目录号 | 产品详情 | 靶点 | |
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T83820 | |||
TNP-GTP是一种荧光衍生物,源自蛋白质合成与糖异生的能量底物鸟苷三磷酸(GTP)。其在水中激发波长为410 nm时,发射最大波长为552 nm,而在40%和80%的N,N-二甲基甲酰胺中,其荧光强度增加,发射波长分别向544 nm和532 nm移动,这是因为N,N-二甲基甲酰胺的极性比水小。TNP-GTP是谷氨酸脱氢酶的抑制剂(Ki = 2.7 μM)。当与谷氨酸脱氢酶结合时,TNP-GTP的荧光强度增加,且发射波长从552 nm变为545 nm,此效果可以通过加入GTP来阻断。TNP-GTP还是嘌呤P2X2和P2X2/3受体的拮抗剂(IC50s分别为0.4和1.2 nM)。它还选择性抑制大鼠可溶性鸟苷酸环化酶(sGC; Ki = 11 nM)高于牛肝谷氨酸脱氢酶(GDH; Ki = 2.7 µM)以及钙调素依赖的B. pertussis腺苷酸环化酶(AC)毒素(Kis在存在锰或镁时分别为20和320 µM)。 | |||
T83726 | |||
Tat-βsyn-degron是一种降低α-synuclein表达的肽。其结构包括HIV-1 Tat质膜跨导域、与β-synuclein氨基酸36-45相对应的α-synuclein结合域βsyn,以及蛋白酶体定向域degron。在肽-蛋白结合实验中,Tat-βsyn-degron能够与重组α-synuclein结合,并在大鼠初级皮质神经元培养中降低α-synuclein水平,这一效应可以通过蛋白酶体抑制剂MG132阻止。体内研究显示,Tat-βsyn-degron (40 mg/kg)能够在过表达人类A53T突变体α-synuclein的M38转基因小鼠的大脑中降低α-synuclein水平,并且在黑质和脑桥中降低磷酸化α-synuclein水平,以及在通过α-synuclein预成纤维诱导的扩散性α-synuclein病理模型小鼠中减少神经炎症。此外,Tat-βsyn-degron (6 µmol/kg, i.p.)在MPTP诱导的帕金森病小鼠模型中,保护多巴胺能神经元,缓解运动缺陷。 |
目录号 | 产品名/同用名 | 种属 | 表达系统 | ||
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TMPY-00382 | Thioredoxin/TRX Protein, Mouse, Recombinant | Mouse | E. coli | ||
Thioredoxin, also known as ATL-derived factor, Surface-associated sulphydryl protein, SASP and TXN, is a nucleus, cytoplasm and secreted protein that belongs to the thioredoxin family. Thioredoxins are proteins that act as antioxidants by facilitating the reduction of other proteins by cysteine thiol-disulfide exchange. Thioredoxins are found in nearly all known organisms and are essential for life in mammals. Thioredoxin / TXN participates in various redox reactions through the reversible oxidation of its active center dithiol to a disulfide and catalyzes dithiol-disulfide exchange reactions. Thioredoxin / TXN plays a role in the reversible S-nitrosylation of cysteine residues in target proteins, and thereby contributes to the response to intracellular nitric oxide. Thioredoxin / TXN nitrosylates the active site Cys of CASP3 in response to nitric oxide (NO), and thereby inhibits caspase-3 activity. Thioredoxin / TXN induces the FOS/JUN AP-1 DNA-binding activity in ionizing radiation (IR) cells through its oxidation/reduction status and stimulates AP-1 transcriptional activity.
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TMPY-02279 | Nucleoside phosphorylase/PNP Protein, Human, Recombinant (His) | Human | E. coli | ||
Purine nucleoside phosphorylase (PNP) is a purine-metabolizing enzyme that catalyzes the reversible phosphorolysis of 6-oxypurine (deoxy)nucleosides to their respective bases and (deoxy)ribose-1-phosphate. It is a key enzyme in the purine salvage pathway of mammalian cells. Purine nucleoside phosphorylase is a transferase that catalyzes the addition of phosphate and removal of a purine base from guanosine and similar nucleosides.PNP defects result in metabolic abnormalities and fatal T cell immunodeficiency. Purine nucleoside phosphorylase (PNP) is a target for leukemia, gout, and autoimmune disorders.
