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Key Documents

SAB4200750

Sigma-Aldrich

Anti-Gelsolin antibody, Mouse Monoclonal

clone GS-2C4, purified from hybridoma cell culture

Sinônimo(s):

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

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About This Item

Código UNSPSC:
12352203
NACRES:
NA.41

fonte biológica

mouse

Nível de qualidade

forma do anticorpo

purified from hybridoma cell culture

tipo de produto de anticorpo

primary antibodies

clone

GS-2C4, monoclonal

forma

buffered aqueous solution

peso molecular

~85 kDa

reatividade de espécies

rabbit, canine, human, mouse, monkey

concentração

~1.0 mg/mL

técnica(s)

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

Isotipo

IgG1

nº de adesão UniProt

Condições de expedição

dry ice

temperatura de armazenamento

−20°C

modificação pós-traducional do alvo

unmodified

Informações sobre genes

human ... GSN(2934)

Descrição geral

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).

Imunogênio

Human plasma gelsolin

Aplicação

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

Ações bioquímicas/fisiológicas

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.

forma física

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

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Código de classe de armazenamento

10 - Combustible liquids

Classe de risco de água (WGK)

WGK 2

Ponto de fulgor (°F)

Not applicable

Ponto de fulgor (°C)

Not applicable


Certificados de análise (COA)

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Visite a Biblioteca de Documentos

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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