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1000 results found for “transaminase”
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Name :
FKBP2 HumanDescription:
FK506 Binding Protein 2 Human Recombinant
FKBP13, FKBP-2, Peptidyl-prolyl cis-trans isomerase FKBP2, PPIase FKBP2, FK506-binding protein 2, Rotamase, Immunophilin FKBP13, 13 kDa FK506-binding protein, 13 kDa FKBP, FKBP-13, FKBP2, PPIase.
Product # :
ENZ-503Price :
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Shipped with Ice Packs
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Description
FKBP2 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 122 amino acids (22-142 a.a.) and having a molecular mass of 13.4 kDa. The FKBP2 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The FKBP2 solution contains 20mM Tris-HCl pH-8, 1mM DTT, and 10% glycerol.
Purity
Greater than 90% as determined by SDS-PAGE.
Biological Activity
Specific activity is > 270 nmoles/min/ug, and is defined as the amount of enzyme that cleaves 1umole of suc-AAFP-pNA per minute at 25C in Tris-Hcl pH8.0 using chymotrypsin.Citations
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Introduction
FKBP2 is part of the immunophilin protein family, which takes part in immunoregulation and basic cellular processes involving protein folding and trafficking. FKBP2 is a cis-trans prolyl isomerase that binds the immunosuppressants FK506 and rapamycin. FKBP2 functions as an ER chaperone and as a component of membrane cytoskeletal scaffolds.
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Synonyms
FKBP13, FKBP-2, Peptidyl-prolyl cis-trans isomerase FKBP2, PPIase FKBP2, FK506-binding protein 2, Rotamase, Immunophilin FKBP13, 13 kDa FK506-binding protein, 13 kDa FKBP, FKBP-13, FKBP2, PPIase.
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Physical Appearance
Sterile Filtered clear colorless solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MATGAEGKRK LQIGVKKRVD HCPIKSRKGD VLHMHYTGKL EDGTEFDSSL PQNQPFVFSL GTGQVIKGWD QGLLGMCEGE KRKLVIPSEL GYGERGAPPK IPGGATLVFE VELLKIERRT EL.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
LIPG Human, HEKDescription:
Lipase Endothelial Human Recombinant, HEK
LIPG, Lipase Endothelial, EDL, EL, Endothelial Cell-Derived Lipase, EC 3.1.1.3, PRO719, Endothelial Lipase, Lipoprotein Lipase H, EC 3.1.1.
Product # :
ENZ-810Price :
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Shipped at Room temp
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Description
LIPG Human Recombinant produced in HEK cells is a single, glycosylated, polypeptide chain (Ser21-Pro500) containing a total of 490 amino acids, having a calculated molecular mass of 55.8kDa. LIPG is fused to a 2 aa N-terminal linker, a 2 aa C-terminal linker and a 6 aa His tag at C-Terminus.
Source
HEK 293.
Formulation
LIPG was filtered (0.4 µm) and lyophilized from a solution in phosphate buffered saline pH 7.5 (PBS), 1% (w/v) Sucrose and 4% (w/v) Mannitol.
Purity
Greater than 85.0% as determined by SDS-PAGE.
Citations
More Info
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Introduction
Lipase Endothelial (LIPG) has extensive phospholipase activity and may be involved in lipoprotein metabolism and vascular biology. The LIPG protein is considered a member of the TG lipase family through its sequence and characteristic lid region which provides substrate specificity for enzymes of the TG lipase family. In addition, the LIPG has triglyceride lipase activities. LIPG hydrolyzes HDLs more efficiently than other lipoproteins. LIPG also binds heparin.
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Synonyms
LIPG, Lipase Endothelial, EDL, EL, Endothelial Cell-Derived Lipase, EC 3.1.1.3, PRO719, Endothelial Lipase, Lipoprotein Lipase H, EC 3.1.1.
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Physical Appearance
Filtered White lyophilized (freeze-dried) powder.
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Stability
Store lyophilized protein at -20°C. Aliquot the product after reconstitution to avoid repeated freezing/thawing cycles. Reconstituted protein can be stored at 4°C for a limited period of time; it does not show any change after two weeks at 4°C.
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Solubility
It is recommended to add deionized water to prepare a working stock solution of approximately 0.5 mg/ml and let the lyophilized pellet dissolve completely. LIPG is not sterile! Please filter the product by an appropriate sterile filter before using it in the cell culture.
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Amino Acid Sequence
ASSPVPFGPE GRLEDKLHKP KATQTEVKPS VRFNLRTSKD PEHEGCYLSV GHSQPLEDCS FNMTAKTFFI IHGWTMSGIF ENWLHKLVSA LHTREKDANV VVVDWLPLAH QLYTDAVNNT RVVGHSIARM LDWLQEKDDF SLGNVHLIGY SLGAHVAGYA GNFVKGTVGR ITGLDPAGPM FEGADIHKRL SPDDADFVDV LHTYTRSFGL SIGIQMPVGH IDIYPNGGDF QPGCGLNDVL GSIAYGTITE VVKCEHERAV HLFVDSLVNQ DKPSFAFQCT DSNRFKKGIC LSCRKNRCNS IGYNAKKMRN KRNSKMYLKT RAGMPFRVYH YQMKIHVFSY KNMGEIEPTF YVTLYGTNAD SQTLPLEIVE RIEQNATNTF LVYTEEDLGD LLKIQLTWEG ASQSWYNLWK EFRSYLSQPR NPGRELNIRR IRVKSGETQR KLTFCTEDPE NTSISPGREL WFRKCRDGWR MKNETSPTVE LP KLHHHHHH.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
CYB5R2 HumanDescription:
Cytochrome B5 Reductase 2 Human Recombinant
CYB5R2, Cytochrome B5 Reductase 2, EC 1.6.2.2, B5R.2, Cytochrome B5 Reductase B5R.2, NADH-Cytochrome B5 Reductase 2, b5R.2.
Product # :
ENZ-799Price :
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Description
CYB5R2 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 299 amino acids (1-276 a.a.) and having a molecular mass of 33.8kDa. CYB5R2 is fused to a 23 amino acid His-tag at N-terminus.
Source
Escherichia Coli.
Formulation
CYB5R2 protein solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 10% glycerol and 1mM DTT.
Purity
Greater than 90.0% as determined by SDS-PAGE.
Citations
More Info
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Introduction
Cytochrome b5 reductase 2 (CYB5R2) is involved in desaturation and elongation of fatty acids, cholesterol biosynthesis, drug metabolism, and, in erythrocyte, methemoglobin reduction. CYB5R2 is responsible for NADH-dependent lucigenin chemiluminescence in spermatozoa by reducing both lucigenin and 2-[4-iodophenyl]-3-[4-nitrophenyl]-5-[2,4-disulfophenyl]-2H tetrazolium monosodium salt (WST-1).
