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Search results

1000 results found for “sulfatase”

Name

Description

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  • View Data Sheet

    Name :

    NQO1 Human, Active

    Description:

    NAD(P)H Dehydrogenase Quinone 1, Active 1 Human Recombinant

    NAD(P)H dehydrogenase (quinone) 1, Quinone reductase 1, QR1, NAD(P)H:quinone oxidoreductase 1, DT-diaphorase, DTD, Azoreductase, Phylloquinone reductase, Menadione reductase, NQO1, DIA4, NMOR1, DHQU, NMORI.

    Product # :

    ENZ-1107

    Price :

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    Description

    NQO1 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 294 amino acids ( 1-274aa ) and having a molecular mass of 33.0 kDa. NQO1 is fused to a 20 amino acid His tag at N-terminus and purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The NQO1 solution (1 mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 1mM DTT and 10% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Biological Activity

    Specific activity is > 1,000 pmol/min/ug. One unit will convert 1 pmoles resazurin to resorufin per minute at pH 7.5 at 25°C.

    Citations

    More Info

    • Introduction

      NQO1 belongs to the NAD(P)H dehydrogenase (quinone) family and encodes a cytoplasmic 2-electron reductase. NQO1 acts as an imperative part of cellular antioxidant defense by detoxifying quinines therefore preventing the formation of reactive oxygen species. It seems that NQO1 serves as a quinone reductase relating to conjugation reactions of hydroquinons involved in detoxification pathways in addition to biosynthetic processes such as the vitamin K-dependent gamma-carboxylation of glutamate residues in prothrombin synthesis. Altered NQO1 expression is seen in many tumors and also linked to Alzheimer’s disease. NQO1 gene mutations are linked to tardive dyskinesia which is an increased risk of hematotoxicity after exposure to benzene, and susceptibility to various forms of cancer.

    • Synonyms

      NAD(P)H dehydrogenase (quinone) 1, Quinone reductase 1, QR1, NAD(P)H:quinone oxidoreductase 1, DT-diaphorase, DTD, Azoreductase, Phylloquinone reductase, Menadione reductase, NQO1, DIA4, NMOR1, DHQU, NMORI.

    • 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 MVGRRALIVL AHSERTSFNY AMKEAAAAAL KKKGWEVVES
      DLYAMNFNPI ISRKDITGKL KDPANFQYPA ESVLAYKEGH LSPDIVAEQK KLEAADLVIF
      QFPLQWFGVP AILKGWFERV FIGEFAYTYA AMYDKGPFRS KKAVLSITTG GSGSMYSLQG
      IHGDMNVILW PIQSGILHFC GFQVLEPQLT YSIGHTPADA RIQILEGWKK RLENIWDETP
      LYFAPSSLFD LNFQAGFLMK KEVQDEEKNK KFGLSVGHHL GKSIPTDNQI KARK

    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.

    Nqo1 Enzyme
  • View Data Sheet

    Name :

    GDA Mouse

    Description:

    Guanine Deaminase Mouse Recombinant

    Guanine deaminase, Guanase, Guanine aminase, Guanine aminohydrolase, GAH.

    Product # :

    ENZ-1058

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    Description

    GDA Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 477 amino acids (1-454 a.a) and having a molecular mass of 53.4kDa.GDA is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    GDA protein solution (0.5mg/ml) containing 20mM Tris-HCl(pH8.0), 0.15M NaCl, 1mM DTT and 10% glycerol .

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Biological Activity

    Specific activity is > 4,000 pmol/min/ug, and is defined as
    the amount of enzyme that convert guanine to xanthine per minute at pH 8.0 at 37°C.

    Citations

    More Info

    • Introduction

      GDA is a member of the ATZ/TRZ family and is in charge for the hydrolytic deamination of guanine. GDA takes part in microtubule assembly. Multiple transcript variants encoding different isoforms have been found for GDA.

    • Synonyms

      Guanine deaminase, Guanase, Guanine aminase, Guanine aminohydrolase, GAH.

    • 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 MGSMCAARTP PLALVFRGTF VHSTWTCPME VLRDHLLGVS DSGKIVFLEE SSQQEKLAKE WCFKPCEIRE LSHHEFFMPG LVDTHIHAPQ YAFAGSNVDL PLLEWLNKYT FPTEQRFRST DVAEEVYTRV VRRTLKNGTT TACYFGTIHT DSSLILAEIT DKFGQRAFVG KVCMDLNDTV PEYKETTEES VKETERFVSE MLQKNYPRVK PIVTPRFTLS CTETLMSELG NIAKTHDLYI QSHISENREE IEAVKSLYPS YKNYTDVYDK NNLLTNKTVM AHGCYLSEEE LNIFSERGAS IAHCPNSNLS LSSGLLNVLE VLKHKVKIGL GTDVAGGYSY SMLDAIRRAV MVSNVLLINK VNEKNLTLKE VFRLATLGGS QALGLDSEIG NFEVGKEFDA LLINPRASDS PIDLFYGDFV GDISEAVIQK FLYLGDDRNI EEVYVGGKQV VPFSSSV.

    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.

    Gda Mouse
  • View Data Sheet

    Name :

    LPCAT1 Human

    Description:

    Lysophosphatidylcholine Acyltransferase Human Recombinant

    AYTL2, lpcat, PFAAP3, Lysophosphatidylcholine acyltransferase 1, LPC acyltransferase 1, LPCAT-1, LysoPC acyltransferase 1, 1-acylglycerophosphocholine O-acyltransferase, 1-alkylglycerophosphocholine O-acetyltransferase, Acetyl-CoA:lyso-platelet-activating factor acetyltransferase, Acetyl-CoA:lyso-PAF acetyltransferase, Lyso-PAF acetyltransferase, LysoPAFAT, Acyltransferase-like 2, Phosphonoformate immuno-associated protein 3.

    Product # :

    ENZ-695

    Price :

    Quantity :

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    • description
    • source
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    Description

    LPCAT1 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 479 amino acids (79-534a.a) and having a molecular mass of 53.4kDa. LPCAT1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The LPCAT1 solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 1M Urea and 10% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      Lysophosphatidylcholine acyltransferase 1 (LPCAT1) is a part of the 1-acyl-sn-glycerol-3-phosphate acyltransferase family. LPCAT1 is a key enzyme for remodeling phospholipids, including phosphatidylcholine. LPCAT1 possesses both acyltransferase and acetyltransferase activities and also mediates the conversion of 1-acyl-sn-glycero-3-phosphocholine (LPC) into phosphatidylcholine (PC). LPCAT1 presents a clear preference for saturated fatty acyl-CoAs, and 1-myristoyl or 1-palmitoyl LPC as acyl donors and acceptors, respectively. LPCAT1 synthesizes phosphatidylcholine in pulmonary surfactant and therefore playing an important role in respiratory physiology.

