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Search results

1000 results found for “peptidase”

Name

Description

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  • View Data Sheet

    Name :

    AKR1C1 Human, His

    Description:

    Aldo-Keto Reductase Family 1 Member C1 Human Recombinant, His Tag

    DDH1, DDH, HAKRC, 20-alpha-HSD, DD1/DD2, HBAB, C9, DD1, H-37, MBAB, MGC8954, 2-ALPHA-HSD, AKR1C1, Aldo-keto reductase family 1 member C1, 20-alpha-hydroxysteroid dehydrogenase, Trans-1,2-dihydrobenzene-1,2-diol dehydrogenase, Indanol dehydrogenase, Dihydrodiol dehydrogenase 1/2, Chlordecone reductase homolog HAKRC, High-affinity hepatic bile acid-binding protein.

    Product # :

    ENZ-496

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    Description

    AKR1C1 Human Recombinant fused to a 20 amino acid His Tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 343 amino acids (1-323 a.a.) and having a molecular mass of 38.9 kDa. The AKR1C1 is fused to a 20 a.a. His Tag at n-terminal and purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The AKR1C1 protein solution (0.5mg/ml) contains 20mM Tris-HCl pH-8, 1mM DTT and 20% glycerol.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    Biological Activity

    Specific activity is > 500 pmol/min/ug, and is defined as the amount of enzyme that catalyze the oxidation of 1.0 pmole 1-Acenaphthenol in the presence of NADP per minute at pH 8.8 at 25°C.

    More Info

    • Introduction

      AKR1C1 transfers progesterone to its inactive state or in other words catalyzes the reaction of 20-alpha-hydroxy progesterone (20-alpha-OHP). In the liver and intestine. AKR1C1 transfers bile and monitors the intrahepatic bile acid concentration though it has a low bile-binding ability. AKR1C1 participates in myelin formation. AKR1C1 is part of the aldo/keto reductase superfamily, which has over 40 known enzymes which catalyze the conversion of aldehydes and ketones to their corresponding alcohols by utilizing NADH and/or NADPH as cofactors thus display overlapping but distinct substrate specificity.

    • Synonyms

      DDH1, DDH, HAKRC, 20-alpha-HSD, DD1/DD2, HBAB, C9, DD1, H-37, MBAB, MGC8954, 2-ALPHA-HSD, AKR1C1, Aldo-keto reductase family 1 member C1, 20-alpha-hydroxysteroid dehydrogenase, Trans-1,2-dihydrobenzene-1,2-diol dehydrogenase, Indanol dehydrogenase, Dihydrodiol dehydrogenase 1/2, Chlordecone reductase homolog HAKRC, High-affinity hepatic bile acid-binding protein.

    • 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

      MGSSHHHHHH SSGLVPRGSH MDSKYQCVKL NDGHFMPVLG FGTYAPAEVP KSKALEATKL AIEAGFRHID SAHLYNNEEQ VGLAIRSKIA DGSVKREDIF YTSKLWCNSH RPELVRPALE RSLKNLQLDY VDLYLIHFPV SVKPGEEVIP KDENGKILFD TVDLCATWEA VEKCKDAGLA KSIGVSNFNR RQLEMILNKP GLKYKPVCNQ VECHPYFNQR KLLDFCKSKD IVLVAYSALG SHREEPWVDP NSPVLLEDPV LCALAKKHKR TPALIALRYQ LQRGVVVLAK SYNEQRIRQN VQVFEFQLTS EEMKAIDGLN RNVRYLTLDI FAGPPNYPFS DEY.

    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.

    Akr1C1 Human
  • View Data Sheet

    Name :

    GLRX2 Human

    Description:

    Glutaredoxin 2 Human Recombinant

    Thioltransferase, Glutathione-dependent oxidoreductase 2, TTR, TTR1, GLRX2, GRX2, GRX-2, GLRX-2, Glutaredoxin 2, CGI133.

    Product # :

    ENZ-466

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    • description
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    Description

    Glutaredoxin-2 Human Recombinant produced in E.Coli is a single, non-glycosylated, Polypeptide chain containing 154 amino acids (20-164 a.a.) and having a molecular mass of 17 kDa. The GRX2 is fused to 9 amino acid His tag at C-Terminus.

    Source

    Escherichia Coli.

    Formulation

    Glutaredoxin-2 solution (0.5mg/ml) contains 20mM Tris-HCl Buffer (pH 8.0), 0.1mM PMSF and 10% glycerol.

    Purity

    Purity of GRX2 is greater than 90% as determined by SDS-PAGE.

    More Info

    • Introduction

      GLRX2 is a multifunctional enzyme with glutathione-dependent oxidoreductase, glutathione peroxidase and glutathione S-transferase (GST) activity. The disulfide bond functions as an electron carrier in the glutathione-dependent synthesis of deoxyribonucleotides by the enzyme ribonucleotide reductase. In addition, it is also involved in reducing cytosolic protein- and non-protein-disulfides in a coupled system with glutathione reductase. Required for resistance to reactive oxygen species (ROS) by directly reducing hydroperoxides and for the detoxification of ROS-mediated damage. Glutaredoxins are a family of glutathione-dependent hydrogen donors that participate in a variety of cellular redox reactions.

    • Synonyms

      Thioltransferase, Glutathione-dependent oxidoreductase 2, TTR, TTR1, GLRX2, GRX2, GRX-2, GLRX-2, Glutaredoxin 2, CGI133.

    • 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

      MSAGWLDRAA GAAGAAAAAA SGMESNTSSS LENLATAPVN QIQETISDNC VVIFSKTSCS YCTMAKKLFH DMNVNYKVVE LDLLEYGNQF QDALYKMTGE RTVPRIFVNG TFIGGATDTH RLHKEGKLLP LVHQCYLKKS KRKEFQLEHH 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.

    Glrx2 Human
  • View Data Sheet

    Name :

    DAAO Human, Active

    Description:

    D-Amino Acid Oxidase Human Recombinant, BioActive

    D-Amino Acid Oxidase 2, D-Amino-Acid Oxidase, EC 1.4.3.3, DAMOX, DAAO, EC 1.4.3, OXDA.

    Product # :

    ENZ-1142

    Price :

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    • description
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    Description

    DAAO Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 367 amino acids (1-347) and having a molecular mass of 41.6 kDa. DAAO Humanis fused to a 20 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    DAAO Human protein (0.5mg/ml) is formulated in 20mM Tris-HCl buffer (pH 8.0), 20% glycerol & 1mM DTT.

    .

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Biological Activity

    Specific activity is > 3.5unit/mg, in which one unit will oxidatively deaminate 1.0 umole of D-alanine to pyruvateper minute at pH 8.5 at 37C, in the presence of catalase.

