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AB50246

Anti-PADI3 / PAD3 antibody

4

(1 Review)

|

(21 Publications)

Rabbit Polyclonal PADI3 / PAD3 antibody. Suitable for IP, ELISA, WB and reacts with Human samples. Cited in 21 publications. Immunogen corresponding to Synthetic Peptide within Human PADI3.

View Alternative Names

PAD3, PDI3, PADI3, Protein-arginine deiminase type-3, Peptidylarginine deiminase III, Protein-arginine deiminase type III

Key facts

Host species

Rabbit

Clonality

Polyclonal

Isotype

IgG

Carrier free

No

Reacts with

Human

Applications

WB, ELISA, IP

applications

Immunogen

Synthetic Peptide within Human PADI3. The exact immunogen used to generate this antibody is proprietary information.

Q9ULW8

Specificity

This antibody reacts specifically with the 75kDa PADI3 / PAD3 protein. It shows no cross reactivity with the other isoforms.

Reactivity data

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Properties and storage information

Form
Liquid
Purity
Whole antiserum
Storage buffer
Constituents: Whole serum
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

Supplementary information

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

PADI3 also known as PAD3 is an enzyme that belongs to the peptidylarginine deiminase family. It converts arginine residues into citrullines in the presence of calcium ions an activity known as citrullination or deimination. PADI3 has a molecular mass of approximately 74 kDa. Expression of this enzyme is found mainly in hair follicles skin and possibly other epithelial tissues where it modifies structural proteins important for tissue organization and function.
Biological function summary

PADI3 plays a role in the formation of the hair shaft by modifying trichohyalin a core structural protein and possibly other substrates within hair matrix keratinocytes. It contributes to the stabilization and structural integrity of hair and skin proteins. Although not massive in function alone PADI3 may work as part of a complex with other proteins to achieve these modifications effectively.

Pathways

PADI3 fits into the intricate web of keratinization and epidermal differentiation processes. It is part of pathways that involve protein deimination alongside proteins such as PAD2 and PAD1 which work together to modify and stabilize intermediate filaments and other structural protein components within the skin and hair.

PADI3 is linked most commonly to hair and skin-related conditions including some forms of alopecia and psoriasis. Studies suggest the enzyme might interact with keratin proteins influencing the abnormal keratinization observed in these disorders. Mutations in PADI3 as well as related proteins like keratin may disrupt normal protein modification and aggregation leading to these pathological conditions.

Product protocols

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

Target data

Catalyzes the deimination of arginine residues of proteins.
See full target information PADI3

Publications (21)

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

International journal of molecular sciences 25: PubMed39201398

2024

Targeting Peptidylarginine Deiminase 3 to Efficiently Suppress Herpes Simplex Virus Type 2 Infection.

Applications

Unspecified application

Species

Unspecified reactive species

Selina Pasquero,Francesca Gugliesi,Matteo Biolatti,Camilla Albano,Greta Bajetto,Linda Trifirò,Stefano Raviola,Valentina Dell'Oste,Marco De Andrea

PLoS pathogens 19:e1011849 PubMed38055760

2023

Citrullination profile analysis reveals peptidylarginine deaminase 3 as an HSV-1 target to dampen the activity of candidate antiviral restriction factors.

Applications

Unspecified application

Species

Unspecified reactive species

Selina Pasquero,Francesca Gugliesi,Matteo Biolatti,Valentina Dell'Oste,Camilla Albano,Greta Bajetto,Gloria Griffante,Linda Trifirò,Bianca Brugo,Stefano Raviola,Davide Lacarbonara,Qiao Yang,Sen Sudeshna,Leonard Barasa,Hafeez Haniff,Paul R Thompson,Santo Landolfo,Marco De Andrea

International journal of molecular sciences 23: PubMed36361903

2022

Differential, Stage Dependent Detection of Peptidylarginine Deiminases and Protein Deimination in Lewy Body Diseases-Findings from a Pilot Study.

Applications

Unspecified application

Species

Unspecified reactive species

Audrey Mercer,Zane Jaunmuktane,Mariya Hristova,Sigrun Lange

ACS omega 7:28378-28387 PubMed35990454

2022

Autocitrullination and Changes in the Activity of Peptidylarginine Deiminase 3 Induced by High Ca Concentrations.

Applications

Unspecified application

Species

Unspecified reactive species

Mizuki Sawata,Hiroki Shima,Kazutaka Murayama,Toshitaka Matsui,Kazuhiko Igarashi,Kazumasa Funabashi,Kenji Ite,Kenji Kizawa,Hidenari Takahara,Masaki Unno

International journal of molecular sciences 23: PubMed35955829

2022

A Pilot Study on Peptidylarginine Deiminases and Protein Deimination in Animal Cancers across Vertebrate Species.

Applications

Unspecified application

Species

Unspecified reactive species

Jameel M Inal,Mariya Hristova,Sigrun Lange

International journal of molecular sciences 23: PubMed35563075

2022

Acute Hypoxia Alters Extracellular Vesicle Signatures and the Brain Citrullinome of Naked Mole-Rats ().

Applications

Unspecified application

Species

Unspecified reactive species

Stefania D'Alessio,Hang Cheng,Liam Eaton,Igor Kraev,Matthew E Pamenter,Sigrun Lange

Antiviral research 200:105278 PubMed35288208

2022

Novel antiviral activity of PAD inhibitors against human beta-coronaviruses HCoV-OC43 and SARS-CoV-2.

Applications

Unspecified application

Species

Unspecified reactive species

Selina Pasquero,Francesca Gugliesi,Gloria Griffante,Valentina Dell'Oste,Matteo Biolatti,Camilla Albano,Greta Bajetto,Serena Delbue,Lucia Signorini,Maria Dolci,Santo Landolfo,Marco De Andrea

Biology 10: PubMed33805829

2021

Post-Translational Protein Deimination Signatures in Plasma and Plasma EVs of Reindeer ().

Applications

Unspecified application

Species

Unspecified reactive species

Stefania D'Alessio,Stefanía Thorgeirsdóttir,Igor Kraev,Karl Skírnisson,Sigrun Lange

International journal of molecular sciences 22: PubMed33573274

2021

Peptidylarginine Deiminase Inhibitor Application, Using Cl-Amidine, PAD2, PAD3 and PAD4 Isozyme-Specific Inhibitors in Pancreatic Cancer Cells, Reveals Roles for PAD2 and PAD3 in Cancer Invasion and Modulation of Extracellular Vesicle Signatures.

Applications

Unspecified application

Species

Unspecified reactive species

Pinar Uysal-Onganer,Stefania D'Alessio,Maria Mortoglou,Igor Kraev,Sigrun Lange

Frontiers in immunology 11:651 PubMed32411128

2020

Deimination Protein Profiles in Reveal Plasma and Extracellular Vesicle-Specific Signatures Relating to Immunity, Metabolic Function, and Gene Regulation.

Applications

Unspecified application

Species

Unspecified reactive species

Michael F Criscitiello,Igor Kraev,Lene H Petersen,Sigrun Lange
View all publications

Product promise

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