    • Synonyms

      AYTL2, lpcat, PFAAP3, Lysophosphatidylcholine acyltransferase 1, LPC acyltransferase 1, LPCAT-1, LysoPC acyltransferase 1, 1-acylglycerophosphocholine O-acyltransferase, 1-alkylglycerophosphocholine O-acetyltransferase, Acetyl-CoA:lyso-platelet-activating factor acetyltransferase, Acetyl-CoA:lyso-PAF acetyltransferase, Lyso-PAF acetyltransferase, LysoPAFAT, Acyltransferase-like 2, Phosphonoformate immuno-associated protein 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

      MGSSHHHHHH SSGLVPRGSH MGSSAEKEPE QPPALWRKVV DFLLKAIMRT MWFAGGFHRV AVKGRQALPT EAAILTLAPH SSYFDAIPVT MTMSSIVMKA ESRDIPIWGT LIQYIRPVFV SRSDQDSRRK TVEEIKRRAQ SNGKWPQIMI FPEGTCTNRT CLITFKPGAF IPGAPVQPVV LRYPNKLDTI TWTWQGPGAL EILWLTLCQF HNQVEIEFLP VYSPSEEEKR NPALYASNVR RVMAEALGVS VTDYTFEDCQ LALAEGQLRL PADTCLLEFA RLVRGLGLKP EKLEKDLDRY SERARMKGGE KIGIAEFAAS LEVPVSDLLE DMFSLFDESG SGEVDLRECV VALSVVCRPA RTLDTIQLAF KMYGAQEDGS VGEGDLSCIL KTALGVAELT VTDLFRAIDQ EEKGKITFAD FHRFAEMYPA FAEEYLYPDQ THFESCAETS PAPIPNGFCA DFSPENSDAG RKPVRKKLD.

    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.

    Lpcat1 Human
  • View Data Sheet

    Name :

    CKMB Human

    Description:

    Creatine Kinase MB Human Recombinant

    CKMB, CK-MB 

     

    Product # :

    CKI-286

    Price :

    Quantity :

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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 :

    AsnRS

    Description:

    Asparagine tRNA Synthetase Brugia Malayi Recombinant

    Asparagine--tRNA ligase, cytoplasmic (EC:6.1.1.22), Asparaginyl-tRNA synthetase, AsnRS, Potentially protective 63 kDa antigen.

    Product # :

    ENZ-941

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    Description

    AsnRS Brugia Malayi Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 568 amino acids (including a 6xHis Tag at N-terminus) and having a molecular mass of 64.5kDa.The AsnRS is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    AsnRS 0.2µm filtered solution containing 20mM HEPES, pH7.4, 100mM NaCl, 5mM MgCl2, 5mM b-Mercaptoethanol and 10 % Glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      The AsnRS enzyme is a member of the ligases family, specifically those forming carbon-oxygen bonds in aminoacyl-tRNA and related compounds. An asparagine-tRNA ligase is an enzyme which catalyzes the chemical reaction: ATP + L-asparagine + tRNAAsn AMP + diphosphate + L-asparaginyl-tRNAAsn. The three substrates of the AsnRS enzyme are ATP, L-asparagine, and tRNA(Asn), whereas its three products are AMP, diphosphate, and L-asparaginyl-tRNA(Asn).

    • Synonyms

      Asparagine--tRNA ligase, cytoplasmic (EC:6.1.1.22), Asparaginyl-tRNA synthetase, AsnRS, Potentially protective 63 kDa antigen.

    • 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 MTVYICPETG DDGNDGSELK PLRTLYQAMI ITKSSKGDFL IRTKKDGKQV WEAASKTALK KSWKRYEQEM LKNEKVAAKM LEKDATEVGV KAALEEAKKV QIELDTSLSY ITGVKIRDLV KHRNERVCIK GWIHRMRRQG KSLMFFILRD GTGFLQVLLM DKLCQTYDAL TVNTECTVEI YGAIKEVPEG KEAPNGHELI ADFWKIIGNA PSGGIDNVLN EEASVDKMLD NRHLVIRGEN AAALLRLRAA ATRAMREHFY NAGYVEVAPP TLVQTQVEGG STLFNLDYFG EQSFLTQSSQ LYLETCIPTL GDVFLHCSVL QGGKISHSST LAEYAHVEAE CPFITLDDLM EKIEELVCDT VDRLLADEEA KKLLEHINPK FQPPERPFLR MEYKDAIKWL QEHNVENEFG NTFTYGEDIA EAAERFMTDT INKPILLNRF PSEIKAFYMQ RDAKDNTLTE SVDLLMPGVG EIVGGSMRIW KFDELSKAFK NVEIDPKPYY WYLDQRLYGT CPHGGYGLGL ERFICWLTNT NHIRDVCLYP RFVGRCVP.

    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.

    Asnrs
  • View Data Sheet

    Name :

    SOS1 Human

    Description:

    Son Of Sevenless Homolog 1 Human Recombinant

    SOS Ras/Rac Guanine Nucleotide Exchange Factor 1, Gingival Fibromatosis, Hereditary, 1, SOS-1, Son Of Sevenless Homolog 1 (Drosophila), Guanine Nucleotide Exchange Factor, Son Of Sevenless Homolog 1, GINGF, GGF1, GF1, HGF, NS4, Son of sevenless homolog 1.

    Product # :

    PRO-2507

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    Description

    SOS1 produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 495 amino acids (564-1049a.a.) and having a molecular mass of 58.0kDa. (Molecular size on SDS-PAGE will appear at approximately 50-70kDa).SOS1 is expressed with a 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    SOS1 protein solution (0.25mg/ml) contains 20mM Tris-HCl (pH 7.5), 30% glycerol, 0.1M NaCl, 1mM DTT & 0.2mM MgCl2.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      SOS1, also known as Gingival Fibromatosis, is a Ras & Rac guanine nucleotide exchange factor. SOS1 is comprised of a number of significant domains. The REM and CDC25 domains provide the catalytic activity of SOS1 towards Ras and the histone fold DH/PH (Dbl homology & Pleckstrin homology) domains function, in tandem, to stimulate GTP/GDP exchange for Rac. Moreover, binding of GTP activates Ras proteins, and subsequent hydrolysis of the bound GTP to GDP and phosphate inactivates signaling by these proteins. GTP binding can be catalyzed by guanine nucleotide exchange factors for RAS, and GTP hydrolysis can be enhanced by GTPase-activating proteins.

    • Synonyms

      SOS Ras/Rac Guanine Nucleotide Exchange Factor 1, Gingival Fibromatosis, Hereditary, 1, SOS-1, Son Of Sevenless Homolog 1 (Drosophila), Guanine Nucleotide Exchange Factor, Son Of Sevenless Homolog 1, GINGF, GGF1, GF1, HGF, NS4, Son of sevenless homolog 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

      ADPEEQMRLP SADVYRFAEP DSEENIIFEE NMQPKAGIPI IKAGTVIKLI ERLTYHMYAD PNFVRTFLTT YRSFCKPQEL LSLIIERFEI PEPEPTEADR IAIENGDQPL SAELKRFRKE YIQPVQLRVL NVCRHWVEHH FYDFERDAYL LQRMEEFIGT VRGKAMKKWV ESITKIIQRK KIARDNGPGH NITFQSSPPT VEWHISRPGH IETFDLLTLH PIEIARQLTL LESDLYRAVQ PSELVGSVWT KEDKEINSPN LLKMIRHTTN LTLWFEKCIV ETENLEERVA VVSRIIEILQ VFQELNNFNG VLEVVSAMNS SPVYRLDHTF EQIPSRQKKI LEEAHELSED HYKKYLAKLR SINPPCVPFF GIYLTNILKT EEGNPEVLKR HGKELINFSK RRKVAEITGE IQQYQNQPYC LRVESDIKRF FENLNPMGNS MEKEFTDYLF NKSLEIEPRN PKPLPRFPKK YSYPLKSPGV RPSNPRPGTH 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.