    More Info

    • Introduction

      D-amino-acid oxidase or DAAO is an enzyme that oxidizes D-amino acids to their imino acids form while using FAD (flavin adenine dinucleotide) as a co-factor, resulting in the formation of ammonia & hydrogen peroxide. the enzyme may take part in keeping the balance of acid base in the kidney tissue. Another role is to detoxifying molecules that abolish D-amino acids aggregated while the cell ages.

    • Synonyms

      D-Amino Acid Oxidase 2, D-Amino-Acid Oxidase, EC 1.4.3.3, DAMOX, DAAO, EC 1.4.3, OXDA.

    • 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 MRVVVIGAGV IGLSTALCIH ERYHSVLQPL DIKVYADRFT PLTTTDVAAG LWQPYLSDPN NPQEADWSQQ TFDYLLSHVH SPNAENLGLF LISGYNLFHE AIPDPSWKDT VLGFRKLTPR ELDMFPDYGY GWFHTSLILE GKNYLQWLTE RLTERGVKFF QRKVESFEEV AREGADVIVN CTGVWAGALQ RDPLLQPGRG QIMKVDAPWM KHFILTHDPE RGIYNSPYII PGTQTVTLGG IFQLGNWSEL NNIQDHNTIW EGCCRLEPTL KNARIIGERT GFRPVRPQIR LEREQLRTGP SNTEVIHNYG HGGYGLTIHW GCALEAAKLF GRILEEKKLS RMPPSHL.

    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.

    Daao Enzyme
  • View Data Sheet

    Name :

    Cyclophilin F Rat

    Description:

    Cyclophilin F Rat Recombinant

    Peptidyl-prolyl cis-trans isomerase F, mitochondrial, PPIase F, Cyclophilin D, CyP-D, CypD, Cyclophilin F, Rotamase F, Ppif, Peptidyl-prolyl cis-trans isomerase F, mitochondrial, PPIase.

    Product # :

    ENZ-903

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    Description

    Cyclophilin F Rat Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 200 amino acids (30-206a.a.) and having a molecular mass of 21.2kDa.Cyclophilin F is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Cyclophilin F protein solution (1mg/ml) containing Phosphate buffered saline (pH7.4), 10% glycerol and 1mM DTT.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Peptidyl-prolyl cis-trans isomerase F, mitochondrial (Cyclophilin-F) accelerates the folding of proteins. Cyclophilin-F catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides and involved in regulation of the mitochondrial permeability transition pore (mPTP). Cyclophilin-F, in cooperation with mitochondrial TP53, is involved in activating oxidative stress-induced necrosis. Cyclophilin-F is also involved in modulation of mitochondrial membrane F1F0 ATP synthase activity and regulation of mitochondrial matrix adenine nucleotide levels. Furthermore, Cyclophilin-F has anti-apoptotic activity independently of mPTP and in cooperation with BCL2 inhibits cytochrome c-dependent apoptosis.

    • Synonyms

      Peptidyl-prolyl cis-trans isomerase F, mitochondrial, PPIase F, Cyclophilin D, CyP-D, CypD, Cyclophilin F, Rotamase F, Ppif, Peptidyl-prolyl cis-trans isomerase F, mitochondrial, PPIase.

    • 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 MGSCSDGGAR GANSSSQNPL VYLDVGADGQ PLGRVVLELK ADVVPKTAEN FRALCTGEKG FGYKGSTFHR VIPAFMCQAG DFTNHNGTGG KSIYGSRFPD ENFTLKHVGP GVLSMANAGP NTNGSQFFIC TIKTDWLDGK HVVFGHVKEG MDVVKKIESF GSKSGKTSKK IVITDCGQLS.

    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.

    Cyclophilin F Rat
  • View Data Sheet

    Name :

    NDUFS5 Human

    Description:

    Histidine NADH Dehydrogenase Fe-S Protein 5 Human Recombinant

    CI-15k, CI15K, NADH dehydrogenase [ubiquinone] iron-sulfur protein 5, Complex I-15 kDa, NADH-ubiquinone oxidoreductase 15 kDa subunit, CI-15 kDa, NDUFS5.

    Product # :

    ENZ-771

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    Description

    NDUFS5 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 129 amino acids (1-106a.a) and having a molecular mass of 14.9kDa. NDUFS5 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The NDUFS5 solution (1mg/ml) contains 20mM Tris-HCl buffer (pH8.0), 10% glycerol and 0.4M Urea.

    Purity

    Greater than 85% as determined by SDS-PAGE.

    More Info

    • Introduction

      Histidine NADH Dehydrogenase Fe-S Protein 5 (NDUFS5) belongs to the NADH dehydrogenase (ubiquinone) iron-sulfur protein family. NDUFS5 is a subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), which doesn’t take part in catalysis. Complex I is transferring the electrons from NADH to the respiratory chain.

    • Synonyms

      CI-15k, CI15K, NADH dehydrogenase [ubiquinone] iron-sulfur protein 5, Complex I-15 kDa, NADH-ubiquinone oxidoreductase 15 kDa subunit, CI-15 kDa, NDUFS5.

    • 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 MGSMPFLDIQ KRFGLNIDRW LTIQSGEQPY KMAGRCHAFE KEWIECAHGI GYTRAEKECK IEYDDFVECL LRQKTMRRAG TIRKQRDKLI KEGKYTPPPH HIGKGEPRP.

    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.

    Ndufs5 Human
  • View Data Sheet

    Name :

    GSTM5 Human

    Description:

    Glutathione S-Transferase MU 5 Human Recombinant

    Glutathione S-transferase mu 5, GSTM5-5, GST class-mu 5, GTM5, glutathione S-alkyltransferase M5, S-(hydroxyalkyl) glutathione lyase M5, EC 2.5.1.18.

    Product # :

    ENZ-623

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    Description

    GSTM5 Human Recombinant produced in E. coli is a single polypeptide chain containing 242 amino acids (1-218) and having a molecular mass of 28.2 kDa.GSTM5 is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    The GSTM5 solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.1M NaCl, 1mM DTT and 10% glycerol.

    Purity

    Greater than 95% as determined by SDS-PAGE.

    More Info

    • Introduction

      Glutathione S-transferase mu 5 (GSTM5) belongs to the glutathione s-transferase (GST) family of proteins. There are 8 families of GST proteins, specifically alpha, kappa, mu, omega, pi, sigma, theta and zeta, each of which is comprised of proteins which have various functions throughout the cell. GSTM5 belongs to the mu class of enzymes which function in the detoxification of electrophilic compounds, including carcinogens, therapeutic drugs, environmental toxins and products of oxidative stress, by conjugation with glutathione. GSTM5 has an imperative role in detoxification. GSTM5 conjugates reduced glutathione to a large number of exogenous and endogenous hydrophobic electrophiles.

