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Requires Ca2+ and calmodulin for activity. The enzyme phosphorylates a specific serine residue in each of the subunits of the dimeric phosphorylase b. For muscle phosphorylase but not liver phosphorylase, this is accompaniedby a further dimerization to form a tetrameric phosphorylase. The enzyme couples muscle contraction with energy production via glycogenolysis-glycolysis by catalysing the Ca2+-dependent phosphorylation and activation of glycogen phosphorylase b. The γ subunit of the tetramericenzyme is the catalytic subunit. Group: Enzymes. Synonyms: dephosphophosphorylase kinase; glycogen phosphorylase kinase; PHK; phosphorylase b kinase; phosphorylase B kinase; phosphorylase kinase (phosphorylating); STK17. Enzyme Commission Number: EC 2.7.11.19. CAS No. 9001-88-1. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-3138; phosphorylase kinase; EC 2.7.11.19; 9001-88-1; dephosphophosphorylase kinase; glycogen phosphorylase kinase; PHK; phosphorylase b kinase; phosphorylase B kinase; phosphorylase kinase (phosphorylating); STK17. Cat No: EXWM-3138.
Phosphorylase kinase
Phosphorylase kinase (PhK) is a biochemical reagent that can be used as a biological material or organic compound for life science related research. Uses: Scientific research. Group: Signaling pathways. Alternative Names: PhK. CAS No. 9001-88-1. Pack Sizes: 500 U; 1000 U. Product ID: HY-P2757.
Phosphorylase Kinase β-Subunit Fragment 420-436
It is the β-subunit fragment (peptide 430-436) of phosphorylase kinase. Phosphokinase is a serine/threonine specific protein kinase that activates glycogen phosphorylase to release glucose-1-phosphate from glycogen. Synonyms: Lys-Arg-Asn-Pro-Gly-Ser-Gln-Lys-Arg-Phe-Pro-Ser-Asn-Cys-Gly-Arg-Asp; L-lysyl-L-arginyl-L-asparagyl-L-prolyl-glycyl-L-seryl-L-glutaminyl-L-lysyl-L-arginyl-L-phenylalanyl-L-prolyl-L-seryl-L-asparagyl-L-cysteinyl-glycyl-L-arginyl-L-aspartic acid; Phosphorylase Kinase b-Subunit Fragment (420-436). Grades: ≥95%. CAS No. 150829-21-3. Molecular formula: C79H131N31O25S. Mole weight: 1947.14.
Native Rabbit Phosphorylase Kinase
Phosphorylase kinase (PhK) is a serine/threonine-specific protein kinase which activates glycogen phosphorylase to release glucose-1-phosphate from glycogen. PhK phosphorylates glycogen phosphorylase at two serine residues, triggering a conformational shift which favors the more active glycogen phosphorylase a form over the less active glycogen phosphorylase b. Phosphorylase kinase contains four subunits each containing an α, β, γ, and creative enzymes component. the creative enzymes component binds 4 calcium molecules and is termed calmodulin while the γ unit acts as the catalytic subunit. Applications: Phosphorylase kinase from rabbit muscle has be...osphorylase kinase; glycogen phosphorylase kinase; PHK; phosphorylase b kinase; phosphorylase B kinase; phosphorylase kinase (phosphorylating); STK17; EC 2.7.11.19; EC 2.7.1.38; 9001-88-1. Enzyme Commission Number: EC 2.7.1.38. CAS No. 9001-88-1. PHK. Activity: > 60 units/mg protein. Storage: -20°C. Form: Lyophilized powder containing (NH4)2SO4, sucrose, β-glycerophosphate and dithioerythritol. Source: Rabbit muscle. Species: Rabbit. Phosphorylase Kinase; dephosphophosphorylase kinase; glycogen phosphorylase kinase; PHK; phosphorylase b kinase; phosphorylase B kinase; phosphorylase kinase (phosphorylating); STK17; EC 2.7.11.19; EC 2.7.1.38; 9001-88-1. Cat No: NATE-0559.
