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  • Ankyrin Repeat Domain

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  • Aprotinin

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  • Transferrin

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  • Anti Coagulation Factors

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  • Natural Albumin

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  • Anti Mouse Lymphocyte

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Search results

1000 results found for “Aldolase”

Name

Description

Product #

Price

Quantity

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  • View Data Sheet

    Name :

    Taq Plus DNA

    Description:

    Taq Plus DNA Polymerase Recombinant

    Taq Plus DNA Polymerase, Taq Plus DNA, TaqPDNA.

    Product # :

    ENZ-309

    Price :

    Quantity :

    Shipping Method :

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    Description

    Taq Plus is a mixture of Taq and Pfu. Taq Plus, which is used to improve the reliability and yield of conventional primer extension reaction. Taq Plus has two following advantages over Taq: (1) high fidelity with an error frequency 1.6/106 (or 0.0016/103) during DNA synthesis. (2) Taq Plus increases the efficiency of polymerization reaction, resulting in a great percentage of extenuation reaction completion up to 10 kb to 30 kb. Pfu has a temperature optimum between 72-78°C and remains > 95% active following 1-hour incubation at 95°C.

    Source

    Recombinant E.coli contains Thermus aquaticus polymerase gene.

    Formulation

    5U/µl.

    Citations

    More Info

    • Synonyms

      Taq Plus DNA Polymerase, Taq Plus DNA, TaqPDNA.

    • Stability

      Stable for 5 days at 10°C, for longer period of time store at -20°C.

    • Optimization of DNA Synthesis

      It is important to ad the reaction components in the following order1. H2O.2. 10 x reaction buffer.3. dNTPs.4. DNA template and primers.5. Taq Plus.

    • Reaction Conditions

      DNA synthesis is performed in 100?l of mixture containing 20-200μm dNTPs, 0.3-1μm Promers, 0.1-0.250 mg of template DNA, 10 ?l of 10 x reaction buffer and 2.5-5 units of Taq Plus. Mix the reaction gently, centrifuge briefly and then overlay with light mineral oil. Initially, denature the reaction by incubating at 95? for 5 minutes and then cool to 40-68? for 5 minutes to allow the primers to anneal to the template DNA.

    • Storage Buffer

      20mM Tris-HCl (pH 8.0), 1mM DTT, 0.1mM EDTA, 100mM KCl, Stabilizers, and 50%glycerol.

    • Note

      All reagents, including Taq Plus, should be mixed immediately before use.

    • Unit Definition

      One unit of the enzyme catalyzes the incorporation of 10nmole of deoxyribonucleotides into a polynucleotide fraction in 30 min at 74°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.

    Taq Plus Dna
  • View Data Sheet

    Name :

    HBsAg adr CHO

    Description:

    Hepatitis B Surface Antigen, adr CHO Recombinant

    Product # :

    HBS-875

    Price :

    Quantity :

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    Description

    Recombinant HBsAg adr produced in CHO cells, the molecular weight is approximately 23-27kDa.

    Source

    CHO.

    Formulation

    Sterile Filtered solution containing 20mM PB and 154mM NaCl.

    Purity

    Greater than 95.0% as determined by RP-HPLC.

    Citations

    More Info

    • Introduction

      HBsAg is the surface antigen of the Hepatitis-B-Virus (HBV) S-gene. The capsid of a virus has different surface proteins from the rest of the virus. The antigen is a protein that binds specifically on one of these surface proteins. It is commonly referred to as the Australian Antigen.

    • Physical Appearance

      Sterile Filtered clear solution.

    • Stability

      HBsAg Should be stored at 4°C, DO NOT FREEZE.

    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.

    Hbsag Adr Cho
  • View Data Sheet

    Name :

    Esterase D Human

    Description:

    Esterase D,S-Formylglutathione Hydrolase Human Recombinant

    S-formylglutathione hydrolase, FGH, Esterase D, ESD, FLJ11763, esterase D/formylglutathione hydrolase.

    Product # :

    ENZ-447

    Price :

    Quantity :

    Shipping Method :

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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.

    • Synonyms

      S-formylglutathione hydrolase, FGH, Esterase D, ESD, FLJ11763, esterase D/formylglutathione hydrolase.

    • 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 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.

    Esterase D Human
  • View Data Sheet

    Name :

    Phosphotransacetylase

    Description:

    Phosphotransacetylase Bacillus S. Recombinant

    Phosphate Acetyltransferase, EC 2.3.1.8, Phosphotransacetylase, phosphoacylase.

    Product # :

    ENZ-1205

    Price :

    Quantity :

    Shipping Method :

    Room Temp Icon

    Shipped at Room temp

    Add To Cart

    More Info

    • description
    • source
    • formulation
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    • Citations

    Description

    Phosphotransacetylase Bacillus Stearothermophilus Recombinant produced in E.Coli is a single, non glycosylated polypeptide chain containing 325 amino acids and having a total molecular mass of 34.7kDa.
    Phosphotransacetylase Recombinant is purified by proprietary chromatographic techniques.

    Source

    E.Coli

    Formulation

    The protein was lyophilized with 0.15M NaCl and 20mM Tris pH-8.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Biological Activity

    Phosphotransacetylase activity is assessed by using the DTNB spectrophotometric method which was found to be greater than 3,000 Units/mg.

    Citations

    More Info

    • Introduction

      Phosphotransacetylase (PTA) is a metabolic enzyme (EC 2.3.1.8) that catalyzes the reversible conversion: acetyl-CoA + Pi ⇄ acetyl-phosphate + CoA. The reversible reaction of acetyl-CoA to acetate node and back, is useful in R&D and biotech assays such as Metabolic engineering, Synthetic biology, Production of biopolymers, Enzymatic synthesis of acetyl-phosphate, bacterial signaling
      and Fermentation.  Phosphotransacetylase controls acetate formation and manipulates acetyl-CoA flux thus is widely used in protein expression, metabolic engineering, and synthetic pathways.

    • Synonyms

      Xylosyltransferase 2, Peptide O-xylosyltransferase 1, Xylosyltransferase II, XT-II, XylT-II, XYLT2, XT2.

    • Physical Appearance

      Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized Phosphate Acetyltransferase although stable at room temperature for 3 weeks, should be stored desiccated below -18C. Upon reconstitution Phosphate Acetyltransferase 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 reconstitute the lyophilized Phosphate Acetyltransferase in
      sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be
      further diluted to other aqueous solutions.

