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Search results

843 results found for “carbonic anhydrase”

Name

Description

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  • View Data Sheet

    Name :

    MMP14 Human, His

    Description:

    Matrix Metalloproteinase-14 Human Recombinant, His Tag

    Matrix Metallopeptidase 14, Matrix Metallopeptidase 14 (Membrane-Inserted), Membrane-Type-1 Matrix Metalloproteinase, Membrane Type 1 Metalloprotease, EC 3.4.24.80, MT-MMP 1, MT1-MMP, MMP-14, MMP-X1, MT1MMP, MTMMP1, Matrix Metalloproteinase 14 (Membrane-Inserted), Membrane-Type Matrix Metalloproteinase 1, Matrix Metalloproteinase-14, EC 3.4.24, MT-MMP, WNCHRS, Matrix metalloproteinase-14, Membrane-type matrix metalloproteinase 1.

    Product # :

    ENZ-1003

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    Description

    MMP14 Human Recombinant produced in Sf9 Baculovirus cells is a single, non-glycosylated polypeptide chain containing 527 amino acids (21-538a.a) and having a molecular mass of 59.9kDa (Molecular size on SDS-PAGE will appear at approximately 35-70kDa). MMP14 is fused to a 6 amino acid His-tag at C-terminus & purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    MMP14 protein solution (0.25mg/ml) containing Phosphate Buffered Saline (pH 7.4) and 10% glycerol.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      Matrix metalloproteinase-14 (MMP14), is a membrane-anchored zinc-binding endopeptidase which is expressed at the leading edge of different invasive carcinomas and also promotes tumor cell invasion through degradation of the extracellular matrix. MMP14 takes a vital part in extracellular matrix, ECM, remodeling by having the capability to degrade type I collagen, activate pro-MMP-2 and process cell adhesion molecules for instance CD44 and integrin alpha V. MMP14 is a key enzyme in many physiological as well as pathological processes for example angiogenesis & tumor invasion.

    • Synonyms

      Matrix Metallopeptidase 14, Matrix Metallopeptidase 14 (Membrane-Inserted), Membrane-Type-1 Matrix Metalloproteinase, Membrane Type 1 Metalloprotease, EC 3.4.24.80, MT-MMP 1, MT1-MMP, MMP-14, MMP-X1, MT1MMP, MTMMP1, Matrix Metalloproteinase 14 (Membrane-Inserted), Membrane-Type Matrix Metalloproteinase 1, Matrix Metalloproteinase-14, EC 3.4.24, MT-MMP, WNCHRS, Matrix metalloproteinase-14, Membrane-type matrix metalloproteinase 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

      ADLALASLGS AQSSSFSPEA WLQQYGYLPP GDLRTHTQRS PQSLSAAIAA MQKFYGLQVT GKADADTMKA MRRPRCGVPD KFGAEIKANV RRKRYAIQGL KWQHNEITFC IQNYTPKVGE YATYEAIRKA FRVWESATPL RFREVPYAYI REGHEKQADI MIFFAEGFHG DSTPFDGEGG FLAHAYFPGP NIGGDTHFDS AEPWTVRNED LNGNDIFLVA VHELGHALGL EHSSDPSAIM APFYQWMDTE NFVLPDDDRR GIQQLYGGES GFPTKMPPQP RTTSRPSVPD KPKNPTYGPN ICDGNFDTVA MLRGEMFVFK ERWFWRVRNN QVMDGYPMPI GQFWRGLPAS INTAYERKDG KFVFFKGDKH WVFDEASLEP GYPKHIKELG RGLPTDKIDA ALFWMPNGKT YFFRGNKYYR FNEELRAVDS EYPKNIKVWE GIPESPRGSF MGSDEVFTYF YKGNKYWKFN NQKLKVEPGY PKSALRDWMG CPSGGRPDEG TEEETEVIII EVDEEGGGAV SHHHHHH.

    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.

    Mmp14 Human
  • View Data Sheet

    Name :

    CCNH Antibody

    Description:

    Cyclin-H, Mouse Anti Human

    CCNH, CAK, p34, p37, Cyclin-H, MO15-associated protein.

    Product # :

    ANT-583

    Price :

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    Formulation

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

    Citations

    More Info

    • Introduction

      CCNH is part of the cyclin family that is known for its protein abundance through the cell cycle. Cyclins act as regulators of CDK kinases. CCNH forms a complex with CDK7 kinase and ring finger protein MAT1. The kinase complex is able to phosphorylate CDK2 and CDC2 kinases, therefore it functions as a CDK-activating kinase (CAK). CCNH and its kinase collaborator are components of TFIIH, as well as RNA polymerase II protein complexes.

    • Synonyms

      CCNH, CAK, p34, p37, Cyclin-H, MO15-associated protein.

    • Physical Appearance

      Sterile filtered colorless solution.

    • Immunogen

      Anti-human CCNH mAb, is derived from hybridization of mouse F0 myeloma cells with spleen cells from BALB/c mice immunized with recombinant human CCNH amino acids 1-323 purified from E. coli.

    • Ig Subclass

      Mouse IgG2b heavy chain and k light chain.

    • Clone

      PAT3G6AT.

    • Applications

      CCNH 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 for Western blot analysis 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

      CCNH 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.

    Ccnh Antibody
  • View Data Sheet

    Name :

    ACY1 Mouse

    Description:

    AminoAcylase-1 Mouse Recombinant

    Aminoacylase-1, ACY-1, N-acyl-L-amino-acid amidohydrolase, Aminoacylase 1, Acy1.

    Product # :

    ENZ-905

    Price :

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    Description

    ACY1 Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 433 amino acids (1-408 a.a) and having a molecular mass of 48.4kDa. ACY1 is fused to a 25 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    ACY1 protein solution (0.25mg/ml) containing Phosphate buffered saline (pH7.4) and 10% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      Acy1 or Aminoacylase1 is a cytosolic, homodimeric, zinc-binding enzyme which catalyzes the hydrolysis of acylated L-amino acids to L-amino acids and acyl group, and has been suggested to operate in the catabolism and salvage of acylated amino acids. ACY1 is localized in chromosome 3p21.1, a region reduced to homozygosity in small-cell lung cancer (SCLC), and its expression has been observed to be reduced or undetectable in SCLC cell lines and tumors.

