Pyruvate Kinase PKLR (PKLR) Human Recombinant Protein

MBS718656 is a recombinant protein targeting PKLR. Also known as Recombinant Human Pyruvate kinase PKLR. Host: E Coli or Yeast or Baculovirus or Mammalian Cell. Plays a key role in glycolysis.

cDNA cloning of human R-type pyruvate kinase and identification of a single amino acid substitution (Thr384-->Met) affecting enzymatic stability in a pyruvate kinase variant (PK Tokyo) associated with hereditary hemolytic anemia.Kanno H., Fujii H., Hirono A., Miwa S.Proc. Natl. Acad. Sci. U.S.A. 88:8218-8221(1991) Human liver type pyruvate kinase complete amino acid sequence and the expression in mammalian cells.Tani K., Fujii H., Nagata S., Miwa S.Proc. Natl. Acad. Sci. U.S.A. 85:1792-1795(1988) Kanno H.Structural analysis of human pyruvate kinase L-gene and identification of the promoter activity in erythroid cells.Kanno H., Fujii H., Miwa S.Biochem. Biophys. Res. Commun. 188:516-523(1992) NIEHS SNPs program Human liver type pyruvate kinase cDNA cloning and chromosomal assignment.Tani K., Fujii H., Tsutsumi H., Sukegawa J., Toyoshima K., Yoshida M.C., Noguchi T., Tanaka T., Miwa S.Biochem. Biophys. Res. Commun. 143:431-438(1987) Molecular basis of impaired pyruvate kinase isozyme conversion in erythroid cells a single amino acid substitution near the active site and decreased mRNA content of the R-type PK.Kanno H., Fujii H., Tsujino G., Miwa S.Biochem. Biophys. Res. Commun. 192:46-52(1993) Mutations in pyruvate kinase.Beutler E., Baronciani L.3.0.CO;2-H>Hum. Mutat. 7:1-6(1996) Hematologically important mutations red cell pyruvate kinase.Baronciani L., Bianchi P., Zanella A.Blood Cells Mol. Dis. 22:85-89(1996) Hematologically important mutations red cell pyruvate kinase (1st update) .Baronciani L., Bianchi P., Zanella A.Blood Cells Mol. Dis. 22:259-264(1996) Hematologically important mutations red cell pyruvate kinase (2nd update) .Baronciani L., Bianchi P., Zanella A.Blood Cells Mol. Dis. 24:273-279(1998) Hematologically important mutations red cell pyruvate kinase (third update) .Bianchi P., Zanella A.Blood Cells Mol. Dis. 26:47-53(2000) Initial characterization of the human central proteome.Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.BMC Syst. Biol. 5:17-17(2011) An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome.Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.J. Proteomics 96:253-262(2014) Structure and function of human erythrocyte pyruvate kinase. Molecular basis of nonspherocytic hemolytic anemia.Valentini G., Chiarelli L.R., Fortin R., Dolzan M., Galizzi A., Abraham D.J., Wang C., Bianchi P., Zanella A., Mattevi A.J. Biol. Chem. 277:23807-23814(2002) Point mutations in the L-type pyruvate kinase gene of two children with hemolytic anemia caused by pyruvate kinase deficiency.Neubauer B., Lakomek M., Winkler H., Parke M., Hofferbert S., Schroter W.Blood 77:1871-1875(1991) Identical point mutations of the R-type pyruvate kinase (PK) cDNA found in unrelated PK variants associated with hereditary hemolytic anemia.Kanno H., Fujii H., Hirono A., Omine M., Miwa S.Blood 79:1347-1350(1992) Low substrate affinity of pyruvate kinase variant (PK Sapporo) caused by a single amino acid substitution (426 Arg-->Gln) associated with hereditary hemolytic anemia.Kanno H., Fujii H., Miwa S.Blood 81:2439-2441(1993) Analysis of pyruvate kinase-deficiency mutations that produce nonspherocytic hemolytic anemia.Baronciani L., Beutler E.Proc. Natl. Acad. Sci. U.S.A. 90:4324-4327(1993) Molecular abnormality of erythrocyte pyruvate kinase deficiency in the Amish.Kanno H., Ballas S.K., Miwa S., Fujii H., Bowman H.S.Blood 83:2311-2316(1994) Mutations in the pyruvate kinase L gene in patients with hereditary hemolytic anemia.Lenzner C., Nuernberg P., Thiele B.