    • Synonyms

      Glutathione S-transferase mu 5, GSTM5-5, GST class-mu 5, GTM5, glutathione S-alkyltransferase M5, S-(hydroxyalkyl) glutathione lyase M5, EC 2.5.1.18.

    • 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 MGSHMPMTLG YWDIRGLAHA IRLLLEYTDS SYVEKKYTLG DAPDYDRSQW LNEKFKLGLD FPNLPYLIDG AHKITQSNAI LRYIARKHNL CGETEEEKIR VDILENQVMD NHMELVRLCY DPDFEKLKPK YLEELPEKLK LYSEFLGKRP WFAGDKITFV DFLAYDVLDM KRIFEPKCLD AFLNLKDFIS RFEGLKKISA YMKSSQFLRG LLFGKSATWN SK

    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.

    Gstm5 Human
  • View Data Sheet

    Name :

    UBE2Q2 Human

    Description:

    Ubiquitin Conjugating Enzyme E2Q2 Human Recombinant

    Ubiquitin-conjugating enzyme E2 Q2, UBE2Q2, E2 ubiquitin-conjugating enzyme Q2, Ubiquitin carrier protein Q2, Ubiquitin-protein ligase Q2, Ubiquitin Conjugating Enzyme E2Q2, Ubiquitin-conjugating enzyme E2 Q2 isoform1.

    Product # :

    ENZ-885

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    Description

    UBE2Q2 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 398 amino acids (1-375a.a.) and having a molecular mass of 45.2kDa.UBE2Q2 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    UBE2Q2 protein solution (0.5mg/ml) containing Phosphate Buffer Saline (pH7.4), 30% glycerol and 1mM DTT.

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Ubiquitin Conjugating Enzyme E2Q2 (UBE2Q2) is a protein coding gene which receives ubiquitin from the E1 complex and catalyzes its covalent attachment to various proteins. UBE2Q2 which is a part of the ubiquitin-conjugating enzyme family is detected in hypopharyngeal head and neck squamous cell carcinoma and in tumor masses.

    • Synonyms

      Ubiquitin-conjugating enzyme E2 Q2, UBE2Q2, E2 ubiquitin-conjugating enzyme Q2, Ubiquitin carrier protein Q2, Ubiquitin-protein ligase Q2, Ubiquitin Conjugating Enzyme E2Q2, Ubiquitin-conjugating enzyme E2 Q2 isoform1.

    • 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 MGSMSVSGLK AELKFLASIF DKNHERFRIV SWKLDELHCQ FLVPQQGSPH SLPPPLTLHC NITESYPSSS PIWFVDSEDP NLTSVLERLE DTKNNNLLRQ QLKWLICELC SLYNLPKHLD VEMLDQPLPT GQNGTTEEVT SEEEEEEEEM AEDIEDLDHY EMKEEEPISG KKSEDEGIEK ENLAILEKIR KTQRQDHLNG AVSGSVQASD RLMKELRDIY RSQSYKTGIY SVELINDSLY DWHVKLQKVD PDSPLHSDLQ ILKEKEGIEY ILLNFSFKDN FPFDPPFVRV VLPVLSGGYV LGGGALCMEL LTKQGWSSAY SIESVIMQIN ATLVKGKARV QFGANKNQYN LARAQQSYNS IVQIHEKNGW YTPPKEDG.

    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.

    Ube2Q2 Human
  • View Data Sheet

    Name :

    TK1 Human

    Description:

    Thymidine Kinase 1 Human Recombinant

    Thymidine kinase 1 soluble, thymidine kinase cytosolic, TK2, EC 2.7.1.21.

    Product # :

    PKA-036

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    Description

    TK1 Human Recombinant produced in E. coli is a single polypeptide chain containing 258 amino acids (1-234) and having a molecular mass of 28.0 kDa.TK1 is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    The TK1 solution (1mg/1ml) contains 20mM Tris-HCl buffer (pH 8.0), 100mM NaCl, 1mM DTT and 20% glycerol.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    More Info

    • Introduction

      Thymidine Kinase 1 (TK1) is a phosphotransferase (a kinase): 2'-deoxythymidine kinase, ATP-thymidine 5'-phosphotransferase. TK1 is present in 2 forms in mammalian cells, TK1 and TK2. Thymidine kinases hold a main function in the synthesis of DNA and thus in cell division, as they are part of the distinctive reaction chain to introduce deoxythymidine (present in the body fluids as a result of degradation of DNA from food and from dead cells) into the DNA. Thymidine kinase is necessary for the action of many antiviral drugs. Thymidine kinase is used to select hybridoma cell lines in production of monoclonal antibodies.

    • Synonyms

      Thymidine kinase 1 soluble, thymidine kinase cytosolic, TK2, EC 2.7.1.21.

    • 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 MGSHMSCINL PTVLPGSPSK TRGQIQVILG PMFSGKSTEL MRRVRRFQIA QYKCLVIKYA KDTRYSSSFC THDRNTMEAL PACLLRDVAQ EALGVAVIGI DEGQFFPDIV EFCEAMANAG KTVIVAALDG TFQRKPFGAI LNLVPLAESV VKLTAVCMEC FREAAYTKRL GTEKEVEVIG GADKYHSVCR LCYFKKASGQ PAGPDNKENC PVPGKPGEAV AARKLFAPQQ ILQCSPAN.

    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.

    Tk1 Human
  • View Data Sheet

    Name :

    NDUFA5 Human

    Description:

    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-657

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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.

    More Info

    • 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.

    • 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.

    • 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 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.

    Ndufa5 Human
  • View Data Sheet

    Name :

    UCHL3 Human

    Description:

    Ubiquitin Carboxyl-Terminal Esterase L3 Human Recombinant

    Ubiquitin Carboxyl-Terminal Esterase L3 (ubiquitin thiolesterase), UCH-L3, Ubiquitin Carboxyl-Terminal Hydrolase Isozyme L3, EC 3.4.19.12.

    Product # :

    ENZ-057

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    Description

    UCHL3 produced in E.Coli is a single, non-glycosylated polypeptide chain containing 250 amino acids (1-230a.a.) and having a molecular mass of 28.3kDa.UCHL3 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The UCHL3 protein solution (1mg/1ml) is formulated in 20mM Tris-HCl buffer (pH8.0)
    1mM DTT and 10% glycerol.

    Purity

    Greater than 95% as determined by SDS-PAGE.

    Biological Activity

    Specific activity: >3,000 pmole/min/ug. Measured by the hydrolysis of Ubiquitin-AMC at pH 8.0, at 37C.

    More Info

    • Introduction

      Ubiquitin carboxyl-terminal hydrolase isozyme L3 belongs to a gene family whose products hydrolyze small C-terminal adducts of ubiquitin to produce the ubiquitin monomer. UCHL3 takes part in the regulation of neuronal development and spermatogenesis and is associated to neurodegenerative diseases. UCHL3 has a 54% homology to UCHL1.