    • Amino Acid Sequence

      TTDLFTALKA KVTGTARKIV FPEGTDDRIL TAASRLATEQ VLQPIVLGDE QAIRVKAAAL GLPLEGVEIV NPRRYGGFDE LVSAFVERRK GKVTEETARE LLFDENYFGT MLVYMGAADG LVSGAAHSTA DTVRPALQII KTKPGVGKTS GVFIMVRGDE KYVFADCAIN IAPNSQDLAE IAVESARTAK MFGLKPRVAL LSFSTKGSAS SPETEKVVEA VRLAKEMAPD LILDGEFQFD AAFVPEVAKK KAPDSVIQGD ANVFIFPSLE AGNIGYKIAQ RLGGFEAVGP ILQGLNKPVN DLSRGCSAED AYKLALITAA QSLGE

    • Unit Definition

      1 unit will convert 1umole of Coenzyme A to acetyl coenzyme A /min/pH-7.5/30˚C using acetyl phosphate as substrate

    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.

    Phosphotransacetylase
  • View Data Sheet

    Name :

    ACY1 Human

    Description:

    Aminoacylase-1 Human Recombinant

    N-acyl-L-amino-acid amidohydrolase, ACY-1, ACY1D, ACYLASE, ACY1,EC 3.5.1.143.

    Product # :

    ENZ-296

    Price :

    Quantity :

    Shipping Method :

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    More Info

    • description
    • source
    • formulation
    • purity
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    • Citations

    Description

    ACY1 Recombinant Human produced in E.Coli is a single, non-glycosylated polypeptide chain containing 428 amino acids (1-408 a.a.) and having a molecular mass of 48kDa. The ACY1 is fused to a 20 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The ACY1 solution (0.5mg/ml) containing 20mM Tris-HCl pH-8, 1mM DTT & 10% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      Aminoacylase-1 is a cytosolic, homodimeric, zinc-binding enzyme that catalyzes the hydrolysis of acylated L-amino acids to L-amino acids and acyl group, and has been postulated to function in the catabolism and salvage of acylated amino acids. ACY1 has been assigned to chromosome 3p21.1, a region reduced to homozygosity in small-cell lung cancer (SCLC), and its expression has been reported to be reduced or undetectable in SCLC cell lines and tumors. The amino acid sequence of human aminoacylase-1 is highly homologous to the porcine counterpart, and ACY1 is the first member of a new family of zinc-binding enzymes.

    • Synonyms

      N-acyl-L-amino-acid amidohydrolase, ACY-1, ACY1D, ACYLASE, ACY1,EC 3.5.1.143.

    • 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 MTSKGPEEEH PSVTLFRQYL RIRTVQPKPD YGAAVAFFEE TARQLGLGCQ KVEVAPGYVV TVLTWPGTNP TLSSILLNSH TDVVPVFKEH WSHDPFEAFK DSEGYIYARG AQDMKCVSIQ YLEAVRRLKV EGHRFPRTIH MTFVPDEEVG GHQGMELFVQ
      RPEFHALRAG FALDEGIANP TDAFTVFYSE RSPWWVRVTS TGRPGHASRF MEDTAAEKLH KVVNSILAFR EKEWQRLQSN PHLKEGSVTS VNLTKLEGGV AYNVIPATMS ASFDFRVAPD VDFKAFEEQL QSWCQAAGEG VTLEFAQKWM HPQVTPTDDS NPWWAAFSRV CKDMNLTLEP EIMPAATDNR YIRAVGVPAL GFSPMNRTPV LLHDHDERLH EAVFLRGVDI YTRLLPALAS VPALPSDS.

    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.

    Acy1 Human
  • View Data Sheet

    Name :

    MVD Human

    Description:

    Mevalonate Decarboxylase Human Recombinant

    Diphosphomevalonate decarboxylase, Mevalonate (diphospho)decarboxylase, MDDase, Mevalonate pyrophosphate decarboxylase, MVD, MPD, FP17780.

    Product # :

    ENZ-226

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    Description

    MVD Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 420 amino acids (1-400) and having a molecular mass of 45.6kDa.MVD is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    The MVD solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH8.0), 20% glycerol and 1mM DTT.

    Purity

    Greater than 85% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      Diphosphomevalonate decarboxylase (MVD) catalyzes the conversion of mevalonate pyrophosphate into isopentenyl pyrophosphate in one of the early steps in cholesterol biosynthesis. MVD decarboxylates and dehydrates its substrate while hydrolyzing ATP. MVD is expressed in the heart, skeletal muscle, lung, liver, brain, pancreas, kidney and placenta.

    • Synonyms

      Diphosphomevalonate decarboxylase, Mevalonate (diphospho)decarboxylase, MDDase, Mevalonate pyrophosphate decarboxylase, MVD, MPD, FP17780.

    • 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 MASEKPLAAV TCTAPVNIAV IKYWGKRDEE LVLPINSSLS VTLHQDQLKT TTTAVISKDF TEDRIWLNGR EEDVGQPRLQ ACLREIRCLA RKRRNSRDGD PLPSSLSCKV HVASVNNFPT AAGLASSAAG YACLAYTLAR VYGVESDLSE VARRGSGSAC RSLYGGFVEW QMGEQADGKD SIARQVAPES HWPELRVLIL VVSAEKKLTG STVGMRASVE TSPLLRFRAE SVVPARMAEM ARCIRERDFP SFAQLTMKDS NQFHATCLDT FPPISYLNAI SWRIIHLVHR FNAHHGDTKV AYTFDAGPNA VIFTLDDTVA EFVAAVWHGF PPGSNGDTFL KGLQVRPAPL SAELQAALAM EPTPGGVKYI IVTQVGPGPQ ILDDPCAHLL GPDGLPKPAA.

    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.

    Mvd Human
  • View Data Sheet

    Name :

    CKMB Human

    Description:

    Creatine Kinase MB Human Recombinant

    CKMB, CK-MB 

     

    Product # :

    CKI-286

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    Description

    Recombinant Human Creatine Kinase MB produced in E.Coli is a single, non-glycosylated, polypeptide chain, having a molecular weight of ~44kDa.The CKMB is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The protein solution contains 50mM Tris-HCL, 5mM B-mercaptoethanol, 1mM EDTA, 5mM disodium Succinate, Ph 8.0 and 50% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      The three isoenzymes (MM, MB, and BB) are found in muscle, cardiac and brain tissues. These recombinant proteins are ideal for calibrating diagnostic instruments and researching neuromuscular diseases. Creatine Kinases can be used for indications in many neuromuscular applications. These disorders include cardiac disease, mitochondrial disorders, inflammatory myopathies, myasthenia, polymyositis, McArdle's disease, NMJ disorders, muscular dystrophy, ALS, hypo and hyperthyroid disorders, central core disease, acid maltase deficiency, myoglobinuria, rhabdomyolysis, motor neuron diseases, rheumatic diseases, and other that create elevated or reduced levels of Creatine Kinases.

    • Physical Appearance

      Sterile Filtered colorless liquid formulation.