    • Synonyms

      Aminoacylase-1, ACY-1, N-acyl-L-amino-acid amidohydrolase, Aminoacylase 1, Acy1.

    • 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 MGSEFMTTKD PESEHPSVTL FRQYLRICTV QPNPDYGGAI TFLEERARQL GLSCQKIEVV PGFVITVLTW PGTNPSLPSI LLNSHTDVVP VFKEHWHHDP FEAFKDSEGY IYARGSQDMK SVSIQYLEAV RRLKSEGHRF PRTIHMTFVP DEEVGGHKGM ELFVKRPEFQ ALRAGFALDE GLANPTDAFT VFYSERSPWW VRVTSTGKPG HASRFIEDTA AEKLHKVISS ILAFREKERQ RLQANPHLKE GAVTSVNLTK LEGGVAYNVV PATMSASFDF RVAPDVDMKA FEKQLQRWCQ EAGEGVTFEF AQKFTEPRMT PTDDSDPWWA AFSGACKAMN LTLEPEIFPA ATDSRYIRAV GIPALGFSPM NRTPVLLHDH NERLHEDIFL RGVDIYTGLL SALASVPTLP GES.

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

    Acy1 Mouse
  • View Data Sheet

    Name :

    AHCY Human, Sf9

    Description:

    Adenosylhomocysteinase Human Recombinant, Sf9

    EC 3.3.1.1, SAHH, AdoHcyase, S-adenosyl-L-homocysteine hydrolase, AHCY, Adenosylhomocysteinase.

    Product # :

    ENZ-1034

    Price :

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    Description

    AHCY Human Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 441 amino acids (1-432 a.a.) and having a molecular mass of 48.8kDa (Migrates at 40-57kDa on SDS-PAGE under reducing conditions). AHCY is fused to a 6 amino acids His-Tag at C-terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

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

    Purity

    Greater than 90% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      AHCY is an enzyme that catalyzes the reversible hydrolysis of S-adenosylhomocysteine (AdoHcy) to adenosine (Ado) and L-homocysteine (Hcy). AHCY controls the intracellular S-adenosylhomocysteine (SAH) concentration that is crucial for transmethylation reactions. AHCY deficiency causes hypermethioninemia.

    • Synonyms

      EC 3.3.1.1, SAHH, AdoHcyase, S-adenosyl-L-homocysteine hydrolase, AHCY, Adenosylhomocysteinase.

    • 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

      ADLMSDKLPY KVADIGLAAW GRKALDIAEN EMPGLMRMRE RYSASKPLKG ARIAGCLHMT VETAVLIETL VTLGAEVQWS SCNIFSTQDH AAAAIAKAGI PVYAWKGETD EEYLWCIEQT LYFKDGPLNM ILDDGGDLTN LIHTKYPQLL PGIRGISEET TTGVHNLYKM MANGILKVPA INVNDSVTKS KFDNLYGCRE SLIDGIKRAT DVMIAGKVAV VAGYGDVGKG CAQALRGFGA RVIITEIDPI NALQAAMEGY EVTTMDEACQ EGNIFVTTTG CIDIILGRHF EQMKDDAIVC NIGHFDVEID VKWLNENAVE KVNIKPQVDR YRLKNGRRII LLAEGRLVNL GCAMGHPSFV MSNSFTNQVM AQIELWTHPD KYPVGVHFLP KKLDEAVAEA HLGKLNVKLT KLTEKQAQYL GMSCDGPFKP DHYRYHHHHH 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.

    Ahcy Human Sf9
  • View Data Sheet

    Name :

    ENPP2 Human

    Description:

    Ectonucleotide Pyrophosphatase-2 Human Recombinant

    ENPP2, ATX, PDNP2, ATX-X, NPP2, PD-IALPHA, Ectonucleotide pyrophosphatase/phosphodiesterase family member 2 isoform 2, ectonucleotide pyrophosphatase/phosphodiesterase 2, ENPP2, E-NPP 2, AUTOTAXIN, Extracellular lysophospholipase D, LysoPLD.

    Product # :

    ENZ-1173

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    Description

    ENPP2 Human Recombinant produced in HEK293 Cells is a single, glycosylated polypeptide chain containing 825 amino acids (49-863a.a) and having a molecular mass of 94.9kDa.ENPP2 is fused to a 6 amino acid His-tag at C-terminus, and is purified by proprietary chromatographic techniques.

    Source

    HEK293 Cells.

    Formulation

    The ENPP2 solution (0.25mg/ml) contains PBS (pH7.4) and 10% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    Biological Activity

    Specific activity is greater than 15,000 units/mg, and defined as the amount of enzyme that hydrolyze 1nmole of bis (pNitrophenyl) phosphate per minute at pH8.7 at 37℃.

    Citations

    More Info

    • Introduction

      Ectonucleotide Pyrophosphatase-2, aka ENPP2, a part of the ectonucleotide pyrophosphatasefamily. ENPP2 is able to cut the phosphodiester bond between the alpha and the beta position of triphosphate nucleotides, acting as an ectonucleotide phosphodiesterase producing pyrophosphate, as most members of the ENPP family. It is unlike ENPP-1 and ENPP-3, has weak activity against nucleotides, but shows a lysophospholipase D activity which allows the formation of LPA and choline from lysophosphatidylcholine. As well, ENPP-2 and LPA are involved in several inflammatory-driven diseases such as arthritis and asthma.

    • Synonyms

      ENPP2, ATX, PDNP2, ATX-X, NPP2, PD-IALPHA, Ectonucleotide pyrophosphatase/phosphodiesterase family member 2 isoform 2, ectonucleotide pyrophosphatase/phosphodiesterase 2, ENPP2, E-NPP 2, AUTOTAXIN, Extracellular lysophospholipase D, LysoPLD.