5-(2-Furanyl)-2-deoxyuridine
Several novel 5-substituted 2'-deoxyuridine (dUrd) analogs were evaluated as substrates for highly purified herpes simplex virus type 1 (HSV-1)-encoded thymidine kinase (TK) derived from HSV-1 TK gene-transfected murine mammary carcinoma FM3A cells, and human platelet thymidine (dThd) phosphorylase. Group: Biochemicals. Alternative Names: 2'-Deoxy-5-(2-furanyl)uridine. Grades: Highly Purified. CAS No. 92233-50-6. Pack Sizes: 50mg. US Biological Life Sciences.
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5-Iodotubercidin
5-Iodotubercidin (NSC 113939), an ATP mimetic, is a potent adenosine kinase inhibitor with an IC 50 of 26 nM. 5-Iodotubercidin (NSC 113939) initiates glycogen synthesis in isolated hepatocytes by causing inactivation of phosphorylase and activation of glycogen synthase. 5-Iodotubercidin (NSC 113939) also inhibits CK1, insulin receptor tyrosine kinase, phosphorylase kinase, PKA, CK2, PKC and Haspin [1] [2] [3]. Uses: Scientific research. Group: Signaling pathways. Alternative Names: NSC 113939; 5-ITu. CAS No. 24386-93-4. Pack Sizes: 10 mM * 1 mL; 2 mg; 5 mg; 25 mg; 50 mg. Product ID: HY-15424.
5-(Trimethylstannyl)-2'-deoxyuridine
Several novel 5-substituted 2'-deoxyuridine analogs were evaluated as substrates for highly purified herpes simplex virus type 1 (HSV-1)-encoded thymidine kinase (TK), which derived from HSV-1 TK gene-transfected murine mammary carcinoma FM3A cells, and human platelet thymidine (dThd) phosphorylase. Uses: Several novel 5-substituted 2'-deoxyuridine (durd) analogs were evaluated as substrates for highly purified herpes simplex virus type 1 (hsv-1)-encoded thymidine kinase (tk) derived from hsv-1 tk gene-transfected murine mammary carcinoma fm3a cells, and h. Synonyms: 2'-Deoxy-5-(trimethylstannyl)uridine. Grades: 97%. CAS No. 146629-34-7. Molecular formula: C12H20N2O5Sn. Mole weight: 391.01.
7-Oxo staurosporine
7-Oxo staurosporine is an antibiotic originally isolated from S. platensis with diverse biological activites. It inhibits PKC, PKA, phosphorylase kinase, EGFR, and c-Src in vitro (IC50s = 9, 26, 5, 200, and 800 nM, respectively). Synonyms: BMY 41950; RK-1409; 7-oxostaurosporine. Grades: ≥98%. CAS No. 125035-83-8. Molecular formula: C28H24N4O4. Mole weight: 480.5.
[acetyl-CoA carboxylase] kinase
Phosphorylates and inactivates EC 6.4.1.2, acetyl-CoA carboxylase, which can be dephosphorylated and reactivated by EC 3.1.3.17, [phosphorylase] phosphatase. The enzyme is more active towards the dimeric form of acetyl-CoA carboxylase than the polymeric form. Phosphorylates serine residues. Group: Enzymes. Synonyms: acetyl coenzyme A carboxylase kinase (phosphorylating); acetyl-CoA carboxylase bound kinase; acetyl-CoA carboxylase kinase; acetyl-CoA carboxylase kinase (cAMP-independent); acetyl-CoA carboxylase kinase 2; acetyl-CoA carboxylase kinase-2; acetyl-CoA carboxylase kinase-3 (AMP-activated); acetyl-coenzyme A carboxylase kinase; ACK2; ACK3; AMPK; I-peptide kinase; STK5. Enzyme Commission Number: EC 2.7.11.27. CAS No. 77000-06-7. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-3147; [acetyl-CoA carboxylase] kinase; EC 2.7.11.27; 77000-06-7; acetyl coenzyme A carboxylase kinase (phosphorylating); acetyl-CoA carboxylase bound kinase; acetyl-CoA carboxylase kinase; acetyl-CoA carboxylase kinase (cAMP-independent); acetyl-CoA carboxylase kinase 2; acetyl-CoA carboxylase kinase-2; acetyl-CoA carboxylase kinase-3 (AMP-activated); acetyl-coenzyme A carboxylase kinase; ACK2; ACK3; AMPK; I-peptide kinase; STK5. Cat No: EXWM-3147.
