Gauss

Inf2 (human) recombinant (full leng ht protein gst tag) 10 µg

Réf. UGAP : 3814425 Réf. Fournisseur : 16143613 Réf. Constructeur : H00064423-P01
Franco de port et d'emballage pour toutes les commandes supérieures à 80€ HT.

Produit ni repris ni échangé excepté en cas d’erreur du prestataire.
La quantité choisie doit être comprise entre 1 et 999 999.

Points clés

Used for AP, Array, ELISA, WB-Re

Actin filaments grow only when actin monomers have access to the fast-growing barbed end of the filament. The geometry of the filament network depends on the actions of the ARP2/3 complex (MIM 604221) and members of the formin family, such as INF2. The ARP2/3 complex binds to the sides of preexisting filaments and nucleates filaments whose barbed ends are quickly blocked by capping proteins, producing brush-like structures, such as those found at the leading edges of crawling cells. In contrast, formins bind to the barbed ends of growing filaments and protect them from capping, creating long filaments that can be cross-linked into bundles, such as those found in actin cables of yeast. Interaction of formins with actin barbed ends occurs through the formin homology-2 (FH2) domain. FH2 domains accelerate filament nucleation, move with the barbed end as the filament grows, and block capping of the barbed end by proteins such as gelsolin (GSN; MIM 137350). The FH1 domain of formins binds to profilin (see MIM 176610) and accelerates elongation from the FH2-bound barbed ends (Bindschadler and McGrath, 2004 [PubMed 15466701]; Chhabra and Higgs, 2006 [PubMed 16818491]).[supplied by OMIM]

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Description

Used for AP, Array, ELISA, WB-Re

Actin filaments grow only when actin monomers have access to the fast-growing barbed end of the filament. The geometry of the filament network depends on the actions of the ARP2/3 complex (MIM 604221) and members of the formin family, such as INF2. The ARP2/3 complex binds to the sides of preexisting filaments and nucleates filaments whose barbed ends are quickly blocked by capping proteins, producing brush-like structures, such as those found at the leading edges of crawling cells. In contrast, formins bind to the barbed ends of growing filaments and protect them from capping, creating long filaments that can be cross-linked into bundles, such as those found in actin cables of yeast. Interaction of formins with actin barbed ends occurs through the formin homology-2 (FH2) domain. FH2 domains accelerate filament nucleation, move with the barbed end as the filament grows, and block capping of the barbed end by proteins such as gelsolin (GSN; MIM 137350). The FH1 domain of formins binds to profilin (see MIM 176610) and accelerates elongation from the FH2-bound barbed ends (Bindschadler and McGrath, 2004 [PubMed 15466701]; Chhabra and Higgs, 2006 [PubMed 16818491]).[supplied by OMIM]

Caractéristiques

Fournisseur
FISHER SCIENTIFIC S.A.S.
Marque
ABNOVA
Référence fabricant
H00064423-P01
Référence distributeur
16143613
Vendu par
10 ug
Quantité
N/A
Lieu de fabrication
Taiwan
Lieu de stockage
France
Délai de péremption à la date de livraison
12 mois
Code à barre
non
Soumis à carboglace
oui
Libellé produit fabricant
10ug inf2 (human) recombinant protein (p01)
Certification
RUO
Marquage CE DIV
non
Type de produit
protéine
Type de protéine
oui
Type d'antibiotique
non
Type d'enzyme
non
Température de conservation (°C)
-80 °C
Température de transport
carboglace
Dispositif stérile
non
Type d'acide nucléique extrait
non
Origine humaine
non
Sans composant animal
non
Matière dangereuse
non
Autres caractéristiques
Abnova Human INF2 Full-length ORF (ENSP00000344000, 1 a.a. - 337 a.a.) Recombinant Protein with GST-tag at N-terminal, Quantity: 10 ug, Format: Liquid, Formulation: 50mM Tris-HCI, 10mM reduced Glutathione, pH-8.0 in the elution buffer., Host Species:
Classification REACH
non
Code douanier
38229000
Nomenclature Nacres
NA.55
Nomenclature IFPEN
NA.55
Nomenclature CEA
SGP01
Nomenclature IRSN
273
Nomenclature INSERM
NA.NA55
Nomenclature CNRS
NA55
Nomenclature CHU
18.551
Nomenclature DGOS
LD10AOOO
Type d’application
ELISA, Western-Blot
Type d'échantillon
protéine
Reprise en cas d’erreur client
non
Domaine de recherche
protéomique