    • Synonyms

      Ubiquitin Carboxyl-Terminal Esterase L3 (ubiquitin thiolesterase), UCH-L3, Ubiquitin Carboxyl-Terminal Hydrolase Isozyme L3, EC 3.4.19.12.

    • 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). Please avoid freeze thaw cycles.

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MEGQRWLPLE ANPEVTNQFL KQLGLHPNWQ FVDVYGMDPE LLSMVPRPVC AVLLLFPITE KYEVFRTEEE EKIKSQGQDV TSSVYFMKQT ISNACGTIGL IHAIANNKDK MHFESGSTLK KFLEESVSMS PEERARYLEN YDAIRVTHET SAHEGQTEAP SIDEKVDLHF IALVHVDGHL YELDGRKPFP INHGETSDET LLEDAIEVCK KFMERDPDEL RFNAIALSAA

    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.

    Uchl3 Human
  • View Data Sheet

    Name :

    GSTA4 Human

    Description:

    Glutathione S-Transferase Alpha 4 Human Recombinant

    Glutathione S-transferase A4, GST class-alpha member 4, Glutathione S-transferase A4-4, GSTA4, GSTA4-4.

    Product # :

    ENZ-600

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    Description

    GSTA4 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 246 amino acids (1-222) and having a molecular mass of 28.3kDa.GSTA4 is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The GSTA4 solution (1mg/ml) contains 20mM Tris-HCl buffer, pH8.0, 20% glycerol, 2mM DTT and 100mM NaCl.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Glutathione S-transferase A4 (GSTA4) is a member of the GST superfamily. The GSTA4 enzyme is involved in cellular defense against toxic, carcinogenic, and pharmacologically active electrophilic compounds. GSTA4 shows an especially high activity with reactive carbonyl compounds such as alk-2-enals. GSTA4 is extremely effective in catalyzing the conjugate addition of reduced glutathione to 4-hydroxynonenal, which is an important product of peroxidative degradation of arachidonic acid and a frequently used biomarker for oxidative damage in tissue. The GSTA4 enzyme is expressed at a high level in the brain, placenta, and skeletal muscle and much lower in the lung and liver.

    • Synonyms

      Glutathione S-transferase A4, GST class-alpha member 4, Glutathione S-transferase A4-4, GSTA4, GSTA4-4.

    • 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 MGSHMAARPK LHYPNGRGRM ESVRWVLAAA GVEFDEEFLE TKEQLYKLQD GNHLLFQQVP MVEIDGMKLV QTRSILHYIA DKHNLFGKNL KERTLIDMYV EGTLDLLELL IMHPFLKPDD QQKEVVNMAQ KAIIRYFPVF EKILRGHGQS FLVGNQLSLA
      DVILLQTILA LEEKIPNILS AFPFLQEYTV KLSNIPTIKR FLEPGSKKKP PPDEIYVRTV YNIFRP.

    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.

    Gsta4 Human
  • View Data Sheet

    Name :

    DCT Human

    Description:

    Dopachrome Tautomerase Human Recombinant

    L-dopachrome tautomerase (EC:5.3.3.12), DCT, DT, L-dopachrome Delta-isomerase Tyrosinase-related protein 2, TRP-2, TRP2, TYRP2.

    Product # :

    ENZ-874

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    Description

    DCT Human Recombinant produced in Sf9 Insect cell is a single, glycosylated polypeptide chain containing 455 amino acids (24-472aa.a) and having a molecular mass of 52.1kDa. DCT is fused to a 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9 Insect cells.

    Formulation

    STK3 protein solution (0.25mg/ml) containing Phosphate Buffered Saline (pH 7.4) and 10% glycerol.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    More Info

    • Introduction

      Dopachrome Tautomerase also known as DCT, belongs to the tyrosinase family. DCT takes a significant part in the synthesis of the melanin pigment including tyrosinase (Tyr), tyrosinase-related protein 1 (Tyrp1). Which are highly involved in eumelanin synthesis. The change among the eumelanin and the pheomelanin pathways is assumed to depend on the presence of cysteine. Hence, in the lack of cysteine, dopaquinone, the product of tyrosinase action, is transformed to cyclodopa (leucodopachrome) and afterwards to dopachrome (and DOPA).

    • Synonyms

      L-dopachrome tautomerase (EC:5.3.3.12), DCT, DT, L-dopachrome Delta-isomerase Tyrosinase-related protein 2, TRP-2, TRP2, TYRP2.

    • 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

      QFPRVCMTVD SLVNKECCPR LGAESANVCG SQQGRGQCTE VRADTRPWSG PYILRNQDDR ELWPRKFFHR TCKCTGNFAG YNCGDCKFGW TGPNCERKKP PVIRQNIHSL SPQEREQFLG ALDLAKKRVH PDYVITTQHW LGLLGPNGTQ PQFANCSVYD FFVWLHYYSV RDTLLGPGRP YRAIDFSHQG PAFVTWHRYH LLCLERDLQR LIGNESFALP YWNFATGRNE CDVCTDQLFG AARPDDPTLI SRNSRFSSWE TVCDSLDDYN HLVTLCNGTY EGLLRRNQMG RNSMKLPTLK DIRDCLSLQK FDNPPFFQNS TFSFRNALEG FDKADGTLDS QVMSLHNLVH SFLNGTNALP HSAANDPIFV VLHSFTDAIF DEWMKRFNPP ADAWPQELAP IGHNRMYNMV PFFPPVTNEE LFLTSDQLGY SYAIDLPVSV EETPGWPTTH HHHHH.

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    Dct Human
  • View Data Sheet

    Name :

    PTPN7 Human

    Description:

    Protein Tyrosine Phosphatase Non Receptor Type-7 Human Recombinant

    Protein tyrosine phosphatase non-receptor type 7, HEPTP, LC-PTP, Hematopoietic protein-tyrosine phosphatase, Protein-tyrosine phosphatase LC-PTP, PTPNI, LPTP, BPTP-4, dual specificity phosphatase 1, protein-tyrosine phosphatase non-receptor-type, stress induced, EC 3.1.3.48.

    Product # :

    PKA-025

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    • More Info

    Description

    PTPN7 Human Recombinant produced in E. coli is a single polypeptide chain containing 384 amino acids (1-360) and having a molecular mass of 43.1kDa.PTPN7 is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    The PTPN7 solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 100mM NaCl, 1mM DTT and 20% glycerol.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    More Info

    • Introduction

      PTPN7 performs specifically on tyrosine-phosphorylated MAPK1. PTPN7 takes part in the regulation of signal transduction and T and B-lymphocyte development.

    • Synonyms

      Protein tyrosine phosphatase non-receptor type 7, HEPTP, LC-PTP, Hematopoietic protein-tyrosine phosphatase, Protein-tyrosine phosphatase LC-PTP, PTPNI, LPTP, BPTP-4, dual specificity phosphatase 1, protein-tyrosine phosphatase non-receptor-type, stress induced, EC 3.1.3.48.

