Recombinant Human Pyruvate Kinase Isozymes R/L (PKLR) Protein (His)

Name: Recombinant Human Pyruvate Kinase Isozymes R/L (PKLR) Protein (His)
Brand: Beta LifeScience
SKU: BLC-04665P
Availability: InStock

Greater than 90% as determined by SDS-PAGE.

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Product Overview

Description	Recombinant Human Pyruvate Kinase Isozymes R/L (PKLR) Protein (His) is produced by our E.coli expression system. This is a full length protein.
Purity	Greater than 90% as determined by SDS-PAGE.
Uniprotkb	P30613
Target Symbol	PKLR
Synonyms	EC 2.7.1.40; KPYR_HUMAN; L-PK; Pk-1; PK1 ; PKL ; Pklg; Pklr; PKR; PKRL; Pyruvate kinase 1; Pyruvate kinase isozymes R/L; Pyruvate kinase liver and blood cell; Pyruvate kinase liver and RBC; Pyruvate kinase liver and red blood cell; Pyruvate kinase liver type; Pyruvate kinase type L; Pyruvate kinase, red cell type; R type/L type pyruvate kinase; R-PK; R-type/L-type pyruvate kinase; Red cell/liver pyruvate kinase; RPK
Species	Homo sapiens (Human)
Expression System	E.coli
Tag	N-6His
Target Protein Sequence	MSIQENISSLQLRSWVSKSQRDLAKSILIGAPGGPAGYLRRASVAQLTQELGTAFFQQQQLPAAMADTFLEHLCLLDIDSEPVAARSTSIIATIGPASRSVERLKEMIKAGMNIARLNFSHGSHEYHAESIANVREAVESFAGSPLSYRPVAIALDTKGPEIRTGILQGGPESEVELVKGSQVLVTVDPAFRTRGNANTVWVDYPNIVRVVPVGGRIYIDDGLISLVVQKIGPEGLVTQVENGGVLGSRKGVNLPGAQVDLPGLSEQDVRDLRFGVEHGVDIVFASFVRKASDVAAVRAALGPEGHGIKIISKIENHEGVKRFDEILEVSDGIMVARGDLGIEIPAEKVFLAQKMMIGRCNLAGKPVVCATQMLESMITKPRPTRAETSDVANAVLDGADCIMLSGETAKGNFPVEAVKMQHAIAREAEAAVYHRQLFEELRRAAPLSRDPTEVTAIGAVEAAFKCCAAAIIVLTTTGRSAQLLSRYRPRAAVIAVTRSAQAARQVHLCRGVFPLLYREPPEAIWADDVDRRVQFGIESGKLRGFLRVGDLVIVVTGWRPGSGYTNIMRVLSIS
Expression Range	1-574aa
Protein Length	Full Length
Mol. Weight	65.8kDa
Research Area	Metabolism
Form	Liquid or Lyophilized powder
Buffer	Liquid form: default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol. Lyophilized powder form: the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, pH 8.0.
Reconstitution	Briefly centrifuged the vial prior to opening to bring the contents to the bottom. Reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL. It is recommended to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20°C/-80°C. The default final concentration of glycerol is 50%.
Storage	1. Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. 2. Avoid repeated freeze-thaw cycles. 3. Store working aliquots at 4°C for up to one week. 4. In general, protein in liquid form is stable for up to 6 months at -20°C/-80°C. Protein in lyophilized powder form is stable for up to 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.