    • 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

      DGSMDSPWTN ISGSCKGRCF ELQEAGPPDC RCDNLCKSYT SCCHDFDELC LKTARGWECT KDRCGEVRNE ENACHCSEDC LARGDCCTNY QVVCKGESHW VDDDCEEIKA AECPAGFVRP PLIIFSVDGF RASYMKKGSK VMPNIEKLRS CGTHSPYMRP VYPTKTFPNL YTLATGLYPE SHGIVGNSMY DPVFDATFHL RGREKFNHRW WGGQPLWITA TKQGVKAGTF FWSVVIPHER RILTILQWLT LPDHERPSVY AFYSEQPDFS GHKYGPFGPE MTNPLREIDK IVGQLMDGLK QLKLHRCVNV IFVGDHGMED VTCDRTEFLS NYLTNVDDIT LVPGTLGRIR SKFSNNAKYD PKAIIANLTC KKPDQHFKPY LKQHLPKRLH YANNRRIEDI HLLVERRWHV ARKPLDVYKK PSGKCFFQGD HGFDNKVNSM QTVFVGYGST FKYKTKVPPF ENIELYNVMC DLLGLKPAPN NGTHGSLNHL LRTNTFRPTM PEEVTRPNYP GIMYLQSDFD LGCTCDDKVE PKNKLDELNK RLHTKGSTEE RHLLYGRPAV LYRTRYDILY HTDFESGYSE IFLMPLWTSY TVSKQAEVSS VPDHLTSCVR PDVRVSPSFS QNCLAYKNDK QMSYGFLFPP YLSSSPEAKY DAFLVTNMVP MYPAFKRVWN YFQRVLVKKY ASERNGVNVI SGPIFDYDYD GLHDTEDKIK QYVEGSSIPV PTHYYSIITS CLDFTQPADK CDGPLSVSSF ILPHRPDNEE SCNSSEDESK WVEELMKMHT ARVRDIEHLT SLDFFRKTSR SYPEILTLKT YLHTYESEIH HHHHH

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    Enpp2 Human
  • View Data Sheet

    Name :

    ENTPD3 Human

    Description:

    Ectonucleoside Triphosphate Diphosphohydrolase 3 Human Recombinant

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

    Product # :

    ENZ-844

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    Description

    ENTPD3 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 465 amino acids (44-485 a.a) and having a molecular mass of 52kDa. ENTPD3 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    ENTPD3 protein solution (0.25mg/ml) containing 20mM Tris-HCl buffer (pH 8.0) and 10% glycerol.

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

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

    • Synonyms

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

    • Physical Appearance

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

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    Entpd3 Human
  • View Data Sheet

    Name :

    POR Human, Active

    Description:

    P450 Oxidoreductase Human Recombinant, Active

    P450 (Cytochrome) Oxidoreductase, EC 1.6.2.4, CYPOR, P450R, CPR, NADPH-Dependent Cytochrome P450 Reductase, NADPH--Cytochrome P450 Reductase, NADPH--cytochrome P450 reductase.

    Product # :

    ENZ-1176

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    Description

    POR produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 686 amino acids (1-680a.a.) and having a molecular mass of 77.9kDa. POR is expressed with a 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    POR protein solution (0.25mg/ml) contains Phosphate buffer saline (pH 7.4) and 10% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Biological Activity

    Specific activity is > 4,000 pmol/min/mg. Defined by the amount of enzyme that  reduction of 1 pmole cytochrome-C by NADPH/min. at pH-8 25C.

    Citations

    More Info

    • Introduction

      P450 Oxidoreductase, also known as POR is a flavoprotein which contributes electrons to all microsomal P450 enzymes. POR is localized to the endoplasmic reticulum, where it is also capable of transfering electrons to heme oxygenase as well as cytochrome b5. POR is structurally related to two separate flavoprotein families; first one is ferredoxin nucleotide reductase and the second flavodoxin.

    • Synonyms

      P450 (Cytochrome) Oxidoreductase, EC 1.6.2.4, CYPOR, P450R, CPR, NADPH-Dependent Cytochrome P450 Reductase, NADPH--Cytochrome P450 Reductase, NADPH--cytochrome P450 reductase.

    • 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

      MINMGDSHVD TSSTVSEAVA EEVSLFSMTD MILFSLIVGL LTYWFLFRKK KEEVPEFTKI QTLTSSVRES SFVEKMKKTG RNIIVFYGSQ TGTAEEFANR LSKDAHRYGM RGMSADPEEY DLADLSSLPE IDNALVVFCM ATYGEGDPTD NAQDFYDWLQ ETDVDLSGVK FAVFGLGNKT YEHFNAMGKY VDKRLEQLGA QRIFELGLGD DDGNLEEDFI TWREQFWLAV CEHFGVEATG EESSIRQYEL VVHTDIDAAK VYMGEMGRLK SYENQKPPFD AKNPFLAAVT TNRKLNQGTE RHLMHLELDI SDSKIRYESG DHVAVYPAND SALVNQLGKI LGADLDVVMS LNNLDEESNK KHPFPCPTSY RTALTYYLDI TNPPRTNVLY ELAQYASEPS EQELLRKMAS SSGEGKELYL SWVVEARRHI LAILQDCPSL RPPIDHLCEL LPRLQARYYS IASSSKVHPN SVHICAVVVE YETKAGRINK GVATNWLRAK EPVGENGGRA LVPMFVRKSQ FRLPFKATTP VIMVGPGTGV APFIGFIQER AWLRQQGKEV GETLLYYGCR RSDEDYLYRE ELAQFHRDGA LTQLNVAFSR EQSHKVYVQH LLKQDREHLW KLIEGGAHIY VCGDARNMAR DVQNTFYDIV AELGAMEHAQ AVDYIKKLMT KGRYSLDVWS HHHHHH.

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    Por Enzyme
  • View Data Sheet

    Name :

    LDHB Mouse

    Description:

    Lactate Dehydrogenase B Mouse Recombinant

    L-lactate dehydrogenase B chain, LDH-B, LDH heart subunit, LDH-H, Ldh-2, Ldh2, Ldhb.

    Product # :

    ENZ-1052

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    Description

    LDHB Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 357 amino acids (1-334 a.a) and having a molecular mass of 39kDa.LDHB is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

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

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Biological Activity

    Specific activity is > 150 units/mg, in which one unit will 1.0 umole of pyruvate to L-lactate and beta-NAD per minute at pH 7.5.

    Citations

    More Info

    • Introduction

      Lactate dehydrogenase (LDH) is an enzyme(EC1.1.1.27) present in a wide variety of organisms, including plants and animals.
      A tetrameric enzyme that catalyses the interconversion of pyruvateand lactate with concomitant interconversion of NADH and NAD+. At high concentrations of pyruvate, the enzyme exhibits feedback inhibition and the rate of conversion of pyruvate to lactate is decreased. In vertebrates, genes for three different subunits (LDH-A, LDH-B and LDH-C) exist.