    • 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 MGSHMVQAHG GRSRAQPLTL SLGAAMTQPP PEKTPAKKHV RLQERRGSNV ALMLDVRSLG AVEPICSVNT PREVTLHFLR TAGHPLTRWA LQRQPPSPKQ LEEEFLKIPS NFVSPEDLDI PGHASKDRYK TILPNPQSRV CLGRAQSQED GDYINANYIR GYDGKEKVYI ATQGPMPNTV SDFWEMVWQE EVSLIVMLTQ LREGKEKCVH YWPTEEETYG PFQIRIQDMK ECPEYTVRQL TIQYQEERRS VKHILFSAWP DHQTPESAGP LLRLVAEVEE SPETAAHPGP IVVHCSAGIG RTGCFIATRI GCQQLKARGE VDILGIVCQL RLDRGGMIQT AEQYQFLHHT LALYAGQLPE EPSP

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    Ptpn7 Human
  • View Data Sheet

    Name :

    MPO Human

    Description:

    Myeloperoxidase Human

    Myeloperoxidase, EC 1.11.1.7, MPO.

    Product # :

    ENZ-074

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    Description

    MPO is a natural protein having a molecular mass of 150kDa containing 2 subunits each of a heavy chain with 64kDa and a light chain with 13kDa. MPO is isolated from human peripheral blood polymorphonuclear leukocytes.

    Source

    Human peripheral blood polymorphonuclear leukocytes.

    Formulation

    MPO solution is supplied in 20mM HEPES buffer pH-7.5, 200mM NaCl and 20% glycerol.

    Purity

    Greater than 80% as determined by SDS-PAGE.

    More Info

    • Introduction

      Myeloperoxidase is an important enzyme used by granulocytes during phagocytic lysis of foreign particles engulfed. In normal tissues and in a variety of myeloproliferative disorders myeloid cells of both neutrophilic and eosinophilic types, at all stages of maturation, exhibit strong cytoplasmic reactivity for MPO. Erythroid precursors, megakaryocytes, lymphoid cells, mast cells, and plasma cells are nonreactive. MPO is not observed in the neoplastic cells of a wide variety of epithelial tumors and sarcomas. MPO is useful in differentiating between myeloid and lymphoid leukemias.

    • Synonyms

      Myeloperoxidase, EC 1.11.1.7, MPO.

    • 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. Avoid multiple 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.

    Mpo Human
  • View Data Sheet

    Name :

    GALK1 Human

    Description:

    Galactokinase 1 Human Recombinant

    Galactose kinase, GK1, GALK, EC 2.7.1.6, GALK1.

    Product # :

    PKA-264

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    Description

    GALK1 Recombinant Human produced in E.Coli is a single, non-glycosylated polypeptide chain containing 412 amino acids (1-392 a.a.) and having a molecular mass of 44.4 kDa. The GALK1 is fused to a 20 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    GALK1 Human (0.5mg/ml) solution containing 20% glycerol 0.1M NaCl and 1mM DTT.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      GALK1 enzyme is needed in the first step of the galactose metabolism pathway.
      (ATP + D-galactose = ADP + alpha-D-galactose 1-phosphate). GALK1 deficinecy lead galactosemia II which is an autosomal recessive deficiency known by congenital cataracts during infancy and presenile cataracts in the adult population. The cataracts are secondary to accumulation of galactitol in the lenses.

    • Synonyms

      Galactose kinase, GK1, GALK, EC 2.7.1.6, GALK1.

    • 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 MAALRQPQVA ELLAEARRAF REEFGAEPEL AVSAPGRVNL IGEHTDYNQG LVLPMALELM TVLVGSPRKD GLVSLLTTSE GADEPQRLQF PLPTAQRSLE PGTPRWANYV KGVIQYYPAA PLPGFSAVVV SSVPLGGGLS SSASLEVATY TFLQQLCPDS GTIAARAQVC QQAEHSFAGM PCGIMDQFIS LMGQKGHALL IDCRSLETSL VPLSDPKLAV LITNSNVRHS LASSEYPVRR RQCEEVARAL GKESLREVQL EELEAARDLV SKEGFRRARH VVGEIRRTAQ AAAALRRGDY RAFGRLMVES HRSLRDDYEV SCPELDQLVE AALAVPGVYG SRMTGGGFGG CTVTLLEASA APHAMRHIQE HYGGTATFYL SQAADGAKVL CL.

    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.

    Galk1 Human
  • View Data Sheet

    Name :

    HDHD2 Human

    Description:

    Haloacid Dehalogenase-Like Hydrolase Domain Containing 2 Human Recombinant

    Haloacid Dehalogenase-like Hydrolase Domain Containing 2, DKFZP564D1378, 3110052N05Rik, DKFZp564D1378.

    Product # :

    ENZ-038

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    Description

    HDHD2 produced in E.Coli is a single, non-glycosylated polypeptide chain containing 279 amino acids (1-259a.a.) and having a molecular mass of 30.6kDa.HDHD2 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The HDHD2 protein solution (1mg/1ml) is formulated in 20mM Tris-HCl buffer (pH 8.0), 0.1M NaCl, 1mM DTT, and 10% glycerol.

    Purity

    Greater than 95% as determined by SDS-PAGE.

    More Info

    • Introduction

      HDHD2 is a member of the HAD-like hydrolase superfamily which includes L-2-haloacid dehalogenase, epoxide hydrolases and phosphatases. There are two active sites in HDHD2 - an L-2-haloacid dehalogenase and a carboxylate group. The L-2-haloacid dehalogenase active site catalyzes the hydrolytic dehalogenation of D- and L-2-haloalkanoic acids, producing L- and D-2-hydroxyalkanoic acids.

    • Synonyms

      Haloacid Dehalogenase-like Hydrolase Domain Containing 2, DKFZP564D1378, 3110052N05Rik, DKFZp564D1378.

    • 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 MAACRALKAV LVDLSGTLHI EDAAVPGAQE ALKRLRGASV IIRFVTNTTK ESKQDLLERL RKLEFDISED EIFTSLTAAR SLLERKQVRP MLLVDDRALP DFKGIQTSDP NAVVMGLAPE HFHYQILNQA FRLLLDGAPL IAIHKARYYK RKDGLALGPG PFVTALEYAT DTKATVVGKP EKTFFLEALR GTGCEPEEAV MIGDDCRDDV GGAQDVGMLG ILVKTGKYRA SDEEKINPPP YLTCESFPHA VDHILQHLL

    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.

    Hdhd2 Human
  • View Data Sheet

    Name :

    CS Human

    Description:

    Citrate Synthase Human Recombinant

    Citrate Synthase, EC 2.3.3.1, Citrate (Si)-Synthase, EC 2.3.3, Citrate synthase, mitochondrial.