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Synonyms
CYB5R2, Cytochrome B5 Reductase 2, EC 1.6.2.2, B5R.2, Cytochrome B5 Reductase B5R.2, NADH-Cytochrome B5 Reductase 2, b5R.2.
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Physical Appearance
Sterile Filtered colorless solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSMNSRRRE PITLQDPEAK YPLPLIEKEK ISHNTRRFRF GLPSPDHVLG LPVGNYVQLL AKIDNELVVR AYTPVSSDDD RGFVDLIIKI YFKNVHPQYP EGGKMTQYLE NMKIGETIFF RGPRGRLFYH GPGNLGIRPD QTSEPKKTLA DHLGMIAGGT GITPMLQLIR HITKDPSDRT RMSLIFANQT EEDILVRKEL EEIARTHPDQ FNLWYTLDRP PIGWKYSSGF VTADMIKEHL PPPAKSTLIL VCGPPPLIQT AAHPNLEKLG YTQDMIFTY.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
SSU72 HumanDescription:
SSU72 RNA Polymerase II CTD Phosphatase Human Recombinant
SSU72 RNA polymerase II CTD phosphatase homolog (S. cerevisiae), HSPC182, CTD phosphatase SSU72, Ssu72 RNA polymerase II CTD phosphatase homolog (yeast), PNAS-120, RNA polymerase II subunit A C-terminal domain phosphatase SSU72, EC 3.1.3.16.
Product # :
ENZ-243Price :
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Description
SSU72 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 217 amino acids (1-194) and having a molecular mass of 25.0kDa.SSU72 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
The SSU72 solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 100mM NaCl, 1mM DTT and 10% glycerol.
Purity
Greater than 95% as determined by SDS-PAGE.
Citations
More Info
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Introduction
SSU72 is an extremely conserved homologue of yeast Ssu72, a CTD phosphatase and a component of the polyadenylation/termination machinery. SSU72 interacts with TFIIB, Rb and DNAM-1 and operates to catalyze the dephosphorylation of target proteins, and taking part in RNA processing and termination via dephosphorylation of Pol II. SSU72 is found in multiple alternatively spliced isoforms.
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Synonyms
SSU72 RNA polymerase II CTD phosphatase homolog (S. cerevisiae), HSPC182, CTD phosphatase SSU72, Ssu72 RNA polymerase II CTD phosphatase homolog (yeast), PNAS-120, RNA polymerase II subunit A C-terminal domain phosphatase SSU72, EC 3.1.3.16.
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Physical Appearance
Sterile Filtered colorless solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSMPSSPLR VAVVCSSNQN RSMEAHNILS KRGFSVRSFG TGTHVKLPGP APDKPNVYDF KTTYDQMYND LLRKDKELYT QNGILHMLDR NKRIKPRPER FQNCKDLFDL ILTCEERVYD QVVEDLNSRE QETCQPVHVV NVDIQDNHEE ATLGAFLICE LCQCIQHTED MENEIDELLQ EFEEKSGRTF LHTVCFY
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
CA8 HumanDescription:
Carbonic Anhydrase 8 Human Recombinant
Carbonic anhydrase VIII, CALS, CARP, CA-VIII, CAMRQ3, CA-related protein, carbonate dehydratase, carbonic anhydrase-like sequence, carbonic anhydrase-related protein.
Product # :
ENZ-235Price :
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Description
CA8 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 314 amino acids (1-290) and having a molecular mass of 35.5kDa.CA8 is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
The CA8 solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 1mM DTT and 20% glycerol.
Purity
Greater than 90% as determined by SDS-PAGE.
Citations
More Info
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Introduction
CA8 was first called CA-related protein since there is a sequence similarity to other identified carbonic anhydrase genes. Still, this protein has no carbonic anhydrase activity - the reversible hydration of carbon dioxide. CA8 still holds a carbonic anhydrase designation due to obvious sequence similarity to other members of the carbonic anhydrase gene family. Mutations in CA8 result in cerebellar ataxia mental retardation and dysequilibrium syndrome type 3 (CMARQ3).
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Synonyms
Carbonic anhydrase VIII, CALS, CARP, CA-VIII, CAMRQ3, CA-related protein, carbonate dehydratase, carbonic anhydrase-like sequence, carbonic anhydrase-related protein.
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Physical Appearance
Sterile Filtered colorless solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSHMADLSF IEDTVAFPEK EEDEEEEEEG VEWGYEEGVE WGLVFPDANG EYQSPINLNS REARYDPSLL DVRLSPNYVV CRDCEVTNDG HTIQVILKSK SVLSGGPLPQ GHEFELYEVR FHWGRENQRG SEHTVNFKAF PMELHLIHWN STLFGSIDEA VGKPHGIAII ALFVQIGKEH VGLKAVTEIL QDIQYKGKSK TIPCFNPNTL LPDPLLRDYW VYEGSLTIPP CSEGVTWILF RYPLTISQLQ IEEFRRLRTH VKGAELVEGC DGILGDNFRP TQPLSDRVIR AAFQ
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
PLA2G2A HumanDescription:
Secreted Phospholipase A2-IIA Human Recombinant
MOM1, PLA2, PLA2B, PLA2L, PLA2S, PLAS1, sPLA2, Phospholipase A2 membrane associated, EC 3.1.1.4, Phosphatidylcholine 2-acylhydrolase, Group IIA phospholipase A2, GIIC sPLA2, Non-pancreatic secretory phospholipase A2, NPS-PLA2, sPLA2-IIA, PLA2G2A.
Product # :
ENZ-290Price :
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Description
Secreted Phospholipase A2-IIA Human Recombinant is manufactured with N-terminal fusion of HisTag. PLA2G2A His-Tagged Fusion Protein is 15.8 kDa containing 124 amino acid residues of the human secreted phospholipase A2-IIA and 16 additional amino acid residues – HisTag.
Source
Escherichia Coli.
Formulation
Lyophilized from 0.5 mg/ml in 0.05M Acetate buffer pH-4.
Purity
Greater than 95% as determined by SDS-PAGE.
Citations
More Info
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Introduction
Phospholipase A2 (PLA2) catalyzes the hydrolysis of the sn-2 position of membrane glycerophospholipids to liberate arachidonic acid (AA), a precursor of eicosanoids including prostaglandins and leukotrienes. The same reaction also produces lysophosholipids, which represent another class of lipid mediators.
The secretory PLA2 (sPLA2) family, in which 10 isozymes have been identified, consists of lowmolecular weight, Ca2+-requiring secretory enzymes that have been implicated in a number of biological processes, such as modification of eicosanoid generation, inflammation, and host defense.
This enzyme has been proposed to hydrolyze phosphatidylcholine (PC) in lipoproteins to liberate lyso- PC and free fatty acids in the arterial wall, thereby facilitating the accumulation of bioactive lipids and modified lipoproteins in atherosclerotic foci.
