protein

Recombinant Human Glycogen phosphorylase, liver form

MBS952730

0.05 mg (E-Coli)

190 USD

Recombinant Protein

Recombinant Human Glycogen phosphorylase, liver form

Glycogen phosphorylase

glycogen phosphorylase, liver form isoform 2; Glycogen phosphorylase, liver form; glycogen phosphorylase, liver form; phosphorylase, glycogen, liver

PYGL

PYGL; PYGL; GSD6

PYGL_HUMAN

E Coli or Yeast or Baculovirus or Mammalian Cell

2-846

813

AKPLTDQEKRRQISIRGIVGVENVAELKKSFNRHLHFTL
VKDRNVATTRDYYFALAHTVRDHLVGRWIRTQQHYYDKC
PKRVYYLSLEFYMGRTLQNTMINLGLQNACDEAIYQLGL
DIEELEEIEEDAGLGNGGLGRLAACFLDSMATLGLAAYG
YGIRYEYGIFNQKIRDGWQVEEADDWLRYGNPWEKSRPE
FMLPVHFYGKVEHTNTGTKWIDTQVVLALPYDTPVPGYM
NNTVNTMRLWSARAPNDFNLR

Greater than 90% as determined by SDS-PAGE.

Liquid containing glycerol; lyophilization may be available upon request.

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

Metabolism

Phosphorylase is an important allosteric enzyme in carbohydrate metabolism. Enzymes from different sources differ in their regulatory mechanisms and in their natural substrates. However, all known phosphorylases share catalytic and structural properties.

Sequence analysis of the cDNA encoding human liver glycogen phosphorylase reveals tissue-specific codon usage.Newgard C.B., Nakano K., Hwang P.K., Fletterick R.J.Proc. Natl. Acad. Sci. U.S.A. 83:8132-8136(1986) Carty M.D., Clancy Y.C., Soeller W.C. Identification of a mutation in liver glycogen phosphorylase in glycogen storage disease type VI.Chang S., Rosenberg M.J., Morton H., Francomano C.A., Biesecker L.G.Hum. Mol. Genet. 7:865-870(1998) Mutations in the liver glycogen phosphorylase gene 'PYGL' underlying glycogenosis type VI.Burwinkel B., Bakker H.D., Herschkovitz E., Moses S.W., Shin Y.S., Kilimann M.W.Am. J. Hum. Genet. 62:785-791(1998) Complete sequencing and characterization of 21,243 full-length human cDNAs.Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.Nat. Genet. 36:40-45(2004) The DNA sequence and analysis of human chromosome 14.Heilig R., Eckenberg R., Petit J.-L., Fonknechten N., Da Silva C., Cattolico L., Levy M., Barbe V., De Berardinis V., Ureta-Vidal A., Pelletier E., Vico V., Anthouard V., Rowen L., Madan A., Qin S., Sun H., Du H., Pepin K., Artiguenave F., Robert C., Cruaud C., Bruels T., Jaillon O., Friedlander L., Samson G., Brottier P., Cure S., Segurens B., Aniere F., Samain S., Crespeau H., Abbasi N., Aiach N., Boscus D., Dickhoff R., Dors M., Dubois I., Friedman C., Gouyvenoux M., James R., Madan A., Mairey-Estrada B., Mangenot S., Martins N., Menard M., Oztas S., Ratcliffe A., Shaffer T., Trask B., Vacherie B., Bellemere C., Belser C., Besnard-Gonnet M., Bartol-Mavel D., Boutard M., Briez-Silla S., Combette S., Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C., Muselet D., Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P., Trybou A., Vega-Czarny N., Bataille E., Bluet E., Bordelais I., Dubois M., Dumont C., Guerin T., Haffray S., Hammadi R., Muanga J., Pellouin V., Robert D., Wunderle E., Gauguet G., Roy A., Sainte-Marthe L., Verdier J., Verdier-Discala C., Hillier L.W., Fulton L., McPherson J., Matsuda F., Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W., Quetier F., Waterston R., Hood L., Weissenbach J.Nature 421:601-607(2003)

255653002

NP_001157412.1

NM_001163940.1

P06737

124.2kD

Glucagon Signaling Pathway (1144996); Glucagon Signaling Pathway (1158201); Glucose Metabolism Pathway (1269959); Glycogen Metabolism Pathway (198856); Glycogen Breakdown (glycogenolysis) Pathway (1269963); Insulin Resistance Pathway (1272486); Insulin Signaling Pathway (83090); Insulin Signaling Pathway (501); Metabolic Pathways (132956); Metabolism Pathway (1269956)

This gene encodes a homodimeric protein that catalyses the cleavage of alpha-1,4-glucosidic bonds to release glucose-1-phosphate from liver glycogen stores. This protein switches from inactive phosphorylase B to active phosphorylase A by phosphorylation of serine residue 15. Activity of this enzyme is further regulated by multiple allosteric effectors and hormonal controls. Humans have three glycogen phosphorylase genes that encode distinct isozymes that are primarily expressed in liver, brain and muscle, respectively. The liver isozyme serves the glycemic demands of the body in general while the brain and muscle isozymes supply just those tissues. In glycogen storage disease type VI, also known as Hers disease, mutations in liver glycogen phosphorylase inhibit the conversion of glycogen to glucose and results in moderate hypoglycemia, mild ketosis, growth retardation and hepatomegaly. Alternative splicing results in multiple transcript variants encoding different isoforms.[provided by RefSeq, Feb 2011]

PYGL: Phosphorylase is an important allosteric enzyme in carbohydrate metabolism. Enzymes from different sources differ in their regulatory mechanisms and in their natural substrates. However, all known phosphorylases share catalytic and structural properties. Defects in PYGL are the cause of glycogen storage disease type 6 (GSD6). A metabolic disorder characterized by mild to moderate hypoglycemia, mild ketosis, growth retardation, and prominent hepatomegaly. Heart and skeletal muscle are not affected. Belongs to the glycogen phosphorylase family. Protein type: Carbohydrate Metabolism - starch and sucrose; EC 2.4.1.1; Transferase. Chromosomal Location of Human Ortholog: 14q21-q22. Cellular Component: cytoplasm; cytosol; plasma membrane. Molecular Function: AMP binding; ATP binding; bile acid binding; drug binding; glucose binding; glycogen phosphorylase activity; protein binding; protein homodimerization activity; purine binding; pyridoxal phosphate binding; vitamin binding. Biological Process: 5-phosphoribose 1-diphosphate biosynthetic process; carbohydrate metabolic process; glucose homeostasis; glucose metabolic process; glycogen catabolic process; glycogen metabolic process. Disease: Glycogen Storage Disease Vi

0.05 mg (E-Coli)

190 USD

0.05 mg (Yeast)

190

0.2 mg (E-Coli)

460

0.2 mg (Yeast)

460

0.5 mg (E-Coli)

750