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855 results found for “Carbonic Anhydrase”
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Name :
GOR E.ColiDescription:
Glutathione Oxidoreductase E.Coli Recombinant
Glutathione reductase, GR, GRase, gor, b3500, JW3467.
Product # :
ENZ-574Price :
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Shipped with Ice Packs
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Description
GOR E.Coli Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 473 amino acids (1-450) and having a molecular mass of 51.2kDa.GOR is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The GOR solution (1mg/ml) contains 20mM Tris-HCl buffer (pH8.0), 10% glycerol, 0.1M NaCl and 1mM DTT.
Purity
Greater than 90.0% as determined by SDS-PAGE.
Biological Activity
The specific activity is > 52 units/ml.
One unit will reduce 1.0 umol of oxidized glutathione per minute at pH 7.5 at 25°C.Citations
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Introduction
Glutathione reductase (Gor) is a member of the class-I pyridine nucleotide disulfide oxidoreductase family. The main role of the Gor protein is to uphold high levels of reduced glutathione in the cytosol. With the associated oxidation of NADPH, Gor transforms oxidized glutathione to the reduced form. The active site of the Gor protein is a redox-active disulfide bond.
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Synonyms
Glutathione reductase, GR, GRase, gor, b3500, JW3467.
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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 MGSMTKHYDY IAIGGGSGGI ASINRAAMYG QKCALIEAKE LGGTCVNVGC VPKKVMWHAA QIREAIHMYG PDYGFDTTIN KFNWETLIAS RTAYIDRIHT SYENVLGKNN VDVIKGFARF VDAKTLEVNG ETITADHILI ATGGRPSHPD IPGVEYGIDS
DGFFALPALP ERVAVVGAGY IAVELAGVIN GLGAKTHLFV RKHAPLRSFD PMISETLVEV MNAEGPQLHT NAIPKAVVKN TDGSLTLELE DGRSETVDCL IWAIGREPAN DNINLEAAGV KTNEKGYIVV DKYQNTNIEG IYAVGDNTGA VELTPVAVAA GRRLSERLFN NKPDEHLDYS
NIPTVVFSHP PIGTVGLTEP QAREQYGDDQ VKVYKSSFTA MYTAVTTHRQ PCRMKLVCVG SEEKIVGIHG IGFGMDEMLQ GFAVALKMGA TKKDFDNTVA IHPTAAEEFV TMR.
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 :
NDUFA5 HumanDescription:
NADH Dehydrogenase 1 Alpha Subcomplex 5 Human Recombinant
NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 5, Complex I subunit B13, Complex I-13kD-B, CI-13kD-B, NADH-ubiquinone oxidoreductase 13 kDa-B subunit, NDUFA5, B13, NUFM, UQOR13, CI-13kB.
Product # :
ENZ-657Price :
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Description
NDUFA5 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 139 amino acids (1-116) and having a molecular mass of 15.8kDa.NDUFA5 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The NDUFA5 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
NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 5 (NDUFA5) is a member of the complex I NDUFA5 subunit family. The human NDUFA5 gene codes for the B13 subunit of complex I of the respiratory chain that transfers electrons from NADH to ubiquinone. The NDUFA5 protein localizes to the inner mitochondrial membrane as part of the seven component-containing, water soluble 'iron-sulfur protein' (IP) fraction of complex I, even though its exact role is undetermined.
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Synonyms
NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 5, Complex I subunit B13, Complex I-13kD-B, CI-13kD-B, NADH-ubiquinone oxidoreductase 13 kDa-B subunit, NDUFA5, B13, NUFM, UQOR13, CI-13kB.
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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 MGSMAGVLKK TTGLVGLAVC NTPHERLRIL YTKILDVLEE IPKNAAYRKY TEQITNEKLA MVKAEPDVKK LEDQLQGGQL EEVILQAEHE LNLARKMREW KLWEPLVEEP PADQWKWPI.
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 :
NDUFS2 HumanDescription:
Histidine NADH Dehydrogenase Fe-S Protein 2 Human Recombinant
CI-49 , NADH dehydrogenase [ubiquinone] iron-sulfur protein 2, mitochondrial, Complex I-49kD, CI-49kD, NADH-ubiquinone oxidoreductase 49 kDa subunit, NDUFS2.
Product # :
ENZ-737Price :
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Description
NDUFS2 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 410 amino acids (77-463a.a) and having a molecular mass of 46.5kDa. NDUFS2 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The NDUFS2 solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.4M Urea and 10% glycerol.
Purity
Greater than 80% as determined by SDS-PAGE.
Citations
More Info
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Introduction
NDUFS2 is a core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) which is a part of the minimal assembly required for catalysis. Complex I takes part in the transfer of electrons from NADH to the respiratory chain. Histidine NADH Dehydrogenase Fe-S Protein 2 (NDUFS2) is required for catalytic activity. Imperfections in NDUFS2 are the source of complex I mitochondrial respiratory chain deficiency, which is characterized by many symptoms including liver failure, cardiomyopathy and neurodegeneration.
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Synonyms
CI-49 , NADH dehydrogenase [ubiquinone] iron-sulfur protein 2, mitochondrial, Complex I-49kD, CI-49kD, NADH-ubiquinone oxidoreductase 49 kDa subunit, NDUFS2.
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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 MGSVKNITLN FGPQHPAAHG VLRLVMELSG EMVRKCDPHI GLLHRGTEKL IEYKTYLQAL PYFDRLDYVS MMCNEQAYSL AVEKLLNIRP PPRAQWIRVL FGEITRLLNH IMAVTTHALD LGAMTPFFWL FEEREKMFEF YERVSGARMH AAYIRPGGVH QDLPLGLMDD IYQFSKNFSL RLDELEELLT NNRIWRNRTI DIGVVTAEEA LNYGFSGVML RGSGIQWDLR KTQPYDVYDQ VEFDVPVGSR GDCYDRYLCR VEEMRQSLRI IAQCLNKMPP GEIKVDDAKV SPPKRAEMKT SMESLIHHFK LYTEGYQVPP GATYTAIEAP KGEFGVYLVS DGSSRPYRCK IKAPGFAHLA GLDKMSKGHM LADVVAIIGT QDIVFGEVDR.
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 :
LACTB E.Coli, His ActiveDescription:
Beta Lactamase E.Coli Recombinant, His Active
Beta-lactamase, Cephalosporinase, ampC, ampA, b4150, JW4111.
Product # :
ENZ-1033Price :
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Description
LACTB produced in E.Coli is a single, non-glycosylated polypeptide chain containing 379 amino acids (20-377 a.a) and having a molecular mass of 41.8kDa. LACTB is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The LACTB solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0) and 10% glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Biological Activity
Specific activity is >700 units/mg, in which One unit will hydrolyze 1.0umole of Nitrocefin per minute at pH 7.0 at 37°C.