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TMPY-01735 | Carbonic Anhydrase 2 Protein, Human, Recombinant (His) | Human | E. coli | ||
The carbonic anhydrases (or carbonate dehydratases) are classified as metalloenzyme for its zinc ion prosthetic group and form a family of enzymes that catalyze the rapid interconversion of carbon dioxide and water to bicarbonate and protons, a reversible reaction that takes part in maintaining acid-base balance in blood and other tissues. The carbonic anhydrasekl (CA) family consists of at least 11 enzymatically active members and a few inactive homologous proteins. Carbonic anhydrase II is one of fourteen forms of human α carbonic anhydrases. Defects in this enzyme are associated with osteopetrosis and renal tubular acidosis. Renal carbonic anhydrase allows the reabsorption of sodium ions in the proximal tubule. Carbonic anhydrase II has been shown to interact with Band 3 and Sodium-hydrogen antiporter 1.
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TMPY-00694 | Carbonic Anhydrase 12 Protein, Human, Recombinant (His) | Human | HEK293 | ||
Carbonic anhydrases (CAs) are a large family of zinc metalloenzymes first discovered in 1933 that catalyze the reversible hydration of carbon dioxide. CAs participate in a variety of biological processes, including respiration, calcification, acid-base balance, bone resorption, and the formation of aqueous humor, cerebrospinal fluid, saliva, and gastric acid. CA12, also known as Car12 and carbonic anhydrase XII, is a type I membrane enzyme of an N-terminal extracellular catalytic domain, a membrane-spanning α-helix, and a small intracellular C-terminal domain. It is highly expressed in colon, kidney, prostate, intestine and activated lymphocytes and moderately expressed in pancreas, ovary, and testis. Overexpression of the CA12 is observed in certain human cancers and is used as a tumor marker. rmCA12 corresponds to the extracellular domain and has both carbonic anhydrase activity and esterase activity.
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TMPY-00690 | Carbonic Anhydrase 9 Protein, Human, Recombinant (His) | Human | HEK293 | ||
Carbonic anhydrases IX (CA IX), also known as membrane antigen MN or CA9, is a member of the carbonic anhydrase (CA) family and may be involved in cell proliferation and cellular transformation. CAs are zinc metalloenzymes that catalyze the reversible hydration of carbon dioxide (H2O + CO2 = H+ + HCO3–) and thus participate in a variety of biological and physical processes. CA IX protein is expressed primarily in carcinoma cells lines, and the expression is cell density dependent and has been shown to be strongly induced by hypoxia, accordingly facilitates adaptation of tumor cells to hypoxic conditions. It is involved in tumorigenesis through many pathways, such as pH regulation and cell adhesion control. CA IX is used as a marker of tumor hypoxia and as a new therapeutic target for many human carcinomas and cancers.Cancer ImmunotherapyImmune CheckpointImmunotherapyTargeted Therapy
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TMPY-00689 | Carbonic Anhydrase 9 Protein, Human, Recombinant (hFc) | Human | HEK293 | ||
Carbonic anhydrases IX (CA IX), also known as membrane antigen MN or CA9, is a member of the carbonic anhydrase (CA) family and may be involved in cell proliferation and cellular transformation. CAs are zinc metalloenzymes that catalyze the reversible hydration of carbon dioxide (H2O + CO2 = H+ + HCO3–) and thus participate in a variety of biological and physical processes. CA IX protein is expressed primarily in carcinoma cells lines, and the expression is cell density dependent and has been shown to be strongly induced by hypoxia, accordingly facilitates adaptation of tumor cells to hypoxic conditions. It is involved in tumorigenesis through many pathways, such as pH regulation and cell adhesion control. CA IX is used as a marker of tumor hypoxia and as a new therapeutic target for many human carcinomas and cancers.Cancer ImmunotherapyImmune CheckpointImmunotherapyTargeted Therapy
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TMPH-01038 | CA5A Protein, Human, Recombinant | Human | HEK293 | ||
Reversible hydration of carbon dioxide. Low activity.
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TMPH-00312 | Malate dehydrogenase Protein, Brucella abortus, Recombinant (His & Myc & SUMO) | Brucella abortus | E. coli | ||
Catalyzes the reversible oxidation of malate to oxaloacetate.
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TMPH-03258 | Carbonic Anhydrase 1 Protein, Rat, Recombinant (His & SUMO) | Rat | E. coli | ||
Reversible hydration of carbon dioxide.
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TMPH-01085 | CHAT Protein, Human, Recombinant (His) | Human | E. coli | ||
Catalyzes the reversible synthesis of acetylcholine (ACh) from acetyl CoA and choline at cholinergic synapses.
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TMPH-00739 | Thioredoxin-1 Protein, E. coli, Recombinant (His) | E. coli | E. coli | ||
Participates in various redox reactions through the reversible oxidation of its active center dithiol to a disulfide and catalyzes dithiol-disulfide exchange reactions.
