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AB238862

Anti-PIH1D1 antibody

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(1 Publication)

Rabbit Polyclonal PIH1D1 antibody. Suitable for IP, IHC-P, ICC/IF and reacts with Human samples. Cited in 1 publication. Immunogen corresponding to Recombinant Full Length Protein corresponding to Human PIH1D1.

View Alternative Names

NOP17, PIH1D1, PIH1 domain-containing protein 1, Nucleolar protein 17 homolog

2 Images
Immunohistochemistry (Formalin/PFA-fixed paraffin-embedded sections) - Anti-PIH1D1 antibody (AB238862)
  • IHC-P

Supplier Data

Immunohistochemistry (Formalin/PFA-fixed paraffin-embedded sections) - Anti-PIH1D1 antibody (AB238862)

Paraffin-embedded human placenta tissue stained for PIH1D1 using ab238862 at 1/100 dilution in immunohistochemical analysis.

Immunocytochemistry/ Immunofluorescence - Anti-PIH1D1 antibody (AB238862)
  • ICC/IF

Supplier Data

Immunocytochemistry/ Immunofluorescence - Anti-PIH1D1 antibody (AB238862)

HeLa (Human epithelial cell line from cervix adenocarcinoma) cells stained for PIH1D1 (green) using ab238862 at 1/200 dilution in ICC/IF. Secondary antibody is Alexa Fluor® 488-conjugated Goat Anti-Rabbit IgG (H+L). The nuclear counterstain is DAPI.

The cells were fixed in 4% formaldehyde, permeabilized tissue using 0.2% Triton X-100 and blocked in 10% normal goat serum. The cells were then incubated with the antibody overnight at 4°C.

Key facts

Host species

Rabbit

Clonality

Polyclonal

Isotype

IgG

Carrier free

No

Reacts with

Human

Applications

IP, ICC/IF, IHC-P

applications

Immunogen

Recombinant Full Length Protein corresponding to Human PIH1D1.

Q9NWS0

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Proteins & Peptides

AB176047

Recombinant Human PIH1D1 protein (denatured) (His tag N-Terminus)

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Reactivity data

{ "title": "Reactivity Data", "filters": { "stats": ["", "Species", "Dilution Info", "Notes"], "tabs": { "all-applications": {"fullname" : "All Applications", "shortname": "All Applications"}, "IP" : {"fullname" : "Immunoprecipitation", "shortname":"IP"}, "IHCP" : {"fullname" : "Immunohistochemistry (Formalin/PFA-fixed paraffin-embedded sections)", "shortname":"IHC-P"}, "ICCIF" : {"fullname" : "Immunocytochemistry/ Immunofluorescence", "shortname":"ICC/IF"} }, "product-promise": { "all": "all", "testedAndGuaranteed": "tested", "guaranteed": "expected", "predicted": "predicted", "notRecommended": "not-recommended" } }, "values": { "Human": { "IP-species-checked": "testedAndGuaranteed", "IP-species-dilution-info": "1/200 - 1/2000", "IP-species-notes": "<p></p>", "IHCP-species-checked": "testedAndGuaranteed", "IHCP-species-dilution-info": "1/20 - 1/200", "IHCP-species-notes": "<p></p>", "ICCIF-species-checked": "testedAndGuaranteed", "ICCIF-species-dilution-info": "1/50 - 1/500", "ICCIF-species-notes": "<p></p>" } } }
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Properties and storage information

Form
Liquid
Purification technique
Affinity purification Protein G
Purification notes
Purity greater than 95%.
Storage buffer
pH: 7.4 Preservative: 0.03% Proclin 300 Constituents: PBS, 50% Glycerol (glycerin, glycerine)
Shipped at conditions
Blue Ice
Appropriate short-term storage duration
1-2 weeks
Appropriate short-term storage conditions
+4°C
Appropriate long-term storage conditions
-20°C
Aliquoting information
Upon delivery aliquot
Storage information
Avoid freeze / thaw cycle
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Supplementary information

This supplementary information is collated from multiple sources and compiled automatically.

PIH1D1 also known as PIH1 domain containing protein 1 plays a mechanical role in stabilizing multi-protein complexes. It weighs approximately 37 kDa. The protein exists mainly within the cytoplasm and nucleus of cells. PIH1D1 is a critical component of the R2TP complex contributing to its structural integrity and function. The R2TP complex plays a significant role in various cellular processes including transcription and the assembly of complexes like snoRNPs.
Biological function summary

PIH1D1 interacts with other proteins to mediate molecular chaperone activities. It forms part of the R2TP complex which stands for RNA polymerase II-associated protein 2; TP is related to tuberous sclerosis complexes. Together with other proteins such as RPAP3 it assists in assembling large multi-subunit complexes. This function is essential in maintaining normal cellular operations and stress responses facilitating the maturation and stabilization of many other proteins.

Pathways

PIH1D1 involves itself in the molecular chaperone network and mTOR signaling pathway. It interacts primarily with proteins related to the chaperone HSP90 where it helps to fold and stabilize newly synthesized proteins. The contact with mTORC1 complex which connects to growth and metabolic pathways illustrates its significant contributions to cell growth regulation and energy status sensing. PIH1D1’s role ensures that the pathways remain functional and adaptable.

Researchers have linked PIH1D1 to certain types of cancer and neurodevelopmental disorders. Its interaction with the tumor suppressor protein TSC1 suggests relevance in cancer pathogenesis where different mutations can disrupt normal cell growth control. Moreover piH1D1's involvement in the assembly of snoRNPs connects it to neurodevelopmental disorders where correct RNA processing is essential. Changes in its function can lead to significant cellular abnormalities contributing to disease progression.
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Product protocols

For this product, it's our understanding that no specific protocols are required. You can visit:
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Target data

Involved in the assembly of C/D box small nucleolar ribonucleoprotein (snoRNP) particles (PubMed : 17636026). Recruits the SWI/SNF complex to the core promoter of rRNA genes and enhances pre-rRNA transcription (PubMed : 22368283, PubMed : 24036451). Mediates interaction of TELO2 with the R2TP complex which is necessary for the stability of MTOR and SMG1 (PubMed : 20864032). Positively regulates the assembly and activity of the mTORC1 complex (PubMed : 24036451).
See full target information PIH1D1
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Publications (1)

Recent publications for all applications. Explore the full list and refine your search

Viruses 11: PubMed31018511

2019

Identification of RUVBL1 and RUVBL2 as Novel Cellular Interactors of the Ebola Virus Nucleoprotein.

Applications

Unspecified application

Species

Unspecified reactive species

M Jane Morwitzer,Sarah R Tritsch,Lisa H Cazares,Michael D Ward,Jonathan E Nuss,Sina Bavari,St Patrick Reid
View all publications
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Product promise

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For full details, please see our Terms & Conditions

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