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Search results

1000 results found for “alkaline phosphatase”

Name

Description

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  • View Data Sheet

    Name :

    PARP2 Human

    Description:

    Poly (ADP-Ribose) Polymerase 2 Human Recombinant

    ADPRT2, ADPRTL2, ADPRTL3, ARTD2, pADPRT-2, PARP-2, Poly [ADP-ribose] polymerase 2, hPARP-2, ADP-ribosyltransferase diphtheria toxin-like 2, NAD (+) ADP-ribosyltransferase 2, Poly [ADP-ribose] synthase 2.

    Product # :

    ENZ-694

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    Description

    PARP2 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 376 amino acids (233-583a.a) and having a molecular mass of 42.5kDa. PARP2 is fused to a 25 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The PARP2 solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.4M urea and 10% glycerol.

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      Poly (ADP-Ribose) Polymerase 2 (PARP2) contains a catalytic domain which is homologous to that of poly (ADP-ribosyl) transferase but lacks an N-terminal DNA binding domain which activates the C-terminal catalytic domain of poly (ADP-ribosyl) transferase. PARP2 is capable of catalyzing a poly (ADP-ribosyl)ation reaction. The basic residues within the N-terminal area of this protein can bear potential DNA-binding properties, and can be engaged in the nuclear and/or nucleolar targeting of the protein. There has been found two alternatively spliced transcript variants encoding distinct isoforms.

    • Synonyms

      ADPRT2, ADPRTL2, ADPRTL3, ARTD2, pADPRT-2, PARP-2, Poly [ADP-ribose] polymerase 2, hPARP-2, ADP-ribosyltransferase diphtheria toxin-like 2, NAD (+) ADP-ribosyltransferase 2, Poly [ADP-ribose] synthase 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 MGSHMQLDLR VQELIKLICN VQAMEEMMME MKYNTKKAPL GKLTVAQIKA GYQSLKKIED CIRAGQHGRA LMEACNEFYT RIPHDFGLRT PPLIRTQKEL SEKIQLLEAL GDIEIAIKLV KTELQSPEHP LDQHYRNLHC ALRPLDHESY EFKVISQYLQ STHAPTHSDY TMTLLDLFEV EKDGEKEAFR EDLHNRMLLW HGSRMSNWVG ILSHGLRIAP PEAPITGYMF GKGIYFADMS SKSANYCFAS RLKNTGLLLL SEVALGQCNE LLEANPKAEG LLQGKHSTKG LGKMAPSSAH FVTLNGSTVP LGPASDTGIL NPDGYTLNYN EYIVYNPNQV RMRYLLKVQF NFLQLW.

    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.

    Parp2 Human
  • View Data Sheet

    Name :

    UBE2G Human

    Description:

    Ubiquitin-Conjugating Enzyme E2G Human Recombinant

    E217K, UBC7, UBE2G, Ubiquitin-conjugating enzyme E2 G1, E2 ubiquitin-conjugating enzyme G1, E217K, UBC7, Ubiquitin carrier protein G1, Ubiquitin-protein ligase G1.

    Product # :

    ENZ-838

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    Description

    UBE2G Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 193 amino acids (1-170 a.a) and having a molecular mass of 21.9kDa.UBE2G is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    UBE2G protein solution (0.5mg/ml) containing Phosphate buffered saline, (pH7.4) 30% glycerol and 1mM DTT.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      Protein modification with ubiquitin is an essential cellular mechanism for targeting abnormal or short-lived proteins for degradation. Ubiquitination involves at least 3 classes of enzymes: ubiquitin-activating enzymes (E1s) ubiquitin-conjugating enzymes (E2s) and ubiquitin-protein ligases (E3s). Ubiquitin-Conjugating Enzyme E2G (UBE2G1) belongs to the E2 ubiquitin-conjugating enzyme family and catalyzes the covalent attachment of ubiquitin to other proteins. UE2G1 protein is involved in degradation of muscle-specific proteins.

    • Synonyms

      E217K, UBC7, UBE2G, Ubiquitin-conjugating enzyme E2 G1, E2 ubiquitin-conjugating enzyme G1, E217K, UBC7, Ubiquitin carrier protein G1, Ubiquitin-protein ligase G1.

    • 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 MGSMTELQSA LLLRRQLAEL NKNPVEGFSA GLIDDNDLYR WEVLIIGPPD TLYEGGVFKA HLTFPKDYPL RPPKMKFITE IWHPNVDKNG DVCISILHEP GEDKYGYEKP EERWLPIHTV ETIMISVISM LADPNGDSPA NVDAAKEWRE DRNGEFKRKV ARCVRKSQET AFE.

    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.

    Ube2G 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

    Price :

    Quantity :

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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 :

    UBE2N Human

    Description:

    Ubiquitin Conjugating Enzyme E2N Human Recombinant

    Ubiquitin-conjugating enzyme E2 N, Bendless-like ubiquitin-conjugating enzyme, Ubc13, Ubiquitin carrier protein N, Ubiquitin-protein ligase N, UBE2N, BLU, MGC8489, UbcH-ben, MGC131857.

    Product # :

    ENZ-104

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    Description

    UBE2N produced in E.Coli is a single, non-glycosylated polypeptide chain containing 172 amino acids (1-152a.a.) and having a molecular mass of 19.3kDa.UBE2N is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    UBE2N solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH8.0), 20% glycerol, 0.1M NaCl and 1mM DTT.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      UBE2N belongs to the E2 ubiquitin-conjugating enzyme family. UBE2N catalyzes the ATP-dependent synthesis of non-canonical polyubiquitin chains, a process which doesn’t set in motion proteasomal degradation. UBE2N mediates the transcription of some target genes and is believed to have a role in cell cycle progression; cellular differentiation and DNA repair mechanisms which ensure cell survival after DNA damage.

    • Synonyms

      Ubiquitin-conjugating enzyme E2 N, Bendless-like ubiquitin-conjugating enzyme, Ubc13, Ubiquitin carrier protein N, Ubiquitin-protein ligase N, UBE2N, BLU, MGC8489, UbcH-ben, MGC131857.