In mice, sPLA2 expression significantly influences HDL particle size and composition and demonstrate that an induction of sPLA2 is required for the decrease in plasma HDL cholesterol in response to inflammatory stimuli. Instillation of bacteria into the bronchi was associated with surfactant degradation and a decrease in large:small ratio of surfactant aggregates in rats.
sPLA2-IIA can exert beneficial action in the context of infectious diseases since recent studies have shown that this enzyme exhibits potent bactericidal effects. Induction of the synthesis of sPLA2-IIA is generally initiated by endotoxin and a limited number of cytokines via paracrine and/or autocrine processes. -
Synonyms
MOM1, PLA2, PLA2B, PLA2L, PLA2S, PLAS1, sPLA2, Phospholipase A2 membrane associated, EC 3.1.1.4, Phosphatidylcholine 2-acylhydrolase, Group IIA phospholipase A2, GIIC sPLA2, Non-pancreatic secretory phospholipase A2, NPS-PLA2, sPLA2-IIA, PLA2G2A.
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Physical Appearance
Filtered lyophilized (freeze-dried) powder.
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Stability
Store lyophilized protein at -20°C. Aliquot the product after reconstitution to avoid repeated freezing/thawing cycles. Reconstituted protein can be stored at 4°C for a limited period of time; it does not show any change after two weeks at 4°C.
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Solubility
It is recommended to add 0.1M Acetate buffer pH-4 to prepare a working stock solution of approximately 0.5mg/ml and let the lyophilized pellet dissolve completely. For conversion into higher pH value, an intensive dilution by relevant buffer to a concentration of 10μg/ml is recomended. In higher concentrations the solubility of the PLA2G2A antigen is limited. Product is not sterile! Please filter the product by an appropriate sterile filter before using it in the cell culture.
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Amino Acid Sequence
MRGSHHHHHH GMASHMNLVN FHRMIKLTTG KEAALSYGFY GCHCGVGGRG SPKDATDRCC VTHDCCYKRL EKRGCGTKFL SYKFSNSGSR ITCAKQDSCR SQLCECDKAA ATCFARNKTT YNKKYQYYSN KHCRGSTPRC.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
PPA2 HumanDescription:
Pyrophosphatase-2 Human Recombinant
PPA2, Pyrophosphatase-2, Inorganic pyrophosphatase 2, mitochondrial, PPase 2, Pyrophosphatase SID6-306, Pyrophosphate phospho-hydrolase 2, HSPC124, Pyrophosphatase (inorganic) 2, SID6-306, Inorganic pyrophosphatase 2, mitochondrial isoform 1.
Product # :
ENZ-815Price :
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Description
PPA2 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 325 amino acids (33-334 a.a) and having a molecular mass of 37.1kDa.PPA2 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
PPA2 protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 10% glycerol, 1mM DTT.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Citations
More Info
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Introduction
PPA2 shares great imagination with members of the inorganic pyrophosphatase (PPase) family. PPA2 is localized to the mitochondrion and owns the signature sequence necessary for the catalytic activity of PPase. PPases catalyze the hydrolysis of pyrophosphate to inorganic phosphate, which is vital for the phosphate metabolism of cells.
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Synonyms
PPA2, Pyrophosphatase-2, Inorganic pyrophosphatase 2, mitochondrial, PPase 2, Pyrophosphatase SID6-306, Pyrophosphate phospho-hydrolase 2, HSPC124, Pyrophosphatase (inorganic) 2, SID6-306, Inorganic pyrophosphatase 2, mitochondrial isoform 1.
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Physical Appearance
Sterile Filtered colorless solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSALYHTEE RGQPCSQNYR LFFKNVTGHY ISPFHDIPLK VNSKEENGIP MKKARNDEYE NLFNMIVEIP RWTNAKMEIA TKEPMNPIKQ YVKDGKLRYV ANIFPYKGYI WNYGTLPQTW EDPHEKDKST NCFGDNDPID VCEIGSKILS CGEVIHVKIL GILALIDEGE TDWKLIAINA NDPEASKFHD IDDVKKFKPG YLEATLNWFR LYKVPDGKPE NQFAFNGEFK NKAFALEVIK STHQCWKALL MKKCNGGAIN CTNVQISDSP FRCTQEEARS LVESVSSSPN KESNEEEQVW HFLGK.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
CKMT2 HumanDescription:
Creatine Kinase, Mitochondrial 2 Human Recombinant
Creatine kinase mitochondrial 2 (sarcomeric), Basic-type mitochondrial creatine kinase, Sarcomeric mitochondrial creatine kinase, creatine kinase S-type, mitochondrial, SMTCK, Mib-CK, EC 2.7.3.2.
Product # :
CKI-276Price :
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Description
CKMT2 Human Recombinant produced in E. coli is a single polypeptide chain containing 405 amino acids (40-419) and having a molecular mass of 46.1 kDa.CKMT2 is fused to a 25 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
The CKMT2 solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.1M NaCl, 1mM DTT and 10% glycerol.
Purity
Greater than 90% as determined by SDS-PAGE.
Citations
More Info
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Introduction
Creatine Kinase, Mitochondrial 2 (CKMT2) is a member of the ATP:guanido phosphotransferase family. CKMT2 is responsible for the transfer of high energy phosphate from mitochondria to the cytosolic carrier, creatine. CKMT2 reversibly catalyzes the transfer of phosphate between ATP and various phosphogens (e.g. creatine phosphate). Creatine kinase isoenzymes have a principal role in energy transduction in tissues with large, variable energy demands, such as skeletal muscle, heart, brain and spermatozoa. Mitochondrial creatine kinase occurs in 2 different oligomeric forms: dimers and octamers, contrary to the exclusively dimeric cytosolic creatine kinase isoenzymes. The CKMT2 gene contains sequences homologous to a number of motifs which are shared among some nuclear genes encoding mitochondrial proteins and therefore may be crucial for the coordinated activation of these genes during mitochondrial biogenesis.
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Synonyms
Creatine kinase mitochondrial 2 (sarcomeric), Basic-type mitochondrial creatine kinase, Sarcomeric mitochondrial creatine kinase, creatine kinase S-type, mitochondrial, SMTCK, Mib-CK, EC 2.7.3.2.
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Physical Appearance
Sterile Filtered colorless solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSHMEVREQ PRLFPPSADY PDLRKHNNCM AECLTPAIYA KLRNKVTPNG YTLDQCIQTG VDNPGHPFIK TVGMVAGDEE SYEVFADLFD PVIKLRHNGY DPRVMKHTTD LDASKITQGQ FDEHYVLSSR VRTGRSIRGL SLPPACTRAE RREVENVAIT ALEGLKGDLA GRYYKLSEMT EQDQQRLIDD HFLFDKPVSP LLTCAGMARD WPDARGIWHN YDKTFLIWIN EEDHTRVISM EKGGNMKRVF ERFCRGLKEV ERLIQERGWE FMWNERLGYI LTCPSNLGTG LRAGVHVRIP KLSKDPRFSK ILENLRLQKR GTGGVDTAAV ADVYDISNID RIGRSEVELV QIVIDGVNYL VDCEKKLERG QDIKVPPPLP QFGKK
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
GSS HumanDescription:
Glutathione Synthetase Human Recombinant
Glutathione synthetase, GSH synthetase, GSH-S, Glutathione synthase, GSHS, MGC14098, GSS.
