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AB181693

Biotin Anti-PKM antibody

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(2 Publications)

Goat Polyclonal KPYM antibody - conjugated to Biotin. Suitable for ELISA, WB and reacts with Rabbit samples. Cited in 2 publications. Immunogen corresponding to Native Full Length Protein corresponding to Human PKM.

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

Key facts

Host species

Goat

Clonality

Polyclonal

Isotype

IgG

Conjugation

Biotin

Excitation/Emission
Carrier free

No

Reacts with

Rabbit

Applications

ELISA, WB

applications

Immunogen

Native Full Length Protein corresponding to Human PKM.

P14618

Specificity

Anti-Pyruvate Kinase has been reported to react with all forms of pyruvate kinase (pan M-PK). Cross reactivity against Pyruvate Kinase from other sources may occur but have not been specifically determined.

Reactivity data

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Properties and storage information

Form
Liquid
Purity
IgG fraction
Purification technique
Ion exchange chromatography
Purification notes
Anti-Pyruvate Kinase Antibody is an IgG fraction antibody purified from monospecific antiserum by a multi-step process which includes delipidation, salt fractionation and ion exchange chromatography followed by extensive dialysis against the buffer.
Storage buffer
Preservative: 0.01% Sodium azide Constituents: 1% BSA, 0.88% Sodium chloride, 0.424% Potassium phosphate solution
Shipped at conditions
Blue Ice
Appropriate short-term storage duration
1-2 weeks
Appropriate short-term storage conditions
+4°C
Appropriate long-term storage conditions
-20°C
Aliquoting information
Upon delivery aliquot
Storage information
Avoid freeze / thaw cycle

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

For this product, it's our understanding that no specific protocols are required. You can visit:

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 (2)

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

Cell communication and signaling : CCS 20:76 PubMed35637461

2022

Podocyte specific deletion of PKM2 ameliorates LPS-induced podocyte injury through beta-catenin.

Applications

Unspecified application

Species

Unspecified reactive species

Mohammed Alquraishi,Samah Chahed,Dina Alani,Dexter L Puckett,Presley D Dowker,Katelin Hubbard,Yi Zhao,Ji Yeon Kim,Laurentia Nodit,Huma Fatima,Dallas Donohoe,Brynn Voy,Winyoo Chowanadisai,Ahmed Bettaieb

Journal of biochemical and molecular toxicology 36:e23070 PubMed35403324

2022

Silencing ATF4 inhibits JMJD3-dependent JUNB/ETS1 axis and mitigates cerebral ischemic injury.

Applications

Unspecified application

Species

Unspecified reactive species

Gang Wu,Xi'an Zhang,Shijun Li,Lina Wang,Jie Bai,Hanxiang Wang,Qing Shu
View all publications

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