    Product # :

    ENZ-824

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    Description

    CS Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 462 amino acids (28-466 a.a) and having a molecular mass of 51.4kDa. CS is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    CS protein solution (1mg/ml) containing 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.

    More Info

    • Introduction

      Citrate synthase also known as CS is a Krebs tricarboxylic acid cycle enzyme which catalyzes the synthesis of citrate from oxaloacetate and acetyl coenzyme A. CS is present in almost all cells capable of oxidative metabolism. CS is nuclear encoded and transported into the mitochondrial matrix, where the mature form is found. The diseases related to CS are: critical illness polyneuropathy and mitochondrial cardiomyopathy.

    • Synonyms

      Citrate Synthase, EC 2.3.3.1, Citrate (Si)-Synthase, EC 2.3.3, Citrate synthase, mitochondrial.

    • 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 MGSASSTNLK DILADLIPKE QARIKTFRQQ HGKTVVGQIT VDMMYGGMRG MKGLVYETSV LDPDEGIRFR GFSIPECQKL LPKAKGGEEP LPEGLFWLLV TGHIPTEEQV SWLSKEWAKR AALPSHVVTM LDNFPTNLHP MSQLSAAVTA LNSESNFARA YAQGISRTKY WELIYEDSMD LIAKLPCVAA KIYRNLYREG SGIGAIDSNL DWSHNFTNML GYTDHQFTEL TRLYLTIHSD HEGGNVSAHT SHLVGSALSD PYLSFAAAMN GLAGPLHGLA NQEVLVWLTQ LQKEVGKDVS DEKLRDYIWN TLNSGRVVPG YGHAVLRKTD PRYTCQREFA LKHLPNDPMF KLVAQLYKIV PNVLLEQGKA KNPWPNVDAH SGVLLQYYGM TEMNYYTVLF GVSRALGVLA QLIWSRALGF PLERPKSMST EGLMKFVDSK SG.

    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.

    Cs Human
  • View Data Sheet

    Name :

    DHFR Mouse

    Description:

    Dihydrofolate Reductase Mouse Recombinant

    Dihydrofolate reductase, DHFR, DHFRP1, AA607882, AI662710, AW555094, 8430436I03Rik.

    Product # :

    ENZ-069

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    Description

    DHFR Mouse Recombinant fused with a 20 amino acid His tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 207 amino acids (1-187 a.a.) and having a molecular mass of 23.8kDa. The DHFR is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The DHFR solution (1 mg/ml) contains 20mM Tris-HCl buffer(pH 8.0), 10% glycerol, 2mM DTT and 0.1M NaCl.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Biological Activity

    Specific activity is > 0.2 units/mg, in which one unit will convert 1.0 umole of 7,8 –dihydrofloate and beta-NADPH to 5,6,7,8-tetrahydrofloate and beta-NADP per min at pH 6.5 at 25C.

    More Info

    • Introduction

      Dihydrofolate reductase (DHFR) is an enzyme that reduces dihydrofolic acid to tetrahydrofolic acid, with NADPH as electron donor that can be converted to the kinds of tetrahydrofolate cofactors applied in 1-carbon transfer chemistry. DHFR converts dihydrofolate into tetrahydrofolate, which is a methyl group shuttle required for the de novo synthesis of purines, thymidylic acid, and specific amino acids. Even though the functional DHFR gene is mapped to chromosome 5, numerous intronless processed pseudogenes or dihydrofolate reductase-like genes are identified on separate chromosomes. DHFR deficiency is associated with megaloblastic anemia. DHFR knockdown plays a role in the anticancer activity of 2-hydroxyoleic acid. DHFR gene insertion/deletion polymorphism is linked to variation in serum and red blood cell folate concentrations in women.

    • Synonyms

      Dihydrofolate reductase, DHFR, DHFRP1, AA607882, AI662710, AW555094, 8430436I03Rik.

    • 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 MVRPLNCIVA VSQNMGIGKN GDLPWPPLRN EFKYFQRMTT TSSVEGKQNL VIMGRKTWFS IPEKNRPLKD RINIVLSREL KEPPRGAHFL AKSLDDALRL IEQPELASKV DMVWIVGGSS VYQEAMNQPG HLRLFVTRIM QEFESDTFFP EIDLGKYKLL PEYPGVLSEV QEEKGIKYKF EVYEKKD.

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    Dhfr Mouse
  • View Data Sheet

    Name :

    G6PD Human

    Description:

    Glucose-6-Phosphate Dehydrogenase Human Recombinant

    G6PD, G6PD1, Glucose-6-phosphate 1-dehydrogenase.

    Product # :

    ENZ-608

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    Description

    G6PD Human Recombinant produced in Hi-5 cells is a single polypeptide chain containing 535 amino acids (1-515) and having a molecular mass of 61.4kDa.G6PD is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Hi-5 cells.

    Formulation

    The G6PD solution (0.5mg/1ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.1mM PMSF, 2mM EDTA, 2mM DTT, 200mM NaCl and 20% glycerol.

    Purity

    Greater than 95% as determined by SDS-PAGE.

    Biological Activity

    Specific activity is > 45 units/ml obtained by measuring the increase of beta-NADPH in absorbance at 340 nm resulting from the reduction of beta NADP. One unit oxidizes 1.0 umole D-glucose-6-phosphate to 6-phospho-D-gluconate per min in the presence of beta-NADP at pH 7.4 at 25C.

    More Info

    • Introduction

      G6PD is the rate-limiting enzyme of the pentose phosphate pathway, a metabolic pathway that supplies reducing energy to cells by maintaining the level of NADPH. G6PD converts glucose-6-phosphate into 6-phosphoglucono-?-lactone and at the same time produces NADPH. The NADPH maintains the level of glutathione in these cells that helps protect the red blood cells against oxidative damage. G6PD deficiency causes acute hemolytic anemia, neonatal jaundice or acute hemolysis. G6PD is a cytosolic enzyme encoded by an X-linked gene whose main function is to produce NADPH, a crucial electron donor in the defense against oxidizing agents and in reductive biosynthetic reactions. G6PD produces pentose sugars for nucleic acid synthesis and is a main producer of NADPH reducing power.

    • Synonyms

      G6PD, G6PD1, Glucose-6-phosphate 1-dehydrogenase.