    • 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 MAGLPRRIIK ETQRLLAEPV PGIKAEPDES NARYFHVVIA GPQDSPFEGG TFKLELFLPE EYPMAAPKVR FMTKIYHPNV DKLGRICLDI LKDKWSPALQ IRTVLLSIQA LLSAPNPDDP LANDVAEQWK TNEAQAIETA RAWTRLYAMN NI.

    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.

    Ube2N Human
  • 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

    Price :

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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.

    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.

    Art4 Human
  • View Data Sheet

    Name :

    IDE Human, Active

    Description:

    Insulin-Degrading Enzyme Human Recombinant

    Insulin-Degrading Enzyme, Abeta-Degrading Protease, Insulysin, EC 3.4.24.56, Insulinase, Insulin Protease, INSULYSIN, EC 3.4.24, IDE, insulin-degrading enzyme isoform 1. 

    Product # :

    ENZ-1192

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    Description

    IDE Human, Active Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain (42-1019 a.a) containing a total of 984 amino acids, having a molecular mass of 114 kDa. IDE is fused to a 6 amino acid His-tag at C-terminus and is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The IDE solution (0.5mg/ml) contains 10% Glycerol, 100mM NaCl, 0.05% Brij35 and 20mM Tris-HCl buffer (pH 7.5).

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    Biological Activity

    Specific activity is greater than 3,000 pmol/min/ug in which 1 unit will convert 1.0 pmole of Mca-RPPGFSAFK(Dnp)-OH to MCA-Pro-Leu-OH per minute at pH 7.5 at 25°C.

    Citations

    More Info

    • Synonyms

      Insulin-Degrading Enzyme, Abeta-Degrading Protease, Insulysin, EC 3.4.24.56, Insulinase, Insulin Protease, INSULYSIN, EC 3.4.24, IDE, insulin-degrading enzyme isoform 1.

    • Physical Appearance

      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

      MNNPAIKRIG NHITKSPEDK REYRGLELAN GIKVLLISDP TTDKSSAALD VHIGSLSDPP NIAGLSHFCE HMLFLGTKKY PKENEYSQFL SEHAGSSNAF TSGEHTNYYF DVSHEHLEGA LDRFAQFFLC PLFDESCKDR EVNAVDSEHE KNVMNDAWRL FQLEKATGNP KHPFSKFGTG NKYTLETRPN QEGIDVRQEL LKFHSAYYSS NLMAVCVLGR ESLDDLTNLV VKLFSEVENK NVPLPEFPEH PFQEEHLKQL YKIVPIKDIR NLYVTFPIPD LQKYYKSNPG HYLGHLIGHE GPGSLLSELK SKGWVNTLVG GQKEGARGFM FFIINVDLTE EGLLHVEDII LHMFQYIQKL RAEGPQEWVF QECKDLNAVA FRFKDKERPR GYTSKIAGIL HYYPLEEVLT AEYLLEEFRP DLIEMVLDKL RPENVRVAIV SKSFEGKTDR TEEWYGTQYK QEAIPDEVIK KWQNADLNGK FKLPTKNEFI PTNFEILPLE KEATPYPALI KDTAMSKLWF KQDDKFFLPK ACLNFEFFSP FAYVDPLHCN MAYLYLELLK DSLNEYAYAA ELAGLSYDLQ NTIYGMYLSV KGYNDKQPIL LKKIIEKMAT FEIDEKRFEI IKEAYMRSLN NFRAEQPHQH AMYYLRLLMT EVAWTKDELK EALDDVTLPR LKAFIPQLLS RLHIEALLHG NITKQAALGI MQMVEDTLIE HAHTKPLLPS
      QLVRYREVQL PDRGWFVYQQ RNEVHNNCGI EIYYQTDMQS TSENMFLELF CQIISEPCFN TLRTKEQLGY IVFSGPRRAN GIQGLRFIIQ SEKPPHYLES RVEAFLITME KSIEDMTEEA FQKHIQALAI RRLDKPKKLS AECAKYWGEI ISQQYNFDRD NTEVAYLKTL TKEDIIKFYK EMLAVDAPRR HKVSVHVLAR EMDSCPVVGE FPCQNDINLS QAPALPQPEV IQNMTEFKRG LPLFPLVKPH INFMAAKLHH HHHH.

    • Background

      Insulin-degrading enzyme (IDE) is a crucial protease that plays a significant role in maintaining glucose homeostasis by degrading insulin and other bioactive peptides. Dysregulation of IDE has been implicated in various metabolic disorders, particularly type 2 diabetes mellitus. IDE is also associated with the clearance of amyloid-beta peptides in the brain, making it relevant to Alzheimer's disease pathology. Studying the recombinant form of IDE is fundamental to understanding its functional mechanisms and exploring potential avenues for therapeutic interventions.

      The primary goal of this research is to express and purify recombinant IDE using diverse expression systems. Recombinant DNA techniques will be employed to construct expression vectors containing the IDE gene, followed by expression in bacterial, yeast, or mammalian cell-based systems. The recombinant IDE will be purified using affinity chromatography or other appropriate methods, facilitating subsequent biochemical and biophysical characterization.

      The second objective is to investigate the substrate specificity and catalytic activity of the purified IDE. In vitro enzymatic assays will be conducted to analyse the ability of the recombinant IDE to degrade insulin and other potential substrates. The effects of various factors, such as pH, temperature, and potential modulators, on IDE activity will be evaluated. Additionally, the interactions between IDE and its substrates will be explored using binding assays.

      The third objective is to elucidate the three-dimensional structure of the IDE recombinant using techniques like X-ray crystallography or nuclear magnetic resonance (NMR) spectroscopy. Structural insights into the active site and binding pockets of IDE will provide valuable information for understanding its substrate recognition and catalytic mechanisms. This knowledge could be instrumental in designing targeted therapeutic compounds.

      By characterizing the IDE recombinant, this research aims to contribute to our understanding of its role in insulin metabolism, glucose regulation, and potential therapeutic applications. The findings from this study may have implications for the development of novel treatments for diabetes and other related disorders.

    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.

