AFfirm™ PKM2 Mouse Monoclonal Antibody - #BF8326
製品説明
*The optimal dilutions should be determined by the end user.
*Tips:
WB: For western blot detection of denatured protein samples. IHC: For immunohistochemical detection of paraffin sections (IHC-p) or frozen sections (IHC-f) of tissue samples. IF/ICC: For immunofluorescence detection of cell samples. ELISA(peptide): For ELISA detection of antigenic peptide.
折りたたみ/展開
CTHBP; Cytosolic thyroid hormone binding protein; Cytosolic thyroid hormone-binding protein; KPYM_HUMAN; MGC3932; OIP 3; OIP-3; OIP3; OPA interacting protein 3; Opa-interacting protein 3; p58; PK muscle type; PK, muscle type; PK2; PK3; PKM; PKM2; pykm; Pyruvate kinase 2/3; Pyruvate kinase 3; Pyruvate kinase isozymes M1/M2; Pyruvate kinase muscle; Pyruvate kinase muscle isozyme; pyruvate kinase PKM; Pyruvate kinase, muscle 2; TCB; THBP1; Thyroid hormone binding protein 1; Thyroid hormone binding protein cytosolic; Thyroid hormone-binding protein 1; Tumor M2 PK; Tumor M2-PK;
免疫原
Specifically expressed in proliferating cells, such as embryonic stem cells, embryonic carcinoma cells, as well as cancer cells.
- P14618 KPYM_HUMAN:
- Protein BLAST With
- NCBI/
- ExPASy/
- Uniprot
MSKPHSEAGTAFIQTQQLHAAMADTFLEHMCRLDIDSPPITARNTGIICTIGPASRSVETLKEMIKSGMNVARLNFSHGTHEYHAETIKNVRTATESFASDPILYRPVAVALDTKGPEIRTGLIKGSGTAEVELKKGATLKITLDNAYMEKCDENILWLDYKNICKVVEVGSKIYVDDGLISLQVKQKGADFLVTEVENGGSLGSKKGVNLPGAAVDLPAVSEKDIQDLKFGVEQDVDMVFASFIRKASDVHEVRKVLGEKGKNIKIISKIENHEGVRRFDEILEASDGIMVARGDLGIEIPAEKVFLAQKMMIGRCNRAGKPVICATQMLESMIKKPRPTRAEGSDVANAVLDGADCIMLSGETAKGDYPLEAVRMQHLIAREAEAAIYHLQLFEELRRLAPITSDPTEATAVGAVEASFKCCSGAIIVLTKSGRSAHQVARYRPRAPIIAVTRNPQTARQAHLYRGIFPVLCKDPVQEAWAEDVDLRVNFAMNVGKARGFFKKGDVVIVLTGWRPGSGFTNTMRVVPVP
PTMs - P14618 基板として
Site | PTM Type | Enzyme | Source |
---|---|---|---|
S2 | Acetylation | Uniprot | |
S2 | Phosphorylation | Uniprot | |
K3 | Acetylation | Uniprot | |
K3 | Methylation | Uniprot | |
K3 | Ubiquitination | Uniprot | |
S6 | Phosphorylation | Uniprot | |
T25 | Phosphorylation | Uniprot | |
S37 | Phosphorylation | P28482 (MAPK1) | Uniprot |
T41 | Phosphorylation | Uniprot | |
T45 | Phosphorylation | Q96GD4 (AURKB) | Uniprot |
C49 | S-Nitrosylation | Uniprot | |
T50 | Phosphorylation | Uniprot | |
S55 | Phosphorylation | Uniprot | |
S57 | Phosphorylation | Uniprot | |
T60 | Phosphorylation | Uniprot | |
K62 | Acetylation | Uniprot | |
K62 | Ubiquitination | Uniprot | |
K66 | Acetylation | Uniprot | |
K66 | Ubiquitination | Uniprot | |
S77 | Phosphorylation | Uniprot | |
T80 | Phosphorylation | Uniprot | |
Y83 | Phosphorylation | Uniprot | |
T87 | Phosphorylation | Uniprot | |
K89 | Acetylation | Uniprot | |
K89 | Ubiquitination | Uniprot | |
R92 | Methylation | Uniprot | |
T93 | Phosphorylation | Uniprot | |
T95 | Phosphorylation | Uniprot | |
S97 | Phosphorylation | Uniprot | |
S100 | Phosphorylation | Uniprot | |
Y105 | Phosphorylation | Q9UM73 (ALK) | Uniprot |
K115 | Acetylation | Uniprot | |
K115 | Ubiquitination | Uniprot | |
K125 | Ubiquitination | Uniprot | |
S127 | Phosphorylation | Uniprot | |
T129 | Phosphorylation | Uniprot | |
K135 | Acetylation | Uniprot | |
K135 | Ubiquitination | Uniprot | |