    • Stability

      CKMB although stable at 10°C for 7 days, should be stored below -18°C.Please prevent freeze-thaw cycles.

    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.

    ckmb-protein
  • View Data Sheet

    Name :

    CTSZ Mouse, Active

    Description:

    Cathepsin-Z, Active Mouse Recombinant

    Cathepsin Z, Cathepsin X, Cysteine-Type Carboxypeptidase, Lysosomal Carboxypeptidase B, Carboxypeptidase LB, Cathepsin B2, Cathepsin IV, Cathepsin Z1, Cathepsin P, Cathepsin Y, EC 3.4.18.1, Preprocathepsin P, CTSX.

    Product # :

    ENZ-1108

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    Description

    CTSZ Mouse Recombinant produced in Baculovirus is a single, glycosylated, polypeptide chain containing 292 amino acids (23-306 aa) and having a molecular mass of 32.8kDa.CTSZ is fused to a 8 amino acid His tag at C-terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    The CTSZ solution (0.5 mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 10% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Biological Activity

    Specific activity is > 3,000 pmol/min/ug. One unit will convert 1 pmole of Mca-PLGL-Dpa-AR-NH2 to MCA- Pro-Leu-OH per minute at pH 3.5 at 25°C.

    Citations

    More Info

    • Introduction

      Cathepsin-Z (CTSZ) is a lysosomal cysteine proteinase and a member of the peptidase C1 family. CTSZ, which is known also as cathepsin X and cathepsin P, exhibits carboxy-monopeptidase and carboxy-dipeptidase activities. CTSZ is expressed ubiquitously in cancer cell lines and primary tumors and as other members of this family, takes part in tumorigenesis.

    • Synonyms

      Cathepsin Z, Cathepsin X, Cysteine-Type Carboxypeptidase, Lysosomal Carboxypeptidase B, Carboxypeptidase LB, Cathepsin B2, Cathepsin IV, Cathepsin Z1, Cathepsin P, Cathepsin Y, EC 3.4.18.1, Preprocathepsin P, CTSX.

    • 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

      ARARLYFRSG QTCYHPIRGD QLALLGRRTY PRPHEYLSPA DLPKNWDWRN VNGVNYASVT
      RNQHIPQYCG SCWAHGSTSA MADRINIKRK GAWPSILLSV QNVIDCGNAG SCEGGNDLPV
      WEYAHKHGIP DETCNNYQAK DQDCDKFNQC GTCTEFKECH TIQNYTLWRV GDYGSLSGRE
      KMMAEIYANG PISCGIMATE MMSNYTGGIY AEHQDQAVIN HIISVAGWGV SNDGIEYWIV
      RNSWGEPWGE KGWMRIVTST YKGGTGDSYN LAIESACTFG DPIVLEHHHH HH

    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.

    Cathepsin Z Mouse
  • View Data Sheet

    Name :

    ENTPD3 Human, sf9

    Description:

    Ectonucleoside Triphosphate Diphosphohydrolase 3 Human Recombinant, sf9

    Ectonucleoside Triphosphate Diphosphohydrolase 3, CD39L3, Ecto-ATP Diphosphohydrolase 3, CD39 Antigen-Like 3, Ecto-ATPDase 3, Ecto-Apyrase 3, Ecto-ATPase 3, EC 3.6.1.5, NTPDase 3, HB6, NTPDase-3.

    Product # :

    ENZ-958

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    Description

    ENTPD3 Human Recombinant produced in in Sf9 Baculovirus cells is a single, non-glycosylated polypeptide chain containing 451 amino acids (44-485a.a) and having a molecular mass of 50.7kDa (Migrates at 50-70kDa on SDS-PAGE under reducing conditions). ENTPD3 is fused to a 6 amino acids His-tag at C-Terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    ENTPD3 protein solution (0.5mg/ml) containing Phosphate Buffered Saline (pH 7.4) and 10% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      Ectonucleoside Triphosphate Diphosphohydrolase 3, also known as ENTPD3, which owns a threefold preference for the hydrolysis of ATP over ADP is similar to E-type nucleotidases (NTPases). ENTPD3 is a protein coding gene which contains four apyrase-conserved areas which is characteristic of NTPases.

    • Synonyms

      Ectonucleoside Triphosphate Diphosphohydrolase 3, CD39L3, Ecto-ATP Diphosphohydrolase 3, CD39 Antigen-Like 3, Ecto-ATPDase 3, Ecto-Apyrase 3, Ecto-ATPase 3, EC 3.6.1.5, NTPDase 3, HB6, NTPDase-3.

    • 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

      ADLQIHKQEV LPPGLKYGIV LDAGSSRTTV YVYQWPAEKE NNTGVVSQTF KCSVKGSGIS SYGNNPQDVP RAFEECMQKV KGQVPSHLHG STPIHLGATA GMRLLRLQNE TAANEVLESI QSYFKSQPFD FRGAQIISGQ EEGVYGWITA NYLMGNFLEK NLWHMWVHPH GVETTGALDL GGASTQISFV AGEKMDLNTS DIMQVSLYGY VYTLYTHSFQ CYGRNEAEKK FLAMLLQNSP TKNHLTNPCY PRDYSISFTM GHVFDSLCTV DQRPESYNPN DVITFEGTGD PSLCKEKVAS IFDFKACHDQ ETCSFDGVYQ PKIKGPFVAF AGFYYTASAL NLSGSFSLDT FNSSTWNFCS QNWSQLPLLL PKFDEVYARS YCFSANYIYH LFVNGYKFTE ETWPQIHFEK EVGNSSIAWS LGYMLSLTNQ IPAESPLIRL PIEPPHHHHHH.

    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.

    Entpd3 Human Sf9
  • View Data Sheet

    Name :

    HK2 Human

    Description:

    Hexokinase-2 Human Recombinant

    Hexokinase-2, EC 2.7.1.1, HK2, Hexokinase type II, HK II, Muscle form hexokinase, HXK2, DKFZp686M1669.

    Product # :

    PKA-227

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    Description

    HK2 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain (aa 1-917) fused to a 20 His tag at the N-terminal encoding the sequence of 937 amino acids in total and having a molecular mass of 104.1 kDa.HXK2 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The protein (1mg/ml) contains 20mM Tris-HCl pH8.0 and 10% glycerol.

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

    Biological Activity

    Specific activity is 3-4 units/ml obtained by measuring the increase of NADPH in absorbance at 340 nm resulting from the reduction of NADP. In the coupled mode, one unit will produce 1.0 umole of NADPH per minute as glucose is phosphorylated by ATP at pH 7.4 at 30C.