    Sos1 Human
  • View Data Sheet

    Name :

    KLK5 Human

    Description:

    Kallikrein-5 Human Recombinant

    Kallikrein-5, Kallikrein-like protein 2, KLK-L2, Stratum corneum tryptic enzyme, KLK5, SCTE, UNQ570/PRO1132, KLKL2.

    Product # :

    ENZ-630

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    Description

    KLK5 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 252 amino acids (67-293) and having a molecular mass of 27.8kDa.KLK5 is fused to a 25 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The KLK5 solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 2M Urea and 20% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      Kallikrein-5 (KLK5) is a member of the serine protease family of proteolytic enzymes. KLK5 is expressed in various tissues including the salivary gland, stomach, uterus, lung, thymus, prostate, colon, brain, thyroid, and trachea. KLK5 expression is up-regulated by estrogens and progestins. KLK5 is secreted and may be involved in desquamation in the epidermis. Kallikreins which are a subgroup of serine proteases, have distinct physiological functions. Many kallikreins are associated with carcinogenesis and some have potential as novel cancer and other disease biomarkers. The KLK5 gene is one of the 15 kallikrein subfamily members located in a cluster on chromosome 19.

    • Synonyms

      Kallikrein-5, Kallikrein-like protein 2, KLK-L2, Stratum corneum tryptic enzyme, KLK5, SCTE, UNQ570/PRO1132, KLKL2.

    • 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 MGSHMIINGS DCDMHTQPWQ AALLLRPNQL YCGAVLVHPQ WLLTAAHCRK KVFRVRLGHY SLSPVYESGQ QMFQGVKSIP HPGYSHPGHS NDLMLIKLNR RIRPTKDVRP INVSSHCPSA GTKCLVSGWG TTKSPQVHFP KVLQCLNISV LSQKRCEDAY PRQIDDTMFC AGDKAGRDSC QGDSGGPVVC NGSLQGLVSW GDYPCARPNR PGVYTNLCKF TKWIQETIQA NS.

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    Klk5 Human
  • View Data Sheet

    Name :

    PON1 Human (170-232)

    Description:

    Paraoxonase-1 (170-232) Human Recombinant

    Serum paraoxonase, arylesterase 1, EC 3.1.1.2, EC 3.1.8.1, PON 1.

    Product # :

    ENZ-1198

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    Description

    The PON1 Human is created as a recombinant protein with a 4kda N-terminal fusion of His Tag. The PON1 His-Tagged Fusion Protein, produced in E. coli, is a 13kDa protein containing 63 amino acid residues of the PON1 Human, 170-232 amino acids.

    Source

    Escherichia Coli.

    Formulation

    Each mg was lyophilized with 1xPBS, 0.4% SDS and 4mM DTT.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    Citations

    More Info

    • Synonyms

      Serum paraoxonase, arylesterase 1, EC 3.1.1.2, EC 3.1.8.1, PON 1.

    • Physical Appearance

      Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Store lyophilized PON1 at -20°C. Aliquot the product after reconstitution to avoid repeated freezing/thawing cycles. Reconstituted protein can be stored at 4°C for a limited period of time; it does not show any change after two weeks at 4°C.

    • Solubility

      It is recommended to add deionized water to prepare a working stock solution of approximately 0.5mg/ml and let the lyophilized pellet dissolve completely. Product is not sterile!

      Please filter the product by an appropriate sterile filter before using it on cell culture.

    • Background

      PON1takes part in the detoxification of organophosphate insecticides such as parathion.

      PON1 is related to high-density lipoprotein (HDL) in the plasma and takes an important part in lipid metabolism and antioxidant defense.

      PON1 was first known for its ability to protect against oxidative stress and hydrolyze organophosphates.

      PON1 reduces oxidative stress by preventing the oxidation of lipids in LDL particles, which is extremely important in mitigating atherosclerosis and other cardiovascular diseases.

      PON1 has anti-inflammatory effects which help reduce inflammatory markers in different disease states.

      PON1 takes part in cholesterol metabolism, influencing the stability and formation of HDL particles, which are vital for lipid transport and reverse cholesterol efflux.

    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.

    Paraoxonase 1 Human
  • View Data Sheet

    Name :

    HNMT Human, Active

    Description:

    Histamine N-Methyltransferase Human Recombinant, Active

     HMT, HNMT-S1, HNMT-S2, MRT51.

    Product # :

    ENZ-1071

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    Description

    HNMT Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 328 amino acids (1-292 a.a) and having a molecular mass of 37.4kDa. HNMT is fused to a 36 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    HNMT protein solution (1mg/ml) containing 20mM, Tris-Hcl (pH8.0) and 10% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    Biological Activity

    Specific activity is > 200 nmol/min/mg, and is defined as the amount of enzyme that transfer 1.0 nmole of methyl group per minute at 37°C.

    Citations

    More Info

    • Introduction

      Histamine N-Methyltransferase or HNMT, is located in the cell cytosol. Sadenosyl-L-methionine acts as a methyl donor for HNMT which inactivates histamine. By inactivation of histamine, it affects the immune system’s response. HNMT acts on histamine in body tissues such as kidney, central nervous system and bronchus. The protein has a crucial part in the airway response to histamine & histamine degradation process and regulation.

    • Synonyms

      HMT, HNMT-S1, HNMT-S2, MRT51.

    • 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).Please avoid freeze-thaw cycles.

    • Amino Acid Sequence

      MRGSHHHHHH GMASMTGGQQ MGRDLYDDDD KDRWGSMASS MRSLFSDHGK YVESFRRFLN HSTEHQCMQE FMDKKLPGII GRIGDTKSEI KILSIGGGAG EIDLQILSKV QAQYPGVCIN NEVVEPSAEQ IAKYKELVAK TSNLENVKFA WHKETSSEYQ SRMLEKKELQ KWDFIHMIQM LYYVKDIPAT LKFFHSLLGT NAKMLIIVVS GSSGWDKLWK KYGSRFPQDD LCQYITSDDL TQMLDNLGLK YECYDLLSTM DISDCFIDGD ENGDLLWDFL TETCNFNATA PPDLRAELGK DLQEPEFSAK KEGKVLFNNT LSFIVIEA.

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    Hnmt Protein
  • View Data Sheet

    Name :

    ART4 Human

    Description:

    ADP-Ribosyltransferase 4 Human Recombinant

    ARTC4, DOK1, CD297 Antigen, Dombrock Blood Group, ADP-Ribosyltransferase 4, Ecto-ADP-Ribosyltransferase 4.

