Rabbit anti-Human PKM1-specific Polyclonal Antibody

Uniprot Id

P14618

Target Species

Human

Target Name

PKM

Target Full Name

Pyruvate kinase PKM

Target Function

Glycolytic enzyme that catalyzes the transfer of a phosphoryl group from phosphoenolpyruvate (PEP) to ADP, generating ATP. 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. The transition between the 2 forms contributes to the control of glycolysis and is important for tumor cell proliferation and survival. In addition to its role in glycolysis, also regulates transcription. Stimulates POU5F1-mediated transcriptional activation. Promotes in a STAT1-dependent manner, the expression of the immune checkpoint protein CD274 in ARNTL/BMAL1-deficient macrophages. Also acts 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. Plays a general role in caspase independent cell death of tumor cells.

Target Subcellular Location

Cytoplasm. Nucleus.

Target Protein Families

Pyruvate kinase family

Target Tissue Specificity

Specifically expressed in proliferating cells, such as embryonic stem cells, embryonic carcinoma cells, as well as cancer cells.

Target Research Area

Signal Transduction

Target Synonyms

CTHBP; Cytosolic thyroid hormone-binding protein; KPYM_HUMAN; OIP-3; Opa-interacting protein 3; p58; pkm; PKM1; PKM2; Pyruvate kinase 2/3; Pyruvate kinase muscle isozyme; Pyruvate kinase PKM; THBP1; Thyroid hormone-binding protein 1; Tumor M2-PK

Target Background

This gene encodes a protein involved in glycolysis. The encoded protein is a pyruvate kinase that catalyzes the transfer of a phosphoryl group from phosphoenolpyruvate to ADP, generating ATP and pyruvate. This protein has been shown to interact with thyroid hormone and may mediate cellular metabolic effects induced by thyroid hormones. This protein has been found to bind Opa protein, a bacterial outer membrane protein involved in gonococcal adherence to and invasion of human cells, suggesting a role of this protein in bacterial pathogenesis. Several alternatively spliced transcript variants encoding a few distinct isoforms have been reported.