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P4HB  Antibody

All P4HB Reagents

Reactivity: Human  
Application: 
10827-MM12-50
10827-MM12-200
10827-MM12-100
10827-MM12-1
50 µg 
200 µg 
100 µg 
1 mg 
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    Reactivity: Human  
    Application: ELISA  IHC-P  
    10827-MM08-50
    10827-MM08-200
    10827-MM08-100
    10827-MM08-1
    50 µg 
    200 µg 
    100 µg 
    1 mg 
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    • Slide 1
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    • Slide 1
    Reactivity: Human  
    Application: ELISA  IF  IP  ICC/IF  
    10827-R016-50
    10827-R016-100
    50 µg 
    100 µg 
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    • Slide 1
    • Slide 1
    Reactivity: Human  
    Application: ELISA  WB  IHC-P  IP  
    10827-RP02-50
    10827-RP02-200
    10827-RP02-100
    50 µg 
    200 µg 
    100 µg 
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    • Slide 1
    • Slide 1
    • Slide 1
    Reactivity: Human  
    Application: ELISA  WB  
    10827-RP01-400
    10827-RP01-200
    10827-RP01-100
    400 µg 
    200 µg 
    100 µg 
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    • Slide 1
    Reactivity: Human  
    Application: FCM  IF  ICC/IF  
    10827-MM03-50
    10827-MM03-200
    10827-MM03-100
    50 µg 
    200 µg 
    100 µg 
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    • Slide 1
    • Slide 1
    Reactivity: Human  
    Application: FCM  
    10827-R016-F-25
    10827-R016-F-100
    25 Test 
    100 Tests 
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    • Slide 1
    Reactivity: Human  
    Application: FCM  
    10827-MM03-F-25
    10827-MM03-F-100
    25 Test 
    100 Tests 
    Add to Cart
    • Slide 1
    Reactivity: Mouse  
    Application: ELISA  WB  IHC-P  IP  
    50638-RP02-50
    50638-RP02-200
    50638-RP02-100
    50 µg 
    200 µg 
    100 µg 
    Add to Cart
    • Slide 1
    • Slide 1
    • Slide 1
    • Slide 1
    Reactivity: Mouse  
    Application: IHC-P  
    50638-R023-50
    50638-R023-100
    50 µg 
    100 µg 
    Add to Cart
    • Slide 1
    • Slide 1
    • Slide 1
    Reactivity: Mouse  
    Application: ELISA  
    50638-RP01-400
    50638-RP01-200
    50638-RP01-100
    400 µg 
    200 µg 
    100 µg 
    Add to Cart

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        P4HB Summary & Protein Information

        P4HB Background

        Gene Summary: This gene encodes the beta subunit of prolyl 4-hydroxylase, a highly abundant multifunctional enzyme that belongs to the protein disulfide isomerase family. When present as a tetramer consisting of two alpha and two beta subunits, this enzyme is involved in hydroxylation of prolyl residues in preprocollagen. This enzyme is also a disulfide isomerase containing two thioredoxin domains that catalyze the formation, breakage and rearrangement of disulfide bonds. Other known functions include its ability to act as a chaperone that inhibits aggregation of misfolded proteins in a concentration-dependent manner, its ability to bind thyroid hormone, its role in both the influx and efflux of S-nitrosothiol-bound nitric oxide, and its function as a subunit of the microsomal triglyceride transfer protein complex.
        General information above from NCBI
        Catalytic activity: Catalyzes the rearrangement of -S-S- bonds in proteins.
        Subunit structure: Homodimer. Monomers and homotetramers may also occur. Also constitutes the structural subunit of prolyl 4-hydroxylase and of the microsomal triacylglycerol transfer protein MTTP in mammalian cells. Stabilizes both enzymes and retain them in the ER without contributing to the catalytic activity (By similarity). Binds UBQLN1. Binds to CD4, and upon HIV-1 binding to the cell membrane, is part of a P4HB/PDI-CD4-CXCR4-gp120 complex. {ECO:0000250}.
        Subcellular location: Endoplasmic reticulum lumen. Melanosome. Cell membrane {ECO:0000305}; Peripheral membrane protein {ECO:0000305}. Note=Highly abundant. In some cell types, seems to be also secreted or associated with the plasma membrane, where it undergoes constant shedding and replacement from intracellular sources (Probable). Localizes near CD4-enriched regions on lymphoid cell surfaces. Identified by mass spectrometry in melanosome fractions from stage I to stage IV. {ECO:0000305}.
        Sequence similarity: Belongs to the protein disulfide isomerase family. {ECO:0000305}.; Contains 2 thioredoxin domains. {ECO:0000255|PROSITE-ProRule:PRU00691}.
        General information above from UniProt

        Protein disulfide-isomerase, also known as Cellular thyroid hormone-binding protein, Prolyl 4-hydroxylase subunit beta, p55 and P4HB, is a peripheral membrane protein which belongs to the protein disulfide isomerase family. P4HB is highly abundant. In some cell types, it seems to be also secreted or associated with the plasma membrane, where it undergoes constant shedding and replacement from intracellular sources. P4HB localizes near CD4-enriched regions on lymphoid cell surfaces. It is identified by mass spectrometry in melanosome fractions from stage I to stage IV. P4HB reduces and may activate fusogenic properties of HIV-1 gp120 surface protein, thereby enabling HIV-1 entry into the cell. P4HB catalyzes the formation, breakage and rearrangement of disulfide bonds. At the cell surface, it seems to act as a reductase that cleaves disulfide bonds of proteins attached to the cell. P4HB may therefore cause structural modifications of exofacial proteins. Inside the cell, it seems to form/rearrange disulfide bonds of nascent proteins. At high concentrations, P4HB functions as a chaperone that inhibits aggregation of misfolded proteins. At low concentrations, it facilitates aggregation (anti-chaperone activity). P4HB may be involved with other chaperones in the structural modification of the TG precursor in hormone biogenesis. It also acts a structural subunit of various enzymes such as prolyl 4-hydroxylase and microsomal triacylglycerol transfer protein MTTP.

        P4HB Alternative Name

        DSI,GIT,PDI,PHDB,PDIA1,PO4DB,PO4HB,PROHB,ERBA2L,P4Hbeta, [homo-sapiens]
        DSI,ERBA2L,GIT,P4HB,P4Hbeta,PDI,PDIA1,PHDB,PO4DB,PO4HB,PROHB, [human]
        ERp59,P4hb,PDI,Pdia1,RP23-84C12.2,Thbp, [mouse]
        PDI,Thbp,ERp59,Pdia1, [mus-musculus]

        P4HB Related Studies

      • Kivirikko KI, et al., 1989, FASEB J., 3 (5): 1609-17.
      • Pihlajaniemi T, et al.,1991, J Hepatol., 13, Suppl 3: S2
      • Fenouillet E., et al., 2001, J. Infect. Dis. 183:744-752.
      • Gevaert K., et al., 2003, Nat. Biotechnol. 21:566-569.
      • Barbouche R., et al., 2003, J. Biol. Chem. 278:3131-3136.
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