Product # :
ENZ-021Price :
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Description
GSS Human Recombinant fused with a 20 amino acid His tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 494 amino acids (1-474 a.a.) and having a molecular mass of 54.5kDa. The GSS is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The GSS solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 1mM DTT and 10% glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Citations
More Info
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Introduction
Glutathione synthetase (GSS) is the second enzyme in the glutathione biosynthesis pathway. GSS catalyses the condensation of gamma-glutamylcysteine and glycine to form glutathione. Defects in the GSS are the cause of glutathione synthetase deficiency aka GSS deficiency or 5-oxoprolinuria or pyroglutamic aciduria, which is a severe form characterized by an increased rate of hemolysis and defective function of the central nervous system.
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Synonyms
Glutathione synthetase, GSH synthetase, GSH-S, Glutathione synthase, GSHS, MGC14098, GSS.
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Physical Appearance
Sterile Filtered colorless solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MGSSHHHHQH SSGLVPRGSH MATNWGSLLQ DKQQLEELAR QAVDRALAEG VLLRTSQEPT SSEVVSYAPF TLFPSLVPSA LLEQAYAVQM DFNLLVDAVS QNAAFLEQTL SSTIKQDDFT ARLFDIHKQV LKEGIAQTVF LGLNRSDYMF QRSADGSPAL KQIEINTISA SFGGLASRTP AVHRHVLSVL SKTKEAGKIL SNNPSKGLAL GIAKAWELYG SPNALVLLIA QEKERNIFDQRAIENELLAR NIHVIRRTFE DISEKGSLDQ DRRLFVDGQE IAVVYFRDGY MPRQYSLQNW EARLLLERSH AAKCPDIATQ LAGTKKVQQE LSRPGMLEML LPGQPEAVAR LRATFAGLYS LDVGEEGDQA IAEALAAPSR FVLKPQREGG GNNLYGEEMV QALKQLKDSE ERASYILMEK IEPEPFENCL LRPGSPARVV QCISELGIFG VYVRQEKTLV MNKHVGHLLR TKAIEHADGG VAAGVAVLDN PYPV.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
PYCR2 HumanDescription:
Pyrroline-5-Carboxylate Reductase 2 Human Recombinant
P5CR2, Pyrroline-5-carboxylate reductase 2 isoform 1, P5C reductase 2.
Product # :
ENZ-118Price :
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Description
PYCR2 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 343 amino acids (1-320 a.a) and having a molecular mass of 36kDa.PYCR2 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
PYCR2 protein solution (0.25mg/ml) in phosphate buffered saline (pH7.4), 50% glycerol, 5mM DTT and 1mM EDTA.
Purity
Greater than 85.0% as determined by SDS-PAGE.
Citations
More Info
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Introduction
Pyrroline-5-carboxylate reductase 2 isoform 1 (PYCR2) is a member of the pyrroline-5-carboxylate reductase family. PYCR2 protein catalyzes the conversion of pyrroline-5-carboxylate to proline, which is the last step in proline biosynthesis. The three substrates of the PYCR2 enzyme are L-proline, NAD+, and NADP+, while its four products are 1-pyrroline-5-carboxylate, NADH, NADPH, and H+.
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Synonyms
P5CR2, Pyrroline-5-carboxylate reductase 2 isoform 1, P5C reductase 2.
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Physical Appearance
Sterile Filtered colorless solution.
-
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSMSVGFIG AGQLAYALAR GFTAAGILSA HKIIASSPEM NLPTVSALRK MGVNLTRSNK ETVKHSDVLF LAVKPHIIPF ILDEIGADVQ ARHIVVSCAA GVTISSVEKK LMAFQPAPKV IRCMTNTPVV VQEGATVYAT GTHALVEDGQ LLEQLMSSVG FCTEVEEDLI DAVTGLSGSG PAYAFMALDA LADGGVKMGL PRRLAIQLGA QALLGAAKML LDSEQHPCQL KDNVCSPGGA TIHALHFLES GGFRSLLINA VEASCIRTRE LQSMADQEKI SPAALKKTLL DRVKLESPTV STLTPSSPGK LLTRSLALGG KKD.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
MRM1 HumanDescription:
Mitochondrial RRNA Methyltransferase 1 Human Recombinant
Mitochondrial rRNA methyltransferase 1 homolog, rRNA methyltransferase 1, mitochondrial, Mitochondrial large ribosomal RNA ribose methylase, MRM1.
Product # :
PRO-1416Price :
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Description
MRM1 Human Recombinant produced in E. coli is a single polypeptide chain containing 356 amino acids (21-353) and having a molecular mass of 38.8kDa. MRM1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
The MRM1 solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 30% glycerol, 1mM DTT and 0.1mM PMSF.
Purity
Greater than 90% as determined by SDS-PAGE.
Citations
More Info
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Introduction
Mitochondrial rRNA methyltransferase 1 homolog (MRM1) is a part of the RNA methyltransferase TrmH family. MRM1 methylates the ribose of guanosine G-2270 in the peptidyl transferase center of the mitochondrial large ribosomal RNA (21S).
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Synonyms
Mitochondrial rRNA methyltransferase 1 homolog, rRNA methyltransferase 1, mitochondrial, Mitochondrial large ribosomal RNA ribose methylase, MRM1.
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Physical Appearance
Sterile Filtered colorless solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSSHAARHG ERPGGEELSR LLLDDLVPTS RLELLFGMTP CLLALQAARR SVARLLLQAG KAGLQGKRAE LLRMAEARDI PVLRPRRQKL DTMCRYQVHQ GVCMEVSPLR PRPWREAGEA SPGDDPQQLW LVLDGIQDPR NFGAVLRSAH FLGVDKVITS RRNSCPLTPV VSKSSAGAME VMDVFSTDDL TGFLQTKAQQ GWLVAGTVGC PSTEDPQSSE IPIMSCLEFL WERPTLLVLG NEGSGLSQEV QASCQLLLTI LPRRQLPPGL ESLNVSVAAG ILLHSICSQR KGFPTEGERR QLLQDPQEPS ARSEGLSMAQ HPGLSSGPEK ERQNEG.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
NUDT3 HumanDescription:
Nudix Type Motif 3 Human Recombinant
Diphosphoinositol polyphosphate phosphohydrolase 1, DIPP-1, Diadenosine 5',5'''-P1,P6-hexaphosphate hydrolase 1, Nucleoside diphosphate-linked moiety X motif 3, Nudix motif 3, NUDT3, DIPP, DIPP1.