Target Details

Target Function	Plays a key role in glycolysis.
Protein Families	Pyruvate kinase family
Database References	HGNC: 9020 OMIM: 102900 KEGG: hsa:5313 STRING: 9606.ENSP00000339933 UniGene: PMID: 29349879 Results show that different residues contribute to the two allosteric functions: regulation by the activator fructose-1,6-bisphosphate (Fru-1,6-BP) and alanine, the inhibitor. Only a small fraction of mutated residues perturbed inhibition by alanine. In contrast, a large percentage of mutated residues influenced activation by Fru-1,6-BP; inhibition by alanine is not simply the reverse of activation by Fru-1,6-BP. PMID: 28407397 PKLR gene sequencing in 15 Spanish patients affected by pyruvate kinase deficiency (PKD) was performed. Six out of the 18 alleles found were new mutations which had not been described previously, with the PKLR c.721G>T mutation being the most prevalent (26.67%), followed by the PKLR c.1456C>T mutation (13.33%). PMID: 27871768 Gene copy number variation (CNV) of the PKLR, FCGR2A, FCGR2C, and FCGR3 genes is associated with malaria severity, and our results provide evidence for a role of CNV in host responses to malaria. PMID: 28605553 Genotype-phenotype correlations for the novel missense mutations found in the PKLR gene in PK deficiency among Tunisian cases were investigated by three-dimensional structure analysis. PMID: 28133914 Data show that pyruvate kinase (PK) activity was decreased in the GATA1 hemizygous state and PKLR c.1284delA variant. PMID: 27342114 An update of PKLR gene mutation database has been presented. (Review) PMID: 26832193 Two Novel Missense Mutations and a 5bp Deletion in the Erythroid-Specific Promoter of the PKLR Gene in Two Unrelated Patients With Pyruvate Kinase Deficient Transfusion-Dependent Chronic Nonspherocytic Hemolytic Anemia. PMID: 26728349 PKLR promotes colorectal cancer liver colonization through induction of glutathione synthesis. PMID: 26784545 Pyruvate kinase variants modulate malaria phenotypes in a Thai population. PMID: 26658699 661G>A and 1528C>T mutations of PKLR gene are associated with pyruvate kinase deficiency. PMID: 26829734 Case Report: unknown mutation in the pyruvate kinase gene (PKLR) identified from a neonate with severe jaundice. PMID: 24969675 This study determined which interactions in the fructose 1,6-bisphosphate binding site of human liver pyruvate kinase contribute to allostery. PMID: 25629396 Partial pyruvate kinase deficiency aggravates the phenotypic expression of band 3 deficiency in a family with hereditary spherocytosis. PMID: 25388786 Hemolytic anemia associated with a novel heterozygous mutation 1183A in the pyruvate kinase gene has been found in two unrelated Jordanian patients. PMID: 24330591 11 patients from 10 unrelated pyruvate kinse deficiency families had 9 different disease-causing PKLR mutations, including 2 new ones: the point mutation c.878A>T (p.Asp293Val) and the frameshift deletion c.1553delG (p.(Arg518Leufs*12). PMID: 24533562 A new type of inherited PK hyperactivity having solely increased expression of a kinetically normal PK-R had no mutations or copy number variants. An upregulatory mutation at an unlinked site is proposed. PMID: 24375447 Herpes simplex virus type 1 virion-derived US11 inhibits type 1 interferon-induced protein kinase R phosphorylation. PMID: 23773021 A global geographical co-distribution between malaria and high frequency of PK deficiency seems to occur suggesting that malaria may be a selective force raising the frequency of this 277Lys variant. PMID: 23082140 investigation of structure-function relationship of the N-terminus of liver pyruvate kinase and its regulation by oxidation/oxidative coupling and post-translational phosphorylation PMID: 23270483 Rich genetic diversity was detected in PKLR, including 59 single-nucleotide polymorphisms and several loss-of-function variants (frequency 1.5%). PMID: 21833022 These results suggest that SARS coronavirus could reduce pyruvate kinase activity via its nucleocapsid protein, and this may in turn cause disease. PMID: 22222284 We identified the pyruvate kinase liver/red cell enzyme gene mutation of 8 children previously diagnosed with pyruvate kinase deficiency who were living in a remote town in the western United States PMID: 21784452 The results reveal an acetylation regulation of pyruvate kinase and the link between lysine acetylation and chaperone-mediated autophagy. PMID: 21700219 Studies indicate that switching from pyruvate kinase spliced isoform PKM1 to PKM2 promotes aerobic glycolysis and provides a selective advantage for tumor formation, and the alternative splicing is controlled by hnRNP family members. PMID: 20978194 Expression of pAkt, GLUT1 and TKTL1 were higher in breast cancer and DCIS than in normal tissue. Surprisingly, M2PK expression was highest in normal breast tissue. PMID: 19655166 Erythrocyte pyruvate kinase was modified with bromopyruvate and the kinetic behavior of the modified enzyme was investigated as model for the mutant enzyme associated with nonspherocytic hemolytic anemia. PMID: 11916152 first crystal structure of recombinant erythrocyte pyruvate kinase and the biochemical characterization of eight mutants found in nonspherocytic hemolytic anemia patients PMID: 11960989 PKLR- GBA region shows almost complete linkage disequilibrium over 70 kb in a set of worldwide populations. PMID: 12107439 Liver pyruvate kinase polymorphisms are associated with type 2 diabetes in northern European Caucasians. PMID: 12196482 regulatory element is a necessary transcriptional regulatory element in the erythroid-specific promoter of the human pyruvate kinase gene PMID: 15727904 The current work exploits a 'natural screen'- the 122 point mutations identified in the human gene encoding the erythrocyte PYK isozyme and associated with nonspherocytic hemolytic anemia. PMID: 16540430 genotype-phenotype association in pyruvate kinase deficiency [review] PMID: 17360088 Northern Ireland has uncovered 4 new cases of pyruvate kinase deficiency. Molecular investigation revealed a total of six different mutations PMID: 17574881 14 different mutations in the coding sequence of the R-PK gene in 74 Iranian individuals with low enzyme activity were identified; the most common were the G1168A and G1529A mutations at exon 11 occurring in 54% of the cases PMID: 17977029 pyruvate kinase deficiency provides protection against infection and replication of P. falciparum in human erythrocytes, raising the possibility that mutant pyruvate kinase alleles may confer a protective advantage against malaria in human populations PMID: 18420493 Pyruvate kinase deficiency protects against malaria in humans PMID: 18460648 The investigators identified a patient with pyruvate kinase deficiency caused by a mutation in the PK-LR gene. PMID: 18683378 identified the -148C>T mutation in the erythroidspecific promoter of PKLR in 3 unrelated patients with low PK activity PMID: 18698090 pyruvate kinase gene mutations are associated with anemia in pyruvate kinase deficient patients. PMID: 18726918 This is the first study to correlate the clinical profile with the molecular defects causing PK deficiency from India where 10 novel mutations that produce non-spherocytic haemolytic anaemia were identified. PMID: 18759866 Data report novel alterations of enzymescinvolved in glucose metabolism, including pyruvate kinase, that may be associated with the pathophysiology of insulin resistance and of renal damage in patients with type 1 diabetes mellitus with nephropathy. PMID: 18840520 Results provided a rationale for the observed enzyme deficiency and contribute to both a better understanding of the genotype-to-phenotype correlation in PK deficiency as well as the enzyme's structure and function. PMID: 19085939 We failed to provide evidence of an association between PKLR rs3020781 and type 2 diabetes, overweight, obesity or related quantitative metabolic phenotypes in large-scale studies of Danes PMID: 19111066 Results are consistent with a mechanism by which phosphorylation at L-PYK Ser12 interrupts an activating interaction of N-terminal residues (including those at positions 7-10) with the main body of the protein, as a means of inhibiting substrate affinity PMID: 19320443 Decreased pyruvate kinase M2 expression to oxaliplatin resistance in patients with colorectal cancer. PMID: 19372549 These data suggest that reduced erythrocyte ATP levels may contribute to the malaria protection displayed by pyruvate kinase deficient erythrocytes in vitro. PMID: 19743919

