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AB131021

Anti-PKM antibody

1

(1 Review)

|

(5 Publications)

Rabbit Polyclonal KPYM antibody. Suitable for IHC-P, IP, WB and reacts with Human samples. Cited in 5 publications. Immunogen corresponding to Synthetic Peptide within Human PKM aa 1-50.

View Alternative Names

OIP3, PK2, PK3, PKM2, PKM, Pyruvate kinase PKM, Cytosolic thyroid hormone-binding protein, Opa-interacting protein 3, Pyruvate kinase 2/3, Pyruvate kinase muscle isozyme, Threonine-protein kinase PKM2, Thyroid hormone-binding protein 1, Tumor M2-PK, Tyrosine-protein kinase PKM2, p58, CTHBP, OIP-3, THBP1

4 Images
Immunohistochemistry (Formalin/PFA-fixed paraffin-embedded sections) - Anti-PKM antibody (AB131021)
  • IHC-P

Unknown

Immunohistochemistry (Formalin/PFA-fixed paraffin-embedded sections) - Anti-PKM antibody (AB131021)

Immunohistochemistry (Formalin/PFA-fixed paraffin-embedded sections) analysis of human stomach tissue labelling PKM with ab131021 at 1/1000 (1μg/ml). Detection : DAB.

Immunohistochemistry (Formalin/PFA-fixed paraffin-embedded sections) - Anti-PKM antibody (AB131021)
  • IHC-P

Unknown

Immunohistochemistry (Formalin/PFA-fixed paraffin-embedded sections) - Anti-PKM antibody (AB131021)

Immunohistochemistry (Formalin/PFA-fixed paraffin-embedded sections) analysis of human osteosarcoma tissue labelling PKM with ab131021 at 1/1000 (1μg/ml). Detection : DAB.

Immunoprecipitation - Anti-PKM antibody (AB131021)
  • IP

Unknown

Immunoprecipitation - Anti-PKM antibody (AB131021)

Detection of PKM2 by Western Blot of Immunprecipitate.

ab131021 at 0.4μg/ml staining PKM in HeLa whole cell lysate immunoprecipitated using ab131021 at 6μg/mg lysate (1 mg/IP; 20% of IP loaded/lane).

Detection : Chemiluminescence with exposure time of 3 seconds.

All lanes:

Immunoprecipitation - Anti-PKM antibody (ab131021)

Predicted band size: 58 kDa

false

Western blot - Anti-PKM antibody (AB131021)
  • WB

Unknown

Western blot - Anti-PKM antibody (AB131021)

All lanes:

Western blot - Anti-PKM antibody (ab131021) at 0.1 µg/mL

Lane 1:

HeLa whole cell lysate at 50 µg

Lane 2:

HeLa whole cell lysate at 15 µg

Lane 3:

293T whole cell lysate at 50 µg

Lane 4:

Jurkat whole cell lysate at 50 µg

Predicted band size: 58 kDa

true

Exposure time: 3s

Key facts

Host species

Rabbit

Clonality

Polyclonal

Isotype

IgG

Carrier free

No

Reacts with

Human

Applications

IP, IHC-P, WB

applications

Immunogen

Synthetic Peptide within Human PKM aa 1-50. The exact immunogen used to generate this antibody is proprietary information.

P14618

Reactivity data

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Properties and storage information

Form
Liquid
Purification technique
Affinity purification Immunogen
Purification notes
ab131021 is affinity purified using an epitope specific to PKM2 immobilized on solid support.
Storage buffer
pH: 7 - 8 Preservative: 0.09% Sodium azide Constituents: 99% Tris citrate/phosphate
Shipped at conditions
Blue Ice
Appropriate short-term storage conditions
+4°C
Appropriate long-term storage conditions
+4°C

Supplementary information

This supplementary information is collated from multiple sources and compiled automatically.

PKM also known as pyruvate kinase muscle isozyme (PKM) and PEP is an enzyme that plays an important role in glycolysis by catalysing the conversion of phosphoenolpyruvate (PEP) to pyruvate yielding ATP in the process. The PKM protein has two isoforms PKM1 and PKM2 which result from alternative splicing of the PKM gene. The mass of PKM2 the more studied isoform is approximately 58 kDa. PKM is expressed in various tissues prominently in skeletal muscle heart brain and many tumor cells. Additionally PKM has significant activity in rapidly proliferating cells suggesting its importance in high-energy demanding environments.
Biological function summary

PKM functions not only in catalyzing the last step of glycolysis but also regulates metabolic and transcriptional processes. Specifically PKM2 is a participant in the regulation of gene expression and cellular response to oxidative stress and nutrient availability. It can exist as a dimer or tetramer with the latter being the more active form in glycolytic pathways while the dimeric form can translocate to the nucleus to perform functions unrelated to its glycolytic activity. These transformations make PKM part of a dynamic complex that responds to various cellular signals.

Pathways

PKM integrates into essential metabolic pathways including the glycolytic pathway and influences the pentose phosphate pathway. It works in conjunction with phosphofructokinase-1 (PFK1) another key glycolytic enzyme synchronizing the energy production process in cells. PKM2's non-metabolic roles involve interactions in signaling pathways related to cellular proliferation and survival often interacting with and modulating proteins like HIF-1α which plays a central role in cellular responses to hypoxia.

PKM2 shows strong connections to cancer and metabolic diseases. Tumor cells often exhibit a shift in expression from PKM1 to PKM2 facilitating the altered metabolism known as the Warburg effect characterized by increased aerobic glycolysis. Its interaction with HIF-1α promotes adaptation to low oxygen environments typical in tumorous growth. Furthermore PKM disruptions or aberrations contribute to metabolic disorders such as diabetes where altered glucose metabolism becomes evident. The protein's behavior in these disease conditions indicates potential targets for therapeutic intervention highlighting the importance of PKM in both normal physiology and pathology.

