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Merck

A0224

Anti-l/s-Afadin antibody produced in rabbit

affinity isolated antibody

동의어(들):

Anti-AF6, Anti-MLL-AF6, Anti-MLLT4, Anti-l-afadin

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제품정보 (DICE 배송 시 비용 별도)

UNSPSC Code:
12352203
NACRES:
NA.41
MDL number:
Conjugate:
unconjugated
Clone:
polyclonal
Application:
ARR, ICC, IF, IHC (f), WB
Citations:
29
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biological source

rabbit

Quality Level

conjugate

unconjugated

antibody form

affinity isolated antibody

antibody product type

primary antibodies

clone

polyclonal

mol wt

antigen ~200 kDa (and 190 kDa)

species reactivity

rat, human, canine, mouse

enhanced validation

independent
Learn more about Antibody Enhanced Validation

technique(s)

immunocytochemistry: suitable, immunohistochemistry (frozen sections): 1:1,000 using mouse liver sections., indirect immunofluorescence: 1:250 using cultured dog (MDCK) cells and of cultured human HepG2 cells, indirect immunofluorescence: 1:500 using frozen sections of mouse liver, microarray: suitable, western blot: 1:1000 using extract of rat brain.

shipped in

dry ice

storage temp.

−20°C

target post-translational modification

unmodified

Gene Information

human ... MLLT4(4301)
mouse ... Mllt4(17356)
rat ... Mllt4(26955)

General description

Afadin is a cell-cell adherens junction, F-actin binding multidomain protein. This adherens junction protein has two splicing variants: the ubiquitously expressed l-afadin, and the smaller s-afadin, which is abundantly expressed in neural tissues. Afadin associates with E-catenin proteins.
S-Afadin is a protein which lacks both the third proline-rich and the F-actin binding regions and is homologous to the human AF-6 (ALL-1 fusion partner from chromosome 6) gene product. Anti-l/s-Afadin is developed in rabbit using a synthetic peptide of rat afadin.

Immunogen

synthetic peptide corresponding to rat l/s afadin sequence, amino acids 1163-1179, with N-terminal cysteine added, conjugated to BSA.

Application

Anti-l/s-Afadin antibody produced in rabbit has been used in :
  • immunocytochemistry
  • immunohistochemistry
  • immunoprecipitation

Biochem/physiol Actions

Anti-l/s-Afadin specifically binds to l-afadin and s-afadin by immunoblotting (approximately 200 and 190 kDa respectively). Additional bands may appear in certain extract preparations in western blot assays. The immunizing peptide specifically inhibits the staining of the I/s-afadin bands. The antibody is specific for human, dog, rat, and mouse l/s-afadin.
s-Afadin binds to several cytoplasmic proteins such as the small guanosine triphosphatase (GTPase) Ras, the tight junction protein ZO-1 2 and the vinculin binding protein ponsin/ sorbin and SH3 domain containing 1 (SH3P12). In addition, l-afadin also binds through its PDZ several integral membrane components such as the Ca2+ -independent homophilic immunoglobulin-like nectin, the junctional adhesion molecule (JAM)4 and a subset of the EphB receptor protein-tyrosine kinases.

Physical form

Solution in 0.01 M phosphate buffered saline, pH 7.4, containing 1% BSA and 15 mM sodium azide

Disclaimer

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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저장 등급

10 - Combustible liquids

wgk

WGK 2

flash_point_f

Not applicable

flash_point_c

Not applicable



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관련 콘텐츠


Afadin: A novel actin filament-binding protein with one PDZ domain localized at cadherin-based cell-to-cell adherens junction
Mandai K, et al.
The Journal of cell biology, 139(2), 517-528 (1997)
Afadin is required for maintenance of dendritic structure and excitatory tone
Srivastava DP, et al.
The Journal of Biological Chemistry, 287(43), 35964-35974 (2012)
The junction-associated protein AF-6 interacts and clusters with specific Eph receptor tyrosine kinases at specialized sites of cell-cell contact in the brain
Buchert M, et al.
The Journal of cell biology, 144(2), 361-371 (1999)