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TMPH-00398 | PPK2 Protein, Chlorobium tepidum, Recombinant (His & Myc) | Chlorobaculum tepidum | E. coli | ||
Catalyzes the reversible transfer of the terminal phosphate of ATP to form a long-chain polyphosphate (polyP).
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TMPH-00515 | PPDK Protein, Entamoeba histolytica, Recombinant (His & SUMO) | Entamoeba histolytica | E. coli | ||
Catalyzes the reversible phosphorylation of pyruvate and phosphate. In E.histolytica and C.symbiosus, PPDK functions in the direction of ATP synthesis.
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TMPJ-00826 | TXN Protein, Human, Recombinant (His) | Human | E. coli | ||
Thioredoxin (TXN) is a member of the Thioredoxin family. Thioredoxin exists as a disulfide-linked homodimer and contains one Thioredoxin domain. Thioredoxin is up-regulated by ionizing radiation. Thioredoxin participates in various redox reactions through the reversible oxidation of its active center dithiol to a disulfide and catalyzes dithiol-disulfide exchange reactions. Thioredoxin also plays a role in the reversible S-nitrosylation of cysteine residues in target proteins, and thereby contributes to the response to intracellular nitric oxide.
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TMPH-03503 | Adenylate kinase Protein, Shigella flexneri, Recombinant (His & Myc & SUMO) | Shigella flexneri | E. coli | ||
Catalyzes the reversible transfer of the terminal phosphate group between ATP and AMP. Plays an important role in cellular energy homeostasis and in adenine nucleotide metabolism.
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TMPH-03259 | Carbonic Anhydrase 2 Protein, Rat, Recombinant (His) | Rat | E. coli | ||
Essential for bone resorption and osteoclast differentiation. Reversible hydration of carbon dioxide. Contributes to intracellular pH regulation in the duodenal upper villous epithelium during proton-coupled peptide absorption. Stimulates the chloride-bicarbonate exchange activity of SLC26A6.
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TMPH-03022 | PstP Protein, Mycobacterium tuberculosis, Recombinant | Mycobacterium tuberculosis | E. coli | ||
Plays an important role in regulating cell division and growth by reversible phosphorylation signaling. May play important roles in regulating cellular metabolism and signaling pathways, which could mediate the growth and development of the cell. Plays a role in establishing and maintaining infection.
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TMPJ-01207 | UPP1 Protein, Human, Recombinant (His) | Human | E. coli | ||
Uridinephosphorylase 1 (UPP1) is a member of the family of pentosyltransferase. UPP1 catalyses the reversible phosphorolysis of uridine to uracil. The expression levels and the enzymatic activity of UPP1 are higher in human solid tumors than in adjacent normal tissues. The high level of UPP1 expression in some tumors makes it a potential prognosticfactor for some cancers, such as oral squamous cell carcinoma. UPP1 is important for the homeostatic regulation of intracellular and plasma uridine concentratios. UPP1 plays an important role in the pyrimidine salvage pathway through its catalysis of the reversible phosphorolysis of uridine to uracil.
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TMPH-03021 | PstP Protein, Mycobacterium tuberculosis, Recombinant (His) | Mycobacterium tuberculosis | E. coli | ||
Plays an important role in regulating cell division and growth by reversible phosphorylation signaling. May play important roles in regulating cellular metabolism and signaling pathways, which could mediate the growth and development of the cell. Plays a role in establishing and maintaining infection.
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TMPH-03584 | Shikimate dehydrogenase Protein, S. epidermidis, Recombinant (His & Myc) | Staphylococcus epidermidis | E. coli | ||
Involved in the biosynthesis of the chorismate, which leads to the biosynthesis of aromatic amino acids. Catalyzes the reversible NADPH linked reduction of 3-dehydroshikimate (DHSA) to yield shikimate (SA). It can also use NAD to oxidize shikimate.
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TMPH-01678 | MMUT Protein, Human, Recombinant (His) | Human | E. coli | ||
Catalyzes the reversible isomerization of methylmalonyl-CoA (MMCoA) (generated from branched-chain amino acid metabolism and degradation of dietary odd chain fatty acids and cholesterol) to succinyl-CoA (3-carboxypropionyl-CoA), a key intermediate of the tricarboxylic acid cycle.
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TMPH-02195 | TXNDC17 Protein, Human, Recombinant (GST) | Human | E. coli | ||
Disulfide reductase. May participate in various redox reactions through the reversible oxidation of its active center dithiol to a disulfide and catalyze dithiol-disulfide exchange reactions. Modulates TNF-alpha signaling and NF-kappa-B activation. Has peroxidase activity and may contribute to the elimination of cellular hydrogen peroxide.
