C1956
Monoclonal Anti-Calcineurin (α-Subunit) antibody produced in mouse
clone CN-A1, ascites fluid
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About This Item
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biological source
mouse
Quality Level
conjugate
unconjugated
antibody form
ascites fluid
antibody product type
primary antibodies
clone
CN-A1, monoclonal
contains
15 mM sodium azide
species reactivity
human, bovine, rat
technique(s)
immunohistochemistry (formalin-fixed, paraffin-embedded sections): suitable using neurons in human ganglia
indirect ELISA: suitable
microarray: suitable
western blot: 1:10,000 using rat brain extract
isotype
IgG1
UniProt accession no.
shipped in
dry ice
storage temp.
−20°C
target post-translational modification
unmodified
Gene Information
human ... PPP3R1(5534)
rat ... Ppp3r1(29748)
General description
Calcineurin (CaN)(heterodimeric enzyme) is a Ca2+/calmodulin (CaM)-stimulated protein phosphatase 3 (PPP3) consisting of a catalytic A subunit (CnA) and a Ca2+-binding regulatory B subunit (CnB). The calcium-binding regulatory subunit (calcineurin B) is coded by the PPP3R1 gene located on human chromosome 2. Protein phosphatase 3, regulatory subunit B, α (PPP3R1) is also known as CALN, CCN1, CNA1, CALNA, PPP2B and CALNA1. The regulatory subunit calcineurin B is widely expressed in brain while the catalytic subunit (calcineurin A) is abundantly expressed in Hassall′s corpuscles, localized in the thymic medulla and represents the terminal stages of thymic medullary epithelium.
Monoclonal Anti-Calcineurin (α-subunit) (mouse IgG1 isotype) is derived from the CN-A1 hybridoma produced by the fusion of mouse myeloma cells and splenocytes from immunized BALB/c mice.
Specificity
In immunoblotting, the product recognizes an epitope located on the α-subunit of calcineurin (61 kDa, also called calcineurin A) and does not cross-react with the β-subunit.
Immunogen
bovine brain calcineurin
Application
Monoclonal Anti-Calcineurin (α-Subunit) antibody produced in mouse has been used in:enzyme linked immuno sorbent assay (ELISA) ,immunohistochemistry, western blotting
Biochem/physiol Actions
Calcineurin is a major soluble calmodulin-binding protein in the brain. It stimulates the expression of the surface molecules CD83, CD80, CD86, CD40 and HLA-DR by promoting secretion of inflammatory cytokines IL-6, TNF-α and IL-1β by human PBMC-derived dendritic cells. It plays an important role in signal transduction, activation of T cell. Calcineurin is an excellent marker enzyme for the detection of neuronal activity and synaptic plasticity after brain damage.
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
10 - Combustible liquids
wgk_germany
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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H Bito et al.
Cell, 87(7), 1203-1214 (1996-12-27)
While changes in gene expression are critical for many brain functions, including long-term memory, little is known about the cellular processes that mediate stimulus-transcription coupling at central synapses. In studying the signaling pathways by which synaptic inputs control the phosphorylation
Colin Rickman et al.
The Journal of biological chemistry, 279(13), 12574-12579 (2004-01-08)
Synaptotagmins are membrane proteins that possess tandem C2 domains and play an important role in regulated membrane fusion in metazoan organisms. Here we show that both synaptotagmins I and II, the two major neuronal isoforms, can interact with the syntaxin/synaptosomal-associated
Jolene M Kim et al.
Neurochemical research (2018-01-05)
Impaired interactions between Calcineurin (Cn) and (Cu/Zn) superoxide dismutase (SOD1) are suspected to be responsible for the formation of hyperphosphorylated protein aggregation in amyotrophic lateral sclerosis (ALS). Serine (Ser)- enriched phosphorylated TDP-43 protein aggregation appears in the spinal cord of
Impaired CuZn Superoxide Dismutase (SOD1) and Calcineurin (Cn) Interaction in ALS: A Presumed Consequence for TDP-43 and Zinc Aggregation in Tg SOD1G93A Rodent Spinal Cord Tissue
Kim Jm, et al.
Neurochemical Research, 44(1), 228-233 (2019)
Anindit Mukherjee et al.
American journal of physiology. Renal physiology, 320(5), F719-F733 (2021-03-16)
Phosphorylation of the thiazide-sensitive NaCl cotransporter (NCC) in the distal convoluted tubule (DCT) is altered rapidly in response to changes in extracellular K+ concentration ([K+]). High extracellular [K+] is believed to activate specific phosphatases to dephosphorylate NCC, thereby reducing its
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