    Ide Human Active
  • View Data Sheet

    Name :

    SAE1/SAE2 Human

    Description:

    SAE1/SAE2 Human Recombinant

    Product # :

    ENZ-1161

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    Description

    SAE1/SAE2 Human Recombinant produced in SF9 is glycosylated, polypeptide chain containing 2 subunits (SAE1 subunit molecular mass is 41kDa & SAE2 subunit molecular mass is 91kDa). The subunits associate to form a complex. The SAE1/SAE2 is expressed with a -10xHis tag and purified by proprietary chromatographic techniques.

    Source

    Sf9 insect cells.

    Formulation

    SAE1/SAE2 is supplied in 20mM HEPES buffer pH-8.0, 200mM NaCl and 20% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      SAE1 and SAE2 form heterodimers which take part in the posttranslational modification of proteins (sumoylation). This process regulates protein structure as well as intracellular localization of the target. SAE1/SAE2 may indicate on dermatomyositis (DM) as autoantibodies against those 2 proteins have been found in patients.

    • 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.

    • 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

      0.3-0.8 µg/ml (depending on the type of ELISA plate and coating buffer). Suitable for labeling of functional groups.

    • Applications

      Western blot with anti SAE1/SAE2 autoantibody positive sample & Polyclonal anti-SAE1 and anti-SAE2 antibodies.

    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.

    Sae1 Sae2
  • View Data Sheet

    Name :

    CKMB1 Human

    Description:

    Creatine Kinase MB Isoenzyme Type-1 Human Recombinant

    Creatine Kinase MB 1, CKMB1

    Product # :

    CKI-269

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    Description

    CKMB1 Human Recombinant produced in E.Coli is a non covalently linked heterodimer that consists of 381 a.a. and having a total Mw of ~85.6kDa. The CKMB1 is purified by proprietary chromatographic techniques.

    Source

    E.Coli

    Formulation

    CKMB1 was lyophilized a concentrated solution containing 20mM Tris, 150mM NaCl, pH-8 and 5% Trehalose.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Biological Activity

    CKMB1 activity was measured kinetically by the CK-NAC assay at 37°C which was found to be between 500-600 units/mg. 1U converts 1µmole of creatine phosphate to creatine/min at 37˚C

    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.

    • Synonyms

      Creatine Kinase MB Isoenzyme Type-1, CK MB1

    • Physical Appearance

      Sterile Filtered white lyophilized powder.

    • Stability

      Lyophilized CKMB1 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution MCSF 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 CKMB1 in sterile 18MΩ-cm H2O at 0.1 mg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      CKM1
      MPFGNTHNKF KLNYKPEEEY PDLSKHNNHM AKVLTLELYK KLRDKETPSG FTVDDVIQTG VDNPGHPFIM TVGCVAGDEE SYEVFKELFD PIISDRHGGY KPTDKHKTDL NHENLKGGDD LDPNYVLSSR VRTGRSIKGY TLPPHCSRGE RRAVEKLSVE ALNSLTGEFK GKYYPLKSMT EKEQQQLIDD HFLFDKPVSP LLLASGMARD WPDARGIWHN DNKSFLVWVN EEDHLRVISM EKGGNMKEVF RRFCVGLQKI EEIFKKAGHP FMWNQHLGYV LTCPSNLGTG LRGGVHVKLA HLSKHPKFEE ILTRLRLQKR GTGGVDTAAV GSVFDVSNAD RLGSSEVEQV QLVVDGVKLM VEMEKKLEKG QSIDDMIPAQ

      CKB
      MPFSNSHNAL KLRFPAEDEF PDLSAHNNHM AKVLTPELYA ELRAKSTPSG FTLDDVIQTG VDNPGHPYIM TVGCVAGDEE SYEVFKDLFD PIIEDRHGGY KPSDEHKTDL NPDNLQGGDD LDPNYVLSSR VRTGRSIRGF CLPPHCSRGE RRAIEKLAVE ALSSLDGDLA GRYYALKSMT EAEQQQLIDD HFLFDKPVSP LLLASGMARD WPDARGIWHN DNKTFLVWVN EEDHLRVISM QKGGNMKEVF TRFCTGLTQI ETLFKSKDYE FMWNPHLGYI LTCPSNLGTG LRAGVHIKLP NLGKHEKFSE VLKRLRLQKR GTGGVDTAAV GGVFDVSNAD RLGFSEVELV QMVVDGVKLL IEMEQRLEQG QAIDDLMPAQ K

    • Background

      What is the molecular weight / Mw of CKMB1 Protein?
      CKMB1 Protein is a non covalently heterodimer having a total Mw of 85.6

      What is the source or expression system of CKMB1 Protein?
      Escherichia Coli.

      What is the Purity of CKMB1 Protein?
      CKMB1 Protein is >95% pure as determined by SDS-PAGE.

      What is the Biological Activity of CKMB1 Protein?
      The activity was determined kinetically by the CK-NAC assay at 37°C which ranges between 500-600 U/mg.

      What is the amino acid sequence of CKMB1 Protein?
      CKM1
      MPFGNTHNKF KLNYKPEEEY PDLSKHNNHM AKVLTLELYK KLRDKETPSG FTVDDVIQTG VDNPGHPFIM TVGCVAGDEE SYEVFKELFD PIISDRHGGY KPTDKHKTDL NHENLKGGDD LDPNYVLSSR VRTGRSIKGY TLPPHCSRGE RRAVEKLSVE ALNSLTGEFK GKYYPLKSMT EKEQQQLIDD HFLFDKPVSP LLLASGMARD WPDARGIWHN DNKSFLVWVN EEDHLRVISM EKGGNMKEVF RRFCVGLQKI EEIFKKAGHP FMWNQHLGYV LTCPSNLGTG LRGGVHVKLA HLSKHPKFEE ILTRLRLQKR GTGGVDTAAV GSVFDVSNAD RLGSSEVEQV QLVVDGVKLM VEMEKKLEKG QSIDDMIPAQ
      CKB
      MPFSNSHNAL KLRFPAEDEF PDLSAHNNHM AKVLTPELYA ELRAKSTPSG FTLDDVIQTG VDNPGHPYIM TVGCVAGDEE SYEVFKDLFD PIIEDRHGGY KPSDEHKTDL NPDNLQGGDD LDPNYVLSSR VRTGRSIRGF CLPPHCSRGE RRAIEKLAVE ALSSLDGDLA GRYYALKSMT EAEQQQLIDD HFLFDKPVSP LLLASGMARD WPDARGIWHN DNKTFLVWVN EEDHLRVISM QKGGNMKEVF TRFCTGLTQI ETLFKSKDYE FMWNPHLGYI LTCPSNLGTG LRAGVHIKLP NLGKHEKFSE VLKRLRLQKR GTGGVDTAAV GGVFDVSNAD RLGFSEVELV QMVVDGVKLL IEMEQRLEQG QAIDDLMPAQ K

      What applications can CKMB1 Protein be used in?
      CKMB1 Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for CKMB1 Protein?
      The endotoxin level is minimal, CKMB1 Protein was purified using conventional chromatography techniques.