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TMPJ-01278 | SENP8 Protein, Human, Recombinant (His) | Human | E. coli | ||
Sentrin-Specific Protease 8 (SENP8) mediates the reversible covalent modification of proteins by NEDD8. SENP8 catalyzes the full-length NEDD8 to generate its mature form and deconjugation of NEDD8 from targeted proteins such as CUL2 , CUL4A in vivo, or p53. but it does not show activity against ubiquitin or SUMO proteins.
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TMPJ-00818 | ALDOC Protein, Human, Recombinant (His) | Human | Human Cells | ||
Fructose-bisphosphate aldolase C (ALDOC) belongs to the class I fructose-bisphosphate aldolase family. It is an enzyme that, in humans, is encoded by the ALDOC gene. ALDOC is expressed exclusively in the hippocampus and Purkinje cells of the brain. ALDOC is a glycolytic enzyme which catalyzes the reversible aldol cleavage of fructose-1,6-biphosphate and fructose 1-phosphate to dihydroxyacetone phosphate and either glyceraldehyde-3-phosphate or glyceraldehydes respectively
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TMPJ-00956 | MDH2 Protein, Human, Recombinant (His) | Human | Human Cells | ||
Malate dehydrogenase, mitochondrial is a 338 amino acids protein that belongs to the LDH/MDH superfamily. MDH type 1 family. MDH2 catalyzes the reversible oxidation of malate to oxaloacetate, utilizing the NAD/NADH cofactor system in the citric acid cycle. MDH2 is localized to the mitochondria and takes part in the malate-aspartate shuttle that functions in the metabolic coordination between cytosol and mitochondria. MDH2 is highly expressed in the adrenal system, small intestine, heart and pancreas.
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TMPY-02250 | Thioredoxin/TRX Protein, Human, Recombinant | Human | E. coli | ||
Thioredoxin, also known as ATL-derived factor, Surface-associated sulphydryl protein, SASP and TXN, is a nucleus, cytoplasm and secreted protein that belongs to the thioredoxin family. Thioredoxins are proteins that act as antioxidants by facilitating the reduction of other proteins by cysteine thiol-disulfide exchange. Thioredoxins are found in nearly all known organisms and are essential for life in mammals. Thioredoxin / TXN participates in various redox reactions through the reversible oxidation of its active center dithiol to a disulfide and catalyzes dithiol-disulfide exchange reactions. Thioredoxin / TXN plays a role in the reversible S-nitrosylation of cysteine residues in target proteins, and thereby contributes to the response to intracellular nitric oxide. Thioredoxin / TXN nitrosylates the active site Cys of CASP3 in response to nitric oxide (NO), and thereby inhibits caspase-3 activity. Thioredoxin / TXN induces the FOS/JUN AP-1 DNA-binding activity in ionizing radiation (IR) cells through its oxidation/reduction status and stimulates AP-1 transcriptional activity.
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TMPY-03386 | ART3 Protein, Human, Recombinant (His) | Human | HEK293 | ||
ART3 is an arginine-specific ADP-ribosyltransferase which belongs to the Arg-specific ADP-ribosyltransferase family. ART3 catalyzes a reversible reaction which modifies proteins by the addition or removal of ADP-ribose to an arginine residue to regulate the function of the modified protein. It is expressed specifically in testis. ART3 pseudogene is located on chromosome 11. ART3 was identified as a susceptibility gene for non-obstructive azoospermia (NOA). It is a novel therapeutic target in the treatment of NOA.
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TMPJ-00313 | Fumarase Protein, Human, Recombinant | Human | E. coli | ||
Fumarase is an enzyme that catalyze the reversible hydration/dehydration of fumarate to S-malate and is involved in the tricarboxylic acid or Krebs cycle. Fumarase exists in both form, cytosolic formand N-terminal extend mitochondrial form. The N-terminal extended form is targeted to the mitochondrion, where the removal of the extension is the same form as in the cytoplasm. Fumarase is thought to act as a tumor suppressor, which deficiency can lead to progressive encephalopathy, cerebral atrophy and development delay.
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TMPH-00713 | Polyphosphate kinase Protein, E. coli, Recombinant (His & Myc) | E. coli | E. coli | ||
Catalyzes the reversible transfer of the terminal phosphate of ATP to form a long-chain polyphosphate (polyP). Can form linear polymers of orthophosphate with chain lengths up to 1000 or more. Can use GTP instead of ATP, but the efficiency of GTP is 5% that of ATP. Also exhibits several other enzymatic activities, which include: ATP synthesis from polyP in the presence of excess ADP, general nucleoside-diphosphate kinase activity, linear guanosine 5'-tetraphosphate (ppppG) synthesis and autophosphorylation.
