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Merck

SAB4200750

Sigma-Aldrich

Anti-Gelsolin antibody, Mouse Monoclonal

clone GS-2C4, purified from hybridoma cell culture

Synonym(e):

Anit-AGEL, Anit-Actin-depolymerizing factor (ADF), Anit-GSN

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About This Item

UNSPSC-Code:
12352203
NACRES:
NA.41

Biologische Quelle

mouse

Qualitätsniveau

Antikörperform

purified from hybridoma cell culture

Antikörper-Produkttyp

primary antibodies

Klon

GS-2C4, monoclonal

Form

buffered aqueous solution

Mol-Gew.

~85 kDa

Speziesreaktivität

rabbit, canine, human, mouse, monkey

Konzentration

~1.0 mg/mL

Methode(n)

immunoblotting: 1-2.5 μg/mL using MDCK cell line extract
immunofluorescence: suitable
immunohistochemistry: 10-20 μg/mL using heat-retrieved formalin-fixed, paraffin-embedded human pancreas sections
immunoprecipitation (IP): suitable

Isotyp

IgG1

UniProt-Hinterlegungsnummer

Versandbedingung

dry ice

Lagertemp.

−20°C

Posttranslationale Modifikation Target

unmodified

Angaben zum Gen

human ... GSN(2934)

Allgemeine Beschreibung

Anti-Gelsolin Antibody, Mouse monoclonal (mouse IgG1 isotype) is derived from the GS-2C4 hybridoma produced by the fusion of mouse myeloma cells and splenocytes from an immunized mouse. Gelsolin operates in at least two variant forms encoded by a single gene and is located both intracellular (in cytosol and mitochondria) and extracellular (in blood plasma).

Immunogen

Human plasma gelsolin

Anwendung

Anti-Gelsolin antibody, Mouse Monoclonal has been used in:
  • immunoblotting
  • immunofluorescence
  • immunohistochemistry
  • immunoprecipitation

Biochem./physiol. Wirkung

Gelsolin, also known as Actin-depolymerizing factor (ADF), GSN, AGEL or Brevin, is a calcium-dependent actin-binding protein. Gelsolin acts as a main modulator of actin filament formation and disassembly and is involved in a variety of cellular mechanisms including apoptosis, signal transduction, transcriptional regulation and epigenetic processes. Plasma gelsolin differs in its sequence from the cytoplasmic variant in possessing a 25-amino acid N-terminal extension. The main function of the cytoplasmic gelsolin is to remodel the actin cytoskeleton. Plasma gelsolin′s main role is to scan for actin fibrils that are released by injured tissue into the bloodstream and to bind them in a scavenger mode preventing actin from increasing the blood viscosity. Gelsolin levels correlate with inflammation and several diseases and pathologies, including cancer, infection, cardiac injury, pulmonary diseases, Alzheimer′s disease and aging thus making it a potential biomarker of diagnostic and prognostic values.

Physikalische Form

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

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Lagerklassenschlüssel

10 - Combustible liquids

WGK

WGK 2

Flammpunkt (°F)

Not applicable

Flammpunkt (°C)

Not applicable


Analysenzertifikate (COA)

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

Die Dokumentenbibliothek aufrufen

D J Kwiatkowski et al.
The Journal of biological chemistry, 260(28), 15232-15238 (1985-12-05)
Gelsolin is a Ca2+-sensitive 90-kDa protein which regulates actin filament length. A molecular variant of gelsolin is present in plasma as a 93-kDa protein. Functional studies have shown that gelsolin contains two actin-binding sites which are distinct in that after
Gelsolin amyloidosis: genetics, biochemistry, pathology and possible strategies for therapeutic intervention
Solomon JP, et al.
Critical Reviews in Biochemistry and Molecular Biology, 47(3), 282-296 (2012)
Membrane cholesterol, lateral mobility, and the phosphatidylinositol 4, 5-bisphosphate-dependent organization of cell actin
Kwik J, et al.
Proceedings of the National Academy of Sciences of the USA, 100(24), 13964-13969 (2003)
C Chaponnier et al.
The Journal of cell biology, 103(4), 1473-1481 (1986-10-01)
Gelsolin, a multifunctional actin-modulating protein, has two actin-binding sites which may interact cooperatively. Native gelsolin requires micromolar Ca2+ for optimal binding of actin to both sites, and for expression of its actin filament-severing function. Recent work has shown that an
Vesicular egress of non-enveloped lytic parvoviruses depends on gelsolin functioning
Bar S, et al.
PLoS Pathogens, 4(8), e1000126-e1000126 (2008)

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