    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.

    Ckmbi Human
  • View Data Sheet

    Name :

    MMP12 Human (1-33)

    Description:

    Matrix Metalloproteinase 12 (1-33 a.a.) Human Recombinant

    Product # :

    ENZ-1201

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    Description

    The MMP12 Human is created as a recombinant protein with a 4kda N-terminal fusion of His Tag. The MMP12 His-Tagged Fusion Protein, produced in E. coli, is a 10kDa protein containing 33 amino acid residues of the MMP12 Human, 1-33 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

    • Physical Appearance

      Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Store lyophilized MMP12 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.

    • Amino Acid Sequence

      MKFLLILLLQ ATASGALPLN SSTSLEKNNV LFG.

    • Background

      Matrix Metalloproteinase 12 also known as MMP12 is 1 of the main enzymes in the MMP family which is primarily produced by macrophages and neutrophils. MMP12 is implicated in the breakdown of elastin and in the development of chronic inflammatory diseases, such as emphysema, COPD and atherosclerosis. MMP12 is upregulated and contributes to tissue remodeling in inflammatory responses which is essential for wound healing and immune defense. MMP12 catalyzes the cleavage of collagen, elastin and other ECM components. Its activity is regulated in normal tissues to avoid pathological degradation.

    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.

    Mmp12 Enzyme
  • View Data Sheet

    Name :

    C.Albicans PLB1

    Description:

    Candida Albicans Phospholipase B1 Recombinant

    Product # :

    PRO-2809

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    Description

    Recombinant Candida Albicans Phospholipase B1 (24-526 a.a) produced in E. coli having a Mw of 52kDa. C.Albicans PLB1 is fused to a 6xHis tag at its C terminal is and purified by proprietary chromatographic technique.

    Source

    Escherichia Coli.

    Formulation

    Phosphate buffer and 25mM K2CO3.

    Purity

    Protein is >90% pure as determined by 10% PAGE (coomassie staining).

    Citations

    More Info

    • 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.

    • Background

      Potential as a Therapeutic Target:

      Understanding the role of PLB1 in fungal pathogenesis opens avenues for developing novel antifungal strategies. Inhibiting PLB1 activity could potentially render C. albicans less virulent and susceptible to host immune defenses. Recombinant Candida Albicans Phospholipase B1 studies play a critical role in identifying and characterizing potential inhibitors that could form the basis for antifungal drug development.

      Challenges and Future Directions:

      While the potential of Recombinant Candida Albicans Phospholipase B1 in antifungal research is promising, challenges persist. Fine-tuning its applications, deciphering its role in different infection scenarios, and optimizing strategies for therapeutic use are critical considerations for translational success. Additionally, understanding the interplay between PLB1 and other virulence factors in C. albicans pathogenesis remains an active area of investigation.

      Recombinant Candida Albicans Phospholipase B1 emerges as a key player in the intricate dance between the fungus and its human host. Its structural insights, enzymatic activities, and implications in host-pathogen interactions position it as a central focus in the exploration of C. albicans virulence. As researchers continue to unravel the molecular intricacies of PLB1, they not only deepen our understanding of fungal pathogenesis but also pave the way for transformative advancements in antifungal drug development, shaping the future of precision medicine in the realm of fungal infections.

    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.

    Candida Albicans Plb1
  • View Data Sheet

    Name :

    FUT5 Human

    Description:

    Fucosyltransferase 5 Human Recombinant

    FUT-5

    Product # :

    ENZ-1199

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    Description

    The FUT5 Human is created as a recombinant protein with a 4kda N-terminal fusion of His Tag. The FUT5 His-Tagged Fusion Protein produced in E. coli, is a 30kDa protein containing 172 amino acid residues of the FUT5 Human, 203-374 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

      FUT-5

    • Physical Appearance

      Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Store lyophilized FUT5 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

      Fucosyltransferase 5 also known as FUT5 is a glycosyltransferase which takes part in the biosynthesis of glycolipids and glycoproteins. FUT5 mainly catalyzes the transfer of fucose (a monosaccharide) to the type 2 chain of oligosaccharides (Galβ1-4GlcNAc). FUT5 takes an important part in various biological processes which include regulation of inflammation, cell-cell interactions and immune response modulation. FUT5 is expressed mainly in tissues such as the pancreas, liver and various immune cells.

    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.

    Fut5 Human
  • View Data Sheet

    Name :

    AK2 Antibody

    Description:

    Adenylate Kinase 2, Mouse Anti Human

    ADK2, AK-2, Adenylate kinase isoenzyme 2 mitochondrial, ATP-AMP transphosphorylase 2, adenylate kinase 2.

    Product # :

    ANT-616

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    Formulation

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

    Citations

    More Info

    • Introduction

      Adenylate kinases plays a role in regulating the adenine nucleotide composition within a cell by catalyzing the reversible transfer of phosphate groups among adenine nucleotides. There are 3 types of adenylate kinase isozymes, AK1, AK2, and AK3 in vertebrates. Expression of these isozymes are tissue-specific and developmentally regulated. AK2 is localized in the mitochondrial intermembrane space and is involved in apoptosis. AK2 is mutated in individuals with reticular dysgenesis.

    • Synonyms

      ADK2, AK-2, Adenylate kinase isoenzyme 2 mitochondrial, ATP-AMP transphosphorylase 2, adenylate kinase 2.

    • Physical Appearance

      Sterile filtered colorless solution.