Product protocols

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Target data

Catalyzes the final rate-limiting step of glycolysis by mediating the transfer of a phosphoryl group from phosphoenolpyruvate (PEP) to ADP, generating ATP (PubMed : 15996096, PubMed : 1854723, PubMed : 20847263). The ratio between the highly active tetrameric form and nearly inactive dimeric form determines whether glucose carbons are channeled to biosynthetic processes or used for glycolytic ATP production (PubMed : 15996096, PubMed : 1854723, PubMed : 20847263). The transition between the 2 forms contributes to the control of glycolysis and is important for tumor cell proliferation and survival (PubMed : 15996096, PubMed : 1854723, PubMed : 20847263).. Isoform M2. Isoform specifically expressed during embryogenesis that has low pyruvate kinase activity by itself and requires allosteric activation by D-fructose 1,6-bisphosphate (FBP) for pyruvate kinase activity (PubMed : 18337823, PubMed : 20847263). In addition to its pyruvate kinase activity in the cytoplasm, also acts as a regulator of transcription in the nucleus by acting as a protein kinase (PubMed : 18191611, PubMed : 21620138, PubMed : 22056988, PubMed : 22306293, PubMed : 22901803, PubMed : 24120661). Translocates into the nucleus in response to various signals, such as EGF receptor activation, and homodimerizes, leading to its conversion into a protein threonine- and tyrosine-protein kinase (PubMed : 22056988, PubMed : 22306293, PubMed : 22901803, PubMed : 24120661, PubMed : 26787900). Catalyzes phosphorylation of STAT3 at 'Tyr-705' and histone H3 at 'Thr-11' (H3T11ph), leading to activate transcription (PubMed : 22306293, PubMed : 22901803, PubMed : 24120661). Its ability to activate transcription plays a role in cancer cells by promoting cell proliferation and promote tumorigenesis (PubMed : 18337823, PubMed : 22901803, PubMed : 26787900). Promotes the expression of the immune checkpoint protein CD274 in BMAL1-deficient macrophages (By similarity). May also act as a translation regulator for a subset of mRNAs, independently of its pyruvate kinase activity : associates with subpools of endoplasmic reticulum-associated ribosomes, binds directly to the mRNAs translated at the endoplasmic reticulum and promotes translation of these endoplasmic reticulum-destined mRNAs (By similarity). Plays a role in caspase independent cell death of tumor cells (PubMed : 17308100).. Isoform M1. Pyruvate kinase isoform expressed in adult tissues, which replaces isoform M2 after birth (PubMed : 18337823). In contrast to isoform M2, has high pyruvate kinase activity by itself and does not require allosteric activation by D-fructose 1,6-bisphosphate (FBP) for activity (PubMed : 20847263).
See full target information PKM

Publications (5)

Recent publications for all applications. Explore the full list and refine your search

Cellular and molecular gastroenterology and hepatology 15:373-392 PubMed36244646

2022

Calcium Channel α2δ1 is Essential for Pancreatic Tumor-Initiating Cells through Sequential Phosphorylation of PKM2.

Applications

Unspecified application

Species

Unspecified reactive species

Jingtao Liu,Ming Tao,Wei Zhao,Qingru Song,Xiaodan Yang,Meng Li,Yanhua Zhang,Dianrong Xiu,Zhiqian Zhang

Cancer cell international 20:363 PubMed32774157

2020

TET2 suppresses nasopharyngeal carcinoma progression by inhibiting glycolysis metabolism.

Applications

Unspecified application

Species

Unspecified reactive species

Xixia Zhang,Jing Yang,Dong Shi,Zhiwei Cao

Cell death & disease 9:988 PubMed30250190

2018

VDAC2 interacts with PFKP to regulate glucose metabolism and phenotypic reprogramming of glioma stem cells.

Applications

Unspecified application

Species

Unspecified reactive species

Kai Zhou,Yue-Liang Yao,Zhi-Cheng He,Cong Chen,Xiao-Ning Zhang,Kai-Di Yang,Yu-Qi Liu,Qing Liu,Wen-Juan Fu,Ya-Ping Chen,Qin Niu,Qing-Hua Ma,Rong Zhou,Xiao-Hong Yao,Xia Zhang,You-Hong Cui,Xiu-Wu Bian,Yu Shi,Yi-Fang Ping

Biomedicine & pharmacotherapy = Biomedecine & phar 107:1692-1704 PubMed30257387

2018

Oviductus ranae protein hydrolysate (ORPH) inhibits the growth, metastasis and glycolysis of HCC by targeting miR-491-5p/PKM2 axis.

Applications

Unspecified application

Species

Unspecified reactive species

Qiuran Xu,Changwei Dou,Xin Liu,Liu Yang,Chao Ni,Jiahui Wang,Yang Guo,Wei Yang,Xiangmin Tong,Dongsheng Huang

Molecular cancer 16:178 PubMed29262861

2017

HSP90 promotes cell glycolysis, proliferation and inhibits apoptosis by regulating PKM2 abundance via Thr-328 phosphorylation in hepatocellular carcinoma.

Applications

Unspecified application

Species

Unspecified reactive species

Qiuran Xu,Jianfeng Tu,Changwei Dou,Jun Zhang,Liu Yang,Xin Liu,Kefeng Lei,Zhikui Liu,Yufeng Wang,Lijie Li,Hangxing Bao,Jiahui Wang,Kangsheng Tu
View all publications

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