Inf2 (human) recombinant (full leng ht protein gst tag) 10 µg
Produit ni repris ni échangé excepté en cas d’erreur du prestataire.
Points clés
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]
Garantie
Garantie 0 Mois
Description
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