Product # :
ENZ-071Price :
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Description
NUDT3 Human Recombinant fused with a 20 amino acid His tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 192 amino acids (1-172 a.a.) and having a molecular mass of 21.6kDa. The NUDT3 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The NUDT3 solution (0.5 mg/ml) contains 20mM Tris-HCl buffer (pH8.0), 0.2M NaCl, 5mM DTT and 20% glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Citations
More Info
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Introduction
NUDT3 is a 172 amino acid cytoplasmic protein which is a member of the nudix hydrolase family and DIPP subfamily. NUDT3 functions as a negative regulator of the ERK 1/2 pathway and hydrolyzes 5-phosphoribose 1-diphosphate. NUDT3 is a monomer which binds magnesium as a cofactor. In addition, NUDT3 is widely expressed but can be found at highest levels in the liver, pancreas, brain and heart.
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Synonyms
Diphosphoinositol polyphosphate phosphohydrolase 1, DIPP-1, Diadenosine 5',5'''-P1,P6-hexaphosphate hydrolase 1, Nucleoside diphosphate-linked moiety X motif 3, Nudix motif 3, NUDT3, DIPP, DIPP1.
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Physical Appearance
Sterile Filtered colorless solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MMKLKSNQTR TYDGDGYKKR AACLCFRSES EEEVLLVSSS RHPDRWIVPG GGMEPEEEPS VAAVREVCEE AGVKGTLGRL VGIFENQERK HRTYVYVLIV TEVLEDWEDS VNIGRKREWF KIEDAIKVLQ YHKPVQASYF ETLRQGYSAN NGTPVVATTY SVSAQSSMSG IR.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
SUMF1 HumanDescription:
Sulfatase Modifying Factor 1 Human Recombinant
Sulfatase modifying factor 1, FGE, C-alpha-formylglycine-generating enzyme 1, FGly-generating enzyme, UNQ3037, AAPA3037, EC 1.8.99.
Product # :
PRO-986Price :
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Description
SUMF1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 304 amino acids (91-374 a.a.) and having a molecular mass of 34.1kDa.SUMF1 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
SUMF1 protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH8.0), 2M UREA, 2mM DTT and 20% glycerol.
Purity
Greater than 85% as determined by SDS-PAGE.
Citations
More Info
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Introduction
SUMF1 is a member of the SUMF family. SUMF1 catalyzes the hydrolysis of sulfate esters by oxidizing a cysteine residue in the substrate sulfatase to an active site 3-oxoalanine residue called C-alpha-formylglycine. Alterations in this gene result in multiple sulfatase deficiency which is a lysosomal storage disorder.
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Synonyms
Sulfatase modifying factor 1, FGE, C-alpha-formylglycine-generating enzyme 1, FGly-generating enzyme, UNQ3037, AAPA3037, EC 1.8.99.
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Physical Appearance
Sterile Filtered colorless solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MVPIPAGVFT MGTDDPQIKQ DGEAPARRVT IDAFYMDAYE VSNTEFEKFV NSTGYLTEAE KFGDSFVFEG MLSEQVKTNI QQAVAAAPWW LPVKGANWRH PEGPDSTILH RPDHPVLHVS WNDAVAYCTW AGKRLPTEAE WEYSCRGGLH NRLFPWGNKL QPKGQHYANI WQGEFPVTNT GEDGFQGTAP VDAFPPNGYG LYNIVGNAWE TSDWWTVHH SVEETLNPKG PPSGKDRVKK GGSYMCHRSY CYRYRCAARS QNTPDSSASN LGFRCAADRL PTMD
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
CA1 Human, ActiveDescription:
Carbonic Anhydrase-1 Human Recombinant, BioActive
CA1, CA-I, CAB.
Product # :
ENZ-1137Price :
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Description
CA1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 281 amino acids (1-261) and having a molecular mass of 31.0 kDa. CA1 Humanis fused to a 20 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
CA1 Human protein (1mg/ml) is formulated in 20mM Tris-HCl buffer (pH 8.0) containing 1mM DTT, 10% glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Biological Activity
Specific activity is > 300pmol/min/ug, and is defined as the amount of enzyme that hydrolyze 1.0pmole of 4-nitrophenyl acetate to 4-nitrophenol per minute at pH 8.0 at 37C.
Citations
More Info
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Introduction
CA, also known as carbonic anhydrase is an enzyme. Its main function revolves around the CO2 + H2O HCO3- + H+ (conversion of carbon dioxide to bicarbonate & protons). CA has a zinc ion in its active site. The main function of CA is to keep acid-base balance in the blood stream and various tissues. This enzyme also assists Carbonic Anhydrase I to move CO2 to and from tissues.
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Synonyms
CA1, CA-I, CAB.
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Physical Appearance
Sterile Filtered clear solution.
-
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MASPDWGYDD KNGPEQWSKL YPIANGNNQS PVDIKTSETK HDTSLKPISV SYNPATAKEI INVGHSFHVN FEDNDNRSVL KGGPFSDSYR LFQFHFHWGS TNEHGSEHTV DGVKYSAELH VAHWNSAKYS SLAEAASKAD GLAVIGVLMK VGEANPKLQK VLDALQAIKT KGKRAPFTNF DPSTLLPSSL DFWTYPGSLT HPPLYESVTW IICKESISVS SEQLAQFRSL LSNVEGDNAV PMQHNNRPTQ PLKGRTVRAS F.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
CA13 HumanDescription:
Carbonic Anhydrase XIII Human Recombinant
Carbonic Anhydrase XIII, Carbonate Dehydratase XIII, EC 4.2.1.1, CA-XIII, Carbonic, Anhydrase 13, CAXIII.
Product # :
ENZ-902Price :
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Description
CA13 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 285 amino acids (1-262a.a) and having a molecular mass of 31.8kDa.CA13 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
CA13 protein solution (0.5mg/ml) containing Phosphate buffered saline (pH7.4),10% glycerol and 1mM DTT.
Purity
Greater than 90.0% as determined by SDS-PAGE.
Biological Activity
Specific activity is > 2,500 pmol/min/ug, and is defined as the amount of enzyme that hydrolyze 1.0 pmole of 4-nitrophenyl acetate to 4-nitrophenol per minute at pH 7.5 at 37C.Citations
More Info
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Introduction
Carbonic Anhydrase XIII, also known as CA13 is a member of the alpha-carbonic anhydrase family, which catalyzes the rapid interconversion of carbon dioxide and water tobicarbonate and protons, a reversible reaction which occurs relatively slowly in the absence of catalyst. Furthermore, the active siteof nearly all carbonic anhydrases contains a zinc ion; they have been classified as metalloenzymes. At least fivedistinct CA families (?, ?, ?, ? and ?) have been found. These families have no significant a.a sequence resemblance and in just about allcases are considered to be an example of convergent evolution. The ?-CAs have been demonstrated in humans.