    Citations

    More Info

    • Introduction

      Hexokinases phosphorylate glucose to produce glucose-6-phosphate, thus committing glucose to the glycolytic pathway. Hexokinase 2 is the predominant form found in skeletal muscle. It localizes to the outer membrane of mitochondria. Expression of this gene is insulin-responsive, and studies in rat suggest that it is involved in the increased rate of glycolysis seen in rapidly growing cancer cells.

    • Synonyms

      Hexokinase-2, EC 2.7.1.1, HK2, Hexokinase type II, HK II, Muscle form hexokinase, HXK2, DKFZp686M1669.

    • 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). Please avoid freeze-thaw cycles.

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MIASHLLAYF FTELNHDQVQ KVDQYLYHMR LSDETLLEIS KRFRKEMEKG LGATTHPTAA VKMLPTFVRS TPDGTEHGEF LALDLGGTNF RVLWVKVTDN GLQKVEMENQ IYAIPEDIMR GSGTQLFDHI AECLANFMDK LQIKDKKLPL GFTFSFPCHQTKLDESFLVS WTKGFKSSGV EGRDVVALIR KAIQRRGDFD IDIVAVVNDT VGTMMTCGYD DHNCEIGLIV GTGSNACYME EMRHIDMVEG DEGRMCINME WGAFGDDGSL NDIRTEFDQE IDMGSLNPGK QLFEKMISGM YMGELVRLIL VKMAKEELLF GGKLSPELLN TGRFETKDISDIEGEKDGIR KAREVLMRLG LDPTQEDCVA THRICQIVST RSASLCAATL AAVLQRIKENKGEERLRSTI GVDGSVYKKH PHFAKRLHKT VRRLVPGCDV RFLRSEDGSG KGAAMVTAVAYRLADQHRAR QKTLEHLQLS HDQLLEVKRR MKVEMERGLS KETHASAPVK MLPTYVCATPDGTEKGDFLA LDLGGTNFRV LLVRVRNGKW GGVEMHNKIY AIPQEVMHGT GDELFDHIVQ CIADFLEYMG MKGVSLPLGF TFSFPCQQNS LDESILLKWT KGFKASGCEG EDVVTLLKEA IHRREEFDLD VVAVVNDTVG TMMTCGFEDP HCEVGLIVGT GSNACYMEEM RNVELVEGEE GRMCVNMEWG AFGDNGCLDD FRTEFDVAVD ELSLNPGKQR FEKMISGMYL GEIVRNILID FTKRGLLFRG RISERLKTRG IFETKFLSQI ESDCLALLQV RAILQHLGLE STCDDSIIVK EVCTVVARRA AQLCGAGMAA VVDRIRENRG LDALKVTVGV DGTLYKLHPH FAKVMHETVK DLAPKCDVSF LQSEDGSGKG AALITAVACR IREAGQR.

    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.

    Hk2 Human
  • View Data Sheet

    Name :

    GSR Human

    Description:

    Glutathione Reductase Human Recombinant

    Glutathione reductase mitochondrial, GR, GRase, GSR, GLUR, GRD1.

    Product # :

    ENZ-202

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    Description

    GSR Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 504 amino acids (43-522) and having a molecular mass of 54.3kDa.GSR is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The GSR solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 1mM DTT, 10% glycerol and 0.1M NaCl.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Biological Activity

    Specific activity: > 29 unit/ml.
    One unit will reduce 1.0 umol of oxidized glutathione per minute at pH 7.5 at 25°C.

    Citations

    More Info

    • Introduction

      Glutathione reductase (GSR) belongs to the class-I pyridine nucleotide-disulfide oxidoreductase family. The GSR enzyme is a homodimeric flavoprotein and has a role in maintaining glutathione (GSH) in its reduced form by catalyzing the reduction of glutathione disulfide (GSSG): GSSG + NADPH + H+ ->2GSH + NADP+. In the majority of eukaryotic cells, GSR upholds the ratio of [GSH] / [GSSG], and partakes in quite a few critical functions such as the detoxification of reactive oxygen species as well as protein and DNA biosynthesis.

    • Synonyms

      Glutathione reductase mitochondrial, GR, GRase, GSR, GLUR, GRD1.

    • 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 MGSMAMACRQ EPQPQGPPPA AGAVASYDYL VIGGGSGGLA SARRAAELGA RAAVVESHKL GGTCVNVGCV PKKVMWNTAV HSEFMHDHAD YGFPSCEGKF NWRVIKEKRD AYVSRLNAIY QNNLTKSHIE IIRGHAAFTS DPKPTIEVSG KKYTAPHILI
      ATGGMPSTPH ESQIPGASLG ITSDGFFQLE ELPGRSVIVG AGYIAVEMAG ILSALGSKTS LMIRHDKVLR SFDSMISTNC TEELENAGVE VLKFSQVKEV KKTLSGLEVS MVTAVPGRLP VMTMIPDVDC LLWAIGRVPN TKDLSLNKLG IQTDDKGHII VDEFQNTNVK GIYAVGDVCG
      KALLTPVAIA AGRKLAHRLF EYKEDSKLDY NNIPTVVFSH PPIGTVGLTE DEAIHKYGIE NVKTYSTSFT PMYHAVTKRK TKCVMKMVCA NKEEKVVGIH MQGLGCDEML QGFAVAVKMG ATKADFDNTV AIHPTSSEEL VTLR.

    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.

    Gsr Human
  • View Data Sheet

    Name :

    CTSE Mouse

    Description:

    Cathepsin-E Mouse Recombinant

    CTSE, A430072003Rik, C920004C08Rik, CatE, CE.

    Product # :

    ENZ-1140

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    Description

    CTSE Mouse produced in Sf9 Insect cells is a single, glycosylated polypeptide chain containing 385 amino acids ( 21-397 a.a.) and having a molecular mass of 41.8 kDa.CTSE is expressed with a 8 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Insect cells.

    Formulation

    CTSE protein solution ( 0.5mg/ml ) contains PBS (pH 7.4) and 10% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      CTSE or cathepsin E is an intracellular aspartic protease from the pepsin protein family. CTSE has a crucial part in protein degradation, creating bioactive proteins & processing antigens. The enzyme is responsible for cleaving at B site, Swedish mutant of amyloid precursor protein and the enzyme shows reactivity with the wild-type APP.

    • Synonyms

      CTSE, A430072003Rik, C920004C08Rik, CatE, CE.

