PCK1 Antibody [D3C9] | Primary Antibodies

Application: Reactivity: Human

Usage Information

Dilution
WB1:10000 - 1:50000 IHC1:100 - 1:250

Application
WB, IHC

Reactivity
Human

Source
Rabbit Monoclonal Antibody

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

Predicted MW Observed MW
39 kDa,69 kDa 39, 69, 67 kDa
^*Why do the predicted and actual molecular weights differ? The following reasons may explain differences between the predicted and actual protein molecular weight.

Positive Control	Human fetal kidney tissue; Human adipose tissue; Human liver tissue; A549 cells; HepG2 cells; HEK-293 cells
Negative Control

Datasheet & SDS

Biological Description

Specificity
PCK1 Antibody [D3C9] detects endogenous levels of total PCK1 protein.

Clone
D3C9

Synonym(s)
PEPCK1; PCK1; PEPCK-C; Serine-protein kinase PCK1

Background
PCK1 (Phosphoenolpyruvate carboxykinase 1, PEPCK-C) is a cytosolic, GTP-dependent enzyme in the lyase family, serving as the rate-limiting catalyst in hepatic gluconeogenesis by decarboxylating oxaloacetate (OAA) to phosphoenolpyruvate (PEP), CO₂, and GDP, thereby channeling TCA cycle intermediates into glucose production from lactate, glycerol, or amino acids during fasting. PCK1 features a 288-residue active site with binding pockets for carboxylate groups from OAA and PEP, Mn²⁺ ions, ribose, and guanine of GTP, as well as regulatory motifs such as Ser90 (the AKT phosphorylation site enabling protein kinase activity) and acetylation sites targeted by p300 for UBR5-mediated ubiquitination and degradation under high glucose. Its primary function is to replenish glucose via the malate-aspartate shuttle through cytosolic OAA regeneration, regulate cataplerosis and anaplerosis to balance TCA cycle flux, and, when Ser90 is phosphorylated by AKT, translocate to the ER as a kinase that phosphorylates INSIG1/2, disrupting SCAP-SREBP complexes to activate lipogenesis genes supporting tumor growth. PCK1 expression is transcriptionally induced by SIRT1, FOXO1, and CREB in response to glucagon and cAMP, and repressed by insulin and Stat3, ensuring metabolic adaptation to nutrient states. In disease, upregulated PCK1 drives hyperglycemia in type 2 diabetes via excess gluconeogenesis, while in cancers such as hepatocellular carcinoma and lung cancer, its kinase and lipogenic roles promote proliferation, xenograft tumor formation, and therapy resistance, whereas knockout of PCK1 impairs tumor anabolism.

Background

PCK1 (Phosphoenolpyruvate carboxykinase 1, PEPCK-C) is a cytosolic, GTP-dependent enzyme in the lyase family, serving as the rate-limiting catalyst in hepatic gluconeogenesis by decarboxylating oxaloacetate (OAA) to phosphoenolpyruvate (PEP), CO₂, and GDP, thereby channeling TCA cycle intermediates into glucose production from lactate, glycerol, or amino acids during fasting. PCK1 features a 288-residue active site with binding pockets for carboxylate groups from OAA and PEP, Mn²⁺ ions, ribose, and guanine of GTP, as well as regulatory motifs such as Ser90 (the AKT phosphorylation site enabling protein kinase activity) and acetylation sites targeted by p300 for UBR5-mediated ubiquitination and degradation under high glucose. Its primary function is to replenish glucose via the malate-aspartate shuttle through cytosolic OAA regeneration, regulate cataplerosis and anaplerosis to balance TCA cycle flux, and, when Ser90 is phosphorylated by AKT, translocate to the ER as a kinase that phosphorylates INSIG1/2, disrupting SCAP-SREBP complexes to activate lipogenesis genes supporting tumor growth. PCK1 expression is transcriptionally induced by SIRT1, FOXO1, and CREB in response to glucagon and cAMP, and repressed by insulin and Stat3, ensuring metabolic adaptation to nutrient states. In disease, upregulated PCK1 drives hyperglycemia in type 2 diabetes via excess gluconeogenesis, while in cancers such as hepatocellular carcinoma and lung cancer, its kinase and lipogenic roles promote proliferation, xenograft tumor formation, and therapy resistance, whereas knockout of PCK1 impairs tumor anabolism.

References
https://pubmed.ncbi.nlm.nih.gov/37102687/ https://pubmed.ncbi.nlm.nih.gov/34020084/

Reference Table for Selecting PVDF Membrane Pore Size Specifications

Protein Size (kDa)	PVDF Transfer Membrane Pore Size (μm)
< 10	0.22
10-20	0.22
20-30	0.45
30-45	0.45
45-70	0.45
80-100	0.45
100-140	0.45
> 140	0.45

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Protein Size (kDa)	Separating Gel Percentage
4-40	20%
12-45	15%
10-70	12.5%
15-100	10%
25-100	8%
60-210	5%