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TMPH-00875 | ACAT1 Protein, Human, Recombinant (His) | Human | E. coli | ||
This is one of the enzymes that catalyzes the last step of the mitochondrial beta-oxidation pathway, an aerobic process breaking down fatty acids into acetyl-CoA. Using free coenzyme A/CoA, catalyzes the thiolytic cleavage of medium- to long-chain 3-oxoacyl-CoAs into acetyl-CoA and a fatty acyl-CoA shortened by two carbon atoms. The activity of the enzyme is reversible and it can also catalyze the condensation of two acetyl-CoA molecules into acetoacetyl-CoA. Thereby, it plays a major role in ketone body metabolism.
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TMPY-03790 | DPYS Protein, Human, Recombinant (His & GST) | Human | Baculovirus-Insect Cells | ||
DPYS, also known as dihydropyrimidinase, belongs to the DHOase family, hydantoinase/dihydropyrimidinase subfamily. DPYS catalyzes the second step of the reductive pyrimidine degradation, the reversible hydrolytic ring opening of dihydropyrimidines. It can catalyzes the ring opening of 5,6-dihydrouracil to N-carbamyl-alanine and of 5,6-dihydrothymine to N-carbamyl-amino isobutyrate. DPYS is expressed at a high level in liver and kidney as a major 2.5-kb transcript and a minor 3.8-kb transcript. Defects in the DPYS gene are linked to dihydropyrimidinuria.
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TMPY-03791 | DPYS Protein, Human, Recombinant | Human | Baculovirus-Insect Cells | ||
DPYS, also known as dihydropyrimidinase, belongs to the DHOase family, hydantoinase/dihydropyrimidinase subfamily. DPYS catalyzes the second step of the reductive pyrimidine degradation, the reversible hydrolytic ring opening of dihydropyrimidines. It can catalyzes the ring opening of 5,6-dihydrouracil to N-carbamyl-alanine and of 5,6-dihydrothymine to N-carbamyl-amino isobutyrate. DPYS is expressed at a high level in liver and kidney as a major 2.5-kb transcript and a minor 3.8-kb transcript. Defects in the DPYS gene are linked to dihydropyrimidinuria.
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TMPJ-00484 | SHMT1 Protein, Human, Recombinant (His) | Human | Human Cells | ||
Serine Hydroxymethyltransferase Cytosolic (SHMT1) is a member of the SHMT family. SHMT1 is a cytoplasmic protein and exists as a homotetramer. SHMT1 catalyzes the reversible conversion of serine and tetrahydrofolate to glycine and 5,10-methylene tetrahydrofolate. This reaction provides one carbon unit for the synthesis of methionine, thymidylate, and purines in the cytoplasm. A reduction in SHMT1 levels would result in less glycine that could affect the nervous system by acting as an agonist to the NMDA receptor and this could be a mechanism behind Smith-Magenis syndrome.
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TMPJ-00601 | Apolipoprotein C-II/APOC2 Protein, Human, Recombinant (His) | Human | E. coli | ||
APOC2 activates the lipoprotein lipase in capillaries, which hydrolyzes triglycerides and thus provides free fatty acids for cells. APOC2 is component of the very low density lipoprotein (VLDL) fraction in plasma. It is also an activator of several triacylglycerol lipases. The association of APOC2 with plasma chylomicrons, VLDL, and HDL is reversible, a function of the secretion and catabolism of triglyceride-rich lipoproteins, and changes rapidly. Defects in APOC2 are the cause of hyperlipoproteinemia type 1B (HLPP1B) which characterized by hypertriglyceridemia, xanthomas, and increased risk of pancreatitis and early atherosclerosis.
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TMPJ-00701 | Carbonic Anhydrase 11 Protein, Human, Recombinant (His) | Human | Human Cells | ||
Carbonic Anhydrase-Related Protein 11 (CA11) is a secreted protein member of the α-carbonic anhydrase family. Carbonic Anhydrases (CAs) are a large family of zinc metalloenzymes that catalyze the reversible hydration of carbon dioxide. They participate in a variety of biological processes, including respiration, calcification, acid-base balance, bone resorption, and the formation of aqueous humor, cerebrospinal fluid, saliva, and gastric acid. CA11 is expressed abundantly in the brain with moderate expression also present in spinal cord and thyroid. CA11 may play a general role in the central nervous system.
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TMPJ-00283 | Carbonic Anhydrase 9 Protein, Human, Recombinant (Avi & His), Biotinylated | Human | Human Cells | ||
Carbonic anhydrases IX (CA IX), also known as membrane antigen MN or CA9, is a member of the carbonic anhydrase (CA) family and may be involved in cell proliferation and cellular transformation. CAs are zinc metalloenzymes that catalyze the reversible hydration of carbon dioxide (H2O + CO2 = H+ + HCO3–) and thus participate in a variety of biological and physical processes. CA9 is a transmembrane enzyme expressed primarily in carcinoma cells. It is one of the best markers for hypoxia and for RCC. Appears to be a novel specific biomarker for a cervical neoplasia.