Citations
More Info
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Introduction
Beta-lactamase is a type of enzyme (EC 3.5.2.6) produced by some bacteria that is responsible for their resistance to beta-lactam antibiotics like penicillins, cephalosporins, cephamycins and carbapenems. These antibiotics have a common element in their molecular structure: a four-atom ring known as a beta-lactam. The lactamase enzyme breaks that ring open, deactivating the molecule's antibacterial properties.
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Synonyms
Beta-lactamase, Cephalosporinase, ampC, ampA, b4150, JW4111.
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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 MAPQQINDIV HRTITPLIEQ QKIPGMAVAV IYQGKPYYFT WGYADIAKKQ PVTQQTLFEL GSVSKTFTGV LGGDAIARGE IKLSDPTTKY WPELTAKQWN GITLLHLATY TAGGLPLQVP DEVKSSSDLL RFYQNWQPAW APGTQRLYAN SSIGLFGALA VKPSGLSFEQ AMQTRVFQPL KLNHTWINVP PAEEKNYAWG YREGKAVHVS PGALDAEAYG VKSTIEDMAR WVQSNLKPLD INEKTLQQGI QLAQSRYWQT GDMYQGLGWE MLDWPVNPDS IINGSDNKIA LAARPVKAIT PPTPAVRASW VHKTGATGGF GSYVAFIPEK ELGIVMLANK NYPNPARVDA AWQILNALQ.
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 :
DsbADescription:
Disulfide Oxidoreductase Recombinant
DsbA, Thiol:disulfide interchange protein dsbA.
Product # :
ENZ-276Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Disulfide Oxidoreductase produced in E.Coli is a periplasmic protein isolated from E. coli, containing 208 amino acids having a molecular mass of 23,149 Dalton. The DsbA is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The protein was lyophilized after from a sterile solution containing 50mM sodium phosphate buffer and 100mM sodium chloride.
Purity
Greater than 95.0% as determined by(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Citations
More Info
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Introduction
DsbA appears to be necessary for correct formulation of disulfide bonds in exported proteins in vivo. DsbA is useful as a standard in immunoblotting. This protein catalyses the reduction and exchange of disulfide bonds and the oxidation of free sulfhydryl groups in vitro. It is the strongest oxidant of the thioredoxin superfamily. This thio/disulfide oxidoreductase is required for efficient disulfide bond formation in the periplasm of E. coli.
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Synonyms
DsbA, Thiol:disulfide interchange protein dsbA.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized DsbA although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution DsbA should be stored at 4°C between 2-7 days and for future use below -18°C.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.
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Solubility
It is recommended to reconstitute the lyophilized DsbA in sterile 18MΩ-cm H2O not less than 100 µg/ml, which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
MKKIWLALAGLVLAFSASAAQYEDGKQYTTLEKPVAGAPQVLEFFSFFCPHCYQFEEVLHISDNVKKKLPEGVKMTKYHVNFMGGDLGKDLTQAWAVAMALGVEDKVTVPLFEGVQKTQTIRSASDIRDVFINAGIKGEEYDAAWNSFVVKSLVAQQEKAAADVQLRGVPAMFVNGKYQLNPQGMDTSNMDVFVQQYADTVKYLSEKK
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 :
PPA YeastDescription:
Inorganic Pyrophosphatase Yeast Recombinant
Inorganic pyrophosphatase, PPA.
Product # :
ENZ-1181Price :
Quantity :
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Description
PPA Yeast Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 286 amino acids and having a molecular mass of 35kDa. Inorganic Pyrophosphatase is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Inorganic pyrophosphatase protein solution (100U/ml) containing 20mM Tris-HCl (25℃, pH 8.0), 100mM KCl, 0.1mM EDTA, 1mM DTT and 50% glycerol.
Purity
Greater than 98.0% as determined by SDS-PAGE.
Citations
More Info
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Introduction
Inorganic pyrophosphatase (ppa) is a member of the Ppase family. PPA is an enzyme which catalyzes the conversion of one molecule of pyrophosphate to two phosphate ions. Since this is a highly exergonic reaction, it can therefore be coupled to unfavorable biochemical transformations in order to drive these transformations to completion. The role of the PPA enzyme is a critical one in the lipid metabolism (including lipid synthesis and degradation), calcium absorption and bone formation, DNA synthesis, as well as other biochemical transformations.
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Synonyms
Inorganic pyrophosphatase, PPA.
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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. Do not store at -70C. 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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Unit Definition
Under standard conditions, 1U is defined as the amount of enzyme required to catalyze the hydrolysis of pyrophosphate (PPi)/min. to produce 1μmol of orthophosphate (Pi). Optimal reaction temp. is 25℃ , activity at 16 ~ 37℃. Cofactor: Mg+2
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 :
HMGCS1 HumanDescription:
3-Hydroxy-3-Methylglutaryl-CoA Synthase 1 Human Recombinant
3-Hydroxy-3-Methylglutaryl-CoA Synthase 1 (Soluble), 3-Hydroxy-3-Methylglutaryl-Coenzyme A Synthase 1 (Soluble), 3-Hydroxy-3-Methylglutaryl Coenzyme A (HMG-CoA) Synthase, EC 2.3.3.10, HMGCS, Hydroxymethylglutaryl-CoA Synthase, Cytoplasmic, 3-Hydroxy-3-Methylglutaryl Coenzyme A Synthase, HMG-CoA Synthase.
Product # :
ENZ-870Price :
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Description
HMGCS1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 543 amino acids (1-520 a.a) and having a molecular mass of 59.7kDa.HMGCS1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
HMGCS1 protein solution (0.5mg/ml) containing Phosphate buffered saline (pH7.4), 10% glycerol and 1mM DTT.
Purity
Greater than 80.0% as determined by SDS-PAGE.
Citations
More Info
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Introduction
3-Hydroxy-3-Methylglutaryl-CoA Synthase 1, also known as HMGCS1 is a member of the Belongs to the HMG-CoA synthase family. HMGCS1 condenses acetyl-CoA with acetoacetyl-CoA to form HMG-CoA, which is the substrate for HMG-CoA reductase.
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Synonyms
3-Hydroxy-3-Methylglutaryl-CoA Synthase 1 (Soluble), 3-Hydroxy-3-Methylglutaryl-Coenzyme A Synthase 1 (Soluble), 3-Hydroxy-3-Methylglutaryl Coenzyme A (HMG-CoA) Synthase, EC 2.3.3.10, HMGCS, Hydroxymethylglutaryl-CoA Synthase, Cytoplasmic, 3-Hydroxy-3-Methylglutaryl Coenzyme A Synthase, HMG-CoA Synthase.