    • 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 MAEQVALSRT QVCGILREEL FQGDAFHQSD THIFIIMGAS GDLAKKKIYP TIWWLFRDGL LPENTFIVGY ARSRLTVADI RKQSEPFFKA TPEEKLKLED FFARNSYVAG QYDDAASYQR LNSHMNALHL GSQANRLFYL ALPPTVYEAV TKNIHESCMS QIGWNRIIVE KPFGRDLQSS DRLSNHISSL FREDQIYRID HYLGKEMVQN LMVLRFANRI FGPIWNRDNI ACVILTFKEP FGTEGRGGYF DEFGIIRDVM QNHLLQMLCL VAMEKPASTN SDDVRDEKVK VLKCISEVQA NNVVLGQYVG NPDGEGEATK GYLDDPTVPR GSTTATFAAV VLYVENERWD GVPFILRCGK ALNERKAEVR LQFHDVAGDI FHQQCKRNEL VIRVQPNEAV YTKMMTKKPG MFFNPEESEL DLTYGNRYKN VKLPDAYERL ILDVFCGSQM HFVRSDELRE AWRIFTPLLH QIELEKPKPI PYIYGSRGPT EADELMKRVG FQYEGTYKWV NPHKL

    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.

    G6Pd Human
  • View Data Sheet

    Name :

    LDHB Human, His

    Description:

    Lactate Dehydrogenase B Human Recombinant, His Tag

    LDH-H, TRG-5, L-lactate dehydrogenase B chain, LDH-B, EC=1.1.1.27, Renal carcinoma antigen NY-REN-46, LDHB.

    Product # :

    ENZ-539

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    Description

    LDHB Recombinant Human produced in E.Coli is a single, non-glycosylated polypeptide chain containing 354 amino acids (1-334 a.a.) and having a molecular mass of 38.8 kDa. The LDHB is fused to a 20 amino acids His-Tag at N-terminus and purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    LDHB Human solution containing 20mM Tris-HCl pH-8, 1mM DTT & 10% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Biological Activity

    Specific activity is > 6 units/mg. in which one unit will convert 1.0 umole of pyruvate to L-lactate and beta-NAD per minute at pH 7.5 at 37°C.

    More Info

    • Introduction

      LDHB is part of the lactate dehydrogenase family. LDHB is an oxidoreductase which catalyses the interconversion of pyruvate and lactate with concomitant interconversion of NADH and NAD+. LDHB catalyzes the oxidation of hydroxybutyrate, and frequently called Hydroxybutyrate Dehydrogenase (HBD). The LDH family consists of three members, LDH-A, LDH-B and LDH-C. LDHs function as powerful markers for germ cell tumors.

    • Synonyms

      LDH-H, TRG-5, L-lactate dehydrogenase B chain, LDH-B, EC=1.1.1.27, Renal carcinoma antigen NY-REN-46, LDHB.

    • 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 MATLKEKLIA PVAEEEATVP NNKITVVGVG QVGMACAISI LGKSLADELA LVDVLEDKLK GEMMDLQHGS LFLQTPKIVA DKDYSVTANS KIVVVTAGVR QQEGESRLNL VQRNVNVFKF IIPQIVKYSP DCIIIVVSNP VDILTYVTWK LSGLPKHRVI GSGCNLDSAR FRYLMAEKLG IHPSSCHGWI LGEHGDSSVA VWSGVNVAGV SLQELNPEMG TDNDSENWKE VHKMVVESAY EVIKLKGYTN WAIGLSVADL IESMLKNLSR IHPVSTMVKG MYGIENEVFL SLPCILNARG LTSVINQKLK DDEVAQLKKS ADTLWDIQKD LKDL.

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    Ldhb Human
  • View Data Sheet

    Name :

    AKR1C3 Human

    Description:

    Aldo-Keto Reductase Family 1 Member C3 Human Recombinant

    DD3, DDX, HAKRB, HAKRe, HA1753, HSD17B5, hluPGFS, KIAA0119, AKR1C3, Aldo-keto reductase family 1 member C3, 3-alpha-HSD type 2, 17-beta-HSD 5, PGFS, DD-3.

    Product # :

    ENZ-1131

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    Description

    AKR1C3 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 323 amino acids (1-323) and having a molecular mass of 36.8 kDa.AKR1C3 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The AKR1C3 solution (1mg/ml) contains 10% Glycerol, 0.1M NaCl, 1mM DTT and 20mM Tris-HCl buffer (pH 8.5).

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    Biological Activity

    Specific activity is > 1,000pmol/min/ug. It is defined by the amount of enzyme that catalyzes oxidation of 1.0pmole 1-Acenaphthenol in the presence of NADP per minute at pH 8.8 at 25˚C.

    More Info

    • Introduction

      Aldo-keto reductase family 1 member C3 isoform 1 or AKR1C3 is an enzyme, part of the aldo-keto reductase family that promotes conversion of ketones & aldehydes to the alcohol forms while using cofactors such as NADPH & NADH. AKR1C3 promotes the reduction of PG molecule (prostaglandin), PQ (phenanthrenequinone) & PGH2. Another role is oxidation of 9 alpha, 11 beta-PGF2 to PGD2. AKR1C3 holds a crucial part in the pathogenesis of allergic diseases like asthma and can also take part in the regulation of cell growth and differentiation.

    • Synonyms

      DD3, DDX, HAKRB, HAKRe, HA1753, HSD17B5, hluPGFS, KIAA0119, AKR1C3, Aldo-keto reductase family 1 member C3, 3-alpha-HSD type 2, 17-beta-HSD 5, PGFS, DD-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

      MDSKHQCVKL NDGHFMPVLG FGTYAPPEVP RSKALEVTKL AIEAGFRHID SAHLYNNEEQ VGLAIRSKIA DGSVKREDIF YTSKLWSTFH RPELVRPALE NSLKKAQLDY VDLYLIHSPM SLKPGEELSP TDENGKVIFD IVDLCTTWEA MEKCKDAGLA KSIGVSNFNR RQLEMILNKP GLKYKPVCNQ VECHPYFNRS KLLDFCKSKD IVLVAYSALG SQRDKRWVDP NSPVLLEDPV
      LCALAKKHKR TPALIALRYQ LQRGVVVLAK SYNEQRIRQN VQVFEFQLTA EDMKAIDGLD RNLHYFNSDS FASHPNYPYS DEY

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    Akr1C3 Protein
  • View Data Sheet

    Name :

    PPIH Human

    Description:

    Cyclophilin-H Human Recombinant

    Oeptidylprolyl Isomerase H, PPIH, CYPH, CYP20, SnuCyp-20, Peptidyl-prolyl cis-trans isomerase H, PPIase H, Rotamase H, U-snRNP-associated cyclophilin SnuCyp-20, USA-CYP, Small nuclear ribonucleoprotein particle-specific cyclophilin H, peptidylprolyl isomerase H, CYP-20, MGC5016, Cyclophilin-H.

    Product # :

    ENZ-379

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    Description

    PPIH Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 177 amino acids (1-177) and having a molecular mass of 19.2 kDa. PPIH is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    1 mg/ml solution containing 1x PBS pH-7.4 10% glycerol.