    • Immunogen

      Anti-human AK2 mAb, is derived from hybridization of mouse F0 myeloma cells with spleen cells from BALB/c mice immunized with a recombinant human AK2 protein 1-239 amino acids purified from E. coli.

    • Ig Subclass

      Mouse IgG1 heavy chain and k light chain.

    • Clone

      PAT7E7AT.

    • Applications

      The 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

      AK2 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.

    Ak2 Antibody
  • View Data Sheet

    Name :

    PDPN P56F7AT Antibody

    Description:

    Podoplanin clone P56F7AT, Mouse Anti Human

    Podoplanin, Glycoprotein 36, PA2.26 antigen, T1A, GP36, GP40, Gp38, OTS8, T1A2, HT1A-1, PA2.26, T1-alpha, PDPN.

    Product # :

    ANT-641

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    Formulation

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

    Citations

    More Info

    • Introduction

      Podoplanin is a small mucin-like type-1 transmembrane protein, typically expressed in various specialized cell types throughout the body. Podoplanin is a type-I integral membrane glycoprotein with diverse distribution in human tissues. PDPN physiological function is related to its mucin-type character. The homologous protein in other species has been described as a differentiation antigen and influenza-virus receptor.
      PDPN is expressed in lymphatic progenitor cells and afterwards during mouse development in lymphatic endothelial cells. Podoplanin is a specific marker for lymph vessel endothelial cells. Over-expression of podoplanin significantly elevates endothelial cell adhesion, migration, and tube formation. Inhibition of Podoplanin expression decreases cell adhesion in human dermal lymphatic endothelial cells. Podoplanin is used as a specific marker for lymphatic endothelium in histopathology.
      Podoplanin expression is increased in nearly all human colon, rectum, and small intestine tumors. AGGRUS may serve as a diagnostic marker that distinguishes seminomas, the majority of which over express the protein, from embryonal carcinoma in testicular germ cell tumors.

    • Synonyms

      Podoplanin, Glycoprotein 36, PA2.26 antigen, T1A, GP36, GP40, Gp38, OTS8, T1A2, HT1A-1, PA2.26, T1-alpha, PDPN.

    • Physical Appearance

      Sterile filtered colorless solution.

    • Immunogen

      Anti-human PDPN mAb, is derived from hybridization of mouse F0 myeloma cells with spleen cells from BALB/c mice immunized with recombinant human PDPN amino acids 99-207 purified from E. coli.

    • Ig Subclass

      Mouse IgG1 heavy chain and k light chain.

    • Clone

      P56F7AT.

    • Applications

      PDPN 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

      PDPN 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.

    Pdpn P56F7At Antibody
  • View Data Sheet

    Name :

    PFKM Antibody

    Description:

    Phosphofructokinase Muscle, Mouse Anti Human

    EC 2.7.1.11, GSD7, PFK-1, PFK1, PFKA, PFKX, Phosphofructokinase-M, Phosphofructokinase 1, Phosphohexokinase, Phosphofructo-1-kinase isozyme A, MGC8699, PFKM. 

    Product # :

    ANT-475

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    Formulation

    1mg/ml containing PBS, pH-7.4, 10% Glycerol and 0.01% Sodium Azide.

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    • Introduction

      PFKM is a regulatory glycolytic enzyme that converts fructose 6-phosphate and ATP into fructose 1,6-bisphosphate (through PFK-1), fructose 2,6-bisphosphate (through PFK-2) and ADP. Three phosphofructokinase isozymes exist in humans: muscle, liver and platelet. Mutations in PFKM gene have been related with glycogen storage disease type VII, also identified as Tarui disease.

    • Synonyms

      EC 2.7.1.11, GSD7, PFK-1, PFK1, PFKA, PFKX, Phosphofructokinase-M, Phosphofructokinase 1, Phosphohexokinase, Phosphofructo-1-kinase isozyme A, MGC8699, PFKM.

    • Physical Appearance

      Sterile Filtered colorless solution.

    • Immunogen

      Anti-human PFKM mAb, clone PAT2F11A, is derived from hybridization of mouse F0 myeloma cells with spleen cells from BALB/c mice immunized with a recombinant human PFKM protein.

    • Ig Subclass

      Mouse IgG2a heavy chain and Kappa light chain.

    • Clone

      PAT2F11A.

    • Applications

      The antibody has been tested by ELISA and Western blot analysis to assure specificity and reactivity. Since application varies, however, each investigation should be titrated by the reagent to obtain optimal results. Recommended dilution range for Western blot analysis is 1:500 ~ 1:2000. Recommended starting dilution is 1:2000.

    • 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

      PFKM antibody was purified from mouse ascitic fluids by protein-G 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.

    Pfkm Antibody
  • View Data Sheet

    Name :

    Tamm Horsfall

    Description:

    Recombinant Human Tamm Horsfall Glycoprotein

    Tamm-Horsfall urinary glycoprotein, THP, FJHN, HNFJ, THGP, MCKD2, ADMCKD2, UMOD, Uromodulin.


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    ENZ-1206

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    Description

    Uromodulin Human Recombinant protein produced from HEK Cells, is a polypeptide chain containing 595 amino acids ( 25-613 a.a. ) and having a total Mw of 65 kDa.

    Source

    HEK293

    Formulation

    The UMOD protein was lyophilized from 0.4μm filtered solution containing 50mM NaCl, 0.02M TRIS, pH 7.5.

    Purity

    Greater than 90.0% as determined by SDS-PAGE analysis.

    SDS-PAGE

    Tamm Horsfall-SDS-PAGE - Product image 1

    Citations

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    • Introduction

      Uromodulin (Tamm–Horsfall protein) is produced mainly by cells in the kidney’s thick ascending limb and is the most abundant protein in normal urine.
      Uromodulin takes part in salt and water regulation, helps prevent urinary tract infections and kidney stones, and influences inflammation and immune activity in the kidney.
      Reduced Uromodulin levels is associated with chronic kidney disease.
      UMOD mutations causes unproper protein folding and thus transported incorrectly, resulting in its accumulation inside kidney tubular cells that damages the tubules and cause kidney disease (ADTKD-UMOD), associated with high uric acid, gout, and progressive kidney failure.