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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 MGSMPGSLPL NAEACWPKDV GIVALEIYFP SQYVDQAELE KYDGVDAGKY TIGLGQAKMG FCTDREDINS LCMTVVQNLM ERNNLSYDCI GRLEVGTETI IDKSKSVKTN LMQLFEESGN TDIEGIDTTN ACYGGTAAVF NAVNWIESSS WDGRYALVVA GDIAVYATGN ARPTGGVGAV ALLIGPNAPL IFERGLRGTH MQHAYDFYKP DMLSEYPIVD GKLSIQCYLS ALDRCYSVYC KKIHAQWQKE GNDKDFTLND FGFMIFHSPY CKLVQKSLAR MLLNDFLNDQ NRDKNSIYSG LEAFGDVKLE DTYFDRDVEK AFMKASSELF SQKTKASLLV SNQNGNMYTS SVYGSLASVL AQYSPQQLAG KRIGVFSYGS GLAATLYSLK VTQDATPGSA LDKITASLCD LKSRLDSRTG VAPDVFAENM KLREDTHHLV NYIPQGSIDS LFEGTWYLVR VDEKHRRTYA RRPTPNDDTL DEGVGLVHSN IATEHIPSPA KKVPRLPATA AEPEAAVISN GEH
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 :
LDHBDescription:
Lactate Dehydrogenase B Recombinant
Lactate Dehydrogenase, EC 1.1.1.27, LDH.
Product # :
ENZ-279Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
The DNA encoding chicken LDH-B is cloned from cDNA library of chicken heart.
Source
Escherichia Coli.
Formulation
The protein (1 mg/ml) was lyophilized with 0.1mg potassium phosphate.
Purity
Greater than 95.0% as determined by:(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
The specific activity was found to be 258 U/mg protein.Citations
More Info
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Introduction
Lactate dehydrogenase (LDH) is an enzyme(EC1.1.1.27) present in a wide variety of organisms, including plants and animals.
A tetrameric enzyme that catalyses the interconversion of pyruvateand lactate with concomitant interconversion of NADH and NAD+. At high concentrations of pyruvate, the enzyme exhibits feedback inhibition and the rate of conversion of pyruvate to lactate is decreased. In vertebrates, genes for three different subunits (LDH-A, LDH-B and LDH-C) exist. -
Synonyms
Lactate Dehydrogenase, EC 1.1.1.27, LDH.
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Physical Appearance
Sterile lyophilized powder.
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Stability
Lyophilized Lactate Dehydrogenase although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution LDH should be stored at 4°C between 2-7 days and for future use below -18°C.Please prevent freeze-thaw cycles.
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Solubility
It is recommended to reconstitute the lyophilized LDH in sterile 18MΩ-cm H2O not less than 100 µg/ml, which can then be further diluted to other aqueous solutions.
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Unit Definition
One unit is defined as 1umol of NAD+ production per minute under the assay conditions (25°C, pH 7.0). Both transaminase activities include a-hydroxyglutarate dehydrogenase activity.
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 :
ALDH5A1 HumanDescription:
Aldehyde Dehydrogenase 5 A1 Human Recombinant
Succinate-semialdehyde dehydrogenase mitochondrial, Aldehyde dehydrogenase family 5 member A1, NAD(+)-dependent succinic semialdehyde dehydrogenase, ALDH5A1, SSADH, SSDH.
Product # :
ENZ-567Price :
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Shipped with Ice Packs
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Description
ALDH5A1 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 509 amino acids (48-535 a.a.) and having a molecular mass of 54.6kDa. The ALDH5A1 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The ALDH5A1 solution (0.5 mg/ml) contains 20mM Tris-HCl buffer(pH 8.0), 10% glycerol
1mM DTT, 0.1M NaCl and 1mM EDTA.Purity
Greater than 90.0% as determined by SDS-PAGE.
Citations
More Info
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Introduction
ALDH5A1 is a mitochondrial NAD(+)-dependent succinic semialdehyde dehydrogenase, which is a member of the aldehyde dehydrogenase family of proteins. The ALDH5A1 protein functions as a mediator to the NADP+-dependent oxidation of aldehydes into acids and has an imperative role in the detoxification of alcohol-derived acetaldehyde, as well as in lipid peroxidation and in the metabolism of corticosteroids, biogenic amines and neurotransmitters. ALDH5A1 is expressed in various tissues, including the liver, heart, lung, brain, kidney and placenta. Deficiency in the ALDH5A1 enzyme, known as 4-hydroxybutyricaciduria, is a rare inborn error in the metabolism of the neurotransmitter 4-aminobutyric acid (GABA). In response to this defect, physiologic fluids from patients accumulate GHB, which is a compound with numerous neuromodulatory properties.
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Synonyms
Succinate-semialdehyde dehydrogenase mitochondrial, Aldehyde dehydrogenase family 5 member A1, NAD(+)-dependent succinic semialdehyde dehydrogenase, ALDH5A1, SSADH, SSDH.
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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 MAGRLAGLSA ALLRTDSFVG GRWLPAAATF PVQDPASGAA LGMVADCGVR EARAAVRAAY EAFCRWREVS AKERSSLLRK WYNLMIQNKD DLARIITAES GKPLKEAHGE ILYSAFFLEW FSEEARRVYG DIIHTPAKDR RALVLKQPIG VAAVITPWNF PSAMITRKVG AALAAGCTVV VKPAEDTPFS ALALAELASQ AGIPSGVYNV IPCSRKNAKE VGEAICTDPL VSKISFTGST TTGKILLHHA ANSVKRVSME LGGLAPFIVF DSANVDQAVA GAMASKFRNT GQTCVCSNQF LVQRGIHDAF VKAFAEAMKK NLRVGNGFEE GTTQGPLINE KAVEKVEKQV NDAVSKGATV VTGGKRHQLG KNFFEPTLLC NVTQDMLCTH EETFGPLAPV IKFDTEEEAI AIANAADVGL AGYFYSQDPA QIWRVAEQLE VGMVGVNEGL ISSVECPFGG VKQSGLGREG SKYGIDEYLE LKYVCYGGL.
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 :
HMGCL Human, Sf9Description:
3-Hydroxymethyl-3-Methylglutaryl-CoA Lyase Human Recombinant, Sf9
3-Hydroxymethyl-3-Methylglutaryl-CoA Lyase, 3-Hydroxymethyl-3-Methylglutaryl-Coenzyme A Lyase, 3-Hydroxy-3-Methylglutarate-CoA Lyase, Hydroxymethylglutaricaciduria, HMG-CoA Lyase, EC 4.1.3.4, HL, Mitochondrial 3-Hydroxy-3-Methylglutaryl-CoA Lyase, Hydroxymethylglutaryl-CoA Lyase, Mitochondrial, 3-Hydroxy-3-Methylglutaryl-CoA Lyase, Hydroxymethylglutaryl-CoA lyase, mitochondrial, HMG-CoA lyase, 3-hydroxy-3-methylglutarate-CoA lyase.
Product # :
ENZ-1056Price :
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Description
HMGCL Human Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 305 amino acids (28-325 a.a.) and having a molecular mass of 32.5kDa (Molecular size on SDS-PAGE will appear at approximately 28-40kDa). HMGCL is expressed with a 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
HMGCL protein solution (1mg/ml) contains Phosphate Buffered Saline (pH 7.4), 20% glycerol and 1mM DTT.
Purity
Greater than 90.0% as determined by SDS-PAGE.
