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

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

Code	CSB-YP018072RB
MSDS	MSDS Datasheet
Size	Pls inquire
Source	Yeast
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Code	CSB-EP018072RB
MSDS	MSDS Datasheet
Size	Pls inquire
Source	E.coli
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Code	CSB-EP018072RB-B
MSDS	MSDS Datasheet
Size	Pls inquire
Source	E.coli
Conjugate	Avi-tag Biotinylated E. coli biotin ligase (BirA) is highly specific in covalently attaching biotin to the 15 amino acid AviTag peptide. This recombinant protein was biotinylated in vivo by AviTag-BirA technology, which method is BriA catalyzes amide linkage between the biotin and the specific lysine of the AviTag.
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Code	CSB-BP018072RB
MSDS	MSDS Datasheet
Size	Pls inquire
Source	Baculovirus
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Code	CSB-MP018072RB
MSDS	MSDS Datasheet
Size	Pls inquire
Source	Mammalian cell
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Product Details
Customer Reviews and Q&A
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)

Protein Length

Partial

Tag Info

Tag type will be determined during the manufacturing process.

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.

Form

Lyophilized powder
Note: We will preferentially ship the format that we have in stock, however, if you have any special requirement for the format, please remark your requirement when placing the order, we will prepare according to your demand.

Buffer before Lyophilization

Tris/PBS-based buffer, 6% Trehalose.

Reconstitution

We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Please reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL.We recommend to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20℃/-80℃. Our default final concentration of glycerol is 50%. Customers could use it as reference.

Troubleshooting and FAQs

Protein FAQs

Storage Condition

Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. Avoid repeated freeze-thaw cycles.

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.

Lead Time

Delivery time may differ from different purchasing way or location, please kindly consult your local distributors for specific delivery time.
Note: All of our proteins are default shipped with normal blue ice packs, if you request to ship with dry ice, please communicate with us in advance and extra fees will be charged.

Notes

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

Datasheet

Please contact us to get it.

Customer Reviews and Q&A

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Target Background

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.

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