Human PKM peptide

Name: Human PKM peptide
SKU: DAG-P1029
Rating: 5 (1 reviews)

Synthetic Human PKM peptide

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COA

SDS

Datasheet

Specificity

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

Nature

Synthetic

Tag/Conjugate

Unconjugated

Purity

70 - 90% by HPLC.

Format

Liquid

Preservative

None

Storage

Shipped at 4°C. Upon delivery aliquot and store at -20°C or -80°C. Avoid repeated freeze / thaw cycles. Information available upon request.

Gene ID

5315

UniProt ID

P14618

Antigen Description

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. [provided by RefSeq, May 2011]

Function

ATP binding; MHC class II protein complex binding; magnesium ion binding; poly(A) RNA binding; potassium ion binding; protein binding; pyruvate kinase activity;

Synonyms

PKM; pyruvate kinase, muscle; PK3; TCB; OIP3; PKM2; CTHBP; THBP1; HEL-S-30; pyruvate kinase PKM; p58; OIP-3; tumor M2-PK; PK, muscle type; pyruvate kinase 2/3; OPA-interacting protein 3; pyruvate kinase isozymes M1/M2; pyruvate kinase muscle isozyme; thyroid hormone-binding protein 1; epididymis secretory protein Li 30; cytosolic thyroid hormone-binding protein; thyroid hormone-binding protein, cytosolic;

Citations

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Datasheet

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Customer Reviews

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A novel VHL alpha isoform inhibits Warburg effect via modulation of PKM splicing

TUMOR BIOLOGY

Authors: Liu, Yanbin; Yang, Haixia; Li, Lin; Chen, She; Zuo, Feifei; Chen, Liang

Abstract

Von Hippel-Lindau (VHL) is the most frequently mutated gene in clear cell renal carcinoma. Here, we identified a novel translational variant of VHL, termed VHL alpha, initiated from an alternative translational start site upstream and in frame with the ATG start codon. We showed that VHL alpha interacts with and regulates heterogeneous nuclear ribonucleoprotein A2B1 (hnRNPA2B1), which consequently modulates pyruvate kinase transcript splicing and reprograms cellular glucose metabolism. Our study demonstrated that a novel VHL isoform may function as a tumor suppressor through inhibiting the Warburg effect.

Spermidine-induced improvement of reconsolidation of memory involves calcium-dependent protein kinase in rats

LEARNING & MEMORY

Authors: Girardi, Bruna Amanda; Ribeiro, Daniela Aymone; Signor, Cristiane; Muller, Michele; Gais, Mayara Ana; Mello, Carlos Fernando; Rubin, Maribel Antonello

Abstract

In this study, we determined whether the calcium-dependent protein kinase (PKC) signaling pathway is involved in the improvement of fear memory reconsolidation induced by the intrahippocampal administration of spermidine in rats. Male Wistar rats were trained in a fear conditioning apparatus using a 0.4-mA footshock as an unconditioned stimulus. Twenty-four hours after training, animals were re-exposed to the apparatus in the absence of shock (reactivation session). Immediately after the reactivation session, spermidine (2-200 pmol/site), the PKC inhibitor 3-[1-(dimethylaminopropyl) indol-3-yl]-4-(indol-3-yl) maleimide hydrochloride (GF 109203X, 0.3-30 pg/site), the antagonist of the polyamine-binding site at the NMDA receptor, arcaine (0.2-200 pmol/site), or the PKC activator phorbol 12-myristate 13-acetate (PMA, 0.02-2 nmol/site) was injected. While the post-reactivation administration of spermidine (20 and 200 pmol/site) and PMA (2 nmol/site) improved memory reconsolidation, GF 109203X (1, 10, and 30 pg/site) and arcaine (200 pmol/site) impaired it. GF 109203X (0.3 pg/site) impaired memory reconsolidation in the presence of spermidine (200 pmol/site). PMA (0.2 nmol/site) prevented the arcaine (200 pmol/site)-induced impairment of memory reconsolidation. Anisomycin (2 mu g/site) also impaired memory reconsolidation in the presence of spermidine (200 pmol/site). Drugs had no effect when they were administered in the absence of reactivation. These results suggest that the spermidine-induced enhancement of memory reconsolidation involves PKC activation.