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TMPY-04755 | AK3L1 Protein, Human, Recombinant | Human | Baculovirus-Insect Cells | ||
Adenylate kinase isoenzyme 4, mitochondrial, also known as ATP-AMP transphosphorylase, Adenylate kinase 3-like, AK4 and AK3L1, is a member theadenylate kinase family. AK4 / AK3L1 is localized to the mitochondrial matrix. Adenylate kinases regulate the adenine and guanine nucleotide compositions within a cell by catalyzing the reversible transfer of phosphate group among these nucleotides. Five isozymes of adenylate kinase have been identified in vertebrates. Expression of these isozymes is tissue-specific and developmentally regulated. AK4 / AK3L1 catalyzes the reversible transfer of the terminal phosphate group between ATP and AMP. It may also be active with GTP. Adenylate kinase 4 ( AK4 / AK3L1 ) is a unique member with no enzymatic activity in the adenylate kinase (AK) family although it shares high sequence homology with other AKs. It remains unclear what physiological function AK4 might play or why it is enzymatically inactive. AK4 / AK3L1 retains the capability of binding nucleotides. It has a glutamine residue instead of a key arginine residue in the active site well conserved in other AKs. The enzymatically inactive AK4 is a stress responsive protein critical to cell survival and proliferation. AK4 / AK3L1 is likely that the interaction with the mitochondrial inner membrane protein ANT is important for AK4 to exert the protective benefits to cells under stress. AK4 / AK3L1 also acts on the specific mechanism of energy metabolism rather than control of the homeostasis of the ADP pool ubiquitously.
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TMPJ-00731 | Carbonic Anhydrase 1 Protein, Human, Recombinant (His) | Human | E. coli | ||
Carbonic Anhydrase 1 (CA1) is a cytosolic enzyme, belonging to the alpha-carbonic anhydrase family. It is highly expressed in erythrocytes and acts as an early marker for erythroid differentiation. Carbonic anhydrase 1 plays a improtant role in many biological processes such as calcification, cellular respiration, bone resorption, acid-base balance. It is activated by imidazole, histamine, L-adrenaline, L- and D-histidine, and L- and D-phenylalanine. At the same time, It is inhibited by sulfonamide derivatives and coumarins. In addition, CA1 is a zinc metalloenzyme that has reversible hydration of carbon dioxide. It can hydrate cyanamide to urea.
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TMPY-04469 | AK3L1 Protein, Human, Recombinant (His & GST) | Human | Baculovirus-Insect Cells | ||
Adenylate kinase isoenzyme 4, mitochondrial, also known as ATP-AMP transphosphorylase, Adenylate kinase 3-like, AK4 and AK3L1, is a member theadenylate kinase family. AK4 / AK3L1 is localized to the mitochondrial matrix. Adenylate kinases regulate the adenine and guanine nucleotide compositions within a cell by catalyzing the reversible transfer of phosphate group among these nucleotides. Five isozymes of adenylate kinase have been identified in vertebrates. Expression of these isozymes is tissue-specific and developmentally regulated. AK4 / AK3L1 catalyzes the reversible transfer of the terminal phosphate group between ATP and AMP. It may also be active with GTP. Adenylate kinase 4 ( AK4 / AK3L1 ) is a unique member with no enzymatic activity in the adenylate kinase (AK) family although it shares high sequence homology with other AKs. It remains unclear what physiological function AK4 might play or why it is enzymatically inactive. AK4 / AK3L1 retains the capability of binding nucleotides. It has a glutamine residue instead of a key arginine residue in the active site well conserved in other AKs. The enzymatically inactive AK4 is a stress responsive protein critical to cell survival and proliferation. AK4 / AK3L1 is likely that the interaction with the mitochondrial inner membrane protein ANT is important for AK4 to exert the protective benefits to cells under stress. AK4 / AK3L1 also acts on the specific mechanism of energy metabolism rather than control of the homeostasis of the ADP pool ubiquitously.
