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AB151071

Anti-HERC1 antibody

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(1 Publication)

Rabbit Polyclonal HERC1 antibody. Suitable for IHC-P and reacts with Human samples. Cited in 1 publication. Immunogen corresponding to Recombinant Fragment Protein within Human Probable E3 ubiquitin-protein ligase HERC1 aa 250-400.

View Alternative Names

Probable E3 ubiquitin-protein ligase HERC1, HECT domain and RCC1-like domain-containing protein 1, HECT-type E3 ubiquitin transferase HERC1, p532, p619, HERC1

1 Images
Immunohistochemistry (Formalin/PFA-fixed paraffin-embedded sections) - Anti-HERC1 antibody (AB151071)
  • IHC-P

Unknown

Immunohistochemistry (Formalin/PFA-fixed paraffin-embedded sections) - Anti-HERC1 antibody (AB151071)

Immunohistochemical analysis of paraffin-embedded Human lymph node tissue labeling HERC1 with ab151071 at 1/50 dilution.

Key facts

Host species

Rabbit

Clonality

Polyclonal

Isotype

IgG

Carrier free

No

Reacts with

Human

Applications

IHC-P

applications

Immunogen

Recombinant Fragment Protein within Human Probable E3 ubiquitin-protein ligase HERC1 aa 250-400. The exact immunogen used to generate this antibody is proprietary information.

Q15751

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Reactivity data

{ "title": "Reactivity Data", "filters": { "stats": ["", "Species", "Dilution Info", "Notes"], "tabs": { "all-applications": {"fullname" : "All Applications", "shortname": "All Applications"}, "IHCP" : {"fullname" : "Immunohistochemistry (Formalin/PFA-fixed paraffin-embedded sections)", "shortname":"IHC-P"} }, "product-promise": { "all": "all", "testedAndGuaranteed": "tested", "guaranteed": "expected", "predicted": "predicted", "notRecommended": "not-recommended" } }, "values": { "Human": { "IHCP-species-checked": "testedAndGuaranteed", "IHCP-species-dilution-info": "1/50 - 1/200", "IHCP-species-notes": "<p></p> Perform heat-mediated antigen retrieval with citrate buffer pH 6 before commencing with IHC staining protocol." }, "Mouse": { "IHCP-species-checked": "predicted", "IHCP-species-dilution-info": "", "IHCP-species-notes": "" }, "Rat": { "IHCP-species-checked": "predicted", "IHCP-species-dilution-info": "", "IHCP-species-notes": "" }, "Cow": { "IHCP-species-checked": "predicted", "IHCP-species-dilution-info": "", "IHCP-species-notes": "" }, "Horse": { "IHCP-species-checked": "predicted", "IHCP-species-dilution-info": "", "IHCP-species-notes": "" }, "Pig": { "IHCP-species-checked": "predicted", "IHCP-species-dilution-info": "", "IHCP-species-notes": "" } } }
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Properties and storage information

Form
Liquid
Purification technique
Affinity purification Immunogen
Storage buffer
pH: 7.2 Preservative: 0.02% Sodium azide Constituents: PBS, 40% Glycerol (glycerin, glycerine)
Shipped at conditions
Blue Ice
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.

HERC1 also called HECT and RLD domain containing E3 ubiquitin protein ligase 1 possesses a significant molecular weight of approximately 532 kDa. The protein functions mechanically as an E3 ubiquitin ligase marking specific proteins for degradation by attaching ubiquitin molecules. HERC1 is expressed across various tissues including the brain indicating its widespread role in cellular regulation. The presence of HECT and RLD domains enables HERC1 to interact with other proteins and facilitate ubiquitination processes effectively.
Biological function summary

HERC1 enhances cellular protein homeostasis by regulating protein turnover through ubiquitination. This protein participates in maintaining cellular equilibrium by tagging unwanted proteins for degradation preventing the accumulation of defective proteins. HERC1 often operates as part of multi-protein complexes ensuring precise control over cell signaling and various cellular activities. The strategic positioning of HERC1 in protein quality control mechanisms emphasizes its dynamic role in cellular health.

Pathways

HERC1 plays a part in the ubiquitin-proteasome pathway and cell cycle regulation. The ubiquitin-proteasome pathway is essential for protein degradation and HERC1's function as an E3 ligase directly influences this system. Within this pathway HERC1 interacts with proteins such as ubiquitin-conjugating enzymes to facilitate orderly protein breakdown. Additionally HERC1 influences cell cycle regulation by controlling the stability of cycle-regulating proteins contributing to proper cell division and growth.

HERC1 is associated with neurodegenerative conditions and cancers. The role of HERC1 in protein ubiquitination and balance indicates its connection to neurological disorders like Alzheimer's disease where protein accumulation is a hallmark feature. Mutations in HERC1 have been linked to disruptions in ubiquitin pathways associating it with cancer development by impacting the degradation of key regulatory proteins. The interplay between HERC1 and the stability of oncogenic proteins accentuates its importance in understanding cancer pathophysiology.
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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 membrane trafficking via some guanine nucleotide exchange factor (GEF) activity and its ability to bind clathrin. Acts as a GEF for Arf and Rab, by exchanging bound GDP for free GTP. Binds phosphatidylinositol 4,5-bisphosphate, which is required for GEF activity. May also act as a E3 ubiquitin-protein ligase which accepts ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a thioester and then directly transfers the ubiquitin to targeted substrates.
See full target information Probable E3 ubiquitin-protein ligase HERC1
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Publications (1)

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

EMBO reports 24:e57228 PubMed37818824

2023

Tetracyclines activate mitoribosome quality control and reduce ER stress to promote cell survival.

Applications

Unspecified application

Species

Unspecified reactive species

Conor T Ronayne,Thomas D Jackson,Christopher F Bennett,Elizabeth A Perry,Noa Kantorovic,Pere Puigserver
View all publications
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