    • 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

      ALHRVPLRRH QSLRKKLRAQ GQLSEFWRSH NLDMTRLSES CNVYSSVNEP LINYLDMEYF GTISIGTPPQ NFTVIFDTGS SNLWVPSVYC TSPACKAHPV FHPSQSDTYT EVGNHFSIQY GTGSLTGIIG ADQVSVEGLT VDGQQFGESV KEPGQTFVNA EFDGILGLGY PSLAAGGVTP VFDNMMAQNL VALPMFSVYL SSDPQGGSGS ELTFGGYDPS HFSGSLNWIP VTKQAYWQIA
      LDGIQVGDTV MFCSEGCQAI VDTGTSLITG PPDKIKQLQE AIGATPIDGE YAVDCATLDT MPNVTFLINE VSYTLNPTDY ILPDLVEGMQ FCGSGFQGLD IPPPAGPLWI LGDVFIRQFY SVFDRGNNQV GLAPAVPLEH 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.

    Ctse Mouse
  • View Data Sheet

    Name :

    ASRGL1 Human

    Description:

    ASRGL1 Human Recombinant

    ALP, ALP1, CRASH, ,Beta-aspartyl-peptidase, Isoaspartyl dipeptidase.

    Product # :

    ENZ-837

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    Description

    ASRGL1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 331 amino acids (1-308 a.a) and having a molecular mass of 34.4kDa.ASRGL1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    ASRGL1 protein solution (0.5mg/ml) containing Phosphate buffer saline, (pH 7.4) ,10% glycerol and 1mM DTT.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      ASRGL1 is a 308 amino acid protein which is a member of the Ntn-hydrolase family. ASRGL1 is an autoantigenic protein which is present in the mid-piece of sperm after obstruction of the male reproductive tract. ASRGL1 is expressed highly in the testis, but is also expressed in the brain, kidney and gastrointestinal tissues. High levels of ASRGL1 are also detected in ovarian, uterine and mammary tumors in comparison with normal tissues of the same origin.

    • Synonyms

      ALP, ALP1, CRASH, ,Beta-aspartyl-peptidase, Isoaspartyl dipeptidase.

    • 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 MGSMNPIVVV HGGGAGPISK DRKERVHQGM VRAATVGYGI LREGGSAVDA VEGAVVALED DPEFNAGCGS VLNTNGEVEM DASIMDGKDL SAGAVSAVQC IANPIKLARL VMEKTPHCFL TDQGAAQFAA AMGVPEIPGE KLVTERNKKR LEKEKHEKGA QKTDCQKNLG TVGAVALDCK GNVAYATSTG GIVNKMVGRV GDSPCLGAGG YADNDIGAVS TTGHGESILK VNLARLTLFH IEQGKTVEEA ADLSLGYMKS RVKGLGGLIV VSKTGDWVAK WTSTSMPWAA AKDGKLHFGI DPDDTTITDL P.

    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.

    Asrgl1 Human
  • View Data Sheet

    Name :

    MMP10 Human

    Description:

    Matrix Metallopeptidase 10 Human Recombinant

    SL-2, STMY2, Stromelysin-2, Matrix metalloproteinase-10, MMP-10, Transin-2, MMP10.

    Product # :

    ENZ-764

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    Description

    MMP10 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 401 amino acids (99-476a.a) and having a molecular mass of 45.4kDa. MMP10 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The MMP10 solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.4M UREA and 10% glycerol.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      MMP10 (Matrix Metallopeptidase 10) which is a part of the matrix metalloproteinase (MMP) is activating procollagenase. MMP10 is part of a cluster of MMP genes which localize to chromosome 11q22.3. MMP10 takes part in the breakdown of extracellular matrix in normal physiological processes, like embryonic development, reproduction, and tissue remodeling, as also in disease processes, such as arthritis and metastasis. The majority MMP's are secreted as inactive proproteins that are activated when cleaved by extracellular proteinases. MMP10 encodes an enzyme which degrades proteoglycans and fibronectin.

    • Synonyms

      SL-2, STMY2, Stromelysin-2, Matrix metalloproteinase-10, MMP-10, Transin-2, MMP10.

    • 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 MGSFSSFPGM PKWRKTHLTY RIVNYTPDLP RDAVDSAIEK ALKVWEEVTP LTFSRLYEGE ADIMISFAVK EHGDFYSFDG PGHSLAHAYP PGPGLYGDIH FDDDEKWTED ASGTNLFLVA AHELGHSLGL FHSANTEALM YPLYNSFTEL AQFRLSQDDV NGIQSLYGPP PASTEEPLVP TKSVPSGSEM PAKCDPALSF DAISTLRGEY LFFKDRYFWR RSHWNPEPEF HLISAFWPSL PSYLDAAYEV NSRDTVFIFK GNEFWAIRGN EVQAGYPRGI HTLGFPPTIR KIDAAVSDKE KKKTYFFAAD KYWRFDENSQ SMEQGFPRLI ADDFPGVEPK VDAVLQAFGF FYFFSGSSQF EFDPNARMVT HILKSNSWLH C.

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    Mmp10 Human
  • View Data Sheet

    Name :

    MPI Human

    Description:

    Mannose Phosphate Isomerase Human Recombinant

    Mannose-6-phosphate isomerase, PMI1, CDG1B, Phosphohexomutase, Phosphomannose isomerase, EC 5.3.1.8, FLJ39201.

    Product # :

    ENZ-169

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    Description

    MPI Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 382 amino acids (1-362) and having a molecular mass of 41.9 kDa.The MPI is fused to a 20 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    The MPI solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.4M Urea and 5% glycerol.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      MPI is a member of the mannose-6-phosphate isomerase type 1 family. Although MPI is expressed in all tissues, it can be found more abundantly in heart, brain and skeletal muscle. Localized to the cytoplasm, MPI exploits zinc as a cofactor and catalyzes the interconversion of fructose-6-phosphate and mannose-6-phosphate. Mutations in the MPI gene are the cause of carbohydrate-deficient glycoprotein syndrome, type Ib.

    • Synonyms

      Mannose-6-phosphate isomerase, PMI1, CDG1B, Phosphohexomutase, Phosphomannose isomerase, EC 5.3.1.8, FLJ39201.

    • 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 MAAPRVFPLS CAVQQYAWGK MGSNSEVARL LASSDPLAQI AEDKPYAELW MGTHPRGDAK ILDNRISQKT LSQWIAENQD SLGSKVKDTF NGNLPFLFKV LSVETPLSIQ AHPNKELAEK LHLQAPQHYP DANHKPEMAI ALTPFQGLCG FRPVEEIVTF LKTAAGNNME DIFGELLLQL HQQYPGDIGC FAIYFLNLLT LKPGEAMFLE ANVPHAYLKG DCVECMACSD NTVRAGLTPK FIDVPTLCEM LSYTPSSSKD RLFLPTRSQE DPYLSIYDPP VPDFTIMKTE VPGSVTEYKV LALDSASILL MVQGTVIAST PTTQTPIPLQ RGGVLFIGAN ESVSLKLTEP KDLLIFRACC LL

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    Mpi Human
  • View Data Sheet

    Name :

    AK3L1 Human

    Description:

    Adenylate Kinase-3 Like 1 Human Recombinant

    AK3, Adenylate kinase 3 alpha like 1, AK3L1, AK4.

