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Merck

S5049

Sigma-Aldrich

Monoclonal Anti-S100A6 antibody produced in mouse

clone CACY-100, ascites fluid

Synonym(e):

Anti-Calcyclin

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About This Item

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

Biologische Quelle

mouse

Konjugat

unconjugated

Antikörperform

ascites fluid

Antikörper-Produkttyp

primary antibodies

Klon

CACY-100, monoclonal

Enthält

15 mM sodium azide

Speziesreaktivität

rat, bovine, human, pig, goat, lizard, canine

Methode(n)

immunohistochemistry (formalin-fixed, paraffin-embedded sections): suitable
immunohistochemistry (frozen sections): suitable
immunoprecipitation (IP): suitable using native preparations
indirect immunofluorescence: 1:4,000 using bovine tongue frozen sections
western blot: suitable using denatured-reduced preparations

Isotyp

IgG1

UniProt-Hinterlegungsnummer

Versandbedingung

dry ice

Lagertemp.

−20°C

Posttranslationale Modifikation Target

unmodified

Angaben zum Gen

human ... S100A6(6277)
rat ... S100a6(85247)

Allgemeine Beschreibung

Monoclonal Anti-S100A6 (Calcyclin) (mouse IgG1 isotype) is derived from the CACY-100 hybridoma produced by the fusion of mouse myeloma cells and splenocytes from an immunized mouse. S100 calcium-binding protein A6 is mapped to human chromosome 1q21.3. S100A6 has been shown to possess 43-47% homology with S-100α, S-100β, and S100A2 (S100L).

Spezifität

Recognizes an epitope located on S100A6 (Calcyclin in the old terminology) in a Ca2+ ion-dependent manner. The product does not react with other members of the EF-hand family such as calmodulin, parvalbumin, intestinal calcium-binding protein, S100A2 (S100L), caltropin, the α chain of S-100 (i.e. in S-100a and S-100ao), or the β chain (i.e. in S-100a and S-100b).

Immunogen

Ca2+-binding proteins from pig stomach tissue

Anwendung

Applications in which this antibody has been used successfully, and the associated peer-reviewed papers, are given below.
Immunohistochemistry (1 paper)

Biochem./physiol. Wirkung

S-100 proteins are calcium-modulated proteins that bind calcium and zinc ions reversibly at physiologic pH and ionic strength, followed by a conformational change in the molecule. S100A6 along with other S100 family proteins bindsprotein phosphatase 5(PP5) in a calcium-dependent manner.

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

12 - Non Combustible Liquids

WGK

nwg

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

I Rehman et al.
British journal of cancer, 91(4), 739-744 (2004-07-29)
S100A6 (Calcyclin) is a calcium-binding protein that has been implicated in a variety of biological functions as well as tumorigenesis. The aim of our study was to investigate the involvement of S100A6 during prostate cancer development and progression. Using immunohistochemistry
S100 Proteins Modulate Protein Phosphatase 5 Function A LINK BETWEEN CA2+ SIGNAL TRANSDUCTION AND PROTEIN DEPHOSPHORYLATION
Yamaguchi F, et al.
The Journal of Biological Chemistry, 287(17), 13787-13798 (2012)
Steven M Schlichtemeier et al.
The Journal of surgical research, 238, 127-136 (2019-02-17)
Hepatocellular carcinoma (HCC) is a common cause of cancer death worldwide. Resection offers the best chance of long-term survival, but a consistent adverse prognostic factor is the presence of microvascular invasion (MVI). In this study, surface-enhanced laser desorption/ionization time-of-flight mass
Binding of transition metals to S100 proteins
Gilston BA, et al.
Science China: Life Sciences, 59(8), 792-801 (2016)
S Keijser et al.
The British journal of ophthalmology, 90(2), 213-217 (2006-01-21)
The authors investigated the expression of S100A1, S100A6, S100B, MelanA, and CEA in conjunctival naevi, primary acquired melanosis (PAM), conjunctival melanoma, and uveal melanoma in order to assess their potential usefulness in the pathological differential diagnosis of these entities. Paraffin

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