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Synonyms
Carbonic Anhydrase XIII, Carbonate Dehydratase XIII, EC 4.2.1.1, CA-XIII, Carbonic, Anhydrase 13, CAXIII.
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Physical Appearance
Sterile Filtered clear solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks.Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSP MGSMSRLSWG YREHNGPIHW KEFFPIADGD QQSPIEIKTK EVKYDSSLRP LSIKYDPSSA KIISNSGHSF NVDFDDTENK SVLRGGPLTG SYRLRQVHLH WGSADDHGSE HIVDGVSYAA ELHVVHWNSD KYPSFVEAAH EPDGLAVLGV FLQIGEPNSQ LQKITDTLDS IKEKGKQTRF TNFDLLSLLP PSWDYWTYPG SLTVPPLLES VTWIVLKQPI NISSQQLAKF RSLLCTAEGE AAAFLVSNHR PPQPLKGRKV RASFH.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
GMPR2 HumanDescription:
Guanosine Monophosphate Reductase 2 Human Recombinant
GMP reductase 2, Guanosine 5''-monophosphate oxidoreductase 2.
Product # :
ENZ-557Price :
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Description
GMPR2 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 368 amino acids (1-348 a.a.) and having a molecular mass of 40 kDa. GMPR2 is fused to a 20 amino acid His-tag at N-terminus and purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
GMPR2 1mg/ml solution contains 20mM Tris pH-8, 1mM DTT and 10% glycerol.
Purity
Greater than 90% as determined by SDS-PAGE.
Citations
More Info
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Introduction
GMPR2 is the single known metabolic step by which guanine nucleotides can be transformed to the pivotal precursor of both adenine and guanine nucleotides. GMPR2 catalyzes the permanent NADPH-dependent reductive deamination of GMP to IMP, and is involved in re-utilization of free intracellular bases and purine nucleosides.
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Synonyms
GMP reductase 2, Guanosine 5''-monophosphate oxidoreductase 2.
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Physical Appearance
Sterile filtered colorless solution.
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Stability
GMPR2 Human Recombinant although stable at 4°C for 1 week, should be stored below -18°C. Please prevent freeze thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MPHIDNDVKL DFKDVLLRPK RSTLKSRSEV DLTRSFSFRN SKQTYSGVPI IAANMDTVGT FEMAKVLCKF
SLFTAVHKHY SLVQWQEFAG QNPDCLEHLA ASSGTGSSDF EQLEQILEAI PQVKYICLDV ANGYSEHFVE FVKDVRKRFP QHTIMAGNVV
TGEMVEELIL SGADIIKVGI GPGSVCTTRK KTGVGYPQLS AVMECADAAH GLKGHIISDG GCSCPGDVAK AFGAGADFVM LGGMLAGHSE
SGGELIERDG KKYKLFYGMS SEMAMKKYAG GVAEYRASEG KTVEVPFKGD VEHTIRDILG GIRSTCTYVG AAKLKELSRR TTFIRVTQQV
NPIFSEAC.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
CTSD MouseDescription:
Cathepsin-D Mouse Recombinant
Ctsd, CatD, CD, Cathepsin D.
Product # :
ENZ-1017Price :
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Description
CTSD produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 398 amino acids (21-410 a.a.) and having a molecular mass of 44.0kDa (Molecular size on SDS-PAGE will appear at approximately 40-57kDa). CTSD is expressed with an 8 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
CTSD protein solution (0.25mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 10% glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
Biological Activity
Specific activity is > 1,000 pmol/min/ug in which one unit will convert 1.0 pmole of Mca-PLGL-Dpa-AR-NH2 to MCA- Pro-Leu-OH per minute at pH 3.5 at 25C.Citations
More Info
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Introduction
Cathepsin D is synthesized as a 54kDa precursor, which is proteolytically processed to an intermediate 48kDa single chain, which matures into more stable 34kDa and 14kDa two chain form. It is an estrogen-regulated lysosomal protease that has been suggested to facilitate cancer cell migration and invasion by digesting the basement membrane, extracellular matrix, and xonnective tissue. Because of its mitogenic and proteolytic activities, it has been implicated as a prognostic marker in many tumor types. Cathepsin D is expressed in epithelial cells as well as in macrophages.
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Synonyms
Ctsd, CatD, CD, Cathepsin D.
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Physical Appearance
Sterile Filtered colorless solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA). Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
IIRIPLRKFT SIRRTMTEVG GSVEDLILKG PITKYSMQSS PKTTEPVSEL LKNYLDAQYY GDIGIGTPPQ CFTVVFDTGS SNLWVPSIHC KILDIACWVH HKYNSDKSST YVKNGTSFDI HYGSGSLSGY LSQDTVSVPC KSDQSKARGI KVEKQIFGEA TKQPGIVFVA AKFDGILGMG YPHISVNNVL PVFDNLMQQK LVDKNIFSFY LNRDPEGQPG GELMLGGTDS KYYHGELSYL NVTRKAYWQV HMDQLEVGNE LTLCKGGCEA IVDTGTSLLV GPVEEVKELQ KAIGAVPLIQ GEYMIPCEKV SSLPTVYLKL GGKNYELHPD KYILKVSQGG KTICLSGFMG MDIPPPSGPL WILGDVFIGS YYTVFDRDNN RVGFANAVVL LEHHHHHH.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
AIMP1 AntibodyDescription:
Aminoacyl tRNA Synthetase Complex-Interacting Multifunctional Protein 1, Mouse Anti Human
Aminoacyl tRNA synthase complex-interacting multifunctional protein 1, Multisynthase complex auxiliary component p43, AIMP1, EMAP2, SCYE1, p43, EMAPII.
Product # :
ANT-619Price :
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Formulation
1mg/ml containing PBS, pH-7.4, 10% Glycerol and 0.02% Sodium Azide.
Citations
More Info
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Introduction
AIMP1 (EMPA2 or p43) is a cytokine that is specifically induced by apoptosis, and it is involved in the control of angiogenesis, inflammation, and wound healing. The release of the AIMP1 cytokine renders the tumor-associated vasculature sensitive to tumor necrosis factor. Furthermore, AIMP1 is involved in the stimulation of inflammatory responses after proteolytic cleavage in tumor cells.
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Synonyms
Aminoacyl tRNA synthase complex-interacting multifunctional protein 1, Multisynthase complex auxiliary component p43, AIMP1, EMAP2, SCYE1, p43, EMAPII.
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Physical Appearance
Sterile filtered colorless solution.
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Immunogen
Anti-human AIMP1 mAb, is derived from hybridization of mouse F0 myeloma cells with spleen cells from BALB/c mice immunized with a recombinant human AIMP1 protein 1-336 amino acids purified from E. coli.
