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Merck

MABN1845

Sigma-Aldrich

Anti-Aldolase C Antibody, N-Term, clone 4A9

clone 4A9, from mouse

Synonym(s):

Fructose-bisphosphate aldolase C, Brain-type aldolase, Aldolase C, N-Term

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About This Item

UNSPSC Code:
12352203
eCl@ss:
32160702

biological source

mouse

antibody form

purified antibody

antibody product type

primary antibodies

clone

4A9, monoclonal

species reactivity

mouse, bovine, rat, human

species reactivity (predicted by homology)

porcine (based on 100% sequence homology), monkey (based on 100% sequence homology), feline (based on 100% sequence homology), canine (based on 100% sequence homology), equine (based on 100% sequence homology)

technique(s)

immunocytochemistry: suitable
western blot: suitable

isotype

IgG1κ

NCBI accession no.

UniProt accession no.

shipped in

wet ice

target post-translational modification

unmodified

Gene Information

human ... ALDOC(230)

General description

Fructose-bisphosphate aldolase C (EC 4.1.2.13; UniProt P09972; also known as Aldolase 3, Brain-type aldolasefructoaldolase C, Fructose-1,6-biphosphate triosephosphate lyase) is encoded by the ALDOC (also known as ALDC) gene (Gene ID 230) in human. Aldolases are glycolytic enzymes that catalyze the reversible aldol cleavage of fructose 1,6-bisphosphate and fructose-1-phosphate to dihydroxyacetone phosphate and glyceraldehyde 3-phosphate. Three aldolase genes (ALDOA, ALDOB, ALDOC) are found in mammals that encode aldolase A, B, and C. Aldolase A is generally considered to be a muscle enzyme, aldolase B a liver enzyme, while aldolase C shows tissue-specific expression in adult brain with low activity in fetal tissues. Aldolase C expression is found in gray matter astrocytes and cells of the pia mater. Aldolase A and C mRNA expressions are mutually exclusive in murine central nervous system by in situ hybridization analysis, with aldolase A mRNA being detected in neurons and aldolase C in astrocytes, Purkinje cells, and some cells of the pia mater. Aldolase C can therefore be a useful marker of astrocytes, although Purkinje cells of the cerebellum also contain high levels of aldolase C.
~39 kDa observed

Immunogen

Epitope: Near N-terminus, 20 amino acids of aldolase C protein
Recombinant protein corresponding to human Aldolase C near the N-terminus.

Application

Research Category
Neuroscience
Research Sub Category
Developmental Signaling
This Anti-Aldolase C Antibody, N-Term, clone 4A9 is validated for use in Western Blotting, Immunocytochemistry for the detection of Aldolase C.
Western Blotting Analysis: 0.5 µg/mL from a representative lot detected Aldolase C in 10 µg of human and mouse brain tissue lysate.
Western Blotting Analysis: A representative lot detected Aldolase C in bovine cerebellum tissue lysate.
Immunocytochemistry: A representative lot selectively stained Aldolase C-positive astrocytes in mixed neuron/glial cultures.

Physical form

Format: Purified
Protein G Purified
Purified mouse monoclonal IgG1κ antibody in buffer containing PBS with 0.05% sodium azide.

Preparation Note

Stable for 1 year at 2-8°C from date of receipt.

Analysis Note

Evaluated by Western Blotting in rat brain tissue lysate.

Western Blotting Analysis: 0.5 µg/mL of this antibody detected Aldolase C in 10 µg of rat brain tissue lysate.

Other Notes

Concentration: Please refer to lot specific datasheet.

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

10 - Combustible liquids

WGK

WGK 2

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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Thomas H Sanderson et al.
PloS one, 8(11), e78627-e78627 (2013-11-14)
Recent advancements in isolation techniques for cytochrome c (Cytc) have allowed us to discover post-translational modifications of this protein. We previously identified two distinct tyrosine phosphorylated residues on Cytc in mammalian liver and heart that alter its electron transfer kinetics

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