (1ug/1*10⁶cells) used under the same conditions. Acquisition of >10,000 events was performed.

Description

Protein disulfide isomerase (PDI), encoded by the P4HB gene, serves as a critical molecular chaperone within the endoplasmic reticulum, where it catalyzes the formation, breakage, and rearrangement of disulfide bonds essential for proper protein folding. Beyond its enzymatic role, PDI functions as the beta subunit of prolyl 4-hydroxylase and has been identified as a cellular thyroid hormone-binding protein, positioning it at the intersection of protein quality control, collagen biosynthesis, and cellular signaling research. Its dysregulation has been implicated in ER stress responses, cancer progression, and neurodegenerative conditions, making it a compelling target for investigators across multiple disciplines.

This recombinant monoclonal antibody, generated against a synthetic peptide derived from human P4HB, offers the reproducibility and sequence-defined consistency that demanding experimental workflows require. As a rabbit IgG produced through recombinant technology, it eliminates the lot-to-lot variability that can compromise longitudinal studies or multi-site collaborations.

Validation across multiple platforms demonstrates genuine experimental flexibility. Western blot analysis detects a band at approximately 60 kDa in HepG2, COLO-205, HeLa, and MCF-7 human cell lysates, as well as mouse liver tissue, confirming cross-species reactivity between human and mouse samples. The slightly higher observed molecular weight compared to the 57 kDa predicted size likely reflects post-translational glycosylation characteristic of ER-resident proteins. Immunohistochemistry staining has been validated in paraffin-embedded human pancreatic cancer tissue, while immunofluorescence and flow cytometry applications have been confirmed in HepG2 and HeLa cells, respectively.

Researchers investigating ER stress pathways, protein folding disorders, or tumor microenvironment biology will find this antibody well-suited for comprehensive target characterization across complementary detection methods.

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Target Background

Function(From Uniprot)

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.

Gene References into Functions

Peroxynitrite preferentially oxidizes the dithiol redox motifs of protein-disulfide isomerase. 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