推荐产品
生物来源
mouse
质量水平
偶联物
unconjugated
抗体形式
ascites fluid
抗体产品类型
primary antibodies
克隆
CN-A1, monoclonal
包含
15 mM sodium azide
种属反应性
human, bovine, rat
技术
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
同位素/亚型
IgG1
UniProt登记号
运输
dry ice
储存温度
−20°C
靶向翻译后修饰
unmodified
基因信息
human ... PPP3R1(5534)
rat ... Ppp3r1(29748)
一般描述
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.
特异性
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.
免疫原
bovine brain calcineurin
应用
Monoclonal Anti-Calcineurin (α-Subunit) antibody produced in mouse has been used in:enzyme linked immuno sorbent assay (ELISA) ,immunohistochemistry, western blotting
生化/生理作用
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.
免责声明
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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储存分类代码
10 - Combustible liquids
WGK
nwg
闪点(°F)
Not applicable
闪点(°C)
Not applicable
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
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
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)
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
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