Citations
More Info
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Introduction
Hydroxymethylglutaryl-CoA lyase (HMGCL) is a mitochondrial matrix protein which is a member of the HMG-CoA lyase family. HMGCL is a homodimer and participates in leucine catabolism and ketogenesis, the hepatic synthesis of ketone bodies which, during fasting, provides a major source of energy for the heart, brain and kidney. More precisely, HMGCL catalyzes the final step of these processes, the cleavage of 3-hydroxy-3-methylglutaryl-CoA to acetoacetic acid and acetyl-CoA.
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Synonyms
3-Hydroxymethyl-3-Methylglutaryl-CoA Lyase, 3-Hydroxymethyl-3-Methylglutaryl-Coenzyme A Lyase, 3-Hydroxy-3-Methylglutarate-CoA Lyase, Hydroxymethylglutaricaciduria, HMG-CoA Lyase, EC 4.1.3.4, HL, Mitochondrial 3-Hydroxy-3-Methylglutaryl-CoA Lyase, Hydroxymethylglutaryl-CoA Lyase, Mitochondrial, 3-Hydroxy-3-Methylglutaryl-CoA Lyase, Hydroxymethylglutaryl-CoA lyase, mitochondrial, HMG-CoA lyase, 3-hydroxy-3-methylglutarate-CoA lyase.
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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.
-
Amino Acid Sequence
MTLPKRVKIV EVGPRDGLQN EKNIVSTPVK IKLIDMLSEA GLSVIETTSF VSPKWVPQMG DHTEVLKGIQ KFPGINYPVL TPNLKGFEAA VAAGAKEVVI FGAASELFTK KNINCSIEES FQRFDAILKA AQSANISVRG YVSCALGCPY EGKISPAKVA EVTKKFYSMG CYEISLGDTI GVGTPGIMKD MLSAVMQEVP LAALAVHCHD TYGQALANTL MALQMGVSVV DSSVAGLGGC PYAQGASGNL ATEDLVYMLE GLGIHTGVNL QKLLEAGNFI CQALNRKTSS KVAQATCKLH HHHHH.
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 :
HPD HumanDescription:
4-Hydroxyphenylpyruvate Dioxygenase Human Recombinant
4HPPD, GLOD3, 4-HPPD, PPD, HPPDase, Glyoxalase Domain Containing 3, 4-HydroxyphenylpYruvate Dioxygenase.
Product # :
ENZ-015Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
HPD produced in E.Coli is a single, non-glycosylated polypeptide chain containing 413 amino acids (1-393a.a.) and having a molecular mass of 47kDa.HPD is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The HPD protein solution (1mg/1ml) is formulated in 20mM Tris-HCl buffer (pH 8.0) 1mM DTT, 50mM NaCl and 20% glycerol.
Purity
Greater than 90% as determined by SDS-PAGE.
Citations
More Info
-
Introduction
4-Hydroxyphenylpyruvate Dioxygenase Isoform-1 is an Fe-containing enzyme, which catalyzes the second reaction in the catabolism of tyrosine the conversion of 4-hydroxyphenylpyruvate to homogentisate. Present as a homodimer, HPD uses zinc as a cofactor to catalyze the third step in the conversion of L-phenylalanine to fumarate and acetoacetic acid. Flaws in the gene encoding HPD result in tyrosinemia type 3 and hawkinsinuria, two inborn defects of metabolism which are related to a number of symptoms, like mental retardation and seizures and hair and urine abnormalities.
-
Synonyms
4HPPD, GLOD3, 4-HPPD, PPD, HPPDase, Glyoxalase Domain Containing 3, 4-HydroxyphenylpYruvate Dioxygenase.
-
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.
-
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MTTYSDKGAK PERGRFLHFH SVTFWVGNAK QAASFYCSKM GFEPLAYRGL ETGSREVVSH VIKQGKIVFV LSSALNPWNK EMGDHLVKHG DGVKDIAFEV EDCDYIVQKA RERGAKIMRE PWVEQDKFGK VKFAVLQTYG DTTHTLVEKM NYIGQFLPGY EAPAFMDPLL PKLPKCSLEM IDHIVGNQPD QEMVSASEWY LKNLQFHRFW SVDDTQVHTE YSSLRSIVVA NYEESIKMPI NEPAPGKKKS QIQEYVDYNG GAGVQHIALK TEDIITAIRH LRERGLEFLS VPSTYYKQLR EKLKTAKIKV KENIDALEEL KILVDYDEKG YLLQIFTKPV QDRPTLFLEV IQRHNHQGFG AGNFNSLFKA FEEEQNLRGN LTNMETNGVV PGM
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 :
IDO1 Human, ActiveDescription:
Indoleamine 2,3-Dioxygenase 1 Human Recombinant, Active
IDO, IDO-1, INDO, Indoleamine 2,3-dioxygenase 1, Indoleamine-pyrrole 2,3-dioxygenase.
Product # :
ENZ-1012Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
IDO1 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 426 amino acids (1-403a.a) and having a molecular mass of 47.7kDa. IDO1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The IDO1 solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 20% glycerol and 1mM DTT.
Purity
Greater than 90% as determined by SDS-PAGE.
Biological Activity
Specific activity is > 300 pmol/min/ug, and is defined as the amount of enzyme that hydrolyze 1.0 pmole of L-Tryptophan to N-formyl-Lkynurenine per minute at pH 6.5 at 25C.Citations
More Info
-
Introduction
Indoleamine 2,3-Dioxygenase 1 (IDO1) catalyzes the primary and rate-limiting stage in tryptophan catabolism to N-formyl-kynurenine. IDO1 affects on various tryptophan substrates including D-tryptophan, and serotonin and is expressed in dendritic cells, monocytes, and macrophages. IDO1 takes part in a range of pathophysiological processes like neuropathology, antimicrobial and antitumor defense, immunoregulation, and antioxidant activity. IDO1 regulates T-cell behavior by its pericellular catabolization of the necessary amino acid tryptophan.
-
Synonyms
IDO, IDO-1, INDO, Indoleamine 2,3-dioxygenase 1, Indoleamine-pyrrole 2,3-dioxygenase.
-
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.
-
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSMAHAMEN SWTISKEYHI DEEVGFALPN PQENLPDFYN DWMFIAKHLP DLIESGQLRE RVEKLNMLSI DHLTDHKSQR LARLVLGCIT MAYVWGKGHG DVRKVLPRNI AVPYCQLSKK LELPPILVYA DCVLANWKKK DPNKPLTYEN MDVLFSFRDG DCSKGFFLVS LLVEIAAASA IKVIPTVFKA MQMQERDTLL KALLEIASCL EKALQVFHQI HDHVNPKAFF SVLRIYLSGW KGNPQLSDGL VYEGFWEDPK EFAGGSAGQS SVFQCFDVLL GIQQTAGGGH AAQFLQDMRR YMPPAHRNFL CSLESNPSVR EFVLSKGDAG LREAYDACVK ALVSLRSYHL QIVTKYILIP ASQQPKENKT SEDPSKLEAK GTGGTDLMNF LKTVRSTTEK SLLKEG.