k-252a
K-252a, a staurosporine analog, inhibits protein kinase, with IC50 values of 470 nM, 140 nM, 270 nM, and 1.7 nM for PKC, PKA, Ca2+/calmodulin-dependent kinase type II, and phosphorylase kinase, respectively. K-252a is a potent inhibitor (IC50 of 3 nM) of the tyrosine protein kinase (TRK) activity of the NGF receptor gp140trk, the product of the trk protooncogene. Uses: Designed for use in research and industrial production. Product Category: Inhibitors. CAS No. 99533-80-9. Molecular formula: C27H21N3O5. Mole weight: 467.47. Purity: >98 %. Product ID: ACM99533809. Alfa Chemistry ISO 9001:2015 Certified. Categories: K252a.
K-252a
K-252a is an antibiotic, PKC, PKA and PKG inhibitor. Shows neurotropic activity by inducing neurite outgrowth. Highly potent cell permeable CaM kinase and phosphorylase inhibitor. Tyrosine protein kinase inhibitor of the TRK family. Antiproliferative and apoptosis inducer. Cell cycle arrest inducer. Potential drug for psoriasis treatment. Source:Isolated from Nonomuraea longicatena chiba. Group: Biochemicals. Grades: Highly Purified. CAS No. 99533-80-9. Pack Sizes: 100ug, 1mg. Molecular Formula: C27H21N3O5. US Biological Life Sciences.
Worldwide
λ Protein phosphatase
λ Protein phosphatase is a serine/threonine phosphatase encoded by bacteriophage Lambda. λ Protein phosphatase is activated with requirement for divalent cations, such as Mn 2+. λ Protein phosphatase is able to dephosphorylate casein, adenovirus E1A protein, and the α subunit of phosphorylase kinase [1]. Uses: Scientific research. Group: Signaling pathways. CAS No. 401941-75-1. Pack Sizes: 10 KU. Product ID: HY-E70373.
Malantide
Malantide, a highly specific substrate for PKA, is a synthetic dodecapeptide derived from the site phosphorylated by cAMP-dependent protein kinase (PKA) on the β-subunit of phosphorylase kinase. Synonyms: H-Arg-Thr-Lys-Arg-Ser-Gly-Ser-Val-Tyr-Glu-Pro-Leu-Lys-Ile-OH; L-arginyl-L-threonyl-L-lysyl-L-arginyl-L-seryl-glycyl-L-seryl-L-valyl-L-tyrosyl-L-alpha-glutamyl-L-prolyl-L-leucyl-L-lysyl-L-isoleucine. Grades: ≥95%. CAS No. 86555-35-3. Molecular formula: C72H124N22O21. Mole weight: 1633.89.
Malantide acetate
Malantide acetate, a highly specific substrate for PKA, is a synthetic dodecapeptide derived from the site phosphorylated by cAMP-dependent protein kinase (PKA) on the β-subunit of phosphorylase kinase. Synonyms: H-Arg-Thr-Lys-Arg-Ser-Gly-Ser-Val-Tyr-Glu-Pro-Leu-Lys-Ile-OH.CH3CO2H; L-arginyl-L-threonyl-L-lysyl-L-arginyl-L-seryl-glycyl-L-seryl-L-valyl-L-tyrosyl-L-alpha-glutamyl-L-prolyl-L-leucyl-L-lysyl-L-isoleucine acetic acid. Grades: ≥95%. Molecular formula: C74H128N22O23. Mole weight: 1693.97.