    • Synonyms

      Tamm-Horsfall urinary glycoprotein, THP, FJHN, HNFJ, THGP, MCKD2, ADMCKD2, UMOD, Uromodulin.

    • Physical Appearance

      Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized UMOD although stable at room temperature for 3 weeks, should be stored at -18C. Upon reconstitution UMOD should be stored at 4C between 2-7 days and for future use below -18C.
      For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).
      Please prevent freeze-thaw cycles.

    • Solubility

      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 in the cell culture.

    • Amino Acid Sequence

      DTSEARWCSE CHSNATCTED EAVTTCTCQE GFTGDGLTCV DLDECAIPGA HNCSANSSCV NTPGSFSCVC PEGFRLSPGL GCTDVDECAE PGLSHCHALA TCVNVVGSYL CVCPAGYRGD GWHCECSPGS CGPGLDCVPE GDALVCADPC QAHRTLDEYW RSTEYGEGYA CDTDLRGWYR FVGQGGARMA ETCVPVLRCN TAAPMWLNGT HPSSDEGIVS RKACAHWSGH CCLWDASVQV KACAGGYYVY NLTAPPECHL AYCTDPSSVE GTCEECSIDE DCKSNNGRWH CQCKQDFNIT DISLLEHRLE CGANDMKVSL GKCQLKSLGF DKVFMYLSDS RCSGFNDRDN RDWVSVVTPA RDGPCGTVLT RNETHATYSN TLYLADEIII RDLNIKINFA CSYPLDMKVS LKTALQPMVS ALNIRVGGTG MFTVRMALFQ TPSYTQPYQG SSVTLSTEAF LYVGTMLDGG DLSRFALLMT NCYATPSSNA TDPLKYFIIQ DRCPHTRDST IQVVENGESS QGRFSVQMFR FAGNYDLVYL HCEVYLCDTM NEKCKPTCSG TRFRSGSVID QSRVLNLGPI TRKGVQATVH HHHHH

    • Background

      Uromodulin is the most abundant protein in normal urine. Its secretion in urine follows proteolytic cleavage of the ectodomain of its glycosyl phosphatidylinosital-anchored counterpart that is situated on the luminal cell surface of the loop of Henle. Uromodulin plays a role as a constitutive inhibitor of calcium crystallization in renal fluids. Secretion of uromodulin in urine provides protection against urinary tract infections caused by uropathogenic bacteria. Defects in Uromodulin expression are associated with the autosomal dominant renal disorders medullary cystic kidney disease-2 (MCKD2) and familial juvenile hyperuricemic nephropathy (FJHN). These disorders are characterized by juvenile onset of hyperuricemia, gout, and progressive renal failure. While several transcript variants may exist for this gene, the full-length natures of only two have been described to date. UMOD is involved in regulating the circulating activity of cytokines as it binds to il-1, il-2 and tnf with high affinity.

      What is the molecular weight/Mw of UMOD Protein?
      UMOD Protein has a total Mw of 65kDa.

      What is the source or expression system of UMOD Protein?
      HEK293.

      What is the Purity of UMOD Protein?
      UMOD Protein is >90% pure as determined by SDS-PAGE.

      What is the Biological Activity of UMOD Protein?
      The biological functionality of UMOD Protein will be determined in the future.

      What is the amino acid sequence of UMOD Protein?
      UMOD Protein is composed from 595 amino acids.

      What applications can UMOD Protein be used in?
      UMOD Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for UMOD Protein?
      The endotoxin level is minimal, UMOD Protein was purified using conventional chromatography techniques.

    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.

    Tamm Horsfall
  • View Data Sheet

    Name :

    IDH1

    Description:

    Isocitrate Dehydrogenase-1 Yeast Recombinant

    Isocitrate dehydrogenase [NADP] cytoplasmic, EC 1.1.1.42, Cytosolic NADP-isocitrate dehydrogenase, Oxalosuccinate decarboxylase, IDH, NADP(+)-specific ICDH, IDP, PICD.

    Product # :

    ENZ-289

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    Description

    Recombinant Saccharomyces Cerevisiae ICDH (NADP) derived from yeast host cells by using over-expression system, is full length same as designated ICD1 from Saccharomyces Cerevisiae. The N-terminal amino acid Phenylalanine residue next to Met is substituted with Alanine for overexpression. The ICDH is purified by proprietary chromatographic techniques.

    Source

    Yeast cells.

    Formulation

    One ml of solution contains 0.075 mol/l KPO4, 50% Glycerol, pH 7.1.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    Biological Activity

    The specific activity was found to be 115 U/mg.

    Citations

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    • Introduction

      Isocitrate Dehydrogenase is an enzyme of the oxidoreductase class that catalyzes the conversion of isocitrate and NAD+ to yield 2-ketoglutarate, carbon dioxide, and NADH. It occurs in cell mitochondria. The enzyme requires Mg2+, Mn2+; it is activated by ADP, citrate, and Ca2+, and inhibited by NADH, NADPH, and ATP. The reaction is the key rate-limiting step of the citric acid (tricarboxylic) cycle.

    • Synonyms

      Isocitrate dehydrogenase [NADP] cytoplasmic, EC 1.1.1.42, Cytosolic NADP-isocitrate dehydrogenase, Oxalosuccinate decarboxylase, IDH, NADP(+)-specific ICDH, IDP, PICD.

    • 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.

    • Unit Definition

      One unit is defined as 1 µmol of NAD+ production per minute under the assay conditions (25°C, pH 7.5).

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    Isocitrate Dehydrogenase
  • View Data Sheet

    Name :

    Protease

    Description:

    Recombinant Protease

    Product # :

    ENZ-354

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    Description

    Protease Recombinant is a fusion protein of glutathione S-transferase (GST) and human rhinovirus (HRV) type 14 3C protease. The protease specifically recognizes a subset of sequences which include the core amino acid sequence Leu-Phe-Gln/Gly-Pro cleaving between the Gln and Gly residues. Substrate recognition and cleavage are likely to be dependent not only upon primary structural signals, but also upon the secondary and tertiary structures of the fusion protein as well.The Recombinant Protease is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Citations

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    • Physical Appearance

      Sterile filtered colorless solution.