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 :
FARS2 HumanDescription:
Phenylalanyl-tRNA Synthetase 2 Human Recombinant
Phenylalanyl-tRNA synthetase mitochondrial, Phenylalanine--tRNA ligase, PheRS, FARS2, FARS1, HSPC320, dJ520B18.2.
Product # :
ENZ-111Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
FARS2 produced in E.Coli is a single, non-glycosylated polypeptide chain containing 436 amino acids (37-451 a.a.) and having a molecular mass of 50.6kDa.FARS2 is fused to a 21 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
FARS2 solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 1mM DTT, 30% glycerol, 1mM EDTA and 0.1M NaCl.
Purity
Greater than 90.0% as determined by SDS-PAGE.
Citations
More Info
-
Introduction
Phenylalanyl-tRNA synthetase 2 mitochondrial (FARS2) is a member of the class II aminoacyl- tRNA synthetase family. FARS2 is a mitochondrial matrix protein. FARS2 when acting as a monomer, catalyzes the ATP-dependent conversion of L-phenylalanine and tRNA (Phe) to L-phenlalanyltRNA (Phe), an event which is vital for proper translation and protein expression.
-
Synonyms
Phenylalanyl-tRNA synthetase mitochondrial, Phenylalanine--tRNA ligase, PheRS, FARS2, FARS1, HSPC320, dJ520B18.2.
-
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.
-
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MPAAECATQR APGSVVELLG KSYPQDDHSN LTRKVLTRVG RNLHNQQHHP LWLIKERVKE HFYKQYVGRF GTPLFSVYDN LSPVVTTWQN FDSLLIPADH PSRKKGDNYY LNRTHMLRAH TSAHQWDLLH AGLDAFLVVG DVYRRDQIDS QHYPIFHQLE AVRLFSKHEL FAGIKDGESL QLFEQSSRSA HKQETHTMEA VKLVEFDLKQ TLTRLMAHLF GDELEIRWVD CYFPFTHPSF EMEINFHGEW LEVLGCGVME QQLVNSAGAQ DRIGWAFGLG LERLAMILYD IPDIRLFWCE DERFLKQFCV SNINQKVKFQ PLSKYPAVIN DISFWLPSEN YAENDFYDLV RTIGGDLVEK VDLIDKFVHP KTHKTSHCYR ITYRHMERTL SQREVRHIHQ ALQEAAVQLL GVEGRF.
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 :
PGD Human, ActiveDescription:
Phosphogluconate Dehydrogenase, Active Human Recombinant
EC 1.1.1.44, 6PGD, PGDH, 6-phosphogluconate dehydrogenase decarboxylating, PGD.
Product # :
ENZ-1128Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
PGD Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 503 amino acids (1-483) and having a molecular mass of 55.3 kDa.PGD Human is fused to a 20 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The PGD solution (1mg/ml) contains 10% Glycerol, 1mM DTT, 0.1M NaCl, and 20mM Tris-HCl buffer (pH 8.0).
Purity
Greater than 90.0% as determined by SDS-PAGE.
Biological Activity
Specific activity is > 10unit/mg. One unit will oxidize 1.0 umole of 6-phospho-D-gluconate to D-ribulose 5- phosphate per minute at pH 8.0 at 25˚C, in the presence of beta-NADP.
Citations
More Info
-
Introduction
6PGD is the 2nd dehydrogenase in the pentose phosphate shift. Pentose is crucial for the biosynthesis of nucleic acid. The pentose phosphate cycle is a prominent source of NADPH. 6PGD deficiency is mostly asymptomatic, and the inheritance of this deasis is autosomal dominant. PGD deficiency elevate the erythrocyte pyruvate kinase levels of activity & decreases glutathione synthetase, which causes hemolysis.
-
Synonyms
EC 1.1.1.44, 6PGD, PGDH, 6-phosphogluconate dehydrogenase decarboxylating, PGD.
-
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.
-
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MAQADIALIG LAVMGQNLIL NMNDHGFVVC AFNRTVSKVD DFLANEAKGT KVVGAQSLKE MVSKLKKPRR IILLVKAGQA VDDFIEKLVP LLDTGDIIID GGNSEYRDTT RRCRDLKAKG ILFVGSGVSG GEEGARYGPS LMPGGNKEAW PHIKTIFQGI AAKVGTGEPC CDWVGDEGAG HFVKMVHNGI EYGDMQLICE AYHLMKDVLG MAQDEMAQAF EDWNKTELDS FLIEITANIL KFQDTDGKHL LPKIRDSAGQ KGTGKWTAIS ALEYGVPVTL IGEAVFARCL SSLKDERIQA SKKLKGPQKF QFDGDKKSFL EDIRKALYAS KIISYAQGFM LLRQAATEFG WTLNYGGIAL MWRGGCIIRS VFLGKIKDAF DRNPELQNLL LDDFFKSAVE NCQDSWRRAV STGVQAGIPM PCFTTALSFY DGYRHEMLPA SLIQAQRDYF GAHTYELLAK PGQFIHTNWT GHGGTVSSSS YNA
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 :
GLA HumanDescription:
Alpha-Galactosidase Human Recombinant
Alpha-galactosidase A, Alpha-D-galactosidase A, Alpha-D-galactoside galactohydrolase, Melibiase, GLA, GALA.
Product # :
ENZ-926Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
GLA produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 406 amino acids (32-429 a.a.) and having a molecular mass of 46.4kDa GLA is expressed with an 8 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
GLA protein solution (0.5mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 10% glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
Citations
More Info
-
Introduction
Alpha-galactosidase A (GLA) is a homodimeric glycoprotein which hydrolyses the terminal alpha-galactosyl moieties from glycolipids and glycoproteins. GLA catalyzes the hydrolysis of melibiose into galactose and glucose. Various mutations in the GLA gene affect the synthesis, processing, and stability of this enzyme, which causes Fabry disease (a rare lysosomal storage disorder which results from a failure to catabolize alpha-D-galactosyl glycolipid moieties).
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Synonyms
Alpha-galactosidase A, Alpha-D-galactosidase A, Alpha-D-galactoside galactohydrolase, Melibiase, GLA, GALA.
-
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.
-
Amino Acid Sequence
LDNGLARTPT MGWLHWERFM CNLDCQEEPD SCISEKLFME MAELMVSEGW KDAGYEYLCI DDCWMAPQRD SEGRLQADPQ RFPHGIRQLA NYVHSKGLKL GIYADVGNKT CAGFPGSFGY YDIDAQTFAD WGVDLLKFDG CYCDSLENLA DGYKHMSLAL NRTGRSIVYS CEWPLYMWPF QKPNYTEIRQ YCNHWRNFAD IDDSWKSIKS ILDWTSFNQE RIVDVAGPGG WNDPDMLVIG NFGLSWNQQV TQMALWAIMA APLFMSNDLR HISPQAKALL QDKDVIAINQ DPLGKQGYQL RQGDNFEVWE RPLSGLAWAV AMINRQEIGG PRSYTIAVAS LGKGVACNPA CFITQLLPVK RKLGFYEWTS RLRSHINPTG TVLLQLENTM QMSLKDLLVE HHHHHH.