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Proteins are sensitive to heat, and freeze-drying can preserve the activity of the majority of proteins. It improves protein stability, extends storage time, and reduces shipping costs. However, freeze-drying can also lead to the loss of the active portion of the protein and cause aggregation and denaturation issues. Nonetheless, these adverse effects can be minimized by incorporating protective agents such as stabilizers, additives, and excipients, and by carefully controlling various lyophilization conditions.

Commonly used protectant include saccharides, polyols, polymers, surfactants, some proteins and amino acids etc. We usually add 8% (mass ratio by volume) of trehalose and mannitol as lyoprotectant. Trehalose can significantly prevent the alter of the protein secondary structure, the extension and aggregation of proteins during freeze-drying process; mannitol is also a universal applied protectant and fillers, which can reduce the aggregation of certain proteins after lyophilization.

Our protein products do not contain carrier protein or other additives (such as bovine serum albumin (BSA), human serum albumin (HSA) and sucrose, etc., and when lyophilized with the solution with the lowest salt content, they often cannot form A white grid structure, but a small amount of protein is deposited in the tube during the freeze-drying process, forming a thin or invisible transparent protein layer.

Reminder: Before opening the tube cap, we recommend that you quickly centrifuge for 20-30 seconds in a small centrifuge, so that the protein attached to the tube cap or the tube wall can be aggregated at the bottom of the tube. Our quality control procedures ensure that each tube contains the correct amount of protein, and although sometimes you can't see the protein powder, the amount of protein in the tube is still very precise.

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