Native Rabbit Phosphorylase a
Phosphorylase A is the active form of glycogen phosphorylase which converts glycogen and orthophosphate (Pi) to glucose 1-phoshate (G-1-P). Phosphorylase A can be inhibited by these compounds:Polychlorinated biphenyls, polychlorinated biphenylols and polybrominated biphenyls. Dimeric phosphorylase b is converted to the more active tetramer, phosphorylase a, by the action of phosphorylase kinase. Phosphorylase a is the active form of glycogen phosphorylase which converts glycogen and orthophosphate (pi) to glucose 1-phoshate (g-1-p). Applications: Phosphorylase from rabbit muscle has been used in a study to assess the molecular mechanisms of oleanolic acid. it has also been use...mission Number: EC 2.4.1.1. CAS No. 9035-74-9. Purity: 2× crystallization. GPBB. Activity: 20-30 units/mg protein. Storage: -20°C. Form: Lyophilized powder containing β-glycerophosphate and EDTA. Source: Rabbit muscle. Species: Rabbit. Phosphorylase a; EC 2.4.1.1; 9032-10-4; muscle phosphorylase a and b; amylophosphorylase; polyphosphorylase; amylopectin phosphorylase; glucan phosphorylase; α-glucan phosphorylase; 1,4-α-glucan phosphorylase; glucosan phosphorylase; granulose phosphorylase; maltodextrin phosphorylase; muscle phosphorylase; myophosphorylase; potato phosphorylase; starch phosphorylase; 1,4-α-D-glucan:phosphate α-D-glucosyltransferase;
Native Rabbit Phosphorylase b
Phosphorylase b is a non-active form and is present in resting muscle. Phosphorylase b kinase activity increases significantly when the Mg2+:ATP ratio exceeds. The breakdown of ATP during muscle contraction is thought to trigger in vivo conversion of phosphorylase b into a. Phosphorylase b is activated by inosine monophosphate. Applications: Phosphorylase b is used to study the conversion mechanism of inactive phosphorylase b to active phosphorylase in muscle. phosphorylase b is used to study which factors influence the conversion of phosphorylase b to phosphorylase a such as temperature, amp, fluoride and detergents. it is used to study phosphorylase b deficiency mutations. t...α-glucan phosphorylase; 1,4-α-glucan phosphorylase; glucosan phosphorylase; granulose phosphorylase; maltodextrin phosphorylase; muscle phosphorylase; myophosphorylase; potato phosphorylase; starch phosphorylase; 1,4-α-D-glucan:phosphate α-D-glucosyltransferase; phosphorylase (ambiguous). Enzyme Commission Number: EC 2.4.1.1. CAS No. 9012-69-5. Purity: 2× crystallization. GPBB. Mole weight: mol wt 97.2 kDa by calculation. Activity: Type I, > 20 units/mg protein; Type II, > 7 units/mg. Storage: -20°C. Form: Type I, Lyophilized powder containing lactose, 5?-AMP, and Mg (OAc)2 (10 μmole per 100 mg protein); Type II, lyophilized powder, light yellow. Sour
non-specific serine/threonine protein kinase
This is a heterogeneous group of serine/threonine protein kinases that do not have an activating compound and are either non-specific or their specificity has not been analysed to date. Group: Enzymes. Synonyms: A-kinase; AP50 kinase; ATP-protein transphosphorylase; calcium-dependent protein kinase C; calcium/phospholipid-dependent protein kinase; cAMP-dependent protein kinase; cAMP-dependent protein kinase A; casein kinase; casein kinase (phosphorylating); casein kinase 2; casein kinase I; casein kinase II; cGMP-dependent protein kinase; CK-2; CKI; CKII; cyclic AMP-dependent protein kinase; cyclic AMP-dependent protein kinase A; cyclic monophosphate-dependent protein kinase; cyclic nucleotide-dependent protein kinase; cyclin-dependent kinase; cytidine 3',5'-cyclic monophosphate-responsive protein kinase; dsk1; glycogen synthase a kinase; glycogen synthase kinase; HIPK2; Hpr kinase; hydroxyalkyl-protein kinase; hydroxyalkyl-protein kinase; M phase-specific cdc2 kinase; mitogen-activated S6 kinase; p82 kinase; phosphorylase b kinase kinase; PKA; protein glutamyl kinase; pr. Enzyme Commission Number: EC 2.7.11.1. STK. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-3128; non-specific serine/threonine protein kinase; EC 2.7.11.1; A-kinase; AP50 kinase;
ornithine carbamoyltransferase
The plant enzyme also catalyses the reactions of EC 2.1.3.6 putrescine carbamoyltransferase, EC 2.7.2.2 carbamate kinase and EC 3.5.3.12 agmatine deiminase, thus acting as putrescine synthase, converting agmatine [(4-aminobutyl)guanidine] and ornithine into putrescine and citrulline, respectively. Group: Enzymes. Synonyms: citrulline phosphorylase; ornithine transcarbamylase; OTC; carbamylphosphate-ornithine transcarbamylase; L-ornithine carbamoyltransferase; L-ornithine carbamyltransferase; L-ornithine transcarbamylase; ornithine carbamyltransferase. Enzyme Commission Number: EC 2.1.3.3. CAS No. 9001-69-8. OTC. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-2016; ornithine carbamoyltransferase; EC 2.1.3.3; 9001-69-8; citrulline phosphorylase; ornithine transcarbamylase; OTC; carbamylphosphate-ornithine transcarbamylase; L-ornithine carbamoyltransferase; L-ornithine carbamyltransferase; L-ornithine transcarbamylase; ornithine carbamyltransferase. Cat No: EXWM-2016.
