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Merck

A6104

Sigma-Aldrich

Anti-ARP2 antibody, Mouse monoclonal

clone FMS96, purified from hybridoma cell culture

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About This Item

MDL-Nummer:
UNSPSC-Code:
12352203
NACRES:
NA.41

Biologische Quelle

mouse

Qualitätsniveau

Konjugat

unconjugated

Antikörperform

purified immunoglobulin

Antikörper-Produkttyp

primary antibodies

Klon

FMS96, monoclonal

Form

buffered aqueous solution

Mol-Gew.

antigen 40-45 kDa

Speziesreaktivität

mouse, human, rat, canine

Verpackung

antibody small pack of 25 μL

Methode(n)

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

Isotyp

IgG1

UniProt-Hinterlegungsnummer

Versandbedingung

dry ice

Lagertemp.

−20°C

Posttranslationale Modifikation Target

unmodified

Angaben zum Gen

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

Allgemeine Beschreibung

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.

Immunogen

recombinant human ARP2

Anwendung

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

Biochem./physiol. Wirkung

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.

Physikalische Form

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

Haftungsausschluss

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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Lagerklassenschlüssel

10 - Combustible liquids

WGK

WGK 3

Flammpunkt (°F)

Not applicable

Flammpunkt (°C)

Not applicable


Analysenzertifikate (COA)

Suchen Sie nach Analysenzertifikate (COA), indem Sie die Lot-/Chargennummer des Produkts eingeben. Lot- und Chargennummern sind auf dem Produktetikett hinter den Wörtern ‘Lot’ oder ‘Batch’ (Lot oder Charge) zu finden.

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In der Dokumentenbibliothek finden Sie die Dokumentation zu den Produkten, die Sie kürzlich erworben haben.

Die Dokumentenbibliothek aufrufen

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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