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Recombinant Rabbit Pyruvate kinase isozymes M1/M2 (PKM2), partial

Recombinant Rabbit Pyruvate kinase isozymes M1/M2 (PKM2), partial

Code
MSDS	MSDS Datasheet
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Source
Conjugate
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Target Background

Product Details

Purity

>85% (SDS-PAGE)

Target Names

PKM

Uniprot NO.

P11974

Alternative Names

PKM; PKM2Pyruvate kinase PKM; EC 2.7.1.40; Pyruvate kinase muscle isozyme

Species

Oryctolagus cuniculus (Rabbit)

Source

Yeast

Expression Region

2-531

Target Protein Sequence

SKSHSEAGS AFIQTQQLHA AMADTFLEHM CRLDIDSAPI TARNTGIICT IGPASRSVET LKEMIKSGMN VARMNFSHGT HEYHAETIKN VRTATESFAS DPILYRPVAV ALDTKGPEIR TGLIKGSGTA EVELKKGATL KITLDNAYME KCDENILWLD YKNICKVVDV GSKVYVDDGL ISLQVKQKGP DFLVTEVENG GFLGSKKGVN LPGAAVDLPA VSEKDIQDLK FGVEQDVDMV FASFIRKAAD VHEVRKILGE KGKNIKIISK IENHEGVRRF DEILEASDGI MVARGDLGIE IPAEKVFLAQ KMIIGRCNRA GKPVICATQM LESMIKKPRP TRAEGSDVAN AVLDGADCIM LSGETAKGDY PLEAVRMQHL IAREAEAAMF HRKLFEELAR SSSHSTDLME AMAMGSVEAS YKCLAAALIV LTESGRSAHQ VARYRPRAPI IAVTRNHQTA RQAHLYRGIF PVVCKDPVQE AWAEDVDLRV NLAMNVGKAR GFFKKGDVVI VLTGWRPGSG FTNTMRVVPV P
Note: The complete sequence may include tag sequence, target protein sequence, linker sequence and extra sequence that is translated with the protein sequence for the purpose(s) of secretion, stability, solubility, etc.
If the exact amino acid sequence of this recombinant protein is critical to your application, please explicitly request the full and complete sequence of this protein before ordering.

Protein Length

Partial

Tag Info

N-terminal His-tagged/Tag-Free
The tag type will be determined during production process. If you have specified tag type, please tell us and we will develop the specified tag preferentially.

Storage Condition

Store at -20°C, for extended storage, conserve at -20°C or -80°C.

Shelf Life

The shelf life is related to many factors, storage state, buffer ingredients, storage temperature and the stability of the protein itself.
Generally, the shelf life of liquid form is 6 months at -20°C/-80°C. The shelf life of lyophilized form is 12 months at -20°C/-80°C.

Notes

Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.

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Target Background

Function(From Uniprot)

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.

Gene References into Functions

the polarity of the residue 113 is central in the partition of K+ into its site and that the substitution of Thr for Leu changes the ion selectivity for the monovalent cation with minor changes in the binding of the substrates. PMID:25474090
In contrast to PK from rabbit tissues, the enzyme from the hare heart and muscles PK is presented by its allosteric isoform which might by advantageous under extreme conditions of the hare's habitation PMID:26027383
Mass spectrometry has been used to determine the number of exchangeable backbone amide protons and the associated rate constants that are altered when PKM binds either the allosteric inhibitor phenylalanine or a nonallosteric analogue of the inhibitor. PMID:23418858
Carboxyl group of the substrate phosphoenolpyruvate is responsible for energetic coupling with phenylalanine binding in the allosteric sites. PMID:23256782
Bound mono- and divalent cations influence the binding of the substrate phosphoenolpyruvate to pyruvate kinase, in particular the binding-induced structural change of the protein and the conformation and interaction of bound phosphoenolpyruvate. PMID:21539324
The structure of rabbit muscle pyruvate kinase-Mn-pyruvate-proline complex reported herein demonstrates that proline binds specifically to the allosteric site of muscle pyruvate kinase. PMID:20629175
In the absence of substrate, SAXS-monitored conformational changes in muscle pyruvate kinase elicited by the binding of phenylalanine (an allosteric inhibitor) are similar to those observed upon binding of alanine or 2-aminobutyric acid. PMID:20712377
Results of an in-depth dissection of the thermodynamic signatures of rabbit muscle pyruvate kinase (RMPK) interacting with metabolites provide novel insights into the mechanism of allosteric regulation of RMPK. PMID:19719244
Simulation of pyruvate kinase regulatory behavior under physiological conditions shows that the thermodynamics involved in the enzyme's regulation are well-tuned to allow maximal response to even minute changes in temperature and ligand concentration. PMID:19719322
Fluorescence study of muscle pyruvate kinase confirms an increase in the isobaric heat capacity associated with entropy-driven R --> T transition and an intriguing role of adenosine diphosphate (ADP) in the enzyme activation process. PMID:19719323