P0713
Anti-Protein Kinase Cζ antibody produced in rabbit
whole antiserum
Sinonimo/i:
Anti-PKC ζ
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About This Item
Numero MDL:
Codice UNSPSC:
12352203
Origine biologica
rabbit
Coniugato
unconjugated
Forma dell’anticorpo
whole antiserum
Tipo di anticorpo
primary antibodies
Clone
polyclonal
PM
antigen 78 kDa
contiene
15 mM sodium azide
Reattività contro le specie
rat, mouse
tecniche
microarray: suitable
western blot: suitable using rat brain extract and mouse NIH3T3 fibroblast cell lysate
N° accesso UniProt
Condizioni di spedizione
dry ice
Temperatura di conservazione
−20°C
Informazioni sul gene
mouse ... Prkcz(18762)
rat ... Prkcz(25522)
Descrizione generale
Protein Kinase C (PKC) is a 76-93 kD phospholipid-dependent enzyme that belongs to serine/threonine protein kinases family. It has a pivotal role in cell growth and differentiation, modulation of neurotransmission, signal transduction and oncogenesis. PKC ζ isoform is expressed mainly in many cells and tissues and is activated by cis- unsaturated fatty acids. Anti-protein kinase C ζ antibody can be used for studying differential tissue expression and intracellular localization of PKC ζ. It can also be used for studying PKC expression in normal and neoplastic tissues. Rabbit anti-protein kinase C ζ antibody reacts specifically with PKC ζ (78 kD) from rat brain extract. The product is also specific for PKC ζ (78-80 kD proteins appearing as doublet) from NIH 3T3 mouse fibroblasts lysate.
Immunogeno
Synthetic peptide corresponding to the C-terminal variable (V5) region (amino acids 577-592) of PKC ζ coupled to KLH.
Stoccaggio e stabilità
For continuous use, store at 2-8 °C for up to one month.For extended storage freeze in working aliquots.Repeated freezing and thawing is not recommended.Storage in "frost-free" freezers is not recommended. Ifslight turbidity occurs upon prolonged storage, clarifythe solution by centrifugation before use.
Esclusione di responsabilità
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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Codice della classe di stoccaggio
12 - Non Combustible Liquids
Classe di pericolosità dell'acqua (WGK)
WGK 3
Punto d’infiammabilità (°F)
Not applicable
Punto d’infiammabilità (°C)
Not applicable
Certificati d'analisi (COA)
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I documenti relativi ai prodotti acquistati recentemente sono disponibili nell’Archivio dei documenti.
Y Nishizuka
Science (New York, N.Y.), 258(5082), 607-614 (1992-10-23)
Hydrolysis of inositol phospholipids by phospholipase C is initiated by either receptor stimulation or opening of Ca2+ channels. This was once thought to be the sole mechanism to produce the diacylglycerol that links extracellular signals to intracellular events through activation
Yimin Zhu et al.
Cellular signalling, 17(9), 1125-1136 (2005-07-05)
Protein kinase C (PKC) is a family of serine/threonine protein kinases that are pivotal in cellular regulation. Since its discovery in 1977, PKCs have been known as cytosolic and peripheral membrane proteins. However, there are reports that PKC can insert
Primary cilia in stem cells and neural progenitors are regulated by neutral sphingomyelinase 2 and ceramide.
He Q, Wang G, Wakade S, et al.
Molecular Biology of the Cell, 25(11), 1715-1729 (2014)
Holly E Lovegrove et al.
Development (Cambridge, England), 146(23) (2019-12-01)
The Drosophila egg chamber comprises a germline cyst surrounded by a tightly organised epithelial monolayer, the follicular epithelium (FE). Loss of integrin function from the FE disrupts epithelial organisation at egg chamber termini, but the cause of this phenotype remains
Elena Rainero et al.
PloS one, 9(6), e97144-e97144 (2014-06-03)
Diacylglycerol kinase α (DGKα), by phosphorylating diacylglycerol into phosphatidic acid, provides a key signal driving cell migration and matrix invasion. We previously demonstrated that in epithelial cells activation of DGKα activity promotes cytoskeletal remodeling and matrix invasion by recruiting atypical
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