LKB1, Antibody

EC 2.7.11.1; kinase LKB1; PJS; Serine/threonine kinase KPM; Serine/threonine protein kinase 11; STK11

For Research Use Only. Not for use in diagnostic procedures.

LKB1 (Phospho-Ser428) antibody detects endogenous levels of LKB1 only when phosphorylated at serine 428.

Affinity-purified fromrabbit antiserum by affinity-chromatography using epitope-specific phosphopeptide. The antibody against non-phosphopeptide was removed by chromatography using non-phosphopeptide corresponding to the phosphorylation site.

In phosphate buffered saline (without Mg2+ and Ca2+), pH 7.4, 150mM NaCl, 0.02% sodium azide and 50% glycerol.

Store at-20 degree C for 1 year.

Small volumes of anti-LKB1 antibody vial(s) may occasionally become entrapped in the seal of the product vial during shipment and storage. If necessary, briefly centrifuge the vial on a tabletop centrifuge to dislodge any liquid in the container`s cap. Certain products may require to ship with dry ice and additional dry ice fee may apply.

Western Blot (WB), Immunohistochemistry (IHC), Immunofluorescence (IF), ELISA (EIA)

WB: 1:500~1:1000
IHC: 1:50~1:100
IF: 1:100~1:500
ELISA: 1:40000

P-peptide-+

Immunohistochemistry analysis of paraffin-embedded human colon carcinoma tissue using LKB1 (Phospho-Ser428) antibody. Western blot analysis of extracts from mouse brain cells, using LKB1 (Phospho-Ser428) antibody.

P-peptide-+ Immunofluorescence analysis of NIH/3T3 cells, using LKB1 (Phospho-Ser428) antibody.

45,387 Da

serine/threonine kinase 11

serine/threonine-protein kinase STK11

Serine/threonine-protein kinase STK11

LKB1; PJS; LKB1; hLKB1  [Similar Products]

This gene, which encodes a member of the serine/threonine kinase family, regulates cell polarity and functions as a tumor suppressor. Mutations in this gene have been associated with Peutz-Jeghers syndrome, an autosomal dominant disorder characterized by the growth of polyps in the gastrointestinal tract, pigmented macules on the skin and mouth, and other neoplasms. Alternate transcriptional splice variants of this gene have been observed but have not been thoroughly characterized. [provided by RefSeq, Jul 2008]

Tumor suppressor serine/threonine-protein kinase that controls the activity of AMP-activated protein kinase (AMPK) family members, thereby playing a role in various processes such as cell metabolism, cell polarity, apoptosis and DNA damage response. Acts by phosphorylating the T-loop of AMPK family proteins, thus promoting their activity: phosphorylates PRKAA1, PRKAA2, BRSK1, BRSK2, MARK1, MARK2, MARK3, MARK4, NUAK1, NUAK2, SIK1, SIK2, SIK3 and SNRK but not MELK. Also phosphorylates non-AMPK family proteins such as STRADA, PTEN and possibly p53/TP53. Acts as a key upstream regulator of AMPK by mediating phosphorylation and activation of AMPK catalytic subunits PRKAA1 and PRKAA2 and thereby regulates processes including: inhibition of signaling pathways that promote cell growth and proliferation when energy levels are low, glucose homeostasis in liver, activation of autophagy when cells undergo nutrient deprivation, and B-cell differentiation in the germinal center in response to DNA damage. Also acts as a regulator of cellular polarity by remodeling the actin cytoskeleton. Required for cortical neuron polarization by mediating phosphorylation and activation of BRSK1 and BRSK2, leading to axon initiation and specification. Involved in DNA damage response: interacts with p53/TP53 and recruited to the CDKN1A/WAF1 promoter to participate in transcription activation. Able to phosphorylate p53/TP53; the relevance of such result in vivo is however unclear and phosphorylation may be indirect and mediated by downstream STK11/LKB1 kinase NUAK1. Also acts as a mediator of p53/TP53-dependent apoptosis via interaction with p53/TP53: translocates to the mitochondrion during apoptosis and regulates p53/TP53-dependent apoptosis pathways. In vein endothelial cells, inhibits PI3K/Akt signaling activity and thus induces apoptosis in response to the oxidant peroxynitrite (in vitro). Regulates UV radiation-induced DNA damage response mediated by CDKN1A. In association with NUAK1, phosphorylates CDKN1A in response to UV radiation and contributes to its degradation which is necessary for optimal DNA repair (PubMed:25329316).

Jenne D.E., Nat. Genet. 18:38-43(1998). Bignell G.R., Cancer Res. 58:1384-1386(1998). Baas A.F., EMBO J. 22:3062-3072(2003).

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