    Product # :

    ENZ-1072

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    Description

    ART4 produced in Sf9 Insect cells is a single, glycosylated polypeptide chain containing 248 amino acids (47-285 a.a.) and having a molecular mass of 28.8kDa (Molecular size on SDS-PAGE will appear at approximately 28-40kDa). ART4 is expressed with a 9 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Insect cells.

    Formulation

    ART4 protein solution (0.25mg/ml) contains Buffered Saline (pH 7.4) and 10% glycerol.

    Purity

    Greater than 85% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      Ecto-ADP-Ribosyltransferase 4 or ART4 is typed as a glycosylphosphatidylinositol (GPI)-linked membrane protein which carries Dombrock blood group antigens. The development of this protein takes place at the highest levels in the fetal liver. the process of the ART4 development is regulated while the erythroid differentiation process occurs. ART4 is a is part of the Ribosyltransferase family.

    • Synonyms

      ARTC4, DOK1, CD297 Antigen, Dombrock Blood Group, ADP-Ribosyltransferase 4, Ecto-ADP-Ribosyltransferase 4.

    • 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

      ADPSEVAIKI DFDFAPGSFD DQYQGCSKQV MEKLTQGDYF TKDIEAQKNY FRMWQKAHLA WLNQGKVLPQ NMTTTHAVAI LFYTLNSNVH SDFTRAMASV ARTPQQYERS FHFKYLHYYL TSAIQLLRKD SIMENGTLCY EVHYRTKDVH FNAYTGATIR FGQFLSTSLL KEEAQEFGNQ TLFTIFTCLG APVQYFSLKK EVLIPPYELF KVINMSYHPR GDWLQLRSTG NLSTYNCQLL KAHHHHHH.

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    Art4 Human
  • View Data Sheet

    Name :

    Benzonase Nuclease, 90%

    Description:

    Benzonase Nuclease Serratia Marcescens Recombinant, 90%

    Product # :

    ENZ-1150

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    Description

    Benzonase Nuclease Serratia Marcescens Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 245 amino acids and having a molecular mass of 30kDa with 2 essential disulfide bonds. Benzonase Nuclease is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The Benzonase Nuclease solution contains 50% glycerol, 50 mM Tris-HCl pH 8.0, 20 mM NaCl and 2 mM MgCl2.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      Serratia marcescens secretes an endonuclease that has exceptionally high specific activity to the medium that surrounds it. The Benzonase Nuclease is mainly used for elimination of nucleic acid contamination from purified proteins, downstream processing, reduction of viscosity etc. Nucleic acid contaminants are caused by nuclease released to the medium. The DNA is being destroyed by the release of the S. marcescens nuclease and it acts as the killer gene for the auto destruction of microorganisms.

    • 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.

    • Specificity

      Unspecific (DNA, RNA) attacks all nucleic acids (single strand, double strand, circular, supercoiled) with no apparent sequence preference. Final reaction product: 5’-mono-phosphate terminated oligonucleotides (3-5 bases). Protease Activity: Not detectable

    • Unit Definition

      1U Benzonase Nuclease is defined as the amount of enzyme that causes a ΔA260 of 1 in 30 min, which corresponds to complete digestion of 37μg DNA. Standard reaction conditions are 1mg/ml sonicated DNA substrate in 50mM Tris-HCl pH 8.0, 0.1mg/ml BSA, 1mM MgCl2, incubated at 37°C.

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    Benzonase Nuclease Enzyme
  • View Data Sheet

    Name :

    ALDH1A1 Human, Active

    Description:

    Aldehyde Dehydrogenase 1A1 Human Recombinant, Active

    ALDC, Aldehyde dehydrogenase cytosolic, Aldehyde dehydrogenase family 1 member A1, ALDH1, ALDH11, ALDH-E1, ALHDII, MGC2318, PUMB1, RalDH1, RALDH1, RALDH 1, Retinal dehydrogenase 1, ALDH1A1.

    Product # :

    ENZ-1179

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    Description

    The ALDH1A1 Human recombinant protein is a single, non-glycosilated polypeptide chain produced in E. coli, having a molecular weight of 54.8kDa and containing 501 amino acids (1-501 a.a.).

    Source

    Escherichia Coli.

    Formulation

    The ALDH1A1 protein solution is formulated at 1mg/ml in 50mM Tris-HCl pH-7.5 and 10% glycerol.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    Biological Activity

    > 700 pmol/min/ug, as determined by the increase of NADH in absorbance at 340nm resulting from the reduction of NAD at pH 8.8 at 37C.                                                                 

    Citations

    More Info

    • Introduction

      ALDH1A1 is part of the aldehyde dehydrogenases family.
      Aldehyde dehydrogenase is the 2nd protein of the main oxidative pathway of alcohol metabolism. Cytosolic and mitochondrial are 2 main liver isoforms of ALDH that are differentiateed by their electrophoretic mobility, kinetic property, & subcellular localization. The majority of Caucasians have two main isozymes, whereas just about 50% of Orientals have only the cytosolic form, excluding the mitochondrial form. ALDH1A1 is also a member of the group of corneal crystallins that assist the transparency of the cornea.
      (Retinal + NAD+ + H2O = retinoate + NADH).

    • Synonyms

      ALDC, Aldehyde dehydrogenase cytosolic, Aldehyde dehydrogenase family 1 member A1, ALDH1, ALDH11, ALDH-E1, ALHDII, MGC2318, PUMB1, RalDH1, RALDH1, RALDH 1, Retinal dehydrogenase 1, ALDH1A1.

    • 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.

    • Amino Acid Sequence

      MSSSGTPDLP VLLTDLKIQY TKIFINNEWH DSVSGKKFPV FNPATEEELC QVEEGDKEDV DKAVKAARQA FQIGSPWRTM DASERGRLLYKLADLIERDR LLLATMESMN GGKLYSNAYL NDLAGCIKTL RYCAGWADKI QGRTIPIDGN FFTYTRHEPI GVCGQIIPWN FPLVMLIWKIGPALSCGNTV VVKPAEQTPL TALHVASLIK EAGFPPGVVN IVPGYGPTAG AAISSHMDID KVAFTGSTEV GKLIKEAAGK SNLKRVTLEL GGKSPCIVLA DADLDNAVEF AHHGVFYHQG QCCIAASRIF VEESIYDEFV RRSVERAKKY ILGNPLTPGV TQGPQIDKEQ YDKILDLIES GKKEGAKLEC GGGPWGNKGY FVQPTVFSNV TDEMRIAKEE IFGPVQQIMK FKSLDDVIKR ANNTFYGLSA GVFTKDIDKA ITISSALQAG TVWVNCYGVV SAQCPFGGFK MSGNGRELGE YGFHEYTEVK TVTVKISQKN S.

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    Aldh1A1 Protein
  • View Data Sheet

    Name :

    HAO1 Mouse

    Description:

    Hydroxyacid Oxidase 1 Mouse Recombinant

    (S)-2-hydroxy-acid oxidase; EC 1.1.3.15, Glycolate oxidase, GOX, GOX1MGC142227;GOXMGC142225, HAO1, HAO-1, HAOX1, hydroxyacid oxidase (glycolate oxidase) 1, hydroxyacid oxidase 1, Hydroxyacid Oxidase1, Hydroxyacid Oxidase-1.

