Accéder au contenu
Merck
Toutes les photos(1)

Principaux documents

Voir toute la documentation

SRP5223

Sigma-Aldrich

PAD1, GST tagged human

recombinant, expressed in baculovirus infected Sf9 cells, ≥70% (SDS-PAGE), buffered aqueous glycerol solution

Synonyme(s) :

HPAD10, PADI1, PDI, PDI1

Se connecterpour consulter vos tarifs contractuels et ceux de votre entreprise/organisme
Toutes les photos(1)

About This Item

Code UNSPSC :
12352200
Nomenclature NACRES :
NA.32

Source biologique

human

Produit recombinant

expressed in baculovirus infected Sf9 cells

Pureté

≥70% (SDS-PAGE)

Forme

buffered aqueous glycerol solution

Poids mol.

~95 kDa

Numéro d'accès NCBI

NM_013358

Application(s)

cell analysis

Conditions d'expédition

dry ice

Température de stockage

−70°C

Informations sur le gène

human ... PADI1(29943)

Description générale

Peptidyl arginine deiminase 1 (PAD1) is a member of the peptidyl arginine deiminase family of enzymes. It is a component of the 26S proteasome, a multiprotein complex that degrades proteins targeted for destruction by the ubiquitin pathway. PAD1 is expressed in the epidermis and uterus. The gene encoding this protein is localized on human chromosome 1p36.13.

Actions biochimiques/physiologiques

Peptidyl arginine deiminases catalyze the post-translational deimination of proteins by converting arginine residues into citrullines in the presence of calcium ions. The overexpression of PAD1 induced a distinctive pattern of multidrug resistance in mammalian cells and moderate resistance to ultraviolet light. PAD1 is also responsible for substrate deubiquitination during proteasomal degradation. It deiminates filaggrin in the last stages of keratinocyte differentiation. Thus, PAD1 has a role in epidermis function and homeostasis. The protein has been genetically associated with rheumatoid arthritis.

Forme physique

Supplied in 50mM Tris-HCl, pH 7.5, 150mM NaCl, 10mM glutathione, 0.1mM EDTA, 0.25mM DTT, 0.1mM PMSF, 25% glycerol.

Notes préparatoires

after opening, aliquot into smaller quantities and store at -70 °C. Avoid repeating handling and multiple freeze/thaw cycles

Remarque sur l'analyse

This protein is not assayed for enzymatic activity.

Code de la classe de stockage

10 - Combustible liquids

Classe de danger pour l'eau (WGK)

WGK 1

Point d'éclair (°F)

Not applicable

Point d'éclair (°C)

Not applicable

Certificats d'analyse (COA)

Recherchez un Certificats d'analyse (COA) en saisissant le numéro de lot du produit. Les numéros de lot figurent sur l'étiquette du produit après les mots "Lot" ou "Batch".

Déjà en possession de ce produit ?

Retrouvez la documentation relative aux produits que vous avez récemment achetés dans la Bibliothèque de documents.

Consulter la Bibliothèque de documents

Citrullination of CXCL8 by peptidylarginine deiminase alters receptor usage, prevents proteolysis, and dampens tissue inflammation.
Proost P
The Journal of Experimental Medicine (2008)
Potential Role of Peptidylarginine Deiminase Enzymes and Protein Citrullination in Cancer Pathogenesis
Sunish Mohanan, et.la
Biochemistry Research International (2012)
The peptidylarginine deiminases expressed in human epidermis differ in their substrate specificities and subcellular locations.
Mechin MC
Cellular and Molecular Life Sciences (2005)
Identification of 45 novel SNPs in the 83-kb region containing peptidylarginine deiminase types 1 and 3 loci on chromosomal band 1p36.13.
Lida A and Nakamura Y
Journal of Human Genetics (2004)
Tingting Yao et al.
Nature, 419(6905), 403-407 (2002-09-28)
The 26S proteasome is responsible for most intracellular proteolysis in eukaryotes. Efficient substrate recognition relies on conjugation of substrates with multiple ubiquitin molecules and recognition of the polyubiquitin moiety by the 19S regulatory complex--a multisubunit assembly that is bound to
Afficher tous les articles scientifiques apparentés

Notre équipe de scientifiques dispose d'une expérience dans tous les secteurs de la recherche, notamment en sciences de la vie, science des matériaux, synthèse chimique, chromatographie, analyse et dans de nombreux autres domaines..

Contacter notre Service technique