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Key Documents

A6104

Sigma-Aldrich

Anti-ARP2 antibody, Mouse monoclonal

clone FMS96, purified from hybridoma cell culture

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About This Item

Numéro MDL:
Code UNSPSC :
12352203
Nomenclature NACRES :
NA.41

Source biologique

mouse

Niveau de qualité

Conjugué

unconjugated

Forme d'anticorps

purified immunoglobulin

Type de produit anticorps

primary antibodies

Clone

FMS96, monoclonal

Forme

buffered aqueous solution

Poids mol.

antigen 40-45 kDa

Espèces réactives

mouse, human, rat, canine

Conditionnement

antibody small pack of 25 μL

Technique(s)

immunocytochemistry: suitable
indirect ELISA: suitable
microarray: suitable
western blot: 0.5-1 μg/mL using total cell extract of C2 mouse myoblast cells

Isotype

IgG1

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 ... ACTR2(10097)
mouse ... Actr2(66713)
rat ... Actr2(289820)

Description générale

ARP2 is part of a complex with 7 subunits called ARP2/3. ARP2 is an actin-related protein that function to regulate the actin cytoskeleton.
Anti-ARP2 antibody, Mouse monoclonal, (mouse IgG1 isotype) is derived from the FMS96 hybridoma produced by the fusion of mouse myeloma cells (NS1 cells) and splenocytes from BALB/c mice immunized with recombinant human ARP2.
Mouse Monoclonal Anti-ARP2 antibody binds to human, canine, rat, and mouse ARP2, 40-45kDa.

Immunogène

recombinant human ARP2

Application

Anti-ARP2 antibody, Mouse monoclonal has been used in:
  • Immunoblotting
  • Immunocytochemistry
  • Enzyme linked immuosorbent assay

Actions biochimiques/physiologiques

Actin-related protein 2 (ARP2) is a part of ARP2/3 complex and play a key role in actin filament formation. It mediates changes in the polymerization state of actin filaments. The Wiskott-Aldrich Syndrome protein (WASP) regulates ARP2/3 complex of proteins. The ARP2/3 complex and its activator spinocerebellar ataxia, autosomal recessive 2 (Scar2) are involved in Golgi polarization in NIH 3T3 cells. However in primary astrocytes, Golgi polarization involves neither actin cytoskeleton or Arp2/3 complex nor any WASP-family of proteins. In a different model, it was found that the ARP2/3 complex was necessary for neutrophil chemotaxis and phagocytosis. By genetic and loss of function studies, it was demonstrated that Scar is the major regulator of the ARP2/3 complex rather than the WASP family of proteins, the latter having more restricted roles in specific cellular events.

Forme physique

Solution in 0.01 M phosphate buffered saline, pH 7.4, containing 15 mM sodium azide.

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

Classe de danger pour l'eau (WGK)

WGK 3

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".

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

Consulter la Bibliothèque de documents

The WASP--Arp2/3 pathway: genetic insights
Vartiainen MK and Machesky LM
Current Opinion in Cell Biology, 16(2) (2004)
Phosphorylation of actin-related protein 2 (Arp2) is required for normal development and cAMP chemotaxis in Dictyostelium
Choi CH, et al.
The Journal of biological chemistry, 288(4) (2013)
The state of the filament.
Aguda, AH.
The Embo Journal, 6, 220-226 (2005)
SCAR is a primary regulator of Arp2/3-dependent morphological events in Drosophila
Zallen JA, et al.
The Journal of cell biology, 156(4) (2002)
Massimiliano Baldassarre et al.
European journal of cell biology, 85(12), 1217-1231 (2006-10-03)
The degradation of extracellular matrix (ECM) by proteases is crucial in physiological and pathological cell invasion alike. In vitro, degradation occurs at specific sites where invasive cells make contact with the ECM via specialized plasma membrane protrusions termed invadopodia. Here

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