    Product # :

    ENZ-1104

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    Description

    HAO1 Mouse Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 393 amino acids (1-370) and having a molecular mass of 43.4 kDa.HAO1 is fused to a 23 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    HAO1 protein (1mg/ml) is containing Phosphate Buffered Saline (pH 7.4) and 10% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    Biological Activity

    Specific activity is > 1,000 pmol/min/ug, and defined as the amount of enzyme that oxidize glyoxylate at pH 8.0 at 25C.

    Citations

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    • Introduction

      Hydroxyacid Oxidase 1 (HAO1) is a part of the superfamily of the alpha hydroxy acid oxidases (HAO) enzymes. HAO1 catalyses the FMN mediated oxidation of glycolate to glyoxylate and glyoxylate to oxalate by reducing oxygen to hydrogen peroxide. HAO1 is expressed mainly in the liver and pancreas and is most active on twocarbon substrates such as glycolate. HAO1 isthe main cause of hyperoxaluria, a disorder in which large deposits of calcium oxalate form kidney stones.

    • Synonyms

      (S)-2-hydroxy-acid oxidase; EC 1.1.3.15, Glycolate oxidase, GOX, GOX1MGC142227;
      GOXMGC142225, HAO1, HAO-1, HAOX1, hydroxyacid oxidase (glycolate oxidase) 1, hydroxyacid oxidase 1, Hydroxyacid Oxidase1, Hydroxyacid Oxidase-1.

    • 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 MGSMLPRLVC ISDYEQHVRS VLQKSVYDYY RSGANDQETL ADNIQAFSRW KLYPRMLRNV ADIDLSTSVL GQRVSMPICV GATAMQCMAH VDGELATVRA CQTMGTGMML SSWATSSIEE VAEAGPEALR WMQLYIYKDR EISRQIVKRA EKQGYKAIFV TVDTPYLGNR IDDVRNRFKL PPQLRMKNFE TNDLAFSPKG NFGDNSGLAE YVAQAIDPSL SWDDITWLRR LTSLPIVVKG ILRGDDAKEA VKHGVDGILV SNHGARQLDG VPATIDVLPE IVEAVEGKVE VFLDGGVRKG TDVLKALALG AKAVFVGRPI IWGLAFQGEK GVQDVLEILK EEFRLAMALS GCQNVKVIDK TLVRKNPLAV SKI.

    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.

    Hao1 Mouse
  • View Data Sheet

    Name :

    MIOX Human

    Description:

    Myo-Inositol Oxygenase Human Recombinant

    Myo-Inositol Oxygenase, Kidney-Specific Protein 32, Aldehyde Reductase (Aldose Reductase) Like 6, Renal-Specific Oxidoreductase, Aldehyde Reductase-Like 6, MI Oxygenase, EC 1.13.99.1, ALDRL6, Inositol Oxygenase, KSP32, RSOR, MIOX.

    Product # :

    ENZ-812

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    Description

    MIOX Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain (Met1-Trp285) containing 295 amino acids including a 10 aa His tag at N-terminus. The total calculated molecular mass is 34.2kDa.

    Source

    Escherichia Coli.

    Formulation

    MIOX was filtered (0.4 µm) and lyophilized in 20mM Tris buffer, 50mM NaCl and 5% (w/v) trehalose, pH 7.5.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      Inositol oxygenase is a non-heme di-iron enzyme which oxidizes myo-inositol to glucuronic acid. In addition, inositol oxygenase oxidizes the less abundant chiro isomer of inositol. MIOX enzyme is a component of the only known pathway for the catabolism of inositol in humans. MIOX is expressed mostly in the kidneys. Reduction of Inositol Oxygenase and accumulation of polyols, such as inositol and xylitol, have been implicated as contributing factors in complications linked with diabetes.

    • Synonyms

      Myo-Inositol Oxygenase, Kidney-Specific Protein 32, Aldehyde Reductase (Aldose Reductase) Like 6, Renal-Specific Oxidoreductase, Aldehyde Reductase-Like 6, MI Oxygenase, EC 1.13.99.1, ALDRL6, Inositol Oxygenase, KSP32, RSOR, MIOX.

    • Physical Appearance

      Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Store lyophilized protein at -20°C. Aliquot the product after reconstitution to avoid repeated freezing/thawing cycles. Reconstituted protein can be stored at 4°C for a limited period of time; it does not show any change after two weeks at 4°C.

    • Solubility

      It is recommended to add deionized water to prepare a working stock solution of approximately 0.5mg/ml and let the lyophilized pellet dissolve completely. MIOX is not sterile! Please filter the product by an appropriate sterile filter before using it in the cell culture.

    • Amino Acid Sequence

      MKHHHHHHASMKVTVGPDPS LVYRPDVDPE VAKDKASFRN YTSGPLLDRV FTTYKLMHTH QTVDFVRSKH AQFGGFSYKK MTVMEAVDLL DGLVDESDPD VDFPNSFHAF QTAEGIRKAH PDKDWFHLVG LLHDLGKVLA LFGEPQWAVV GDTFPVGCRP QASVVFCDST FQDNPDLQDP RYSTELGMYQ PHCGLDRVLM SWGHDEYMYQ VMKFNKFSLP PEAFYMIRFH SFYPWHTGRD YQQLCSQQDL AMLPWVREFN KFDLYTKCPD LPDVDKLRPY YQGLIDKYCP GILSW.

    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.

    Miox 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.

    Citations

    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 :

    SEPX1 Human

    Description:

    Selenoprotein X 1 Human Recombinant

    Methionine-R-sulfoxide reductase B1, MsrB1, Selenoprotein X, SelX, SEPX1, SELR, SELX, HSPC270, MGC3344.

    Product # :

    PRO-260

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    Description

    SEPX1 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 136 amino acids (1-116 a.a.) and having a molecular mass of 14.8kDa. In bacteria, the selenocystein (Sec/U) element is positioned directly following the UGA codon within the reading frame for the selenoprotein so we mutated Sec-95 to Cys. The SEPX1 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The SEPX1 solution (0.5 mg/ml) contains 20mM Tris-HCl Buffer (pH 7.5), 1mM DTT, 0.1mM PMSF, 2mM EDTA and 10% Glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      Methionine sulfoxide reductase B1 (SEPX1 or MSRB1), is a selenoprotein that contains a selenocysteine (Sec) residue at its active site. The selenocysteine is encoded by the UGA codon that usually signals translation termination. SEPX1 is a member of the methionine sulfoxide reductase B (MsrB) family, and is expressed in an assortment of adult and fetal tissues. MSRs (Methionine sulfoxide reductases) catalyze the reduction of free and protein-bound methionine sulfoxides to corresponding methionines. The oxidation of methionine by ROS creates a diastereomeric mixture of methionine-S-sulfoxide (Met-S-SO) and methionine-R-sulfoxide (Met-R-SO). Two separate enzyme families evolved for reduction of these sulfoxides, with methionine-S-sulfoxide reductase (MsrA) being stereospecific for Met-S-SO and methionine-R-sulfoxide reductase (MsrB) for Met-R-SO.