    • Synonyms

      L-lactate dehydrogenase B chain, LDH-B, LDH heart subunit, LDH-H, Ldh-2, Ldh2, 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 MGSMATLKEK LIASVADDEA AVPNNKITVV GVGQVGMACA ISILGKSLAD ELALVDVLED KLKGEMMDLQ HGSLFLQTPK IVADKDYSVT ANSKIVVVTA GVRQQEGESR LNLVQRNVNV FKFIIPQIVK YSPDCTIIVV SNPVDILTYV TWKLSGLPKH RVIGSGCNLD SARFRYLMAE KLGIHPSSCH GWILGEHGDS SVAVWSGVNV AGVSLQELNP EMGTDNDSEN WKEVHKMVVD SAYEVIKLKG YTNWAIGLSV ADLIESMLKN LSRIHPVSTM VKGMYGIENE VFLSLPCILN ARGLTSVINQ KLKDDEVAQL RKSADTLWDI QKDLKDL.

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    Ldhb Mouse
  • View Data Sheet

    Name :

    PREP Human

    Description:

    Prolyl Endopeptidase Human Recombinant

    Prolyl Endopeptidase, Post-Proline Cleaving Enzyme, EC 3.4.21.26, PEP, PE, DJ355L5.1 (Prolyl Endopeptidase), Prolyl Oligopeptidase, Prolyl endopeptidase.

    Product # :

    ENZ-828

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    Description

    PREP Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 733 amino acids (1-710 a.a) and having a molecular mass of 83.1kDa. PREP is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    PREP protein solution (0.25mg/ml) containing PBS buffer (pH 7.4), 30% glycerol and 1mM DTT.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      Prolyl Endopeptidase , also known as PREP is a cytosolic prolyl endopeptidase which cleaves peptide bonds on the C-terminal side of prolyl residues within peptides which are up to about 30 a.a long. In addition, Prolyl endopeptidases have been shown to be implicated in the maturation and degradation of peptide hormones and neuropeptides.

    • Synonyms

      Prolyl Endopeptidase, Post-Proline Cleaving Enzyme, EC 3.4.21.26, PEP, PE, DJ355L5.1 (Prolyl Endopeptidase), Prolyl Oligopeptidase, Prolyl endopeptidase.

    • 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 MGSMLSLQYP DVYRDETAVQ DYHGHKICDP YAWLEDPDSE QTKAFVEAQN KITVPFLEQC PIRGLYKERM TELYDYPKYS CHFKKGKRYF YFYNTGLQNQ RVLYVQDSLE GEARVFLDPN ILSDDGTVAL RGYAFSEDGE YFAYGLSASG SDWVTIKFMK VDGAKELPDV LERVKFSCMA WTHDGKGMFY NSYPQQDGKS DGTETSTNLH QKLYYHVLGT DQSEDILCAE FPDEPKWMGG AELSDDGRYV LLSIREGCDP VNRLWYCDLQ QESSGIAGIL KWVKLIDNFE GEYDYVTNEG TVFTFKTNRQ SPNYRVINID FRDPEESKWK VLVPEHEKDV LEWIACVRSN FLVLCYLHDV KNILQLHDLT TGALLKTFPL DVGSIVGYSG QKKDTEIFYQ FTSFLSPGII YHCDLTKEEL EPRVFREVTV KGIDASDYQT VQIFYPSKDG TKIPMFIVHK KGIKLDGSHP AFLYGYGGFN ISITPNYSVS RLIFVRHMGG ILAVANIRGG GEYGETWHKG GILANKQNCF DDFQCAAEYL IKEGYTSPKR LTINGGSNGG LLVAACANQR PDLFGCVIAQ VGVMDMLKFH KYTIGHAWTT DYGCSDSKQH FEWLVKYSPL HNVKLPEADD IQYPSMLLLT ADHDDRVVPL HSLKFIATLQ YIVGRSRKQS NPLLIHVDTK AGHGAGKPTA KVIEEVSDMF AFIARCLNVD WIP.

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    Prep Human
  • View Data Sheet

    Name :

    CES1G Mouse

    Description:

    Carboxylesterase 1G Mouse Recombinant

    Liver carboxylesterase 1, Acyl-coenzyme A:cholesterol acyltransferase, Carboxylesterase 1G, ES-x, CES1G.

    Product # :

    ENZ-947

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    Description

    CES1G produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 556 amino acids (19-565 a.a.) and having a molecular mass of 61.9kDa (Migrates at 50-70kDa on SDS-PAGE under reducing conditions). CES1G is expressed with a 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    CES1G protein solution (0.5mg/ml) containing Phosphate Buffered Saline (pH 7.4) and 10% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    Biological Activity

    Specific activity is > 2,000 pmol/min/ug and is defined as the amount of enzyme that hydrolyze 1pmole of p-nitrophenyl acetate to p-nitrophenol per minute at pH 7.5 at 37C.

    Citations

    More Info

    • Introduction

      Carboxylesterase 1 (CES1G) belongs to a large family of carboxylesterases that are liable for the hydrolysis of ester and amide bonds. CES1G is also participates in the detoxification of xenobiotics prodrugs. CES1G shares the serine hydrolase fold observed in other esterases. CES1G found in rats and mice and is expressed mainly in liver, but also in kidney and lung.

    • Synonyms

      Liver carboxylesterase 1, Acyl-coenzyme A:cholesterol acyltransferase, Carboxylesterase 1G, ES-x, CES1G.

    • 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

      ADPHPSLPPV VHTVHGKVLG KYVTLEGFSQ PVAVFLGVPF AKPPLGSLRF APPEPAEPWS FVKHTTSYPP LCYQNPEAAL RLAELFTNQR KIIPHKFSED CLYLNIYTPA DLTQNSRLPV MVWIHGGGLV IDGASTYDGV PLAVHENVVV VVIQYRLGIW GFFSTEDEHS RGNWGHLDQV AALHWVQDNI ANFGGNPGSV TIFGESAGGE SVSVLVLSPL AKNLFHRAIA QSSVIFNPCL FGRAARPLAK KIAALAGCKT TTSAAMVHCL RQKTEDELLE VSLKMKFGTV DFLGDPRESY PFLPTVIDGV LLPKAPEEIL AEKSFNTVPY MVGINKHEFG WIIPMFLDFP LSERKLDQKT AASILWQAYP ILNISEKLIP AAIEKYLGGT EDPATMTDLF LDLIGDIMFG VPSVIVSRSH RDAGAPTYMY EYQYRPSFVS DDRPQELLGD HADELFSVWG APFLKEGASE EEINLSKMVM KFWANFARNG NPNGEGLPHW PEYDQKEGYL QIGVPAQAAH RLKDKEVDFW TELRAKETAE RSSHREHVEL HHHHHH.

