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Key Documents

SAB4200318

Sigma-Aldrich

Anti-PRKACA antibody produced in rabbit

~1.0 mg/mL, affinity isolated antibody

Synonym(s):

Anti-PKA Cα, Anti-PKACA, Anti-cAMP-dependent protein kinase catalytic subunit α

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About This Item

UNSPSC Code:
12352203
NACRES:
NA.44

biological source

rabbit

conjugate

unconjugated

antibody form

affinity isolated antibody

antibody product type

primary antibodies

clone

polyclonal

form

buffered aqueous solution

mol wt

antigen ~40 kDa

species reactivity

human

concentration

~1.0 mg/mL

technique(s)

western blot: 0.25-0.5 μg/mL using lysates of HEK-293T cells over-expressing human PRKACA.

UniProt accession no.

shipped in

dry ice

storage temp.

−20°C

target post-translational modification

unmodified

Gene Information

human ... PRKACA(5566)

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General description

PRKACA is a serine threonine kinase that phosphorylates various proteins to facilitate several cellular functions. For instance, PRAKACA phosphorylates TRPC1 channel to modulate Ca2+ entry in endothelial tissues and regulates DNA binding functions by phosphorylation of NF-κB p50. PRAKACA also mediates tight junction barrier activity by phosphorylation of claudin-3. Additionally, PRAKACA has been associated with body mass index of asthma patients and the pathogenesis of diabetic osteoporosis
Anti-PRKACA antibody is specific for human PRKACA. In immunoblotting, staining of the PRKACA band is specifically inhibited by the immunizing peptide.

Immunogen

synthetic peptide corresponding to the N-terminal region of human PRKACA, conjugated to KLH. The corresponding sequence differs by 2 and 3 amino acids in mouse and rat, respectively

Application

Anti-PRKACA antibody is suitable for use in western blot (0.25-0.5 μg/mL) using lysates of HEK-293T cells over-expressing human PRKACA.

Physical form

Solution in 0.01 M phos­phate buffered saline, pH 7.4, containing 15 mM sodium azide.

Disclaimer

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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Storage Class

10 - Combustible liquids

flash_point_f

Not applicable

flash_point_c

Not applicable


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Amy Murphy et al.
American journal of human genetics, 85(1), 87-96 (2009-07-07)
Asthma incidence and prevalence are higher in obese individuals. A potential mechanistic basis for this relationship is pleiotropy. We hypothesized that significant linkage and candidate-gene association would be found for body mass index (BMI) in a population ascertained on asthma
Weiwei Wang et al.
Molecular and cellular biochemistry, 338(1-2), 115-122 (2009-12-02)
Patients with diabetes tend to have an increased incidence of osteoporosis that may be related to hyperglycemia. In this study, we investigated the effects of high glucose on differentiation of human osteoblastic MG-63 cells and involved intracellular signal transduction pathways.
Hancheng Guan et al.
The Journal of biological chemistry, 280(11), 9957-9962 (2005-01-12)
The NF-kappaB p50/p50 homodimer is mainly associated with transcriptional repression. Previously, we demonstrated that phosphorylation of NF-kappaB p50 Ser(337) is critical for DNA binding. Here, we report that p50 Ser(337) is constitutively phosphorylated by the protein kinase A catalytic subunit
Theresa D'Souza et al.
The Journal of biological chemistry, 280(28), 26233-26240 (2005-05-21)
Claudins are integral membrane proteins essential in the formation and function of tight junctions (TJs). Disruption of TJs, which have essential roles in cell permeability and polarity, is thought to contribute to epithelial tumorigenesis. Claudin-3 and -4 are frequently overexpressed
Gias U Ahmmed et al.
The Journal of biological chemistry, 279(20), 20941-20949 (2004-03-16)
The TRPC1 (transient receptor potential canonical-1) channel is a constituent of the nonselective cation channel that mediates Ca2+ entry through store-operated channels (SOCs) in human endothelial cells. We investigated the role of protein kinase Calpha (PKCalpha) phosphorylation of TRPC1 in

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