    • Stability

      Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. Avoid multiple freeze-thaw cycles.

    • Cleavage Conditions

      For Cleavage of a Fusion Protein: During cleavage reactions, it is recommended that samples be removed at various time points and analyzed by SDS-PAGE to estimate the yield, purity, and extent of digestion. The amount of PreScission Protease, temperature and length of incubation required for complete digestion of a given GST fusion partner may vary depending on the fusion partner. Optimal conditions for each fusion should be determined in pilot experiments. Digestion may be improved by adding TritonTM X-100, TweenTM 20, NonidetTM, or NP40 to a concentration of 0.01%. Concentrations of these detergents up to 1% do not inhibit PreScission Protease.

    • Cleavage Buffer

      50mM Tris-HCl, pH-7.0 (at 25°C), 150mM NaCl, 1mM EDTA, 1mM dithiothreitol. Chill to 5°C prior to use.

    • Unit Definition

      One unit will cleave ?90% of 100 µg of a test GST-fusion protein in Cleavage Buffer (50mM Tris-HCl, 150 mM NaCl, 1 mM EDTA, 1 mM DTT, pH 7.0 at 25°C) at 5°C for 16 hours.

    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.

    Protease Enzyme
  • View Data Sheet

    Name :

    ACE2 Mouse

    Description:

    Angiotensin Converting Enzyme 2 Mouse Recombinant

    ACE2, 2010305L05Rik, Angiotensin I Converting Enzyme, Angiotensin I Converting, Enzyme (Peptidyl-Dipeptidase A), Angiotensin-Converting Enzyme Homolog, Angiotensin-Converting Enzyme, ACE-Related Carboxypeptidase, Metalloprotease MPROT15, Peptidyl-Dipeptidase A, ACEH, EC 3.4.17.23, EC 3.4.17.

    Product # :

    ENZ-1123

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    Description

    ACE2 Mouse produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 731 amino acids (18-740 aa) and having a molecular mass of 84.5kDa. ACE2 is fused to a 6 amino acid His-Tag at C-terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    The ACE2 solution contains 10% Glycerol and Phosphate-Buffered Saline (pH 7.4).

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Biological Activity

    Greater than 200pmol/min/ug, and is defined as the amount of enzyme that hydrolysis 1 pmole of McaYVADAPK(Dnp)-OH per min. at pH-7.5, at 25C.

    Citations

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    • Introduction

      ACE-2 (Angiotensin converting enzyme 2) an enzyme bound to cell membranes in various organs such as intestines arteries , lungs, heart & kidney. ACE2 an entry receptor of SARS coronaviruses as well as SARS-CoV-2,.The coronavirus spike (S) glycoprotein is a class I viral fusion antigen located on the external envelope of the virion that takes part in a critical part in viral infection by identifying host cell receptors and facilitating fusion of the viral and cellular membranes. 2 main domains in coronavirus S1 have been recognized, the N-terminal domain and C-terminal domain. One or the other and/or both S1 domains function as a receptor-binding domain. SARS-CoV + MERS-CoV equally use C-domain to attach their receptors.ACE2 is a type I transmembrane antigen with an extracellular N-terminal domain having the catalytic site and an intracellular C-terminal tail. ACE2 obtains a signal peptide, a transmembrane domain, and a single metalloproteinase active site containing an HEXXH zinc-binding domain. ACE-2 plays a role as a mono-carboxypeptidase which degrades Ang I to produce the nonapeptide Ang 1–9 and Ang II to create the heptapeptide Ang 1–7.

    • Synonyms

      ACE2, 2010305L05Rik, Angiotensin I Converting Enzyme, Angiotensin I Converting, Enzyme (Peptidyl-Dipeptidase A), Angiotensin-Converting Enzyme Homolog, Angiotensin-Converting Enzyme, ACE-Related Carboxypeptidase, Metalloprotease MPROT15, Peptidyl-Dipeptidase A, ACEH, EC 3.4.17.23, EC 3.4.17.

    • 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

      QSLTEENAKT FLNNFNQEAE DLSYQSSLAS WNYNTNITEE NAQKMSEAAA KWSAFYEEQS KTAQSFSLQE IQTPIIKRQL QALQQSGSSA LSADKNKQLN TILNTMSTIY STGKVCNPKN PQECLLLEPG LDEIMATSTD YNSRLWAWEG WRAEVGKQLR PLYEEYVVLK NEMARANNYN DYGDYWRGDY EAEGADGYNY NRNQLIEDVE RTFAEIKPLY EHLHAYVRRK LMDTYPSYIS PTGCLPAHLL GDMWGRFWTN LYPLTVPFAQ KPNIDVTDAM MNQGWDAERI FQEAEKFFVS VGLPHMTQGF WANSMLTEPA DGRKVVCHPT AWDLGHGDFR IKMCTKVTMD NFLTAHHEMG HIQYDMAYAR QPFLLRNGAN EGFHEAVGEI MSLSAATPKH LKSIGLLPSD FQEDSETEIN FLLKQALTIV GTLPFTYMLE KWRWMVFRGE IPKEQWMKKW WEMKREIVGV VEPLPHDETY CDPASLFHVS NDYSFIRYYT RTIYQFQFQE ALCQAAKYNG SLHKCDISNS TEAGQKLLKM LSLGNSEPWT KALENVVGAR NMDVKPLLNY FQPLFDWLKE QNRNSFVGWN TEWSPYADQS IKVRISLKSA LGANAYEWTN NEMFLFRSSV AYAMRKYFSI IKNQTVPFLE EDVRVSDLKP RVSFYFFVTS PQNVSDVIPR SEVEDAIRMS RGRINDVFGL NDNSLEFLGI HPTLEPPYQPPVTLEHHHHH H.

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    Ace2 Mouse
  • View Data Sheet

    Name :

    DCXR Human, Bioactive

    Description:

    Dicarbonyl/L-Xylulose Reductase Human Recombinant, Bioactive

    DCR, HCR2, HCRII, KIDCR, P34H, SDR20C1, Dicarbonyl/L-Xylulose Reductase, EC=1.1.1.10, Carbonyl reductase II, Kidney dicarbonyl reductase, Sperm surface protein P34H.