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

    Ces1 Mouse
  • View Data Sheet

    Name :

    LTA4H Human

    Description:

    Leukotriene A4 Hydrolase Human Recombinant

    Leukotriene A-4 hydrolase isoform1, LTA-4 hydrolase, Leukotriene A(4) hydrolase, LTA4.

    Product # :

    ENZ-869

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    Description

    LTA4H Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 634 amino acids (1-611 a.a) and having a molecular mass of 71.7kDa.LTA4H is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    LTA4H protein solution (0.25mg/ml) in Phosphate buffered saline (pH7.4), 20% glycerol and 1mM DTT.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      Leukotriene A-4 hydrolase (LTA4H) is a bifunctional enzyme that converts leukotriene A4 to leukotriene B4 and functions as an aminopeptidase. The LTA4H enzyme is a member of the family of hydrolases, specifically those acting on ether bonds (ether hydrolases). LTA4H participates in arachidonic acid metabolism.

    • Synonyms

      Leukotriene A-4 hydrolase isoform1, LTA-4 hydrolase, Leukotriene A(4) hydrolase, LTA4.

    • 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 MGSMPEIVDT CSLASPASVC RTKHLHLRCS VDFTRRTLTG TAALTVQSQE DNLRSLVLDT KDLTIEKVVI NGQEVKYALG ERQSYKGSPM EISLPIALSK NQEIVIEISF ETSPKSSALQ WLTPEQTSGK EHPYLFSQCQ AIHCRAILPC QDTPSVKLTY TAEVSVPKEL VALMSAIRDG ETPDPEDPSR KIYKFIQKVP IPCYLIALVV GALESRQIGP RTLVWSEKEQ VEKSAYEFSE TESMLKIAED LGGPYVWGQY DLLVLPPSFP YGGMENPCLT FVTPTLLAGD KSLSNVIAHE ISHSWTGNLV TNKTWDHFWL NEGHTVYLER HICGRLFGEK FRHFNALGGW GELQNSVKTF GETHPFTKLV VDLTDIDPDV AYSSVPYEKG FALLFYLEQL LGGPEIFLGF LKAYVEKFSY KSITTDDWKD FLYSYFKDKV DVLNQVDWNA WLYSPGLPPI KPNYDMTLTN ACIALSQRWI TAKEDDLNSF NATDLKDLSS HQLNEFLAQT LQRAPLPLGH IKRMQEVYNF NAINNSEIRF RWLRLCIQSK WEDAIPLALK MATEQGRMKF TRPLFKDLAA FDKSHDQAVR TYQEHKASMH PVTAMLVGKD LKVD.

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    Lta4H Human
  • View Data Sheet

    Name :

    UPP1 Salmonella

    Description:

    Uridine Phosphorylase Salmonella Typhimurium Recombinant

    Uridine phosphorylase, EC 2.4.2.3, UrdPase, UPase, StUP.

    Product # :

    ENZ-348

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    Description

    Uridine phosphorylase Salmonella typhimurium Recombinantproduced in E.Coli is a non-glycosylated, polypeptide having a total molecular mass of 163068 Dalton.

    Source

    Escherichia Coli.

    Formulation

    The UPase was lyophilized from 1mg/ml solution containing 25mM Tris-HCl, pH 8.0, 0.15M NaCl.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      Uridine phosphorylase from Salmonella typhimurium (StUP) catalyzes the reversible phosphorolysis of uridine with the formation of ribose-1-phosphate and uracil.

    • Synonyms

      Uridine phosphorylase, EC 2.4.2.3, UrdPase, UPase, StUP.

    • Physical Appearance

      Sterile Filtered white lyophilized powder.

    • Stability

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

    • Enzymatic Activity

      30 U/mg protein.

    • Unit Definition

      One unit phosphorylates 1μm of uridine within 1 min at pH 7.3.

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    Uridine Phosphorylase Salmonella Typhimurium
  • View Data Sheet

    Name :

    Urokinase Human

    Description:

    Urokinase Human

    Urokinase, Abbokinase, Urokinase-type Plasminogen Activator,uPA, EC 3.4.21.73, UK.

    Product # :

    ENZ-264

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    Description

    Urokinase is a two-chain glycoprotein containing 411 amino acids with 12 disulfide bonds. Its molecular weight is 54,000 Dalton.

    Source

    Human urine.

    Formulation

    The Urokinase was lyophilized from a concentrated (1mg/ml) solution containing phosphate buffer.

    Purity

    Greater than 90.0%.

    Citations

    More Info

    • Introduction

      Urokinase (UK) is a serine protease, which is one of biological plasminogen activators.
      It is involved in a number of biological functions including fibrinolysis, embryogenesis, cell migration, tissue remodeling, ovulation, and wound healing.
      It can be obtained from human urine or kidney cell culture.

    • Synonyms

      Urokinase, Abbokinase, Urokinase-type Plasminogen Activator,uPA, EC 3.4.21.73, UK.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized Urokinase although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Urokinase should be stored at 4°C between 2-7 days and for future use below -18°C.Please prevent freeze-thaw cycles.

    • Solubility

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

    • Contaminants

      Free of: Hepatitis B surface antigen, Hepatitis C antibody and HIV I and II.

    • Specific Activity

      187,973IU/mg.

    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.

    Urokinase Human
  • View Data Sheet

    Name :

    HMOX1 Antibody

    Description:

    Heme Oxygenase 1, Mouse Anti Human

    HO-1, HSP32, bK286B10, HMOX-1, Heme oxygenase 1, HMOX1, HO, HO1.