K136 | Ubiquitination | Uniprot | |
K141 | Acetylation | Uniprot | |
K141 | Ubiquitination | Uniprot | |
T143 | Phosphorylation | Uniprot | |
Y148 | Phosphorylation | P00533 (EGFR) | Uniprot |
K151 | Acetylation | Uniprot | |
K151 | Ubiquitination | Uniprot | |
C152 | S-Nitrosylation | Uniprot | |
Y161 | Phosphorylation | Uniprot | |
K162 | Acetylation | Uniprot | |
K162 | Ubiquitination | Uniprot | |
K166 | Acetylation | Uniprot | |
K166 | Sumoylation | Uniprot | |
K166 | Ubiquitination | Uniprot | |
S172 | Phosphorylation | Uniprot | |
Y175 | Phosphorylation | Uniprot | |
S182 | Phosphorylation | Uniprot | |
K186 | Acetylation | Uniprot | |
K186 | Ubiquitination | Uniprot | |
K188 | Acetylation | Uniprot | |
K188 | Ubiquitination | Uniprot | |
T195 | Phosphorylation | Uniprot | |
S202 | Phosphorylation | Uniprot | |
S205 | Phosphorylation | Uniprot | |
K206 | Acetylation | Uniprot | |
K206 | Ubiquitination | Uniprot | |
K207 | Acetylation | Uniprot | |
K207 | Ubiquitination | Uniprot | |
S222 | Phosphorylation | Uniprot | |
K224 | Acetylation | Uniprot | |
K224 | Sumoylation | Uniprot | |
K224 | Ubiquitination | Uniprot | |
K230 | Acetylation | Uniprot | |
K230 | Ubiquitination | Uniprot | |
S243 | Phosphorylation | Uniprot | |
K247 | Ubiquitination | Uniprot | |
S249 | Phosphorylation | Uniprot | |
R255 | Methylation | Uniprot | |
K256 | Ubiquitination | Uniprot | |
K261 | Acetylation | Uniprot | |
K261 | Ubiquitination | Uniprot | |
K266 | Acetylation | Uniprot | |
K266 | Ubiquitination | Uniprot | |
S269 | Phosphorylation | Uniprot | |
K270 | Sumoylation | Uniprot | |
K270 | Ubiquitination | Uniprot | |
R278 | Methylation | Uniprot | |
S287 | Phosphorylation | Uniprot | |
K305 | Acetylation | Uniprot | |
K305 | Ubiquitination | Uniprot | |
K311 | Ubiquitination | Uniprot | |
R319 | Methylation | Uniprot | |
K322 | Ubiquitination | Uniprot | |
C326 | S-Nitrosylation | Uniprot | |
T328 | Phosphorylation | Uniprot | |
K336 | Ubiquitination | Uniprot | |
K337 | Ubiquitination | Uniprot | |
S346 | Phosphorylation | Uniprot | |
S362 | Phosphorylation | Uniprot | |
T365 | Phosphorylation | Uniprot | |
K367 | Acetylation | Uniprot | |
K367 | Ubiquitination | Uniprot | |
Y370 | Phosphorylation | Uniprot | |
Y390 | Phosphorylation | Uniprot | |
T405 | O-Glycosylation | Uniprot | |
S406 | O-Glycosylation | Uniprot | |
S406 | Phosphorylation | Uniprot | |
T409 | Phosphorylation | Uniprot | |
T412 | Phosphorylation | Uniprot | |
S420 | Phosphorylation | Uniprot | |
K422 | Acetylation | Uniprot | |
C423 | S-Nitrosylation | Uniprot | |
C424 | S-Nitrosylation | Uniprot | |
S425 | Phosphorylation | Uniprot | |
T432 | Phosphorylation | Uniprot | |
K433 | Acetylation | Uniprot | |
K433 | Ubiquitination | Uniprot | |
S434 | Phosphorylation | Uniprot | |
Y444 | Phosphorylation | Uniprot | |
T454 | Phosphorylation | Q9P1W9 (PIM2) | Uniprot |
Y466 | Phosphorylation | Uniprot | |
R467 | Methylation | Uniprot | |
C474 | S-Nitrosylation | Uniprot | |
K475 | Ubiquitination | Uniprot | |
K498 | Acetylation | Uniprot | |
K498 | Ubiquitination | Uniprot | |
K505 | Ubiquitination | Uniprot | |
T513 | Phosphorylation | Uniprot | |