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 :
Collagen-III BovineDescription:
Bovine Collagen-III
Product # :
PRO-2731Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Mouse Collagen-III is a natural protein purified from washed dissected tissue into dilute acetic acid. Collagen-I is purified by proprietary chromatographic techniques.
Source
Bovine washed dissected tissue.
Formulation
Collagen-III was lyophilized without additives.
Purity
> 90.0%.
Citations
More Info
-
Introduction
Collagen, a major component of the extracellular matrix, is a fibrous protein that provides tensile strength to tissues giving them structural integrity. Collagen and its derivative, gelatin, have been widely used in medical, pharmaceutical and consumer products for more than 100 years. The supply of these materials, created from animal remains, is both abundant and inexpensive. However, most formulations are not highly purified and have the potential to cause an inflammatory reaction in some product users. In addition, concerns have been raised over the last several years about the potential for contamination of bovine products with the agent that causes mad cow disease and its human variant, Creutzfeldt-Jakob Disease. Animal collagens are subject to extensive modifications that continue over the life of the molecule in the extracellular space. These differences influence both the extractability of collagens from tissue and the biophysical characteristics of these collagens. As a result, collagens isolated from tissues exhibit significant lot-to-lot variability and, as bulk materials, are often analytically intractable. Products that contain animal-derived collagen can induce potentially harmful inflammatory or immune responses in humans and pose risk of contamination with viruses or prions, potentially life-threatening pathogens. Recombinant collagens are essentially identical to the native collagen protein thereby reducing the risk of inflammation, immune response, and disease as compared to animal-sourced collagen.
-
Physical Appearance
Filtered White lyophilized (freeze-dried) powder.
-
Stability
Lyophilized Collagen-III although stable at room temperature for 3 weeks, should be stored desiccated below -18C. Upon reconstitution Collagen-III should be stored at 4C between 2-7 days and for future use below -18C.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.
-
Solubility
It is recommended to add 20 mM acetic acid to prepare a working stock solution of 1-5 mg/ml, which can then be further diluted to other aqueous solutions. Suspension should be shaken or stirred for several hours or overnight between 2-8°C.
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 :
ASMT HumanDescription:
Acetylserotonin O-Methyltransferase Human Recombinant
HIOMT, HIOMTY, Acetylserotonin O-methyltransferase , Hydroxyindole O-methyltransferase , ASMT.
Product # :
ENZ-664Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
ASMT Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 318 amino acids (1-298 a.a) and having a molecular mass of 35.3kDa.ASMT is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The ASMT solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0) , 1M Urea and 10% glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
Citations
More Info
-
Introduction
ASMT is a member of the methyltransferase superfamily. ASMT participates in melatonin biosynthesis. ASMT Expressed in brain, retina and pineal gland, ASMT utilities to catalyze the final reaction in the synthesis of melatonin, particularly the conversion of S-adenosyl-L-methionine and N-acetylserotonin to S-adenosyl-Lhomocysteine and melatonin.
-
Synonyms
HIOMT, HIOMTY, Acetylserotonin O-methyltransferase , Hydroxyindole O-methyltransferase , ASMT.
-
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.
-
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSSEDQAYR LLNDYANGFM VSQVLFAACE LGVFDLLAEA PGPLDVAAVA AGVRASAHGT ELLLDICVSL KLLKVETRGG KAFYRNTELS SDYLTTVSPT SQCSMLKYMG RTSYRCWGHL ADAVREGRNQ YLETFGVPAE ELFTAIYRSE GERLQFMQAL QEVWSVNGRS VLTAFDLSVF PLMCDLGGDF FKDPLPEADL YILARVLHDW ADGKCSHLLE RIYHTCKPGG GILVIESLLD EDRRGPLLTQ LYSLNMLVQT EGQERTPTHY HMLLSSAGFR DFQFKKTGAI YDAILARK
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 :
UBE2D2 HumanDescription:
Ubiquitin Conjugating Enzyme E2D2 Human Recombinant
Ubiquitin-conjugating enzyme E2D 2 (homologous to yeast UBC4/5), UBC4, Ubiquitin carrier protein D2, Ubiquitin-conjugating enzyme E2-17 kDa 2, Ubiquitin-protein ligase D2, UBCH5B, EC 6.3.2.19, E2(17)KB2, PUBC1, UBC4/5, UBC5B, UBCH4.
Product # :
ENZ-1036Price :
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Description
UBE2D2 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 147 amino acids (1-147) and having a molecular mass of 16.7kDa. The UBE2D2 is purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
The UBE2D2 solution (0.5mg/ml) contains 20mM MES (pH6.0), 50mM NaCl and 1mM DTT.
Purity
Greater than 95% as determined by SDS-PAGE.
Citations
More Info
-
Introduction
UBE2D2 belongs to the E2 ubiquitin-conjugating enzyme family. UBE2D2 takes part in the ubiquitination of the tumor-suppressor protein p53, which is induced by an E3 ubiquitin-protein ligase. UBE2D2 catalyzes ubiquitination of IkB-alpha in a SCFB-TRCP and phosphorylation dependent method.
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Synonyms
Ubiquitin-conjugating enzyme E2D 2 (homologous to yeast UBC4/5), UBC4, Ubiquitin carrier protein D2, Ubiquitin-conjugating enzyme E2-17 kDa 2, Ubiquitin-protein ligase D2, UBCH5B, EC 6.3.2.19, E2(17)KB2, PUBC1, UBC4/5, UBC5B, UBCH4.
-
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.
-
Amino Acid Sequence
MALKRIHKEL NDLARDPPAQ CSAGPVGDDM FHWQATIMGP NDSPYQGGVF FLTIHFPTDY PFKPPKVAFT TRIYHPNINS NGSICLDILR SQWSPALTIS KVLLSICSLL CDPNPDDPLV PEIARIYKTD REKYNRIARE WTQKYAM.
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 :
UBE2W HumanDescription:
Ubiquitin Conjugating Enzyme E2W Human Recombinant
Probable ubiquitin-conjugating enzyme E2 W, Ubiquitin carrier protein W, Ubiquitin-protein ligase W, UBE2W, hUBC-16, FLJ11011.
Product # :
ENZ-117Price :
Quantity :
Shipping Method :
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Description
UBE2W produced in E.Coli is a single, non-glycosylated polypeptide chain containing 171 amino acids (1-151 a.a.) and having a molecular mass of 19.5kDa.UBE2W is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
UBE2W solution (1mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 10% glycerol, 2mM DTT and 0.1M NaCl.
Purity
Greater than 90.0% as determined by SDS-PAGE.
