Datasheet

Biological Description

Specificity	PKD/PKCμ Antibody [D22N3] detects endogenous levels of total PKD/PKCμ protein.
Background	Protein Kinase D (PKD) isoforms, including PKD1 (PKCμ), PKD2, and PKD3, are serine/threonine kinases involved in a variety of cellular processes regulated by PKC-dependent phosphorylation. PKDs have a conserved architecture with an N-terminal regulatory region containing two cysteine-rich C1 domains that bind diacylglycerol (DAG), and a pleckstrin homology (PH) domain, which exerts autoinhibition over their catalytic C-terminal kinase domain. Activation of PKD isoforms requires phosphorylation of two conserved serine residues in the activation loop (Ser744 and Ser748 for PKD1), mainly by PKCs. Additionally, PKD autophosphorylates at the C-terminal serine (Ser916 in PKD1), which correlates with increased catalytic activity. PKD isoforms regulate secretion, gene expression, cell proliferation, Golgi apparatus trafficking, muscle contraction, oxidative stress response, and play roles in signaling pathways related to cardiac hypertrophy, angiogenesis, and cancer progression. Protein kinase D (PKD) regulates cell migration, survival, and chemoresistance in part by phosphorylating class II histone deacetylases (HDACs), thereby modulating the epigenetic control of gene expression. Dysregulation of PKD activity is implicated in pathological conditions such as cancer and cardiovascular diseases.

Specificity

PKD/PKCμ Antibody [D22N3] detects endogenous levels of total PKD/PKCμ protein.

Background

Protein Kinase D (PKD) isoforms, including PKD1 (PKCμ), PKD2, and PKD3, are serine/threonine kinases involved in a variety of cellular processes regulated by PKC-dependent phosphorylation. PKDs have a conserved architecture with an N-terminal regulatory region containing two cysteine-rich C1 domains that bind diacylglycerol (DAG), and a pleckstrin homology (PH) domain, which exerts autoinhibition over their catalytic C-terminal kinase domain. Activation of PKD isoforms requires phosphorylation of two conserved serine residues in the activation loop (Ser744 and Ser748 for PKD1), mainly by PKCs. Additionally, PKD autophosphorylates at the C-terminal serine (Ser916 in PKD1), which correlates with increased catalytic activity. PKD isoforms regulate secretion, gene expression, cell proliferation, Golgi apparatus trafficking, muscle contraction, oxidative stress response, and play roles in signaling pathways related to cardiac hypertrophy, angiogenesis, and cancer progression. Protein kinase D (PKD) regulates cell migration, survival, and chemoresistance in part by phosphorylating class II histone deacetylases (HDACs), thereby modulating the epigenetic control of gene expression. Dysregulation of PKD activity is implicated in pathological conditions such as cancer and cardiovascular diseases.

Usage Information

Application

WB, IP

Dilution

WB	IP
1:1000	1:100

Reactivity

Human, Monkey

Source

Rabbit Monoclonal Antibody

MW

115 kDa

Storage Buffer

PBS, pH 7.2+50% Glycerol+0.05% BSA+0.01% NaN3

Storage
(from the date of receipt)

-20°C (avoid freeze-thaw cycles), 2 years

Exprimental Methods

References

https://pubmed.ncbi.nlm.nih.gov/11943587/
https://pubmed.ncbi.nlm.nih.gov/28174535/

PKD/PKCμ Antibody [D22N3]

Biological Description

Usage Information

References

Application Data