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Monoclonal Anti-Calcineurin (α-Subunit) antibody produced in mouse

clone CN-A1, ascites fluid

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About This Item

Numéro MDL:
Code UNSPSC :
12352203
Nomenclature NACRES :
NA.44

Source biologique

mouse

Niveau de qualité

Conjugué

unconjugated

Forme d'anticorps

ascites fluid

Type de produit anticorps

primary antibodies

Clone

CN-A1, monoclonal

Contient

15 mM sodium azide

Espèces réactives

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

Numéro d'accès UniProt

Conditions d'expédition

dry ice

Température de stockage

−20°C

Modification post-traductionnelle de la cible

unmodified

Informations sur le gène

human ... PPP3R1(5534)
rat ... Ppp3r1(29748)

Description générale

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.

Spécificité

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.

Immunogène

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

Actions biochimiques/physiologiques

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.

Clause de non-responsabilité

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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Code de la classe de stockage

10 - Combustible liquids

Classe de danger pour l'eau (WGK)

nwg

Point d'éclair (°F)

Not applicable

Point d'éclair (°C)

Not applicable


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Consulter la Bibliothèque de documents

Maya Fujita et al.
Biological & pharmaceutical bulletin, 41(5), 786-796 (2018-05-02)
Although calcineurin is abundantly expressed in the nervous system and involved in neurite extension and synaptic plasticity in neurons, little is known about its roles in glial cells. To investigate the roles of calcineurin in glial cells, we generated glial
Satyanarayana Paturi et al.
Mechanisms of ageing and development, 131(3), 202-209 (2010-02-16)
Sarcopenia is the loss of muscle mass and strength which occurs with aging. Whether the molecular basis of sarcopenia differs with muscle type and across sex is not well understood. Here we examine how aging affects the regulation of protein
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
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
Raúl Pardo et al.
The Journal of neuroscience : the official journal of the Society for Neuroscience, 26(5), 1635-1645 (2006-02-03)
Huntington's disease (HD) is caused by an abnormal expanded polyglutamine (polyQ) repeat in the huntingtin protein. Insulin-like growth factor-1 acting through the prosurvival kinase Akt mediates the phosphorylation of huntingtin at S421 and inhibits the toxicity of polyQ-expanded huntingtin in

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