    Purity

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

    Biological Activity

    Specific activity is > 220 nmoles/min/mg, and is defined as the amount of enzyme that cleaves 1umole of suc-AAFP-pNA per minute at 25C in Tris-Hcl pH8.0 using chymotrypsin.

    More Info

    • Introduction

      PPIH is a part of the peptidyl-prolyl cis-trans isomerase (PPIase) family. PPIases catalyze the cis-trans isomerization of proline imidic peptide bonds in oligopeptides and increase protein folding. PPIH enzyme is a precise factor of the complex that comprises pre-mRNA processing factors PRPF3, PRPF4, and PRPF18, as well as U4/U5/U6 tri-snRNP. PPIH possess PPIase activity and acts as a protein chaperone that mediates the interactions between different proteins inside the spliceosome.

    • Synonyms

      Oeptidylprolyl Isomerase H, PPIH, CYPH, CYP20, SnuCyp-20, Peptidyl-prolyl cis-trans isomerase H, PPIase H, Rotamase H, U-snRNP-associated cyclophilin SnuCyp-20, USA-CYP, Small nuclear ribonucleoprotein particle-specific cyclophilin H, peptidylprolyl isomerase H, CYP-20, MGC5016, Cyclophilin-H.

    • 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

      MAVANSSPVN PVVFFDVSIG GQEVGRMKIE LFADVVPKTA ENFRQFCTGEFRKDGVPIGY KGSTFHRVIK DFMIQGGDFV NGDGTGVASI YRGPFADENF KLRHSAPGLL SMANSGPSTN GCQFFITCSK CDWLDGKHVV FGKIIDGLLV MRKIENVPTG PNNKPKLPVV ISQCGEM.

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    Ppih Human
  • View Data Sheet

    Name :

    C-Peptide

    Description:

    C-Peptide

    Product # :

    HOR-046

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    Description

    C-Peptide Synthetic is a single, non-glycosylated polypeptide chain containing 31 amino acids, having a molecular mass of 3020 Dalton and a Molecular formula of C129H211N35O48S .

    Formulation

    The protein was lyophilized with no additives.

    Purity

    Greater than 97.0% as determined by analysis by RP-HPLC.

    More Info

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized C-Peptide although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution C-Peptide 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.

    • Solubility

      It is recommended to reconstitute the lyophilized C-Peptide in sterile 18MΩ-cm H2O not less than 100 µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      H-Glu-Ala-Glu-Asp-Leu-Gln-Val-Gly-Gln-Val-Glu-Leu-Gly-Gly-Gly-Pro-Gly-Ala-Gly-Ser-Leu-Gln-Pro-Leu-Ala-Leu-Glu-Gly-Ser-Leu-Gln-OH.

    • Background

      C-peptide, a small peptide derived from proinsulin, has garnered increasing attention in recent years for its multifaceted physiological functions and clinical significance, particularly in the context of diabetes mellitus. While initially considered a mere byproduct of insulin synthesis, research has revealed that C-peptide exerts unique biological effects, extending beyond glycemic control. This research endeavors to comprehensively investigate the roles of C-peptide, shedding light on its diverse functions and potential applications in diabetes management and other areas of healthcare.

      The primary objective of this study is to unravel the mechanisms underlying the physiological actions of C-peptide. In vitro experiments using cellular and tissue models will be conducted to explore how C-peptide interacts with cellular receptors and signaling pathways. This includes investigations into its influence on insulin secretion, glucose uptake, and endothelial function. Understanding these mechanisms is essential for delineating the potential therapeutic applications of C-peptide.

      The second objective is to assess the clinical relevance of C-peptide in diabetes management. Clinical trials involving individuals with type 1 and type 2 diabetes will be conducted to evaluate the effects of exogenous C-peptide administration on glycemic control, insulin sensitivity, and microvascular complications. These studies may provide valuable insights into the use of C-peptide as an adjunct therapy in diabetes treatment.

      The third objective is to explore the broader implications of C-peptide in healthcare. Research will investigate the potential role of C-peptide in conditions beyond diabetes, such as its effects on cardiovascular health, neuroprotection, and wound healing. Understanding the multifunctional properties of C-peptide may open up new avenues for therapeutic interventions in various medical specialties.

      By delving into the diverse functions of C-peptide, this research aims to expand our knowledge of its physiological roles and clinical applications. The findings may lead to innovative approaches for diabetes management and offer insights into the broader healthcare implications of C-peptide.

    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.

    C Peptide
  • View Data Sheet

    Name :

    PLA2G7 Human

    Description:

    Secreted Phospholipase A2-VII Human Recombinant

    Platelet-activating factor acetylhydrolase, PAF acetylhydrolase, PAF 2-acylhydrolase, LDL-associated phospholipase A2, LDL-PLA(2), 2-acetyl-1-alkylglycerophosphocholine esterase, 1-alkyl-2-acetylglycerophosphocholine esterase, PLA2G7, PAFAH, LP-PLA2, LDL-PLA2.

    Product # :

    ENZ-436

    Price :

    Quantity :

    Shipping Method :

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    More Info

    • description
    • source
    • formulation
    • purity
    • More Info

    Description

    PLA2G7 Human Recombinant produced in E.Coli is single, a non-glycosylated, Polypeptide chain containing 420 amino acids fragment (22-441) having a total molecular mass of 52.29kDa and fused with a 4.5kDa amino-terminal hexahistidine tag. The PLA2G7 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    PLA2G7 protein is supplied in 20mM Tris-HCl pH-8.0, 1mM EDTA and 50% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      PLA2G7 is a secreted enzyme which catalyzes the degradation of platelet-activating factor to biologically inactive products. The PLA2G7 enzyme is produced by inflammatory cells and hydrolyzes oxidised phospholipids in LDL. In the blood, PLA2G7 goes mainly with LDL and less than 20% is coupled with HDL.
      PLA2G7 is implicated in the development of atherosclerosis and is also a marker for cardiac disease. PLA2G7 might have a major physiologic effect in the presence of inflammatory bodily responses.
      PLA2G7 alters the action of PAF (platelet-activating factor) by hydrolyzing the sn-2 ester bond to yield the biologically inactive lyso-PAF. PLA2G7 has specificity for substrates with a short residue at the sn-2 position. PLA2G7 is inactive against long-chain phospholipids.
      PLA2G7 gene defects are the source of platelet-activating factor acetylhydrolase deficiency, which is a trait that is present in 27% of the Japanese population.

    • Synonyms

      Platelet-activating factor acetylhydrolase, PAF acetylhydrolase, PAF 2-acylhydrolase, LDL-associated phospholipase A2, LDL-PLA(2), 2-acetyl-1-alkylglycerophosphocholine esterase, 1-alkyl-2-acetylglycerophosphocholine esterase, PLA2G7, PAFAH, LP-PLA2, LDL-PLA2.

    • 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. Please avoid 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.

    Pla2G7 Human
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