    Product # :

    PKA-346

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    Description

    AK3L1 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 259 amino acids (1-223) and having a molecular mass of 29.3 kDa. The AK3L1 is fused with 35 amino acid His-tag at N-terminus.AK3L1 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    AK3L1 solution containing 20mM Tris-HCl pH-8, 2mM DTT and 20% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      AK3L1 is an affiliate of the adenylate kinase family of enzymes. AK3L1 enzyme is restricted to the mitochondrial matrix. Adenylate kinases-3 regulates the adenine and guanine nucleotide compositions within a cell by means of catalyzing the reversible transfer of phosphate group among these nucleotides. 5 different isozymes of adenylate kinase have been identified in vertebrates. The enzyme expression of various adenylate kinase isozymes is growth regulated and tissue-specific.

    • Synonyms

      AK3, Adenylate kinase 3 alpha like 1, AK3L1, AK4.

    • 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

      MRGSHHHHHH GMASMTGGQQ MGRDLYDDDD KDRWGSMASK LLRAVILGPP GSGKGTVSQR IAQNFGLQHL SSGHFLRENIKASTEVGEMA KQYIEKSLLV PDHVITRLMM SELENRRGQH WLLDGFPRTL GQAEALDKIC EVDLVISLNI PFETLKDRLS RRWIHPPSGR VYNLDFNPPH VHGIDDVTGE PLVQQEDDKP EAVAARLRQY KDVAKPVIEL YKSRGVLHQF SGTETNKIWP YVYTLFSNKI TPIQSKEAY.

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    Ak3L1 Human
  • View Data Sheet

    Name :

    HPGDS Human

    Description:

    Hematopoietic Prostaglandin D Synthase Human Recombinant

    Hematopoietic prostaglandin D synthase, H-PGDS, GST class-sigma, Glutathione S-transferase, Glutathione-dependent PGD synthase, Glutathione-requiring prostaglandin D synthase, Prostaglandin-H2 D-isomerase, HPGDS, GSTS, PGDS, PTGDS2GSTS, PGD2, GSTS1-1.

    Product # :

    ENZ-616

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    Description

    HPGDS Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 223 amino acids (1-199 a.a.) and having a molecular mass of 25.9kDa.HPGDS is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    HPGDS protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH8.0), 10% glycerol, 0.15M NaCl and 1mM DTT.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      Hematopoietic Prostaglandin D Synthase (HPGDS) belongs to the sigma class glutathione-S-transferase family. The HPGDS enzyme catalyzes the conversion of PGH2 to PGD2 and has a role in the production of prostanoids in the immune system and mast cells. The presence of the HPGDS enzyme can be utilized to identify the differentiation stage of human megakaryocytes. Furthermore, HPGDS is a prostaglandin involved in smooth muscle contraction/relaxation and an effective inhibitor of platelet aggregation, and the conjugation of glutathione with a extensive range of aryl halides and organic isothiocyanates. In addition, HPGDS displays low glutathione-peroxidase activity towards cumene hydroperoxide. HPGDS is expressed in a number of megakaryocytic cell lines but not in platelets. HPGDS is highly expressed in the adipose tissue, macrophages and placenta; however it is expressed at lower levels in the lung, heart, lymph nodes, appendix, bone marrow and fetal liver.

    • Synonyms

      Hematopoietic prostaglandin D synthase, H-PGDS, GST class-sigma, Glutathione S-transferase, Glutathione-dependent PGD synthase, Glutathione-requiring prostaglandin D synthase, Prostaglandin-H2 D-isomerase, HPGDS, GSTS, PGDS, PTGDS2GSTS, PGD2, GSTS1-1.

    • 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 MGSHMPNYKL TYFNMRGRAE IIRYIFAYLD IQYEDHRIEQ ADWPEIKSTL PFGKIPILEV DGLTLHQSLA IARYLTKNTD LAGNTEMEQC HVDAIVDTLD DFMSCFPWAE KKQDVKEQMF NELLTYNAPH LMQDLDTYLG GREWLIGNSV TWADFYWEIC
      STTLLVFKPD LLDNHPRLVT LRKKVQAIPA VANWIKRRPQ TKL.

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    Hpgds Human
  • View Data Sheet

    Name :

    ARG1 Human

    Description:

    Arginase-1 Human Recombinant

    EC 3.5.3.1, Arginase 1, Type I Arginase, Liver-Type Arginase.

    Product # :

    ENZ-517

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    Description

    ARG1 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 330 amino acids (1-322a.a.) and having a molecular mass of 35.8kDa. ARG1 protein is fused to an 8 amino acid His tag at C-terminus and is purified by standard chromatography.

    Source

    Escherichia Coli.

    Formulation

    ARG1 Human protein solution (0.5mg/ml) containing 20mM Tris-HCl pH-8, 2mM DTT, 0.1M NaCl & 20% glycerol.

    Purity

    Greater than 85% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      ARG1 catalyzes the hydrolysis of arginine to ornithine and urea. 2 isoforms of mammalian arginase exist which vary in their tissue distribution, subcellular localization, immunologic crossreactivity and physiologic role. ARG1 is a cytosolic enzyme and expressed widely in the liver as part of the urea cycle. Inherited deficiency of this ARG1 causes argininemia, which is an autosomal recessive disorder characterized by hyperammonemia.

    • Synonyms

      EC 3.5.3.1, Arginase 1, Type I Arginase, Liver-Type Arginase.

    • 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

      MSAKSRTIGI IGAPFSKGQP RGGVEEGPTV LRKAGLLEKL KEQECDVKDY GDLPFADIPN DSPFQIVKNP RSVGKASEQL AGKVAEVKKN GRISLVLGGD HSLAIGSISG HARVHPDLGV IWVDAHTDIN TPLTTTSGNL HGQPVSFLLK ELKGKIPDVP GFSWVTPCIS AKDIVYIGLR DVDPGEHYIL KTLGIKYFSM TEVDRLGIGK VMEETLSYLL GRKKRPIHLS FDVDGLDPSF TPATGTPVVG GLTYREGLYI TEEIYKTGLL SGLDIMEVNP SLGKTPEEVT RTVNTAVAIT LACFGLAREG NHKPIDYLNP PKLEHHHHHH.

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    Arg1 Human
  • View Data Sheet

    Name :

    SPR Mouse

    Description:

    Sepiapterin Reductase Mouse Recombinant

    SDR38C1, SPR, Dystonia, Sepiapterin reductase, mCG_128676.

