PKM Antibody [F7K24] | Primary Antibodies

Application: Reactivity: Mouse, Rat, Human

Usage Information

Dilution
WB1:10000 IF1:50 FCM1:50

Application
WB, IF, FCM

Reactivity
Mouse, Rat, 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
58 kDa 58 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	Mouse lung; Human skeletal muscle; Rat skeletal muscle; Mouse skeletal muscle; HeLa cells; Jurkat cells; A549 cells
Negative Control

Datasheet & SDS

Biological Description

Specificity
PKM Antibody [F7K24] detects endogenous levels of total PKM protein.

Clone
F7K24

Synonym(s)
OIP3; PK2; PK3; PKM2; PKM; Pyruvate kinase 2/3; Pyruvate kinase muscle isozyme; Threonine-protein kinase PKM2; Tumor M2-PK; Tyrosine-protein kinase PKM2; p58; CTHBP; OIP-3; THBP1

Background
PKM, or pyruvate kinase muscle isozyme, is encoded by the PKM gene through mutually exclusive alternative splicing of exons 9 and 10, resulting in two isoforms: PKM1, which has high constitutive activity and is found predominantly in differentiated tissues such as skeletal muscle, brain, and heart, and PKM2 IS prevalent in proliferating cells and tumors. PKM catalyzes the final rate-limiting step of glycolysis by transferring a phosphate group from phosphoenolpyruvate (PEP) to ADP, thereby generating pyruvate and ATP. The enzyme’s activity is allosterically regulated by fructose-1,6-bisphosphate (FBP), which promotes formation of the highly active tetrameric structure over the less active dimeric form. PKM2 consists of A (N-terminal), B (FBP-binding), and C (C-terminal catalytic) domains and contains key regulatory sites such as Ser37, whose phosphorylation facilitates nuclear translocation and enables non-glycolytic moonlighting functions in its dimeric form. While the primary function of PKM is to control glycolytic flux in tissues with high energy demand, PKM2 uniquely regulates gene expression and chromatin remodeling during myoblast proliferation and differentiation by mediating the incorporation of SWI/SNF subunits DPF2 and BAF250a into myogenic promoters, facilitating phosphorylation of histone H3 at threonine 11 directly and H3 at threonine 6 and 45 indirectly via AKT and PKC pathways, and influencing expression of metabolic genes specific to PKM1 versus genes involved in differentiation and cell division that are uniquely regulated by PKM2. PKM integrates glycolysis with the pentose phosphate pathway, works in concert with phosphofructokinase 1 (PFK1), modulates HIF-1α activity under hypoxic conditions as seen in the Warburg effect in cancer, and supports tumor cell proliferation and survival. PKM includes isoform switches, with increased PKM2 expression observed in many cancers to support aerobic glycolysis, involvement in metabolic disorders such as diabetes, and critical roles in myogenesis where knockdown of PKM2 impairs muscle cell differentiation. Temporal shifts in isoform expression occur, with PKM2 predominant during embryonic development and a switch to PKM1 postnatally in muscle, emphasizing the dynamic interplay between metabolic and transcriptional regulation.

Background

PKM, or pyruvate kinase muscle isozyme, is encoded by the PKM gene through mutually exclusive alternative splicing of exons 9 and 10, resulting in two isoforms: PKM1, which has high constitutive activity and is found predominantly in differentiated tissues such as skeletal muscle, brain, and heart, and PKM2 IS prevalent in proliferating cells and tumors. PKM catalyzes the final rate-limiting step of glycolysis by transferring a phosphate group from phosphoenolpyruvate (PEP) to ADP, thereby generating pyruvate and ATP. The enzyme’s activity is allosterically regulated by fructose-1,6-bisphosphate (FBP), which promotes formation of the highly active tetrameric structure over the less active dimeric form. PKM2 consists of A (N-terminal), B (FBP-binding), and C (C-terminal catalytic) domains and contains key regulatory sites such as Ser37, whose phosphorylation facilitates nuclear translocation and enables non-glycolytic moonlighting functions in its dimeric form. While the primary function of PKM is to control glycolytic flux in tissues with high energy demand, PKM2 uniquely regulates gene expression and chromatin remodeling during myoblast proliferation and differentiation by mediating the incorporation of SWI/SNF subunits DPF2 and BAF250a into myogenic promoters, facilitating phosphorylation of histone H3 at threonine 11 directly and H3 at threonine 6 and 45 indirectly via AKT and PKC pathways, and influencing expression of metabolic genes specific to PKM1 versus genes involved in differentiation and cell division that are uniquely regulated by PKM2. PKM integrates glycolysis with the pentose phosphate pathway, works in concert with phosphofructokinase 1 (PFK1), modulates HIF-1α activity under hypoxic conditions as seen in the Warburg effect in cancer, and supports tumor cell proliferation and survival. PKM includes isoform switches, with increased PKM2 expression observed in many cancers to support aerobic glycolysis, involvement in metabolic disorders such as diabetes, and critical roles in myogenesis where knockdown of PKM2 impairs muscle cell differentiation. Temporal shifts in isoform expression occur, with PKM2 predominant during embryonic development and a switch to PKM1 postnatally in muscle, emphasizing the dynamic interplay between metabolic and transcriptional regulation.

References
https://pubmed.ncbi.nlm.nih.gov/33453989/ https://pubmed.ncbi.nlm.nih.gov/38645038/

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%