    Product # :

    ANT-683

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    Formulation

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

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    • Introduction

      HMOX1 cleaves the heme ring at the alpha methene bridge to form Biliverdin. Biliverdin is then converted to Bilirubin by Biliverdin reductase. In physiological state, the highest activity of HMOX1 is found in the spleen, where senescent erythrocytes are sequestrated and destroyed. Heme Oxygenase-1 is involved in the regulation of cardiovascular function and its adaptive response to a variety of stressors. HMOX1 is induced in the colon of ulcerative colitis. HMOX1 is found to overexpress with a higher extent of intraplaque angiogenesis implies a multi-faceted role for HMOX1 in modulating the progression of atherosclerosis. HMOX1 expression reduced LPS-stimulated secretion of MCP-1, IL-6, IL-10, and TNF-alpha in murine and human macrophages.

    • Synonyms

      HO-1, HSP32, bK286B10, HMOX-1, Heme oxygenase 1, HMOX1, HO, HO1.

    • Physical Appearance

      Sterile filtered colorless solution.

    • Immunogen

      Anti-human HMOX1 mAb, is derived from hybridization of mouse F0 myeloma cells with spleen cells from BALB/c mice immunized with recombinant human HMOX1 amino acids 1-266 purified from E. coli.

    • Ig Subclass

      Mouse IgG2a heavy chain and K light chain.

    • Clone

      PAT1D6AT.

    • Applications

      HMOX1 antibody has been tested by ELISA, Western blot analysis, Flow cytometry and ICC/IF to assure specificity and reactivity. Since application varies, however, each investigation should be titrated by the reagent to obtain optimal results.

    • 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

      HMOX1 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.

    Hmox1 Antibody
  • View Data Sheet

    Name :

    MMP 8 Human

    Description:

    Matrix Metalloproteinase-8 Human Recombinant

    EC 3.4.24.34, Matrix metalloproteinase-8, MMP-8, PMNL-CL, HNC, CLG1.

    Product # :

    ENZ-301

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    Description

    Matrix Metalloproteinase-8 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain having a molecular mass of 75 kDa.The MMP-8 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The MMP-8 protein solution (100 units/ml) in 0.05M Tris-HCl buffer, pH 7.6, 0.2M NaCl, 5mM CaCl2, 0.0025% NaN3 and 0.1% BSA.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    Biological Activity

    100 units/ml after activation with APMA by solution assay method.
    One unit of collagenolytic activity is defined as the cleavage of 1µg of collagen per minute by the solution method.

    Citations

    More Info

    • Introduction

      Full-length recombinant human neutrophil MMP-8, latent form.
      Matrix metalloproteinase 8 (MMP-8), degrades interstitial collagens, acting preferentially on collagen type I.
      Increased full-length MMP-8 protein was associated with infiltration into the skin of neutrophils, which are the major cell type that expresses MMP-8.
      MMP-8 is synthesized and stored in specific granules in neutrophil leukocytes. MMP-8 activity is therefore regulated by factors such as surface-bound ligands (IgG or complement components) that release it through degranulation.Once released and activated through proteolytic or oxidative mechanisms, MMP-8 plays a major role in the connective tissue turnover that accompanies inflammatory processes.

    • Synonyms

      EC 3.4.24.34, Matrix metalloproteinase-8, MMP-8, PMNL-CL, HNC, CLG1.

    • 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. Avoid multiple freeze-thaw cycles.

    • Applications

      Used as a standard for analyzing mammalian colagenase activity.

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

    Mmp8 Human
  • View Data Sheet

    Name :

    Benzonase Nuclease, 99%

    Description:

    Benzonase Nuclease Serratia Marcescens Recombinant, 99%

    Product # :

    ENZ-1112

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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 99.0% 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.

    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.

    Benzonase Nuclease
  • View Data Sheet

    Name :

    PAFAH2 Human

    Description:

    Platelet-Activating Factor Acetylhydrolase 2 Human Recombinant

    HSD-PLA2, Platelet-activating factor acetylhydrolase 2, cytoplasmic, Serine-dependent phospholipase A2, SD-PLA2, hSD-PLA2.

    Product # :

    ENZ-899

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    Description

    PAFAH2 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 415 amino acids (1-392 a.a) and having a molecular mass of 46.4kDa.PAFAH2 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    PAFAH2 protein solution (1mg/ml) in Phosphate buffered saline (pH7.4), 20% glycerol and 1mM DTT.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      Platelet-activating factor acetylhydrolase 2 cytoplasmic (PAFAH2) has a marked selectivity for phospholipids with short acyl chains at the sn-2 position. PAFAH2 may share a mutual physiologic function with the plasma-type enzyme.

    • Synonyms

      HSD-PLA2, Platelet-activating factor acetylhydrolase 2, cytoplasmic, Serine-dependent phospholipase A2, SD-PLA2, hSD-PLA2.

    • 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 MGSMGVNQSV GFPPVTGPHL VGCGDVMEGQ NLQGSFFRLF YPCQKAEETM EQPLWIPRYE YCTGLAEYLQ FNKRCGGLLF NLAVGSCRLP VSWNGPFKTK DSGYPLIIFS HGLGAFRTLY SAFCMELASR GFVVAVPEHR DRSAATTYFC KQAPEENQPT NESLQEEWIP FRRVEEGEKE FHVRNPQVHQ RVSECLRVLK ILQEVTAGQT VFNILPGGLD LMTLKGNIDM SRVAVMGHSF GGATAILALA KETQFRCAVA LDAWMFPLER DFYPKARGPV FFINTEKFQT MESVNLMKKI CAQHEQSRII TVLGSVHRSQ TDFAFVTGNL IGKFFSTETR GSLDPYEGQE VMVRAMLAFL QKHLDLKEDY NQWNNLIEGI GPSLTPGAPH HLSSL.

    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.

    Pafah2 Human
  • View Data Sheet

    Name :

    UBE2G2 Human

    Description:

    Ubiquitin-Conjugating Enzyme E2G2 Human Recombinant

    Ubiquitin-conjugating enzyme E2 G2, E2 ubiquitin-conjugating enzyme G2, Ubiquitin carrier protein G2, Ubiquitin-protein ligase G2, UBE2G2, Ubiquitin-Conjugating Enzyme E2G2, Ubiquitin-conjugating enzyme E2 G2 isoform 1, UBC7.