Citations
More Info
-
Introduction
UBE2W receives ubiquitin from the E1 complex and catalyzes its covalent attachment to other proteins. In vitro, UBE2W catalyzes monoubiquitination and 'Lys-11'-linked polyubiquitination. UBE2W is broadly expressed, particularly at highest levels in the testis.
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Synonyms
Probable ubiquitin-conjugating enzyme E2 W, Ubiquitin carrier protein W, Ubiquitin-protein ligase W, UBE2W, hUBC-16, FLJ11011.
-
Physical Appearance
Sterile filtered colorless solution.
-
Stability
UBE2W Human Recombinant although stable at 4°C for 1 week, should be stored below -18°C. Please prevent freeze thaw cycles.
-
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MASMQKRLQK ELLALQNDPP PGMTLNEKSV QNSITQWIVD MEGAPGTLYE GEKFQLLFKF SSRYPFDSPQ VMFTGENIPV HPHVYSNGHI CLSILTEDWS PALSVQSVCL SIISMLSSCK EKRRPPDNSF YVRTCNKNPK KTKWWYHDDT C.
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 :
HK1/2/3 AntibodyDescription:
Hexokinase-1/2/3, Mouse Anti Human
Hexokinase-3, EC 2.7.1.1, Hexokinase type III, HK III, HXK3, HK3.
Product # :
ANT-726Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Formulation
1mg/ml containing PBS, pH-7.4, 10% Glycerol and 0.02% Sodium Azide.
Citations
More Info
-
Introduction
Hexokinases phosphorylate glucose to produce glucose-6-phosphate, thus committing glucose to the glycolytic pathway. HK3 encodes hexokinase 3. Similar to hexokinases 1 and 2, this allosteric enzyme is inhibited by its product glucose-6-phosphate. Hexokinase3 lacks the hydrophobic N-terminal sequence critical for targeting to mitochondria. Hexpkinase3 may have anabolic functions, providing H6P for glycogen or lipid synthesis.
-
Synonyms
Hexokinase-3, EC 2.7.1.1, Hexokinase type III, HK III, HXK3, HK3.
-
Physical Appearance
Sterile filtered colorless solution.
-
Immunogen
Anti-human HK1/2/3mAb, is derived from hybridization of mouse F0 myeloma cells with spleen cells from BALB/c mice immunized with recombinant human HK1/2/3amino acids 1-923 purified from E. coli.
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Ig Subclass
Mouse IgG1 heavy chain and κ light chain.
-
Clone
PAT4C12AT.
-
Applications
HK1/2/3antibody has been tested by ELISA and Western blot analysis to assure specificity and reactivity. Since application varies, however, each investigation should be titrated by the reagent to obtain optimal results.
-
Type
Mouse Anti Human Monoclonal.
-
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.
-
Purification Method
HK1/2/3 antibody was purified from mouse ascitic fluids 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 :
ACPP Human, Sf9Description:
Acid Phosphatase Prostate, Human Recombinant, sf9
Acid Phosphatase, Prostate, Thiamine Monophosphatase, Ecto-5-Nucleotidase, 5-Nucleotidase, EC 3.1.3.2, TMPase, 5-NT, Prostatic Acid Phosphatase, Prostatic Acid Phosphotase, EC 3.1.3.5, ACP-3 , ACP3, PAP.
Product # :
ENZ-968Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
ACPP produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 360 amino acids (33-386 a.a.) and having a molecular mass of 41.8kDa (Migrates at 40-57kDa on SDS-PAGE under reducing conditions). ACPP is expressed with a 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
ACPP protein solution (0.5mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 10% glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Citations
More Info
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Introduction
Acid phosphatase, prostate (ACPP) is a non-specific tyrosine phosphatase, which dephosphorylates a varied number of substrates under acidic conditions (pH 4-6) including alkyl, aryl, and acyl orthophosphate monoesters and phosphorylated proteins. ACPP has lipid phosphatase activity and inactivates lysophosphatidic acid in seminal plasma.
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Synonyms
Acid Phosphatase, Prostate, Thiamine Monophosphatase, Ecto-5-Nucleotidase, 5-Nucleotidase, EC 3.1.3.2, TMPase, 5-NT, Prostatic Acid Phosphatase, Prostatic Acid Phosphotase, EC 3.1.3.5, ACP-3 , ACP3, PAP.
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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
KELKFVTLVF RHGDRSPIDT FPTDPIKESS WPQGFGQLTQ LGMEQHYELG EYIRKRYRKF LNESYKHEQV YIRSTDVDRT LMSAMTNLAA LFPPEGVSIW NPILLWQPIP VHTVPLSEDQ LLYLPFRNCP RFQELESETL KSEEFQKRLH PYKDFIATLG KLSGLHGQDL FGIWSKVYDP LYCESVHNFT LPSWATEDTM TKLRELSELS LLSLYGIHKQ KEKSRLQGGV LVNEILNHMK RATQIPSYKK LIMYSAHDTT VSGLQMALDV YNGLLPPYAS CHLTELYFEK GEYFVEMYYR NETQHEPYPL MLPGCSPSCP LERFAELVGP VIPQDWSTEC MTTNSHQGTE DSTDHHHHHH.
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 :
ALPP Human, ActiveDescription:
Alkaline Phosphatase Placental Human Recombinant, BioActive
3 ALPP, Alkaline phosphatase Regan isozyme, Placental alkaline phosphatase 1, PLAP-1, ALP, PLAP, Alkaline phosphatase placental type, EC 3.1.3.1, PLAP-1, Alkaline phosphatase Regan isozyme.
Product # :
ENZ-1133Price :
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Description
ALPP Human produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 494 amino acids (23-506 a.a.) and having a molecular mass of 53.9kDa. ALPP is expressed with a 10 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
ALPP protein solution (0.5mg/ml) containing Phosphate-Buffered Saline (pH 7.4) and 10% glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Biological Activity
Specific activity is > 2,500unit/mg, and is defined as the amount of enzyme that hydrolyze 1.0nmole of pnitrophenyl phosphate (pNPP) per minute at pH 7.5 at 37C.
Citations
More Info
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Introduction
Placental alkaline phosphatase also known as PLAP is a membranal siaglycoprotein enzyme typicallyfoundin high concentration in syncytiotrophoblasts in the placenta amid the 3th trimester of gestation. The expression of PLAP was at firstconsidered to be onlyin the term placenta, though, a human PLAP-like variant has been found,thathas more than 85% homology with PLAP itself. PLAP is expressed strictly in normal term placenta, endocervix & fallopian tube and in ovarian and proximal gastrointestinal tumors. It is also widely expressed in germ cell tumors and more recently found in seminomas.
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Synonyms
3 ALPP, Alkaline phosphatase Regan isozyme, Placental alkaline phosphatase 1, PLAP-1, ALP, PLAP, Alkaline phosphatase placental type, EC 3.1.3.1, PLAP-1, Alkaline phosphatase Regan isozyme.