    • Synonyms

      Methionine-R-sulfoxide reductase B1, MsrB1, Selenoprotein X, SelX, SEPX1, SELR, SELX, HSPC270, MGC3344.

    • 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 MSFCSFFGGE VFQNHFEPGV YVCAKCGYEL FSSRSKYAHS SPWPAFTETI HADSVAKRPE HNRSEALKVS CGKCGNGLGH EFLNDGPKPG QSRFCIFSSS LKFVPKGKET SASQGH.

    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.

    Sepx1 Human
  • View Data Sheet

    Name :

    NUDT3 Human

    Description:

    Nudix Type Motif 3 Human Recombinant

    Diphosphoinositol polyphosphate phosphohydrolase 1, DIPP-1, Diadenosine 5',5'''-P1,P6-hexaphosphate hydrolase 1, Nucleoside diphosphate-linked moiety X motif 3, Nudix motif 3, NUDT3, DIPP, DIPP1.

    Product # :

    ENZ-071

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    Description

    NUDT3 Human Recombinant fused with a 20 amino acid His tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 192 amino acids (1-172 a.a.) and having a molecular mass of 21.6kDa. The NUDT3 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The NUDT3 solution (0.5 mg/ml) contains 20mM Tris-HCl buffer (pH8.0), 0.2M NaCl, 5mM DTT and 20% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      NUDT3 is a 172 amino acid cytoplasmic protein which is a member of the nudix hydrolase family and DIPP subfamily. NUDT3 functions as a negative regulator of the ERK 1/2 pathway and hydrolyzes 5-phosphoribose 1-diphosphate. NUDT3 is a monomer which binds magnesium as a cofactor. In addition, NUDT3 is widely expressed but can be found at highest levels in the liver, pancreas, brain and heart.

    • Synonyms

      Diphosphoinositol polyphosphate phosphohydrolase 1, DIPP-1, Diadenosine 5',5'''-P1,P6-hexaphosphate hydrolase 1, Nucleoside diphosphate-linked moiety X motif 3, Nudix motif 3, NUDT3, DIPP, DIPP1.

    • 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 MMKLKSNQTR TYDGDGYKKR AACLCFRSES EEEVLLVSSS RHPDRWIVPG GGMEPEEEPS VAAVREVCEE AGVKGTLGRL VGIFENQERK HRTYVYVLIV TEVLEDWEDS VNIGRKREWF KIEDAIKVLQ YHKPVQASYF ETLRQGYSAN NGTPVVATTY SVSAQSSMSG IR.

    ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

    Nudt3 Human
  • View Data Sheet

    Name :

    TOP1 Bovine

    Description:

    DNA Topoisomerase-I Bovine

    DNA topoisomerase 1, EC 5.99.1.2, DNA topoisomerase I, TOP1, Scl-70.

    Product # :

    ENZ-656

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    Description

    Bovine DNA Topoisomerase-I shows multiple bands between 76-109 KDa and is purified from bovine tissues by proprietary chromatographic techniques.

    Source

    Bovine tissues.

    Formulation

    TOP1 is supplied in 20mM HEPES buffer pH-7.5, 400mM NaCl and 20% glycerol.

    Purity

    Greater than 95% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      TOP1 is an important nuclear enzyme that interconverts supercoiled DNA to the necessary topological conformations for standard DNA replication and transcription. TOP1 is the target antigen for TOP1 autoantibodies. TOP1 antibodies are a specific marker in scleroderma patients (specificity 98-100%) and are related with the existence of diffuse skin involvement and pulmonary fibrosis. In human tissues top1 enzyme is primarily synthesized as a protein with a molecular weight of 100-kDa. Most of this precursor is then proteolytically processed to a 70-kDa size, from which the TOP1 antigen has derived its name.

    • Synonyms

      DNA topoisomerase 1, EC 5.99.1.2, DNA topoisomerase I, TOP1, Scl-70.

    • 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.

    • Immunological Functions

      1. Binds IgG-type human auto-antibodies. 2. Standard ELISA test (checkerboard analysis of positive/negative samples) and immunodot test with positive/negative samples.

    • coating concentration

      0.5-0.8 µg/ml (depending on the type of ELISA plate and coating buffer). Suitable for labeling of functional groups.

    • Applications

      Western blot with anti TOP1 autoantibody positive sample.

    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.

    Top1 Bovine
  • View Data Sheet

    Name :

    PPM1G Human, 546 a.a.

    Description:

    Protein Phosphatase 1G 546 a.a. Human Recombinant

    Protein Phosphatase 1G, PP2CG, PPP2CG, MGC1675, MGC2870, PP2C GAMMA, EC 3.1.3.16, Protein phosphatase 2C isoform gamma, PP2C-gamma, Protein phosphatase magnesium-dependent 1 gamma, Protein phosphatase 1C, PPM1G, PPM1C.

    Product # :

    ENZ-156

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    Description

    PPM1G Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 566 amino acids (1-546) and having a molecular mass of 61.4 kDa. The PPM1G is fused to a 20 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    The PPM1G solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 1mM DTT, 0.1M NaCl, 0.1mM PMSF and 20% glycerol.

    Purity

    Greater than 85% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      PPM1G is part of the PP2C family of Ser/Thr protein phosphatases which are known to be negative regulators of cell stress response pathways. PPM1G is accountable for the dephosphorylation of Pre-mRNA splicing factors, an important factor for the formation of functional spliceosome. PPM1G regulates cell cycle progression.
      PPM1G mediates histone dephosphorylation/exchange in response to DNA damage or checkpoint recovery in higher eukaryotes.
      The degradation of p21/WAF1 induced by PPM1G is mediated in a proteasome-dependent manner.
      Protein phosphatase 1G regulates assembly and function of the beta-catenin degradation complex.

    • Synonyms

      Protein Phosphatase 1G, PP2CG, PPP2CG, MGC1675, MGC2870, PP2C GAMMA, EC 3.1.3.16, Protein phosphatase 2C isoform gamma, PP2C-gamma, Protein phosphatase magnesium-dependent 1 gamma, Protein phosphatase 1C, PPM1G, PPM1C.

    • 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 MGAYLSQPNT VKCSGDGVGA PRLPLPYGFS AMQGWRVSME DAHNCIPELD SETAMFSVYD GHGGEEVALY CAKYLPDIIK DQKAYKEGKL QKALEDAFLA IDAKLTTEEV IKELAQIAGR PTEDEDEKEK VADEDDVDNE EAALLHEEAT MTIEELLTRY GQNCHKGPPH SKSGGGTGEE PGSQGLNGEA GPEDSTRETP SQENGPTAKA YTGFSSNSER GTEAGQVGEP GIPTGEAGPS CSSASDKLPR VAKSKFFEDS EDESDEAEEE EEDSEECSEE EDGYSSEEAE NEEDEDDTEE AEEDDEEEEE EMMVPGMEGK EEPGSDSGTT AVVALIRGKQ LIVANAGDSR CVVSEAGKAL DMSYDHKPED EVELARIKNA GGKVTMDGRV NGGLNLSRAI GDHFYKRNKN LPPEEQMISA LPDIKVLTLT DDHEFMVIAC DGIWNVMSSQ EVVDFIQSKI SQRDENGELR LLSSIVEELL DQCLAPDTSG DGTGCDNMTC IIICFKPRNT AELQPESGKR KLEEVLSTEG AEENGNSDKK KKAKRD

    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.