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Ig Subclass
Mouse IgG2a heavy chain and Kappa light chain.
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Clone
PAT6D10AT.
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Applications
The antibody has been tested by ELISA, Western blot analysis, Flow cytometry and ICC/IF to assure specificity and reactivity. Since application varies, however, each investigation should be titrated by the reagent to obtain optimal results.
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Type
Mouse Anti Human Monoclonal.
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Storage Procedures
For periods up to 1 month store at 4°C, for longer periods of time, store at -20°C. Prevent freeze thaw cycles.
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Purification Method
AIMP1 antibody was purified by protein-A affinity chromatography.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
Esterase D HumanDescription:
Esterase D,S-Formylglutathione Hydrolase Human Recombinant
S-formylglutathione hydrolase, FGH, Esterase D, ESD, FLJ11763, esterase D/formylglutathione hydrolase.
Product # :
ENZ-447Price :
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Description
Esterase-D Human Recombinant fused with a 20 amino acid His tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 302 amino acids (1-282 a.a.) and having a molecular mass of 33.6kDa.The Esterase-D is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The Esterase-D solution contains 20mM Tris-HCl buffer (pH8.0) and 10% glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Citations
More Info
-
Introduction
Formylglutathione hydrolase (Esterase D) is a member of the esterase D family. Esterase D is a serine hydrolase involved in the detoxification of formaldehyde. Esterase D is active toward various substrates including O-acetylated sialic acids, and it may possibly be involved in the recycling of sialic acids. Esterase D is used as a genetic marker for retinoblastoma and Wilson's disease.
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Synonyms
S-formylglutathione hydrolase, FGH, Esterase D, ESD, FLJ11763, esterase D/formylglutathione hydrolase.
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Physical Appearance
Sterile Filtered colorless solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MALKQISSNK CFGGLQKVFE HDSVELNCKM KFAVYLPPKA ETGKCPALYW LSGLTCTEQN FISKSGYHQS ASEHGLVVIA PDTSPRGCNI KGEDESWDFG TGAGFYVDAT EDPWKTNYRM YSYVTEELPQ LINANFPVDP QRMSIFGHSM GGHGALICAL KNPGKYKSVS AFAPICNPVL CPWGKKAFSG YLGTDQSKWK AYDATHLVKS YPGSQLDILI DQGKDDQFLL DGQLLPDNFI AACTEKKIPV VFRLQEDYDH SYYFIATFIT DHIRHHAKYL NA.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
Cyclophilin A HumanDescription:
Cyclophilin-A Human Recombinant
Peptidylprolyl isomerase A, CYPA, CYPH, MGC12404, MGC23397, MGC117158, PPIase A, Rotamase A, PPIA, Peptidyl-prolyl cis-trans isomerase A, EC 5.2.1.8, Cyclophilin A, Cyclosporin A-binding protein.
Product # :
ENZ-359Price :
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Description
Cyclophilin-A Human Recombinant fused with a 20 amino acid His tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 185 amino acids (1-165 a.a.) and having a molecular mass of 20 kDa. PPIase-A is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
1 mg/ml solution containing 20mM Tris-HCl 8.0, 20mM NaCl, 0.5mM DTT and 10% glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Biological Activity
Specific activity is > 650 nmol/min/mg, and is defined as the amount of enzyme that cleaves 1nmole of suc-AAFP-PNA per minute at 37°C in Tris-HCl pH8.0 using chymotrypsin.
Citations
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Introduction
PPIases catalyze the cis-trans isomerization of proline imidic peptide bonds in oligopeptides and accelerate the folding of proteins. Cyclophilin-A is a cyclosporin binding-protein and may play a role in cyclosporin A-mediated immunosuppression. Cyclophilin-A can also interact with several HIV proteins, including p55 gag, Vpr, and capsid protein, and has been shown to be necessary for the formation of infectious HIV virions. Multiple pseudogenes that map to different chromosomes have been reported.
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Synonyms
Peptidylprolyl isomerase A, CYPA, CYPH, MGC12404, MGC23397, MGC117158, PPIase A, Rotamase A, PPIA, Peptidyl-prolyl cis-trans isomerase A, EC 5.2.1.8, Cyclophilin A, Cyclosporin A-binding protein.
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Physical Appearance
Sterile filtered colorless solution.
-
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MVNPTVFFDI AVDGEPLGRV SFELFADKVP KTAENFRALSTGEKGFGYKG SCFHRIIPGF MCQGGDFTRH NGTGGKSIYG EKFEDENFIL KHTGPGILSMANAGPNTNGS QFFICTAKTE WLDGKHVVFG KVKEGMNIVE AMERFGSRNG KTSKKITIADCGQLE.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
IDNK E.ColiDescription:
Thermosensitive Gluconokinase E.Coli Recombinant
Thermosensitive gluconokinase, Gluconate kinase 1, idnK.
Product # :
PKA-060Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
IDNK E.Coli Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 210 amino acids (1-187 a.a) and having a molecular mass of 23.4kDa. IDNK is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
IDNK protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 10% glycerol and 1mM DTT.
Purity
Greater than 95% as determined by SDS-PAGE.
Citations
More Info
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Introduction
Thermosensitive Gluconokinase, also known as IDNK is a 187 a.a protein which is a member of the gluconokinase gntK/gntV family. IDNK catalyzes theconversion of ATP and D-gluconate to ADP and 6-phospho-D-gluconate. In addition, IDNK is considered to take part in gender determination, deletion of the distal portion of 9p is able to lead to a development of male to female sex reversal, the phenotype of a female with a male X, Y genotype.
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Synonyms
Thermosensitive gluconokinase, Gluconate kinase 1, idnK.
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Physical Appearance
Sterile Filtered colorless solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSMAGESFI LMGVSGSGKT LIGSKVAALL SAKFIDGDDL HPAKNIDKMS QGIPLSDEDR LPWLERLNDA SYSLYKKNET GFIVCSSLKK QYRDILRKGS PHVHFLWLDG DYETILARMQ RRAGHFMPVA LLKSQFEALE RPQADEQDIV RIDINHDIAN VTEQCRQAVL AIRQNRICAK EGSASDQRCE.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
FBP1 HumanDescription:
Fructose-1,6-Bisphosphatase 1 Human Recombinant
FBP1, FBP, D-fructose-1,6-bisphosphate 1-phosphohydrolase 1, FBPase 1, Fructose-1,6-bisphosphatase 1.
Product # :
ENZ-454Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
The FBP1 Human recombinant protein is a single, non-glycosilated polypeptide chain produced in E. coli, having a molecular weight of 39kDa and containing 358 amino acids (1-338 a.a.). The FBP1 enzyme is fused to a 20 amino acid His-Tag at N-terminus and purified by proprietary chromatography techniques.
Source
Escherichia Coli.