    Product # :

    ENZ-884

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    Description

    UBE2G2 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 188 amino acids (1-165a.a.) and having a molecular mass of 21kDa.UBE2G2 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    UBE2G2 protein solution (1mg/ml) containing Phosphate buffered saline (pH7.4), 10% glycerol and 1mM DTT.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      Ubiquitin-Conjugating Enzyme E2G2 (UBE2G2) is a protein coding gene which is a part of the E2 ubiquitin-conjugating enzyme family. UBE2G2 accepts ubiquitin from the E1 complex and catalyzes its covalent attachment to various proteins. UBE2G2 is ubiquitously expressed mainly in adult muscle. UBE2G2 also takes part in endoplasmic reticulum-associated degradation (ERAD).

    • Synonyms

      Ubiquitin-conjugating enzyme E2 G2, E2 ubiquitin-conjugating enzyme G2, Ubiquitin carrier protein G2, Ubiquitin-protein ligase G2, UBE2G2, Ubiquitin-Conjugating Enzyme E2G2, Ubiquitin-conjugating enzyme E2 G2 isoform 1, UBC7.

    • 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 MGSMAGTALK RLMAEYKQLT LNPPEGIVAG PMNEENFFEW EALIMGPEDT CFEFGVFPAI LSFPLDYPLS PPKMRFTCEM FHPNIYPDGR VCISILHAPG DDPMGYESSA ERWSPVQSVE KILLSVVSML AEPNDESGAN VDASKMWRDD REQFYKIAKQ IVQKSLGL.

    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.

    Ube2G2 Human
  • View Data Sheet

    Name :

    MMP 3 Human, HEK

    Description:

    Matrix Metalloproteinase-3 Human Recombinant, HEK

    Stromelysin-1, EC 3.4.24.17, Matrix metalloproteinase-3, MMP-3, Transin-1, SL-1, STMY, STR1, STMY1, MGC126102, MGC126103, MGC126104.

    Product # :

    ENZ-284

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    • sds-page
    • Citations

    Description

    MMP-3 Human Recombinant produced in HEK293 cells is a proform of the Human MMP3 [Tyr18-Cys477 (Lys45Glu)] and fused with a ployhistide tag at the C-terminus, having an Mw of 52kDa. MMP-3 is purified by proprietary chromatographic techniques.

    Source

    HEK293 cells.

    Formulation

    The MMP-3 is supplied as a 0.2µm filtered solution in 20mM Tris-HCl, 150mM NaCl and 0.05% Brij35, pH 7.5.

    Purity

    Greater than 95% as determined by SDS-PAGE.

    Biological Activity

    The activity was measured by its ability to cleave the fluorogenic peptide substrate, Mca-RPKPVE-Nval-WRK(Dnp)-NH2. The specific activity is > 150 pmoles/min/µg.
    Recombinant Human MMP-3 protein pro form needs to be activated with Chymotrypsin.
    Activation Protocol:
    1. Dilute MMP3 to 20µg/ml in the Assay Buffer: 50mM Tris, 10mM CaCl2, 150mM NaCl, 0.05% (w/v) and Brij 35, pH 7.5.
    2. Activate MMP3 by adding Chymotrypsin(Sigma, Catalog#C­3142,1mg/ml stock in 1mM HCl) to a final concentration of 5ug/ml.
    3. Incubate at 37°C for 30 minutes.
    4. Stop activation with 2mM PMSF. Pre-warm the PMSF to 37°C prior to adding to sample.

    sds-page

    mmp-3 human hek sds-page - Product image 1

    Citations

    More Info

    • Introduction

      MMP-3 enzyme is also known as Stromelysin-1or as Transin-1 which hydrolyzes natural collagen at physiological pH and temperature. It dissolves the intervertebral nucleus pulposus and annulus fibrosus of Herniated Lumbar Intervertebral Disk . MMP-3 hydrolyzes components of the extracellular matrix like proteoglycan, laminin, fibronectin, gelatin and collagen types III, IV and IX. It also activates pro-MMP-9 and pro-MMP-8 and superactivates plasmin activated MMP-1. MMP-3 is secreted as a latent proenzyme and is activated by a variety of proteinases, e.g. plasmin, trypsin, chymotrypsin, cathepsin G or human neutrophil elastase. MMP-3 was found to be capable of activating the precursor of IL1-beta.

    • Synonyms

      Stromelysin-1, EC 3.4.24.17, Matrix metalloproteinase-3, MMP-3, Transin-1, SL-1, STMY, STR1, STMY1, MGC126102, MGC126103, MGC126104.

    • 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.

    Mmp3 Human
  • View Data Sheet

    Name :

    SDSL Human

    Description:

    Serine Dehydratase-Like Human Recombinant

    Serine dehydratase-like, SDS-RS1, Serine dehydratase 2, TDH, L-serine dehydratase/L-threonine deaminase, SDH 2, serine dehydratase related sequence 1, EC 4.3.1.17, EC 4.3.1.19.

    Product # :

    ENZ-180

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    Description

    SDSL Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 353 amino acids (1-329) and having a molecular mass of 37.3 kDa.SDSL is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    The SDSL solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 2mM DTT, 0.1M NaCl and 10% glycerol.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      SDSL belongs to the serine/threonine dehydratase family and function as a serinespecific dehydratase. SDSL utilizes pyridoxal phosphate and is one of three key enzymes which take part in the metabolism of Glycine and serine.

    • Synonyms

      Serine dehydratase-like, SDS-RS1, Serine dehydratase 2, TDH, L-serine dehydratase/L-threonine deaminase, SDH 2, serine dehydratase related sequence 1, EC 4.3.1.17, EC 4.3.1.19.

    • 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 MGSHMDGPVA EHAKQEPFHV VTPLLESWAL SQVAGMPVFL KCENVQPSGS FKIRGIGHFC QEMAKKGCRH LVCSSGGNAG IAAAYAARKL GIPATIVLPE STSLQVVQRL QGEGAEVQLT GKVWDEANLR AQELAKRDGW ENVPPFDHPL IWKGHASLVQ ELKAVLRTPP GALVLAVGGG GLLAGVVAGL LEVGWQHVPI IAMETHGAHC FNAAITAGKL VTLPDITSVA KSLGAKTVAA RALECMQVCK IHSEVVEDTE AVSAVQQLLD DERMLVEPAC GAALAAIYSG LLRRLQAEGC LPPSLTSVVV IVCGGNNINS RELQALKTHL GQV.

    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.