    Ppm1G Human 546Aa
  • View Data Sheet

    Name :

    UGP2 Human

    Description:

    UDP-Glucose Pyrophosphorylase 2 Human Recombinant

    UDP-Glucose Pyrophosphorylase 2,UDP-Glucose Pyrophosphorylase 1, EC 2.7.7.9, UGPP2, UDPGP, UGP1, UTP--Glucose-1-Phosphate Uridylyltransferase 2Uridyl Diphosphate Glucose Pyrophosphorylase-1, Uridyl Diphosphate Glucose Pyrophosphorylase 2, UTP--Glucose-1-Phosphate Uridylyltransferase , UTP-Glucose-1-Phosphate, Uridyltransferase, UDP-Glucose Pyrophosphorylase , UDP-Glucose Diphosphorylase, UGPase 2, UDPGP2, PHC379, UGPase, UGPP1, UDPG.

    Product # :

    ENZ-832

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    Description

    UGP2 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 531 amino acids (1-508 a.a) and having a molecular mass of 59.3kDa.UGP2 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    UGP2 protein solution (0.25mg/ml) containing Phosphate buffered saline (pH7.4) 30% glycerol and 1mM DTT.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      UDP-Glucose Pyrophosphorylase 2, also known as UGP2 is an essential intermediary in mammalian carbohydrate inter conversions. UGP2 transfers a glucose moiety from glucose-1-phosphate to MgUTP and forms UDP-glucose and MgPPi. UDP-glucose is a direct precursor of glycogen in the liver and muscle tissue, moreover in lactating mammary gland it is converted to UDP-galactose which is next converted to lactose.

    • Synonyms

      UDP-Glucose Pyrophosphorylase 2,UDP-Glucose Pyrophosphorylase 1, EC 2.7.7.9, UGPP2, UDPGP, UGP1, UTP--Glucose-1-Phosphate Uridylyltransferase 2Uridyl Diphosphate Glucose Pyrophosphorylase-1, Uridyl Diphosphate Glucose Pyrophosphorylase 2, UTP--Glucose-1-Phosphate Uridylyltransferase , UTP-Glucose-1-Phosphate, Uridyltransferase, UDP-Glucose Pyrophosphorylase , UDP-Glucose Diphosphorylase, UGPase 2, UDPGP2, PHC379, UGPase, UGPP1, UDPG.

    • 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 MGSMSRFVQD LSKAMSQDGA SQFQEVIRQE LELSVKKELE KILTTASSHE FEHTKKDLDG FRKLFHRFLQ EKGPSVDWGK IQRPPEDSIQ PYEKIKARGL PDNISSVLNK LVVVKLNGGL GTSMGCKGPK SLIGVRNENT FLDLTVQQIE HLNKTYNTDV PLVLMNSFNT DEDTKKILQK YNHCRVKIYT FNQSRYPRIN KESLLPVAKD VSYSGENTEA WYPPGHGDIY ASFYNSGLLD TFIGEGKEYI FVSNIDNLGA TVDLYILNHL MNPPNGKRCE FVMEVTNKTR ADVKGGTLTQ YEGKLRLVEI AQVPKAHVDE FKSVSKFKIF NTNNLWISLA AVKRLQEQNA IDMEIIVNAK TLDGGLNVIQ LETAVGAAIK SFENSLGINV PRSRFLPVKT TSDLLLVMSN LYSLNAGSLT MSEKREFPTV PLVKLGSSFT KVQDYLRRFE SIPDMLELDH LTVSGDVTFG KNVSLKGTVI IIANHGDRID IPPGAVLENK IVSGNLRILD H.

    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.

    Ugp2 Human
  • View Data Sheet

    Name :

    CTSZ Antibody

    Description:

    Cathepsin-Z, Mouse Anti Human

    Cathepsin Z preproprotein, Cathepsin Z, CTSX, Cathepsin P, Cathepsin X, CTSZ, Cathepsin-Z.

    Product # :

    ANT-528

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    Formulation

    1mg/ml containing PBS, pH-7.4, 10% Glycerol and 0.02% Sodium Azide.

    Citations

    More Info

    • Introduction

      Cathepsin-Z (CTSZ) is a lysosomal cysteine proteinase and member of the peptidase C1 family. CTSZ, which has been also known 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, similar to other members of this family, takes part in tumorigenesis.

    • Synonyms

      Cathepsin Z preproprotein, Cathepsin Z, CTSX, Cathepsin P, Cathepsin X, CTSZ, Cathepsin-Z.

    • Physical Appearance

      Sterile filtered colorless solution.

    • Immunogen

      Anti-human CTSZ mAb, clone PAT6G11AT, is derived from hybridization of mouse F0 myeloma cells with spleen cells from BALB/c mice immunized with a recombinant human CTSZ protein 62-303 amino acids purified from E. coli.

    • Ig Subclass

      Mouse IgG2b heavy chain and k light chain.

    • Clone

      PAT6G11AT.

    • Applications

      The antibody has been tested by ELISA, Western blot analysis to assure specificity and reactivity. Since application varies, however, each investigation should be titrated by the reagent to obtain optimal results. Recommended starting dilution is 1:1000.

    • Type

      Mouse Anti Human Monoclonal.

    • Storage Procedures

      For periods up to 1 month store at 4°C, for longer periods of time, store at -20°C. Prevent freeze thaw cycles.

    • Purification Method

      CTSZ antibody was purified from mouse ascitic fluids by protein-A affinity chromatography.

    ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

    Ctsz Antibody
  • View Data Sheet

    Name :

    MCSFR Human

    Description:

    Colony Stimulating Factor 1 Receptor Human Recombinant

    Macrophage colony-stimulating factor 1 receptor, CSF-1 receptor (EC:2.7.10.1), CSF-1-R, CSF-1R, M-CSF-R, Proto-oncogene c-Fms, CD115, CSF1R, FMS. 

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    CYT-1068

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    Description

    MCSFR produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 737 amino acids (20-517a.a.) and having a molecular mass of 82.1kDa. (Molecular size on SDS-PAGE will appear at approximately 70-100kDa).MCSFR is expressed with a 239 amino acid hIgG-His tag at C-Terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

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

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    Biological Activity

    Measured by its ability to inhibit M-CSF dependent proliferation of M-NFS-60 mouse myelogenous leukemia lymphoblast cells. The ED50 for this effect is less or equal to 100ng/ml in the presence of 10 ng/ml M-CSF.

    Citations

    More Info

    • Introduction

      MCSFR which is also familiar as CSF1R, is part of the type3 subfamily of receptor tyrosine kinases. MCSFR is expressed mainly on cells of the monocyte and macrophage lineage, stem cells, and in the growing placenta. Most of the biological effects of this cytokine are mediated by MCSFR. MCSFR contains an extracellular ligand-binding domain, a single membrane-spanning segment, and an intracellular tyrosine kinase domain. Originally CSF1 and this receptor were implicated as vital for normal trophoblastic implantation as well as monocyte development. The role of CSF1/CSF1R in normal mammary gland development is actually very interesting since this connection has also been discovered in the biology of breast cancer with the results of abnormal expression of CSF1 and its receptor. Likewise, in Alzheimer's disease and after brain injuries an increased level of CSF1R was found in the microglia, which causes the microglia to become more active.