-J., Reis A., Brabec V., Sakalova A., Jacobasch G.Blood 83:2817-2822(1994) Molecular study of pyruvate kinase deficient patients with hereditary nonspherocytic hemolytic anemia.Baronciani L., Beutler E.J. Clin. Invest. 95:1702-1709(1995) Study of the molecular defects in pyruvate kinase (PK) deficient patients affected by hereditary nonspherocytic hemolytic anemia (HNHA) .Baronciani L., Westwood B., Beutler E.J. Invest. Med. 43:341A-341A(1995) G-to-T transition at cDNA nt 110 (K37Q) in the PKLR (pyruvate kinase) gene is the molecular basis of a case of hereditary increase of red blood cell ATP.Beutler E., Westwood B., van Zwieten R., Roos D.3.0.CO;2-Z>Hum. Mutat. 9:282-285(1997) Molecular characterization of the PK-LR gene in pyruvate kinase deficient Spanish patients.Zarza R., Alvarez R., Pujades A., Nomdedeu B., Carrera A., Estella J., Remacha A., Sanchez J.M., Morey M., Cortes T., Perez Lungmus G., Bureo E., Vives Corrons J.L.Br. J. Haematol. 103:377-382(1998) A new sickle cell disease phenotype associating Hb S trait, severe pyruvate kinase deficiency (PK Conakry) , and an alpha-2 globin gene variant (Hb Conakry) .Cohen-Solal M., Prehu C., Wajcman H., Poyart C., Bardakdjian-Michau J., Kister J., Prome D., Valentin C., Bachir D., Galacteros F.Br. J. Haematol. 103:950-956(1998) Novel mutations and structural implications in R-type pyruvate kinase-deficient patients from Southern Italy.Pastore L., della Morte R., Frisso G., Alfinito F., Vitale D., Calise R.M., Ferraro F., Zagari A., Rotoli B., Salvatore F.3.0.CO;2-G>Hum. Mutat. 11:127-134(1998) Molecular characterization of the PK-LR gene in sixteen pyruvate kinase-deficient patients.Zanella A., Bianchi P., Fermo E., Iurlo A., Zappa M., Vercellati C., Boschetti C., Baronciani L., Cotton F.Br. J. Haematol. 113:43-48(2001) Fifteen novel mutations in PKLR associated with pyruvate kinase (PK) deficiency structural implications of amino acid substitutions in PK.van Wijk R., Huizinga E.G., van Wesel A.C.W., van Oirschot B.A., Hadders M.A., van Solinge W.W.Hum. Mutat. 30:446-453(2009) Exome sequencing and unrelated findings in the context of complex disease research ethical and clinical implications.Lyon G.J., Jiang T., Van Wijk R., Wang W., Bodily P.M., Xing J., Tian L., Robison R.J., Clement M., Lin Y., Zhang P., Liu Y., Moore B., Glessner J.T., Elia J., Reimherr F., van Solinge W.W., Yandell M., Hakonarson H., Wang J., Johnson W.E., Wei Z., Wang K.Discov. Med. 12:41-55(2011)

Small volumes of PKLR recombinant protein vial(s) may occasionally become entrapped in the seal of the product vial during shipment and storage. If necessary, briefly centrifuge the vial on a tabletop centrifuge to dislodge any liquid in the container`s cap. Certain products may require to ship with dry ice and additional dry ice fee may apply.