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S5049

Sigma-Aldrich

Monoclonal Anti-S100A6 antibody produced in mouse

clone CACY-100, ascites fluid

Synonym(s):

Anti-Calcyclin

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About This Item

MDL number:
UNSPSC Code:
12352203
NACRES:
NA.41

biological source

mouse

Quality Level

conjugate

unconjugated

antibody form

ascites fluid

antibody product type

primary antibodies

clone

CACY-100, monoclonal

contains

15 mM sodium azide

species reactivity

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

technique(s)

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

isotype

IgG1

UniProt accession no.

shipped in

dry ice

storage temp.

−20°C

target post-translational modification

unmodified

Gene Information

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

General description

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).

Specificity

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

Application

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

Biochem/physiol Actions

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.

Disclaimer

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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Storage Class Code

12 - Non Combustible Liquids

WGK

nwg

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable


Certificates of Analysis (COA)

Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.

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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)
Probing the S100 protein family through genomic and functional analysis
Ravasi T, et al.
Genomics, 84(1), 10-22 (2004)
Barbara Sobiak et al.
Journal of cellular biochemistry, 117(5), 1092-1098 (2015-10-08)
Epidermal Differentiation Complex (EDC) is a gene cluster on human chromosome 1 q21, which comprises genes encoding four protein families: S100, S100 fused (SFTP), small proline-rich region (SPRR) and late cornified envelope (LCE) proteins. Contrary to the latter three families, which
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)

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