    Product # :

    ENZ-1055

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    Description

    SPR Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 285 amino acids (1-262 a.a) and having a molecular mass of 30.3kDa.SPR is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    SPR protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH8.5), 1mM DTT and 10% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      Sepiapterin Reductase is an aldo-keto reductase that catalyzes the NADPH-dependent reduction of pteridine derivatives and is essential in the biosynthesis of BH4. Mutations in Sepiapterin Reductase gene result in DOPA-responsive dystonia due to sepiaterin reductase deficiency defined by the presence of sustained involuntary muscle contractions, often leading to abnormal postures. Sepiapterin reductase is part of the short-chain dehydrogenase/reductase family which reduces exogenous carbonyl compounds as well as phenylpropanedione. Sepiapterin reductase is an important enzyme for the biosynthesis of tetrahydrobiopterin, an necessary cofactor for aromatic amino acid hydrolases together with tyrosine hydroxylase, the rate-limiting enzyme in dopamine synthesis.

    • Synonyms

      SDR38C1, SPR, Dystonia, Sepiapterin reductase, mCG_128676.

    • Physical Appearance

      Sterile filtered colourless 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 MGSMEAGGLG CAVCVLTGAS RGFGRALAPQ LARLLSPGSV MLVSARSESM LRQLKEELGA QQPDLKVVLA AADLGTEAGV QRLLSAVREL PRPEGLQRLL LINNAATLGD VSKGFLNVND LAEVNNYWAL NLTSMLCLTS GTLNAFQDSP GLSKTVVNIS SLCALQPYKG WGLYCAGKAA RDMLYQVLAA EEPSVRVLSY APGPLDNDMQ QLARETSKDP ELRSKLQKLK SDGALVDCGT SAQKLLGLLQ KDTFQSGAHV DFYDC.

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    Spr Mouse
  • View Data Sheet

    Name :

    NUDT16L1 Human

    Description:

    Nudix Type Motif 16 Like-1 Human Recombinant

    Protein syndesmos, NUDT16-like protein 1, NUDT16L1, SDOS, MGC11275.

    Product # :

    ENZ-079

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    Description

    NUDT16L1 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 231 amino acids (1-211 a.a.) and having a molecular mass of 25.5kDa. The NUDT16L1 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The NUDT16L1 solution (0.5 mg/ml) contains 20mM Tris-HCl buffer (pH8.0), 20% glycerol, 0.1M NaCl and 1mM DTT.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      Syndesmos (NUDT16L1) is a cytoplasmic protein which interacts specifically with the cytoplasmic domain of syndecan-4, and co-localizes with syndecan-4 in focal contacts. NUDT16L1 interacts with the focal adhesion adaptor protein paxillin. The binding of NUDT16L1 to paxillin is direct, and these interactions are triggered by the activation of protein kinase C.

    • Synonyms

      Protein syndesmos, NUDT16-like protein 1, NUDT16L1, SDOS, MGC11275.

    • 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).Please prevent freeze-thaw cycles.

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MSTAAVPELK QISRVEAMRL GPGWSHSCHA MLYAANPGQL FGRIPMRFSV LMQMRFDGLL GFPGGFVDRR FWSLEDGLNR VLGLGLGCLR LTEADYLSSH LTEGPHRVVA HLYARQLTLE QLHAVEISAV HSRDHGLEVL GLVRVPLYTQ KDRVGGFPNF LSNAFVSTAK CQLLFALKVL NMMPEEKLVE ALAAATEKQK KALEKLLPAS S.

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    Nudt16L1 Human
  • View Data Sheet

    Name :

    BPGM Human

    Description:

    2,3-Bisphosphoglycerate Mutase Human Recombinant

    Bisphosphoglycerate mutase, EC 5.4.2.4, BPGM, 2,3-bisphosphoglycerate mutase erythrocyte, 2,3-bisphosphoglycerate synthase, BPG-dependent PGAM.

    Product # :

    ENZ-505

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    Description

    BPGM Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 267 amino acids (1-259 a.a.) and having a molecular mass of 31 kDa. The BPGM is fused to an 8 amino acid His Tag at C-Terminus and purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The BPGM solution (0.5mg/ml) contains 20mM Tris-HCl (pH 8.0), 1mM DTT and 10% glycerol.

    Purity

    Greater than 95% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      BPGM is found at high concentrations in red blood cells where it binds to and decreases the oxygen affinity of hemoglobin. PGM deficiency increases the oxygen affinity of cells. BPGM is a multifunctional enzyme that catalyzes 2,3-DPG synthesis through its synthetase activity, and 2,3-DPG degradation using its phosphatase activity. BPGM has phosphoglycerate phosphomutase activity. Mutations in BPGM cause hemolytic anemia. BPGM catalyzes the reaction of EC 5.4.2.1 (mutase) and EC 3.1.3.13 (phosphatase), but with a reduced activity.

    • Synonyms

      Bisphosphoglycerate mutase, EC 5.4.2.4, BPGM, 2,3-bisphosphoglycerate mutase erythrocyte, 2,3-bisphosphoglycerate synthase, BPG-dependent PGAM.

    • Physical Appearance

      Sterile Filtered clear 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

      MSKYKLIMLR HGEGAWNKEN RFCSWVDQKL NSEGMEEARN CGKQLKALNF EFDLVFTSVL NRSIHTAWLI LEELGQEWVP VESSWRLNERHYGALIGLNR EQMALNHGEE QVRLWRRSYN VTPPPIEESH PYYQEIYNDR RYKVCDVPLD QLPRSESLKD VLERLLPYWN ERIAPEVLRG KTILISAHGN SSRALLKHLE GISDEDIINI TLPTGVPILL ELDENLRAVG PHQFLGDQEA IQAAIKKVED QGKVKQAKKL EHHHHHH.

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    Bpgm Human
  • View Data Sheet

    Name :

    C12ORF5 Human

    Description:

    Chromosome 12 Open Reading Frame 5 Human

    Fructose-2,6-bisphosphatase TIGAR, TP53-induced glycolysis and apoptosis regulator, TIGAR, C12orf5.

    Product # :

    PRO-1791

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    Description

    TIGAR Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 270 amino acids and having a molecular mass of 30.1kDa. The TIGAR is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    TIGAR was Lyophilized from a 0.2 µm filtered concentrated solution in 20mM Tris-HCl, pH8.5, 150mM NaCl.

    Purity

    Greater than 95.0% as determined by:
    (a) Analysis by RP-HPLC.
    (b) Analysis by SDS-PAGE.

    Citations

    More Info

    • Introduction

      TIGAR is a p53-inducible enzyme which catalyzes the hydrolysis of fructose-2-6 bisphosphate (F-2-6-BP) to fructose-6-phosphate and inorganic phosphate. F-2-6-BP is an influential activator of 6-phosphofructose-1 kinase (the rate limiting enzyme of glycolysis). By lowering the intracellular level of F-2-6-BP, TIGAR expression leads to increased glucose processing through the pentose phosphate pathway, the main cellular source for NADPH.