    • Synonyms

      Macrophage colony-stimulating factor 1 receptor, CSF-1 receptor (EC:2.7.10.1), CSF-1-R, CSF-1R, M-CSF-R, Proto-oncogene c-Fms, CD115, CSF1R, FMS.

    • 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

      IPVIEPSVPE LVVKPGATVT LRCVGNGSVE WDGPPSPHWT LYSDGSSSIL STNNATFQNT GTYRCTEPGD PLGGSAAIHL YVKDPARPWN VLAQEVVVFE DQDALLPCLL TDPVLEAGVS LVRVRGRPLM RHTNYSFSPW HGFTIHRAKF IQSQDYQCSA LMGGRKVMSI SIRLKVQKVI PGPPALTLVP AELVRIRGEA AQIVCSASSV DVNFDVFLQH NNTKLAIPQQ SDFHNNRYQK VLTLNLDQVD FQHAGNYSCV ASNVQGKHST SMFFRVVESA YLNLSSEQNL IQEVTVGEGL NLKVMVEAYP GLQGFNWTYL GPFSDHQPEP KLANATTKDT YRHTFTLSLP RLKPSEAGRY SFLARNPGGW RALTFELTLR YPPEVSVIWT FINGSGTLLC AASGYPQPNV TWLQCSGHTD RCDEAQVLQV WDDPYPEVLS QEPFHKVTVQ SLLTVETLEH NQTYECRAHN SVGSGSWAFI PISAGAHTHP PDEFLFTPLE PKSCDKTHTC PPCPAPELLG GPSVFLFPPK PKDTLMISRT PEVTCVVVDV SHEDPEVKFN WYVDGVEVHN AKTKPREEQY NSTYRVVSVL TVLHQDWLNG KEYKCKVSNK ALPAPIEKTI SKAKGQPREP QVYTLPPSRD ELTKNQVSLT CLVKGFYPSD IAVEWESNGQ PENNYKTTPP VLDSDGSFFL YSKLTVDKSR WQQGNVFSCS VMHEALHNHY TQKSLSLSPG KHHHHHH.

    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.

    Csf1R Human
  • View Data Sheet

    Name :

    MIF Human, GST

    Description:

    Macrophage Migration Inhibitor Factor Human Recombinant, GST tag

    Macrophage Migration Inhibitory Factor (Glycosylation-Inhibiting Factor), Phenylpyruvate Tautomerase, L-Dopachrome Tautomerase, L-Dopachrome Isomerase, GLIF, MMIF, GIF, Macrophage Migration Inhibitory Factor, Glycosylation-Inhibiting Factor, EC 5.3.3.12, EC 5.3.2.1, Macrophage migration inhibitory factor.

    Product # :

    CYT-401

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    • source
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    • Citations

    Description

    MIF Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 345 amino acids (1-115 a.a) and having a molecular mass of 39.2kDa. MIF is fused to a 230 amino acid GST-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    MIF protein solution (1mg/ml) containing Phosphate Buffered Saline (pH7.4) and 10% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      The cytokine Macrophage migration inhibitory factor (MIF) has been identified to be secreted by the pituitary gland and the monocyte/macrophage and to play an important role in endotoxic shock. MIF has the unique property of being released from macrophages and T cells in response to physiological concentrations of glucocorticoids. The secretion of MIF is tightly regulated and decreases at high, anti-inflammatory steroid concentration.

    • Synonyms

      Macrophage Migration Inhibitory Factor (Glycosylation-Inhibiting Factor), Phenylpyruvate Tautomerase, L-Dopachrome Tautomerase, L-Dopachrome Isomerase, GLIF, MMIF, GIF, Macrophage Migration Inhibitory Factor, Glycosylation-Inhibiting Factor, EC 5.3.3.12, EC 5.3.2.1, Macrophage migration inhibitory factor.

    • 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

      MSPILGYWKI KGLVQPTRLL LEYLEEKYEE HLYERDEGDK WRNKKFELGL EFPNLPYYID GDVKLTQSMA IIRYIADKHN MLGGCPKERA EISMLEGAVL DIRYGVSRIA YSKDFETLKV DFLSKLPEML KMFEDRLCHK TYLNGDHVTH PDFMLYDALD VVLYMDPMCL DAFPKLVCFK KRIEAIPQID KYLKSSKYIA WPLQGWQATF GGGDHPPKSD LVPRGSPEFA MPMFIVNTNV PRASVPDGFL SELTQQLAQA TGKPPQYIAV HVVPDQLMAF GGSSEPCALC SLHSIGKIGG AQNRSYSKLL CGLLAERLRI SPDRVYINYY DMNAANVGWN NSTFA.

    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.

    Mif Human Gst
  • View Data Sheet

    Name :

    CYB5R2 Human

    Description:

    Cytochrome B5 Reductase 2 Human Recombinant

    CYB5R2, Cytochrome B5 Reductase 2, EC 1.6.2.2, B5R.2, Cytochrome B5 Reductase B5R.2, NADH-Cytochrome B5 Reductase 2, b5R.2.

    Product # :

    ENZ-799

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    Description

    CYB5R2 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 299 amino acids (1-276 a.a.) and having a molecular mass of 33.8kDa. CYB5R2 is fused to a 23 amino acid His-tag at N-terminus.

    Source

    Escherichia Coli.

    Formulation

    CYB5R2 protein solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 10% glycerol and 1mM DTT.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      Cytochrome b5 reductase 2 (CYB5R2) is involved in desaturation and elongation of fatty acids, cholesterol biosynthesis, drug metabolism, and, in erythrocyte, methemoglobin reduction. CYB5R2 is responsible for NADH-dependent lucigenin chemiluminescence in spermatozoa by reducing both lucigenin and 2-[4-iodophenyl]-3-[4-nitrophenyl]-5-[2,4-disulfophenyl]-2H tetrazolium monosodium salt (WST-1).

    • Synonyms

      CYB5R2, Cytochrome B5 Reductase 2, EC 1.6.2.2, B5R.2, Cytochrome B5 Reductase B5R.2, NADH-Cytochrome B5 Reductase 2, b5R.2.

    • 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 MGSMNSRRRE PITLQDPEAK YPLPLIEKEK ISHNTRRFRF GLPSPDHVLG LPVGNYVQLL AKIDNELVVR AYTPVSSDDD RGFVDLIIKI YFKNVHPQYP EGGKMTQYLE NMKIGETIFF RGPRGRLFYH GPGNLGIRPD QTSEPKKTLA DHLGMIAGGT GITPMLQLIR HITKDPSDRT RMSLIFANQT EEDILVRKEL EEIARTHPDQ FNLWYTLDRP PIGWKYSSGF VTADMIKEHL PPPAKSTLIL VCGPPPLIQT AAHPNLEKLG YTQDMIFTY.

    ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

    Cyb5R2 Human
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