    Sdsl Human
  • View Data Sheet

    Name :

    TOP1 70kDa Human

    Description:

    DNA Topoisomerase-I 70kDa Recombinant Human

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

    Product # :

    ENZ-073

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    Description

    Recombinant TOP1 70kDa protein is an enzyme fragment having a molecular mass of 72KDa (pH 9.4). TOP1 70kDa protein is fused to a hexa-histidine purification tag.

    Source

    Sf9 insect cells.

    Formulation

    TOP1 70kDa is supplied in 20mM HEPES buffer pH-8.0, 500mM 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 70kDa autoantibody positive sample or monoclonal anti-hexa-His-tag antibody.

    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 70Kda Human
  • View Data Sheet

    Name :

    LDHB Human

    Description:

    Lactate Dehydrogenase B Human Recombinant

    Lactate Dehydrogenase B, Renal Carcinoma Antigen NY-REN-46, LDH Heart Subunit, EC 1.1.1.27, LDH-B, LDH-H, Epididymis Secretory Protein Li 281, Testicular Secretory Protein Li 25, Lactate Dehydrogenase H Chain, HEL-S-281, EC 1.1.1 , LDHBD, TRG-5.

    Product # :

    ENZ-967

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    Description

    LDHB Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 334 amino acids (1-334) and having a molecular mass of 36.6kDa.

    Source

    Escherichia Coli.

    Formulation

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

    Purity

    Greater than 90% as determined by SDS-PAGE.

    Biological Activity

    Specific activity is >300 units/mg, in which 1 unit will convert 1.0 umole of pyruvate to L-lactate and beta-NAD per min at pH 7.5 at 37°.

    Citations

    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

      Lactate Dehydrogenase B, Renal Carcinoma Antigen NY-REN-46, LDH Heart Subunit, EC 1.1.1.27, LDH-B, LDH-H, Epididymis Secretory Protein Li 281, Testicular Secretory Protein Li 25, Lactate Dehydrogenase H Chain, HEL-S-281, EC 1.1.1 , LDHBD, TRG-5.

    • 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

      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.

    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.

    Human Ldhb
  • View Data Sheet

    Name :

    GLUL Human, Active

    Description:

    Glutamine Synthetase Human Recombinant, Active

    Glutamine synthetase, GLUL Active, GLUL, Glutamine Synthetase, Active, GLNS, GS, PIG43, PIG59, Glutamate decarboxylase (EC:4.1.1.15), Glutamate--ammonia ligase.

    Product # :

    ENZ-974

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    Description

    GLUL Recombinant Human produced in E.Coli is a single, non-glycosylated polypeptide chain containing 373 amino acids (1-373) and having a molecular mass of 42kDa.

    Source

    Escherichia Coli.

    Formulation

    GLUL protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH8.0), 10% glycerol 1mM DTT and 0.1mM PMSF.

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

    Biological Activity

    Specific activity is > 2.000 pmol/min/ug, and is defined as the amount of enzyme that convert L-glutamate to L-glutamine per miunte at pH 7.5 at 37C in coupled system with PK/LDH.

    Citations

    More Info

    • Introduction

      GLUL catalyzes the synthesis of glutamine from glutamate and ammonia. Glutamine is a major source of energy and that takes part in cell proliferation, inhibition of apoptosis, and cell signaling. GLUL is expressed during early fetal stages, and has a role in maintaining body pH by removing ammonia from circulation. Mutations in GLUL gene are related with congenital glutamine deficiency.

    • Synonyms

      Glutamine synthetase, GLUL Active, GLUL, Glutamine Synthetase, Active, GLNS, GS, PIG43, PIG59, Glutamate decarboxylase (EC:4.1.1.15), Glutamate--ammonia ligase.

    • 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

      MTTSASSHLN KGIKQVYMSL PQGEKVQAMY IWIDGTGEGL RCKTRTLDSE PKCVEELPEW NFDGSSTLQS EGSNSDMYLV PAAMFRDPFR KDPNKLVLCE VFKYNRRPAE TNLRHTCKRI MDMVSNQHPW FGMEQEYTLM GTDGHPFGWP SNGFPGPQGP YYCGVGADRA YGRDIVEAHY RACLYAGVKI AGTNAEVMPA QWEFQIGPCE GISMGDHLWV ARFILHRVCE DFGVIATFDP KPIPGNWNGA GCHTNFSTKA MREENGLKYI EEAIEKLSKR HQYHIRAYDP KGGLDNARRL TGFHETSNIN DFSAGVANRS ASIRIPRTVG QEKKGYFEDR RPSANCDPFS VTEALIRTCL LNETGDEPFQ YKN.

    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.

    Glul Human Active
  • View Data Sheet

    Name :

    ProMatrilysin

    Description:

    ProMatrix Metalloproteinase-7 Recombinant

    Product # :

    ENZ-272

    Price :

    Quantity :

    Shipping Method :

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    More Info

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

    Description

    Matrix metalloproteinase-7 (MMP-7) also known as matrilysin and PUMP (EC 3.4.24.23) cleaves a number of substrates including collagen types IV and X, elastin, fibronectin, gelatin, laminin and proteoglycans. MMP-7 is closely related to the stromelysin family members but is encoded by a different gene. MMP-7 is the smallest of all the MMPs consisting of a pro-peptide domain and a catalytic domain. It lacks the hemopexin-like domain common to other members of the MMPs. MMP-7 is secreted as a 28 kDa proenzyme and can be activated in vitro by organomercurials and trypsin and in vivo by MMP-3 to a 18 kDa active MMP-7 enzyme. Once activated, MMP-7 can activate pro-MMP-1 and pro-MMP-9 but not pro-MMP-2. MMP-7 is widely expressed having been reported in elevated levels in cycling endometrium as well as in colorectal cancers and adenomas, hepatocellular carcinomas, rectal carcinomas, and approximately 50% of gliomas.

    Source

    Escherichia Coli.

    Formulation

    The protein contains the following additives 25mM Tris-HCl (pH 7.5),150mM NaCl, 5mM CaCl2, 0.01% Brij-35 and 0.02% NaN3.

    Purity

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

    Biological Activity

    The specific activity was found to be 1400 IU/mg.

    Citations

    More Info

    • Physical Appearance

      Sterile clear liquid 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.

    • Unit Definition

      One unit is defined as the digestion of 1 µg Azocoll/min at 37°C.

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

    Promatrilysin
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