    • Synonyms

      Fructose-2,6-bisphosphatase TIGAR, TP53-induced glycolysis and apoptosis regulator, TIGAR, C12orf5.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized TIGAR stable at room temperature for 3 weeks, should be stored desiccated below -18C. Upon reconstitution TIGAR 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 reconstitute the lyophilized TIGAR in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      MARFALTVVR HGETRFNKEK IIQGQGVDEP LSETGFKQAA AAGIFLNNVK FTHAFSSDLM RTKQTMHGIL ERSKFCKDMT VKYDSRLRER KYGVVEGKAL SELRAMAKAA REECPVFTPP GGETLDQVKM RGIDFFEFLC QLILKEADQK EQFSQGSPSN CLETSLAEIF PLGKNHSSKV NSDSGIPGLA ASVLVVSHGA YMRSLFDYFL TDLKCSLPAT LSRSELMSVT PNTGMSLFII NFEEGREVKP TVQCICMNLQ DHLNGLTETR

    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.

    Tigar Human
  • View Data Sheet

    Name :

    TXNRD1 Human

    Description:

    Thioredoxin Reductase 1 Human Recombinant

    Thioredoxin reductase 1 cytoplasmic, TR, GRIM-12, Gene associated with retinoic and IFN-induced mortality 12 protein, KM-102-derived reductase-like factor, Thioredoxin reductase TR1, TXNRD1, GRIM12, KDRF, TR1, TXNR, TRXR1, MGC9145.

    Product # :

    ENZ-518

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    Description

    TXNRD1 Human Recombinant produced in E.Coli is a single, non-glycosylated,polypeptide chain containing 508 amino acids (161-647 a.a.) and having a molecular mass of 55.7 kDa. TXNRD1 protein is fused to a 21 amino acid His tag at N-terminus and is purified by standard chromatography.

    Source

    Escherichia Coli.

    Formulation

    TXNRD1 Human solution (0.5mg/ml) containing 1x PBS pH-7.4 & 20% glycerol.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    Biological Activity

    Specific activity is > 15 units/mg, and was measured in a coupled assay with 5,5'-Dithiobis(2-nitrobenzoic acid)(DTNB)and NADPH. The amount of TNB generated by NADPH was measured in absorbance at 412 nm.

    Citations

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    • Introduction

      TXNRD1 belongs to the selenium-containing pyridine nucleotide-disulphide oxidoreductase family, which has a conserved catalytic site of Cys-Val-Asn-Val-Gly-Cys. TXNRD1 decreases thioredoxins as well as other substrates, and participates in selenium metabolism and protection against oxidative stress. Inhibition of TXNRD1 activity serves as a potential treatment for cancer, AIDS and other autoimmune diseases as well as bacterial infections and parasitic diseases.

    • Synonyms

      Thioredoxin reductase 1 cytoplasmic, TR, GRIM-12, Gene associated with retinoic and IFN-induced mortality 12 protein, KM-102-derived reductase-like factor, Thioredoxin reductase TR1, TXNRD1, GRIM12, KDRF, TR1, TXNR, TRXR1, MGC9145.

    • 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 MYDYDLIIIG GGSGGLAAAK EAAQYGKKVM VLDFVTPTPL GTRWGLGGTC VNVGCIPKKL MHQAALLGQALQDSRNYGWK VEETVKHDWD RMIEAVQNHI GSLNWGYRVA LREKKVVYEN AYGQFIGPHR IKATNNKGKE KIYSAERFLI ATGERPRYLGIPGDKEYCIS SDDLFSLPYC PGKTLVVGAS YVALECAGFL AGIGLDVTVM VRSILLRGFD QDMANKIGEH MEEHGIKFIR QFVPIKVEQIEAGTPGRLRV VAQSTNSEEI IEGEYNTVML AIGRDACTRK IGLETVGVKI NEKTGKIPVT DEEQTNVPYI YAIGDILEDK VELTPVAIQAGRLLAQRLYA GSTVKCDYEN VPTTVFTPLE YGACGLSEEK AVEKFGEENI EVYHSYFWPL EWTIPSRDNN KCYAKIICNT KDNERVVGFH VLGPNAGEVT QGFAAALKCG LTKKQLDSTI GIHPVCAEVF TTLSVTKRSG ASILQAGC.

    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.

    Txnrd1 Human
  • View Data Sheet

    Name :

    PRSS3 Human

    Description:

    Protease Serine 3 Human Recombinant

    Protease Serine 3 (Mesotrypsin), Protease Serine 4 (Trypsin 4, Brain), Brain Trypsinogen, Mesotrypsinogen, Trypsin III, Trypsinogen IV, Trypsinogen 5, Pancreatic Trypsinogen III, MTG, TRY3, PRSS4, T9, EC 3.4.21.

    Product # :

    ENZ-735

    Price :

    Quantity :

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    More Info

    • description
    • source
    • formulation
    • purity
    • More Info
    • Citations

    Description

    PRSS3 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 247 amino acids (81-304) and having a molecular mass of 26.0kDa.PRSS3 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The PRSS3 solution contains 20mM Tris-HCl buffer (pH 8.0), 0.4M Urea and 10% glycerol.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      PRSS3 is a trypsinogen, and a member of the trypsin family of serine proteases. PRSS3 is expressed in the pancreas and brain and is unaffected by common trypsin inhibitors. It is active on peptide linkages involving the carboxyl group of lysine or arginine. PRSS3 is restricted to the locus of T cell receptor beta variable orphans on chromosome 9. 4 different isoforms encoded by 4 transcript variants were identified for this gene.

    • Synonyms

      Protease Serine 3 (Mesotrypsin), Protease Serine 4 (Trypsin 4, Brain), Brain Trypsinogen, Mesotrypsinogen, Trypsin III, Trypsinogen IV, Trypsinogen 5, Pancreatic Trypsinogen III, MTG, TRY3, PRSS4, T9, EC 3.4.21.

    • 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 MGSIVGGYTC EENSLPYQVS LNSGSHFCGG SLISEQWVVS AAHCYKTRIQ VRLGEHNIKV LEGNEQFINA AKIIRHPKYN RDTLDNDIML IKLSSPAVIN ARVSTISLPT APPAAGTECL ISGWGNTLSF GADYPDELKC LDAPVLTQAE CKASYPGKIT NSMFCVGFLE GGKDSCQRDS GGPVVCNGQL QGVVSWGHGC AWKNRPGVYT KVYNYVDWIK DTIAANS

    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.

    Prss3 Human
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