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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
ADLMIIPVEE ENPDFWNREA AEALGAAKKL QPAQTAAKNL IIFLGDGMGV STVTAARILK GQKKDKLGPE LPLAMDRFPY VALSKTYNVD KHVPDSGATA TAYLCGVKGN FQTIGLSAAA RFNQCNTTRG NEVISVMNRA KKAGKSVGVV TTTRVQHASP AGTYAHTVNR NWYSDADVPA SARQEGCQDI ATQLISNMDI DVILGGGRKY MFRMGTPDPE YPDDYSQGGT RLDGKNLVQE WLAKRQGARY VWNRTELMQA SLDPSVTHLM GLFEPGDMKY EIHRDSTLDP SLMEMTEAAL RLLSRNPRGF FLFVEGGRID HGHHESRAYR ALTETIMFDD AIERAGQLTS EEDTLSLVTA DHSHVFSFGG YPLRGSSIFG LAPGKARDRK AYTVLLYGNG PGYVLKDGAR PDVTESESGS PEYRQQSAVP LDEETHAGED VAVFARGPQA HLVHGVQEQT FIAHVMAFAA CLEPYTACDL APPAGTTDHH HHHH.
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 :
ARSA Mouse, ActiveDescription:
Arylsulfatase A Mouse Recombinant, Active
Arylsulfatase A, Arsa, As-2, AS-A, As2, ASA, AW212749, TISP73.
Product # :
ENZ-1088Price :
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Shipped with Ice Packs
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Description
ARSA Mouse Recombinant produced in Sf9 is a single, glycosylated polypeptide chain containing 498 amino acids (18-506) and having a molecular mass of 53.2kDa (Molecular size on SDS-PAGE will appear at approximately 50-70kDa).ARSA Mouse is fused to an 9 amino acid His-Tag at C-terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
ARSA protein solution (0.5mg/ml) containing Phosphate Buffered Saline (pH 7.4) and 10% glycerol.
Purity
Greater than 95% as determined by SDS-PAGE.
Citations
More Info
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Introduction
Arylsulfatase A (ARSA) hydrolyzes cerebrosidesulfate to cerebroside and sulfate. ARSA is inhibited by phosphate. The phosphate develops a covalent bond with the active site 3-oxoalanine. ARSA gene defects cause metachromatic leucodystrophy (MLD), a progressive demyelination disease which results in various neurological symptoms and ultimately death.
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Synonyms
Arylsulfatase A, Arsa, As-2, AS-A, As2, ASA, AW212749, TISP73.
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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
ADPSPPNILL IFADDLGYGD LGSYGHPSST TPNLDQLAEG GLRFTDFYVP VSLCTPSRAA LLTGRLPVRSGMYPGVLGPS SQGGLPLEEVTLAEVLAARG YLTGMAGKWH LGVGPEGAFL PPHQGFHRFL GIPYSHDQGP CQNLTCFPPD IPCKGGCDQG LVPIPLLANL TVEAQPPWLPGLEARYVSFS RDLMADAQRQ GRPFFLYYAS HHTHYPQFSG QSFTKRSGRG PFGDSLMELD GAVGALMTTV GDLGLLEETL VIFTADNGPELMRMSNGGCSGLLRCGKGTT FEGGVREPAL VYWPGHITPG VTHELASSLD LLPTLAALTG APLPNVTLDG VDISPLLLGT GKSPRKSVFFYPPYPDEIHG VFAVRNGKYK AHFFTQGSAH SDTTSDPACH AANRLTAHEP PLLYDLSQDP GENYNVLESI EGVSPEALQA LKHIQLLKAQYDAAMTFGPS QIAKGEDPAL QICCQPSCTP HPVCCHCPGS QSHHHHHH.
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 :
ALDH3A1 HumanDescription:
Aldehyde Dehydrogenase 3 Family Member A1 Human Recombinant
Aldehyde dehydrogenase 3 family member A1, aldehyde dehydrogenase, dimeric NADP-preferring, ALDH-3, aldehyde dehydrogenase isozyme, ALDHIII, MGC104062, aldehyde dehydrogenase type III, Aldehyde dehydrogenase, stomach aldehyde dehydrogenase, EC 1.2.1.53, aldehyde dehydrogenase 3A, Aldehyde dehydrogenase.
Product # :
ENZ-479Price :
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Shipped with Ice Packs
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Description
ALDH3A1 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 473 amino acids (1-453 a.a.) and having a molecular mass of 52.5 kDa. ALDH3A1 is fused to a 20 amino acid His Tag at N-terminus and purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
ALDH3A1 solution containing 20mM Tris-HCl pH-8, 0.1M NaCl and 10% glycerol.
Purity
Greater than 95% as determined by SDS-PAGE.
Biological Activity
Specific activity was found to be < 1 units/ml. Activity was obtained by measuring the increase of NADP in absorbance at 340 nm resulting from the reduction of NAD. 1 unit will oxidize 1umole of acetaldehyde to acetic acid per minute at pH 8 at 25°C in the presence of beta-NAD, potassium and thiols.Citations
More Info
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Introduction
ALDH3A1 is involved in the detoxification of alcohol-derived acetaldehyde. ALDH3A1 participates in the metabolism of corticosteroids, biogenic amines, neurotransmitters, and lipid peroxidation. ALDH3A1 oxidizes aromatic aldehyde substrates and toxic aldehydes. ALDH3A1 forms a cytoplasmic homodimer that oxidizes aromatic and medium-chain saturated and unsaturated aldehyde substrates. ALDH3A1 promotes resistance to UV and 4-hydroxy-2-nonenal-induced oxidative damage in the cornea.
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Synonyms
Aldehyde dehydrogenase 3 family member A1, aldehyde dehydrogenase, dimeric NADP-preferring, ALDH-3, aldehyde dehydrogenase isozyme, ALDHIII, MGC104062, aldehyde dehydrogenase type III, Aldehyde dehydrogenase, stomach aldehyde dehydrogenase, EC 1.2.1.53, aldehyde dehydrogenase 3A, Aldehyde dehydrogenase.
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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 MSKISEAVKR ARAAFSSGRT RPLQFRIQQL EALQRLIQEQ EQELVGALAA DLHKNEWNAY YEEVVYVLEE IEYMIQKLPE WAADEPVEKT PQTQQDELYI HSEPLGVVLV IGTWNYPFNL TIQPMVGAIA AGNAVVLKPS ELSENMASLL ATIIPQYLDK DLYPVINGGV PETTELLKER FDHILYTGST GVGKIIMTAA AKHLTPVTLE LGGKSPCYVD KNCDLDVACR RIAWGKFMNS GQTCVAPDYI LCDPSIQNQI VEKLKKSLKE FYGEDAKKSR DYGRIISARH FQRVMGLIEG QKVAYGGTGD AATRYIAPTI LTDVDPQSPV MQEEIFGPVLPIVCVRSLEE AIQFINQREK PLALYMFSSN DKVIKKMIAE TSSGGVAAND VIVHITLHSL PFGGVGNSGM GSYHGKKSFE TFSHRRSCLV RPLMNDEGLK VRYPPSPAKM TQH.
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.