protein

Recombinant Human Phosphofructokinase, Muscle

MBS144030

0.005 mg

140 USD

Recombinant Protein

Recombinant Human Phosphofructokinase, Muscle

Phosphofructokinase

PFKM Human; Phosphofructokinase, Muscle Human Recombinant; EC 2.7.1.11; GSD7; PFK-1; PFK1; PFKA; PFKX; Phosphofructokinase-M; Phosphofructokinase 1; Phosphohexokinase; Phosphofructo-1-kinase isozyme A; MGC8699; PFKM

ATP-dependent 6-phosphofructokinase, muscle type isoform 2; ATP-dependent 6-phosphofructokinase, muscle type; ATP-dependent 6-phosphofructokinase, muscle type; 6-phosphofructo-1-kinase; 6-phosphofructokinase type A; ATP-PFK; PFK-A; phosphofructo-1-kinase isozyme A; phosphofructokinase 1; phosphofructokinase, polypeptide X; phosphofructokinase-M; phosphohexokinase; protein phosphatase 1, regulatory subunit 122; phosphofructokinase, muscle; 6-phosphofructokinase type APhosphofructo-1-kinase isozyme A

PFKM

PFKM; PFKM; GSD7; PFK1; PFKA; PFKX; PFK-1; ATP-PFK; PPP1R122; ; PFK-M

PFKAM_HUMAN

E Coli

780

MGSSHHHHHH SSGLVPRGSH MTHEEHHAAK TLGIGKAIAV LTSGGDAQGM NAAVRAVVRV GIFTGARVFF VHEGYQGLVD GGDHIKEATW ESVSMMLQLG GTVIGSARCK DFREREGRLR AAYNLVKRGI TNLCVIGGDG SLTGADTFRS EWSDLLSDLQ KAGKITDEEA TKSSYLNIVG LVGSIDNDFC GTDMTIGTDS ALHRIMEIVD AITTTAQSHQ RTFVLEVMGR HCGYLALVTS LSCGADWVFI PECPPDDDWE EHLCRRLSET RTRGSRLNII IVAEGAIDKN GKPITSEDIK NLVVKRLGYD TRVTVLGHVQ RGGTPSAFDR ILGSRMGVEA VMALLEGTPD TPACVVSLSG NQAVRLPLME CVQVTKDVTK AMDEKKFDEA LKLRGRSFMN NWEVYKLLAH VRPPVSKSGS HTVAVMNVGA PAAGMNAAVR STVRIGLIQG NRVLVVHDGF EGLAKGQIEE AGWSYVGGWT GQGGSKLGTK RTLPKKSFEQ ISANITKFNI QGLVIIGGFE AYTGGLELME GRKQFDELCI PFVVIPATVS NNVPGSDFSV GADTALNTIC TTCDRIKQSA AGTKRRVFII ETMGGYCGYL ATMAGLAAGA DAAYIFEEPF TIRDLQANVE HLVQKMKTTV KRGLVLRNEK CNENYTTDFI FNLYSEEGKG IFDSRKNVLG HMQQGGSPTP FDRNFATKMG AKAMNWMSGK IKESYRNGRI FANTPDSGCV LGMRKRALVF QPVAELKDQT DFEHRIPKEQ WWLKLRPILK ILAKYEIDLD TSDHAHLEHI TRKRSGEAAV.

Greater than 80% as determined by SDS-PAGE.

PFKM Human solution (0.5mg/ml) containing 20mM Trsi HCL pH-8, 5mM DTT, 0.2M NaCl and 20% glycerol. Sterile filtered colorless solution.

0.5 mg/ml

PFKM human although stable at 4 degree C for 1 week, should be stored desiccated below -18 degree C. Please prevent freeze thaw cycles.

PROTEIN KINASES; Enzymes; Protein Kinases

Description: PFKM Human Recombinant produced in E Coli is a single, non-glycosylated, polypeptide chain containing 800 amino acids (1-780 a.a.) and having a molecular mass of 87.3 kDa. PFKM protein is fused to a 20 amino acid His-Tag at N-terminus and purified by standard chromatography. Introduction: PFKM is a regulatory glycolytic enzyme that converts fructose 6-phosphate and ATP into fructose 1,6-bisphosphate (through PFK-1), fructose 2,6-bisphosphate (through PFK-2) and ADP. Three phosphofructokinase isozymes exist in humans: muscle, liver and platelet. Mutations in PFKM gene have been related with glycogen storage disease type VII, also identified as Tarui disease.

4505749

NP_000280.1

NM_000289.5

P08237

AMPK Signaling Pathway (989139); AMPK Signaling Pathway (992181); Biosynthesis Of Amino Acids Pathway (790012); Biosynthesis Of Amino Acids Pathway (795174); Carbon Metabolism Pathway (814926); Carbon Metabolism Pathway (817567); Central Carbon Metabolism In Cancer Pathway (1059538); Central Carbon Metabolism In Cancer Pathway (1084231); Disease Pathway (530764); Fructose And Mannose Metabolism Pathway (82930)

Three phosphofructokinase isozymes exist in humans: muscle, liver and platelet. These isozymes function as subunits of the mammalian tetramer phosphofructokinase, which catalyzes the phosphorylation of fructose-6-phosphate to fructose-1,6-bisphosphate. Tetramer composition varies depending on tissue type. This gene encodes the muscle-type isozyme. Mutations in this gene have been associated with glycogen storage disease type VII, also known as Tarui disease. Alternatively spliced transcript variants have been described.[provided by RefSeq, Nov 2009]

PFKM: phosphofructokinase, muscle type. An ubiquitous metabolic enzyme involved in the synthesis and degradation of fructose 2,6-bisphosphate. Key control step of glycolysis. An allosteric enzyme activated by ADP, AMP, or fructose bisphosphate and inhibited by ATP or citrate. Activity: ATP D-fructose 6-phosphate = ADP D-fructose 1,6-bisphosphate. The holoenzyme consists of 4 subunits. The liver and muscle enzymes are homo-tetramers of four liver or muscle isoforms, respectively. The red blood cell enzyme consists hetero-tetramers of the muscle and liver isoforms. A subunit composition with a higher proportion of platelet type subunits is found in platelets, brain and fibroblasts. Defects in PFKM are the cause of glycogen storage disease VII (GSD-VII) also known as Tarui disease. Two alternatively spliced isoforms have been described. Protein type: Carbohydrate Metabolism - glycolysis and gluconeogenesis; Carbohydrate Metabolism - galactose; Carbohydrate Metabolism - fructose and mannose; Kinase, other; Carbohydrate Metabolism - pentose phosphate pathway; EC 2.7.1.11. Chromosomal Location of Human Ortholog: 12q13.3. Cellular Component: 6-phosphofructokinase complex; apical plasma membrane; cytosol. Molecular Function: protein C-terminus binding; identical protein binding; protein binding; protein homodimerization activity; metal ion binding; kinase binding; ATP binding; 6-phosphofructokinase activity. Biological Process: muscle maintenance; glycolysis; carbohydrate metabolic process; carbohydrate phosphorylation; glucose metabolic process; positive regulation of insulin secretion; pathogenesis; fructose 6-phosphate metabolic process; glucose homeostasis; protein oligomerization. Disease: Glycogen Storage Disease Vii

0.005 mg

140 USD

0.02 mg

205

1 mg

3490