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SAB4200750

Sigma-Aldrich

Anti-Gelsolin antibody, Mouse Monoclonal

clone GS-2C4, purified from hybridoma cell culture

Synonim(y):

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

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About This Item

Kod UNSPSC:
12352203
NACRES:
NA.41

pochodzenie biologiczne

mouse

Poziom jakości

200

forma przeciwciała

purified from hybridoma cell culture

rodzaj przeciwciała

primary antibodies

klon

GS-2C4, monoclonal

Postać

buffered aqueous solution

masa cząsteczkowa

~85 kDa

reaktywność gatunkowa

rabbit, canine, human, mouse, monkey

stężenie

~1.0 mg/mL

metody

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

izotyp

IgG1

numer dostępu UniProt

P06396

Warunki transportu

dry ice

temp. przechowywania

−20°C

docelowa modyfikacja potranslacyjna

unmodified

informacje o genach

human ... GSN(2934)

Opis ogólny

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

Zastosowanie

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

Działania biochem./fizjol.

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.

Postać fizyczna

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

10 - Combustible liquids

Klasa zagrożenia wodnego (WGK)

WGK 2

Temperatura zapłonu (°F)

Not applicable

Temperatura zapłonu (°C)

Not applicable

Certyfikaty analizy (CoA)

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Dokumenty związane z niedawno zakupionymi produktami zostały zamieszczone w Bibliotece dokumentów.

Odwiedź Bibliotekę dokumentów

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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