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Polyclonal Antibody Immunoprecipitation Negative Regulation of Exocytosis

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey, Mouse, Rat

Application Methods: Immunoprecipitation, Western Blotting

Background: α-Synuclein is a protein of 140-amino acids expressed abundantly in the brain. α-Synuclein is also the main component of pathogenic Lewy bodies and Lewy neurites. Research studies have shown that mutations of the α-synuclein gene are linked to Parkinson's disease (1).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey, Mouse, Rat

Application Methods: Immunoprecipitation, Western Blotting

Background: Cyclin-dependent kinases (CDKs) are serine/threonine kinases that are activated by cyclins and govern eukaryotic cell cycle progression. While CDK5 shares high sequence homology with its family members, it is thought mainly to function in postmitotic neurons to regulate the cytoarchitecture of these cells. Analogous to cyclins, the regulatory subunits p35 and p39 associate with and activate CDK5 despite the lack of sequence homology. CDK5 is ubiquitously expressed, with high levels of kinase activity detected primarily in the nervous system due to the narrow expression pattern of p35 and p39 in post-mitotic neurons. A large number of CDK5 substrates have been identified although no substrates have been specifically attributed to p35 or p39. Substrates of CDK5 include p35, PAK1, Src, β-catenin, tau, neurofilament-H, neurofilament-M, synapsin-1, APP, DARPP32, PP1-inhibitor, and Rb. p35 is rapidly degraded (T1/2 <20 min) by the ubiquitin-proteasome pathway (1). However, p35 stability increases as CDK5 kinase activity decreases, likely as a result of decreased phosphorylation of p35 at Thr138 by CDK5 (2). Proteolytic cleavage of p35 by calpain produces p25 upon neurotoxic insult, resulting in prolonged activation of CDK5 by p25. Research studies have shown accumulation of p25 in neurodegenerative diseases, such as Alzheimer's disease and amyotrophic lateral sclerosis (ALS) (3,4).

$260
100 µl
APPLICATIONS
REACTIVITY
Mouse

Application Methods: Immunoprecipitation, Western Blotting

Background: RANTES/CCL5 (regulated upon activation, T cell expressed and secreted) is a member of the "C-C" or β family of chemokines that induce inflammation and are associated with a number of inflammatory disorders (1,2). RANTES is produced and secreted mainly by CD8+ T cells, macrophages, and platelets, as well as epithelial cells, fibroblasts and some solid tumors (2-7). RANTES acts as a chemoattractant and has other regulatory functions on a number of cell types including monocytes, memory T cells, NK cells, eosinophils, basophils, dendritic cells, and mast cells (3, 7-9). Signaling by RANTES is mediated by several G-protein coupled receptors (GPCRs), including CCR1, CCR3, CCR4 and CCR5.

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey, Mouse, Rat

Application Methods: Flow Cytometry, Immunofluorescence (Immunocytochemistry), Immunoprecipitation, Western Blotting

Background: Calcineurin, also known as protein phosphatase 2B (PP2B), is a calmodulin-dependent, calcium-activated, serine/threonine protein phosphatase composed of a catalytic subunit (calcineurin A) and a tightly bound regulatory subunit (calcineurin B) (1). Calcineurin A is highly homologous to protein phosphatases 1 and 2A. Calcineurin B, like calmodulin, contains four EF-hand, calcium-binding motifs.Calcineurin signaling has been implicated in a broad spectrum of cellular processes including cell-cycle regulation, stress response and apoptosis and is required for proper cardiovascular and skeletal muscle development (2,3). Calcineurin-mediated dephosphorylation of the nuclear factor of activated T cells (NFAT) transcription factor is essential for NFAT activation and nuclear translocation and early gene expression in T lymphocytes (2,3). Calcineurin is the target of the immunosuppressive drugs Cyclosporin A and FK506, both of which block the activation of quiescent T cells after T cell receptor engagement (2,3). Cyclosporin A and FK506 bind to the immunophilins, cyclophilin and FKBP respectively and the immunophilin-drug complex binds to calcineurin and blocks substrate binding.