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TMPY-02277 | Carbonic Anhydrase 7 Protein, Human, Recombinant (His) | Human | E. coli | ||
Carbonic anhydrase 7, also known as carbonate dehydratase VII, carbonic anhydrase VII, CA-VII and CA7, is a cytoplasm protein which belongs to thealpha-carbonic anhydrase family. Carbonic anhydrases are a large family of zinc metalloenzymes that catalyze the reversible hydration of carbon dioxide. They participate in a variety of biological processes, including respiration, calcification, acid-base balance, bone resorption, and the formation of aqueous humor, cerebrospinal fluid, saliva, and gastric acid. Carbonic anhydrases show extensive diversity in tissue distribution and in their subcellular localization. CA7 / CA-VII is predominantly expressed in the salivary glands. Alternative splicing in the coding region results in multiple transcript variants encoding different isoforms.
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TMPY-01877 | CA5A Protein, Human, Recombinant (His) | Human | E. coli | ||
Carbonic anhydrase 5A, mitochondrial, also known as Carbonate dehydratase VA, Carbonic anhydrase VA, CA-VA and CA5A, is a member of thealpha-carbonic anhydrase family. Carbonic anhydrases (CAs) are a large family of zinc metalloenzymes first discovered in 1933 that catalyze the reversible hydration of carbon dioxide. CAs participate in a variety of biological processes, including respiration, calcification, acid-base balance, bone resorption, and the formation of aqueous humor, cerebrospinal fluid, saliva, and gastric acid. CA5A / CA-VA is activated by histamine, L-adrenaline, L- and D-histidine, and L- and D-phenylalanine. It is inhibited by coumarins, sulfonamide derivatives such as acetazolamide and Foscarnet (phosphonoformate trisodium salt).
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TMPY-02111 | Carbonic Anhydrase 2 Protein, Mouse, Recombinant (His) | Mouse | E. coli | ||
The carbonic anhydrases (or carbonate dehydratases) are classified as metalloenzyme for its zinc ion prosthetic group and form a family of enzymes that catalyze the rapid interconversion of carbon dioxide and water to bicarbonate and protons, a reversible reaction that takes part in maintaining acid-base balance in blood and other tissues. The carbonic anhydrasekl (CA) family consists of at least 11 enzymatically active members and a few inactive homologous proteins. Carbonic anhydrase II is one of fourteen forms of human α carbonic anhydrases. Defects in this enzyme are associated with osteopetrosis and renal tubular acidosis. Renal carbonic anhydrase allows the reabsorption of sodium ions in the proximal tubule. Carbonic anhydrase II has been shown to interact with Band 3 and Sodium-hydrogen antiporter 1.
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TMPY-03755 | Glycerol 3 Phosphate Dehydrogenase/GPD1 Protein, Human, Recombinant (His) | Human | E. coli | ||
GPD1 (Glycerol-3-Phosphate Dehydrogenase 1) is a Protein Coding gene. 2 alternatively spliced human isoforms have been reported. GPD1 is a member of the NAD-dependent glycerol-3-phosphate dehydrogenase family. The encoded protein plays a critical role in carbohydrate and lipid metabolism by catalyzing the reversible conversion of dihydroxyacetone phosphate (DHAP) and reduced nicotine adenine dinucleotide (NADH) to glycerol-3-phosphate (G3P) and NAD+. It also reduces nicotine adenine dinucleotide (NADH) to glycerol-3-phosphate (G3P) and NAD+. Meanwhile, GPD1 and mitochondrial glycerol-3-phosphate dehydrogenase also form a glycerol phosphate shuttle that facilitates the transfer of reducing equivalents from the cytosol to mitochondria. Diseases associated with GPD1 include Hypertriglyceridemia, Transient Infantile, and Myopathy, Distal, 1.
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TMPY-02453 | CROT Protein, Human, Recombinant (474 Leu/Val, His) | Human | Baculovirus-Insect Cells | ||
Carnitine octanoyltransferase (CROT or COT), also known as octanoyl-CoA: L-carnitine O-octanoyltransferase, medium-chain/long-chain carnitine acyltransferase, and carnitine medium-chain acyltransferase, is a carnitine acyltransferase belonging to the family of transferases, specifically those acyltransferases transferring groups other than aminoacyl groups that catalyzes the reversible transfer of fatty acyl groups between CoA and carnitine. Carnitine octanoyltransferase (CROT or COT) facilitate the transport of medium- and long-chain fatty acids through the peroxisomal and mitochondrial membranes. It is physiologically inhibited by malonyl-CoA. COT also has functions in efficiently converting one of the end products of the peroxisomal beta-oxidation of pristanic acid, 4, 8-dimethylnonanoyl-CoA, to its corresponding carnitine ester.