Formulation
The FBP1 protein solution is formulated in 20mM Tris-HCl pH-8, 1mM DTT and 10% glycerol.
Purity
Greater than 90% as determined by SDS-PAGE.
Citations
More Info
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Introduction
FBP1 is a gluconeogenesis regulatory protein which catalyzes the hydrolysis of fructose 1,6-bisphosphate to fructose 6-phosphate and inorganic phosphate. FBP1 deficiency is associated with hypoglycemia and metabolic acidosis. FBP1 regulates mouse endogenous glucose production. FBP1 coupled with phosphofructokinase (PFK) takes part in the metabolism of pancreatic islet cells.
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Synonyms
FBP1, FBP, D-fructose-1,6-bisphosphate 1-phosphohydrolase 1, FBPase 1, Fructose-1,6-bisphosphatase 1.
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Physical Appearance
Sterile Filtered clear solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MADQAPFDTD VNTLTRFVME EGRKARGTGE LTQLLNSLCT AVKAISSAVR KAGIAHLYGI AGSTNVTGDQ VKKLDVLSND LVMNMLKSSF ATCVLVSEED KHAIIVEPEK RGKYVVCFDP LDGSSNIDCL VSVGTIFGIY RKKSTDEPSE KDALQPGRNL VAAGYALYGS ATMLVLAMDC GVNCFMLDPA IGEFILVDKD VKIKKKGKIY SLNEGYARDF DPAVTEYIQR KKFPPDNSAP YGARYVGSMV ADVHRTLVYG GIFLYPANKK SPNGKLRLLY ECNPMAYVME KAGGMATTGK EAVLDVIPTD IHQRAPVILG SPDDVLEFLK VYEKHSAQ.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
PLA2G2E HumanDescription:
Secreted Phospholipase A2-IIE Human Recombinant
Group IIE secretory phospholipase A2, EC 3.1.1.4, Phosphatidylcholine 2-acylhydrolase GIIE, GIIE sPLA2, sPLA(2)-IIE, sPLA2-IIE, PLA2G2E.
Product # :
ENZ-327Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Secreted Phospholipase A2-IIE Human Recombinant manufactured with N-terminal His-Tag. PLA2G2E His-Tagged Fusion Protein is 15.8 kDa protein containing 123 amino acid residues of the human secreted phospholipase A2-IIE and 16 additional amino acid residues – His-Tag (underlined).
Source
Escherichia Coli.
Formulation
Sterile filtered and lyophilized from 0.5 mg/ml in 0.05M Acetate buffer pH-4.
Purity
Greater than 95% as determined by SDS PAGE.
Citations
More Info
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Introduction
Phospholipase A2 (PLA2) catalyzes the hydrolysis of the sn-2 position of membrane glycerophospholipids to liberate arachidonic acid (AA), a precursor of eicosanoids including prostaglandins and leukotrienes. The same reaction also produces lysophosholipids, which represent another class of lipid mediators.
The secretory PLA2 (sPLA2) family, in which 10 isozymes have been identified, consists of low molecular weight, Ca2+-requiring secretory enzymes that have been implicated in a number of biological processes, such as modification of eicosanoid generation, inflammation, and host defense.This enzyme has been proposed to hydrolyze phosphatidylcholine (PC) in lipoproteins to liberate lyso-PC and free fatty acids in the arterial wall, thereby facilitating the accumulation of bioactive lipids and modified lipoproteins in atherosclerotic foci.
In mice, sPLA2 expression significantly influences HDL particle size and composition and demonstrate that an induction of sPLA2 is required for the decrease in plasma HDL cholesterol in response to inflammatory stimuli. Instillation of bacteria into the bronchi was associated with surfactant degradation and a decrease in large:small ratio of surfactant aggregates in rats. -
Synonyms
Group IIE secretory phospholipase A2, EC 3.1.1.4, Phosphatidylcholine 2-acylhydrolase GIIE, GIIE sPLA2, sPLA(2)-IIE, sPLA2-IIE, PLA2G2E.
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Physical Appearance
Sterile Filtered lyophilized (freeze-dried) powder.
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Stability
Store lyophilized protein at -20°C. Aliquot the product after reconstitution to avoid repeated freezing/thawing cycles. Reconstituted protein can be stored at 4°C for a limited period of time; it does not show any change after two weeks at 4°C.
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Solubility
Add 0.2 ml of 0.1M Acetate buffer pH-4 and let the lyophilized pellet dissolve completely. For conversion into higher pH value, we recommend intensive dilution by relevant buffer to a concentration of 10 μg/ml. In higher concentrations the solubility of this antigen is limited.
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Amino Acid Sequence
MRGSHHHHHH GMASHMNLVQ FGVMIEKMTG KSALQYNDYG CYCGIGGSHW PVDQTDWCCH AHDCCYGRLE KLGCEPKLEK YLFSVSERGI FCAGRTTCQR LTCECDKRAA LCFRRNLGTY NRKYAHYPNK LCTGPTPPC
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
KLK11 HumanDescription:
Kallikrein-11 Human Recombinant
Kallikrein-11, hK11, Hippostasin, Serine protease 20, Trypsin-like protease, Kallikrein-11 inactive chain 1, Kallikrein-11 inactive chain 2, KLK11, PRSS20, TLSP, UNQ649/PRO1279, Kallikrein 11.
Product # :
ENZ-816Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
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Description
KLK11 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 226 amino acids (54-278 a.a) and having a molecular mass of 24.8kDa.
Source
Escherichia Coli.
Formulation
KLK11 protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 10% glycerol and 0.4M Urea.
Purity
Greater than 85.0% as determined by SDS-PAGE.
Citations
More Info
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Introduction
Kallikreins are a subgroup of serine proteases having various physiological functions. Numerous kallikreins are involved in carcinogenesis. Kallikrein-11 (KLK11) which is a multifunctional protease is 1 of the 15 kallikrein subfamily members found in a cluster on chromosome 19. KLK11 cleaves synthetic peptides after arginine but not lysine residues.
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Synonyms
Kallikrein-11, hK11, Hippostasin, Serine protease 20, Trypsin-like protease, Kallikrein-11 inactive chain 1, Kallikrein-11 inactive chain 2, KLK11, PRSS20, TLSP, UNQ649/PRO1279, Kallikrein 11.
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Physical Appearance
Sterile Filtered colorless solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MIIKGFECKP HSQPWQAALF EKTRLLCGAT LIAPRWLLTA AHCLKPRYIV HLGQHNLQKE EGCEQTRTAT ESFPHPGFNN SLPNKDHRND IMLVKMASPV SITWAVRPLT LSSRCVTAGT SCLISGWGST SSPQLRLPHT LRCANITIIE HQKCENAYPG NITDTMVCAS VQEGGKDSC GDSGGPLVCN QSLQGIISWG QDPCAITRKP GVYTKVCKYV DWIQET.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.