S519 | Phosphorylation | Uniprot | |
T524 | Phosphorylation | Uniprot |
PTMs - P14618 酵素として
研究背景
Glycolytic enzyme that catalyzes the transfer of a phosphoryl group from phosphoenolpyruvate (PEP) to ADP, generating ATP. Stimulates POU5F1-mediated transcriptional activation. Plays a general role in caspase independent cell death of tumor cells. 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. Promotes in a STAT1-dependent manner, the expression of the immune checkpoint protein CD274 in ARNTL/BMAL1-deficient macrophages (By similarity).
ISGylated.
Under hypoxia, hydroxylated by EGLN3.
Acetylation at Lys-305 is stimulated by high glucose concentration, it decreases enzyme activity and promotes its lysosomal-dependent degradation via chaperone-mediated autophagy.
FGFR1-dependent tyrosine phosphorylation is reduced by interaction with TRIM35.
Cytoplasm. Nucleus.
Note: Translocates to the nucleus in response to different apoptotic stimuli. Nuclear translocation is sufficient to induce cell death that is caspase independent, isoform-specific and independent of its enzymatic activity.
Specifically expressed in proliferating cells, such as embryonic stem cells, embryonic carcinoma cells, as well as cancer cells.
Monomer and homotetramer. Exists as a monomer in the absence of D-fructose 1,6-bisphosphate (FBP), and reversibly associates to form a homotetramer in the presence of FBP. The monomeric form binds T3. Tetramer formation induces pyruvate kinase activity. The tetrameric form has high affinity for the substrate and is associated within the glycolytic enzyme complex. Exists in a nearly inactive dimeric form in tumor cells and the dimeric form has less affinity for the substrate. Binding to certain oncoproteins such as HPV-16 E7 oncoprotein can trigger dimerization. FBP stimulates the formation of tetramers from dimers. Interacts with HERC1, POU5F1 and PML. Interacts (isoform M2) with EGLN3; the interaction hydroxylates PKM under hypoxia and enhances binding to HIF1A. Interacts (isoform M2) with HIF1A; the interaction is enhanced by binding of EGLN3, promoting enhanced transcription activity under hypoxia. Interacts (isoform M2, but not isoform M1) with TRIM35; this interaction prevents FGFR1-dependent tyrosine phosphorylation. Interacts with JMJD8.
Belongs to the pyruvate kinase family.
研究領域
· Human Diseases > Endocrine and metabolic diseases > Type II diabetes mellitus.
· Human Diseases > Infectious diseases: Viral > Human papillomavirus infection.
· Human Diseases > Cancers: Overview > Viral carcinogenesis.
· Human Diseases > Cancers: Overview > Central carbon metabolism in cancer. (View pathway)
· Metabolism > Carbohydrate metabolism > Glycolysis / Gluconeogenesis.
· Metabolism > Nucleotide metabolism > Purine metabolism.
· Metabolism > Carbohydrate metabolism > Pyruvate metabolism.
· Metabolism > Global and overview maps > Metabolic pathways.
· Metabolism > Global and overview maps > Carbon metabolism.
· Metabolism > Global and overview maps > Biosynthesis of amino acids.
· Organismal Systems > Endocrine system > Glucagon signaling pathway.
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