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TMPY-01351 | Carbonic Anhydrase 10 Protein, Human, Recombinant (His) | Human | HEK293 | ||
Carbonic anhydrase X, also called carbonic anhydrase - related protein X (CARPX) and CA1, belongs to the CA family of zinc metalloenzymes which catalyze the reversible hydration of carbon dioxide in various biological processes such as respiration, renal tubular acidification and bone resorption. The secreted protein CARPX without CA activity (hydration of CO2) is identified as an acatalytic member of the alpha-carbonic anhydrase subgroup. CARP X expression is detected in the adult total brain and almost all parts of the central nervous system, but not in the fetal brain. Accordingly, CARP X is suggested to play a role in the development of central nervous system, especially the brain. The same CARP X protein are encoded by multiple transcript variants of this gene.
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TMPY-02302 | Carbonic Anhydrase 10 Protein, Mouse, Recombinant (His) | Mouse | HEK293 | ||
Carbonic anhydrase X, also called carbonic anhydrase - related protein X (CARPX) and CA1, belongs to the CA family of zinc metalloenzymes which catalyze the reversible hydration of carbon dioxide in various biological processes such as respiration, renal tubular acidification and bone resorption. The secreted protein CARPX without CA activity (hydration of CO2) is identified as an acatalytic member of the alpha-carbonic anhydrase subgroup. CARP X expression is detected in the adult total brain and almost all parts of the central nervous system, but not in the fetal brain. Accordingly, CARP X is suggested to play a role in the development of central nervous system, especially the brain. The same CARP X protein are encoded by multiple transcript variants of this gene.
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TMPY-00693 | Carbonic Anhydrase 10 Protein, Human, Recombinant | Human | HEK293 | ||
Carbonic anhydrase X, also called carbonic anhydrase - related protein X (CARPX) and CA1, belongs to the CA family of zinc metalloenzymes which catalyze the reversible hydration of carbon dioxide in various biological processes such as respiration, renal tubular acidification and bone resorption. The secreted protein CARPX without CA activity (hydration of CO2) is identified as an acatalytic member of the alpha-carbonic anhydrase subgroup. CARP X expression is detected in the adult total brain and almost all parts of the central nervous system, but not in the fetal brain. Accordingly, CARP X is suggested to play a role in the development of central nervous system, especially the brain. The same CARP X protein are encoded by multiple transcript variants of this gene.
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TMPJ-00497 | CTSB Protein, Human, Recombinant (His) | Human | Human Cells | ||
Cathepsin B is an enzymatic protein belonging to the peptidase (or protease) families. The protein encoded by this gene is a lysosomal cysteine protease composed of a dimer of disulfide-linked heavy and light chains, both produced from a single protein precursor. It is a member of the peptidase C1 family. At least five transcript variants encoding the same protein have been found for this gene. Cystatin-B / CSTB is an intracellular thiol proteinase inhibitor. Tightly binding reversible inhibitor of cathepsins L, H and B. Cystatin-B / CSTB is able to form a dimer stabilized by noncovalent forces, inhibiting papain and cathepsins l, h and b. Cystatin-B / CSTB is also thought to play a role in protecting against the proteases leaking from lysosomes.
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TMPY-00513 | Carbonic Anhydrase 4 Protein, Human, Recombinant (His) | Human | CHO | ||
The carbonic anhydrases (or carbonate dehydratases) are classified as metalloenzyme for its zinc ion prosthetic group and form a family of enzymes that catalyze the rapid interconversion of carbon dioxide and water to bicarbonate and protons, a reversible reaction that takes part in maintaining acid-base balance in blood and other tissues. The carbonic anhydrasekl (CA) family consists of at least 11 enzymatically active members and a few inactive homologous proteins. Carbonic anhydrase IV (CAIV) is a membrane-associated enzyme anchored to plasma membrane surfaces by a phosphatidylinositol glycan linkage. CAIV is a high-activity isozyme in CO2hydration comparable to that of CAII. Furthermore, CAIV is more active in HCO3-dehydration than is CAII. However, the esterase activity of CAIV is decreased 150-fold compared to CAII.
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TMPY-01706 | Carbonic Anhydrase 8 Protein, Human, Recombinant (His) | Human | E. coli | ||
The carbonic anhydrases (or carbonate dehydratases) are classified as metalloenzyme for its zinc ion prosthetic group and form a family of enzymes that catalyze the rapid interconversion of carbon dioxide and water to bicarbonate and protons, a reversible reaction that takes part in maintaining acid-base balance in blood and other tissues. The carbonic anhydrasekl (CA) family consists of at least 11 enzymatically active members and a few inactive homologous proteins. Carbonic anhydrase protein (CA) VIII, which is a member of the CA gene family, has been shown to have no catalytic CA activity and its biological function is still unknown. Increased expression of CA-RP VIII was observed in 78% of colorectal carcinomas. It suggested that CA-RP VIII plays a role in the process of invasion in colorectal cancer.
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