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Key Documents

SAB1401801

Sigma-Aldrich

Anti-INF2 antibody produced in mouse

purified immunoglobulin, buffered aqueous solution

Synonyme(s) :

C14orf151, C14orf173, DKFZp762A0214, FLJ22056, MGC13251, pp9484

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About This Item

Code UNSPSC :
12352203
Nomenclature NACRES :
NA.41

Source biologique

mouse

Conjugué

unconjugated

Forme d'anticorps

purified immunoglobulin

Type de produit anticorps

primary antibodies

Clone

polyclonal

Forme

buffered aqueous solution

Espèces réactives

human

Technique(s)

western blot: 1 μg/mL

Numéro d'accès NCBI

Numéro d'accès UniProt

Conditions d'expédition

dry ice

Température de stockage

−20°C

Modification post-traductionnelle de la cible

unmodified

Informations sur le gène

human ... INF2(64423)

Description générale

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

Immunogène

INF2 (NP_116103, 1 a.a. ~ 234 a.a) full-length human protein.

Sequence
MSVKEGAQRKWAALKEKLGPQDSDPTEANLESADPELCIRLLQMPSVVNYSGLRKRLEGSDGGWMVQFLEQSGLDLLLEALARLSGRGVARISDALLQLTCVSCVRAVMNSRQGIEYILSNQGYVRQLSQALDTSNVMVKKQVFELLAALCIYSPEGHVLTLDALDHYKTVCSQQYRFSIVMNELSGSDNVPYVVTLLSVINAVILGPEDLRARTQLRNEFIGLQLLDVLARLR

Forme physique

Solution in phosphate buffered saline, pH 7.4

Clause de non-responsabilité

Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.

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Code de la classe de stockage

10 - Combustible liquids

Point d'éclair (°F)

Not applicable

Point d'éclair (°C)

Not applicable


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Consulter la Bibliothèque de documents

Balajikarthick Subramanian et al.
Journal of the American Society of Nephrology : JASN, 31(2), 374-391 (2020-01-12)
Mutations in the gene encoding inverted formin-2 (INF2), a member of the formin family of actin regulatory proteins, are among the most common causes of autosomal dominant FSGS. INF2 is regulated by interaction between its N-terminal diaphanous inhibitory domain (DID)
Shuangshuang Zhao et al.
Cytoskeleton (Hoboken, N.J.), 77(1-2), 16-24 (2019-12-11)
Formins and tropomyosins (Tpms) are two central components of the microfilaments. Formins are involved in the nucleation and polymerization of actin filaments, and Tpms form along the actin stress fibers to regulate their dynamics. However, the correlation between formins and

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