pdGp
pdGp, also known as pyruvate dehydrogenase kinase, is a remarkably efficacious and highly targeted inhibitor of the glycogen phosphorylase (Gp). Synonyms: 2'- Deoxyguanosine- 3', 5'- O- bisphosphate, sodium salt. Grades: ≥ 95% by HPLC. CAS No. 16174-59-7. Molecular formula: C10H15N5O10P2. Mole weight: 427.2.
Phosphatase from Escherichia coli, Recombinant
A phosphatase is an enzyme that removes a phosphate group from its substrate by hydrolysing phosphoric acid monoesters into a phosphate ion and a molecule with a free hydroxyl group (see dephosphorylation). This action is directly opposite to that of phosphorylases and kinases, which attach phosphate groups to their substrates by using energetic molecules like ATP. A common phosphatase in many organisms is alkaline phosphatase. Another large group of proteins present in archaea, bacteria, and eukaryote exhibits deoxyribonucleotide and ribonucleotide phosphatase or pyrophosphatase activities that catalyse the decomposition of dNTP/NTP into dNDP/NDP and a free phosphate ... phosphatase is collectively called as protein phosphatase, which removes a phosphate group from the phosphorylated amino acid residue of the substrate protein. Protein phosphorylation is a common posttranslational modification of protein catalyzed by protein kinases, and protein phosphatases reverse the effect. Group: Enzymes. Synonyms: HAD2. Enzyme Commission Number: EC 3.1.3.-. Purity: >95 % as judged by SDS-PAGE. Phosphatase. Mole weight: 26827.7 Da. Activity: 1.905 U/mg. Storage: Store at 4°C (shipped at room temperature). Form: Supplied in 3.2 M ammonium sulphate. Source: Escherichia coli str. K-12 substr. MG1655. Phosphatase; HAD2; EC 3.1.3.-. Cat No: NATE-1226.
Staurosporin
Staurosporine is an alkaloid isolated from the culture broth of Streptomyces staurospores and is a super-potent, cell permeable PKC inhibitor (IC50=0.7); at higher concentrations Staurosporine inhibits other protein kinases: CDK2/cyclin A (IC50=7uM) and CDK4/cyclin D (IC50=3-10uM). At a concentration of 50-100nM it is a functional neurotrophins agonist promoting neurite outgrowth in neuroblastoma, pheochromocytoma and brain primary neuronal cultures. Staurosporine inhibits a variety of kinases including PKA, PKG, MLCK, CaMK, tyrosine kinases, and phosphorylase kinase. This compound displays selectivity toward the PKC isoforms, inhibiting PKCα, PKC β, PKCγ, PKCδ, and PKCε, but not PKC?, and induces PKC translocation. Staurosporine also inhibits topoisomerase II directly by interaction with the ATP binding site, augments PMA-induced ornithine decarboxylase, and activates a bcl-2-regulated apoptosis pathway. Source:Streptomyces staurosporeus. Group: Biochemicals. Alternative Names: Antibiotic AM2282; Antibiotic 230; CCRIS 3272. Grades: Highly Purified. CAS No. 62996-74-1. Pack Sizes: 100ug, 1mg, 5mg, 10mg. Molecular Formula: C28H26N4O3, Molecular Weight: 466.53. US Biological Life Sciences.
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