    Product # :

    ENZ-1029

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    Description

    DCXR Recombinant Human produced in E.Coli is a single, non-glycosylated polypeptide chain containing 264 amino acids (1-244 a.a.) and having a molecular mass of 28 kDa. The DCXR is fused to a 20 amino acids His-Tag at N-terminus and purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The DCXR (0.5mg/ml) solution containing 20mM Tris-HCl buffer (pH 8.0), 1mM DTT, 20% glycerol and 50mM NaCl.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Biological Activity

    Specific activity is > 1,800 pmol/min/ug and is defined as the amount of enzyme that oxidize 1pmole of xylitol to L-xylulose per minute at pH 10.0 at 37C.

    Citations

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    • Introduction

      DCXR catalyzes the NADPH-dependent reduction of numerous pentoses, tetroses, trioses, alpha-dicarbonyl molecules and L-xylulose. DCXR takes part in the uronate cycle of glucose metabolism. DCXR participates in the water absorption and cellular osmoregulation in the proximal renal tubules by producing xylitol, an osmolyte, thus preventing osmolytic stress from occurring in the renal tubules.

    • Synonyms

      DCR, HCR2, HCRII, KIDCR, P34H, SDR20C1, Dicarbonyl/L-Xylulose Reductase, EC=1.1.1.10, Carbonyl reductase II, Kidney dicarbonyl reductase, Sperm surface protein P34H.

    • 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 MELFLAGRRV LVTGAGKGIG RGTVQALHAT GARVVAVSRT QADLDSLVRE CPGIEPVCVD LGDWEATERA LGSVGPVDLL VNNAAVALLQ PFLEVTKEAF DRSFEVNLRA VIQVSQIVAR GLIARGVPGA IVNVSSQCSQ RAVTNHSVYC STKGALDMLT KVMALELGPH KIRVNAVNPT VVMTSMGQAT WSDPHKAKTM LNRIPLGKFA EVEHVVNAIL FLLSDRSGMT TGSTLPVEGG FWAC.

    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.

    Dcxr Human Bioactive
  • View Data Sheet

    Name :

    IDI1 Human

    Description:

    Isopentenyl-Diphosphate Delta Isomerase 1 Human Recombinant

    Isopentenyl-diphosphate Delta-isomerase 1, Isopentenyl pyrophosphate isomerase 1, IPP isomerase 1, IPPI1, IDI1, IPP1.

    Product # :

    ENZ-189

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    Description

    IDI1 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 248 amino acids (1-228) and having a molecular mass of 28.6kDa.IDI1 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    The IDI1 solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 1mM DTT, 10% glycerol and 0.1M NaCl.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      Isopentenyl-diphosphate isomerase 1 (IDI1) belongs to the IPP isomerase type I family and is involved in cholesterol biosynthesis. IDI1 is a peroxisomally-localized enzyme which catalyzes the interconversion of isopentenyl diphosphate (IPP) to its highly electrophilic isomer, dimethylallyl diphosphate (DMAPP), which is the substrate for the sequential reaction that results in the synthesis of farnesyl diphosphate and, eventually, cholesterol. Peroxisomal deficiency diseases such as Zellweger syndrome and neonatal adrenoleukodystrophy show a reduction in IPP isomerase activity.

    • Synonyms

      Isopentenyl-diphosphate Delta-isomerase 1, Isopentenyl pyrophosphate isomerase 1, IPP isomerase 1, IPPI1, IDI1, IPP1.

    • 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 MMPEINTNHL DKQQVQLLAE MCILIDENDN KIGAETKKNC HLNENIEKGL LHRAFSVFLF NTENKLLLQQ RSDAKITFPG CFTNTCCSHP LSNPAELEES DALGVRRAAQ RRLKAELGIP LEEVPPEEIN YLTRIHYKAQ SDGIWGEHEI DYILLVRKNV
      TLNPDPNEIK SYCYVSKEEL KELLKKAASG EIKITPWFKI IAATFLFKWW DNLNHLNQFV DHEKIYRM.

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    Idi1 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.

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    Nudt3 Human
  • View Data Sheet

    Name :

    ErbB3 Human, sf9

    Description:

    Tyrosine Kinase ErbB-3 Human Recombinant, sf9

    Tyrosine Kinase ErbB-3, sf9, ErbB3 sf9, Receptor tyrosine-protein kinase erbB-3, ERBB3, Proto-oncogene-like protein c-ErbB-3, Tyrosine kinase-type cell surface receptor HER3, HER3, Receptor tyrosine-protein kinase erbB-3 isoform, c-erbB-3, ErbB-3, erbB3-S, LCCS2, MDA-BF-1, p180-ErbB3, p45-sErbB3, p85-sErbB3.

    Product # :

    PKA-081

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    Description

    ErbB3 Human Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 863 amino acids (20-643 a.a.) and having a molecular mass of 95.6kDa (Migrates at 100-150kDa on SDS-PAGE under reducing conditions).ErbB3 is expressed with a 239 amino acid hIgG-His tag at C-Terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    ErbB3 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.

    Citations

    More Info

    • Introduction

      ErbB3, also called Her3 (human epidermal growth factor receptor 3), is a type I membrane glycoprotein that is a member of the ErbB family of tyrosine kinase receptors. ErbB family members serve as receptors for the epidermal growth factor (EGF) family of growth factors. Among ErbB family members, ErbB3 is unique in that it contains a defective kinase domain. ErbB3 is expressed in keratinocytes, melanocytes, skeletal muscle cells, embryonic myoblasts and Schwann cells. Monomeric ErbB3 serves as a low affinity receptor for the heregulins (HRG). ErbB3 can induce specific antibody production in vivo, hence to inhibit tumor cell growth. ErbB-3 can be used to treat early, medium and advanced or post-operative breast cancer with over-expression of ErbB2. According to its mechanism of action, ErbB3 is classified as a therapeutic for cancer.

    • Synonyms

      Tyrosine Kinase ErbB-3, sf9, ErbB3 sf9, Receptor tyrosine-protein kinase erbB-3, ERBB3, Proto-oncogene-like protein c-ErbB-3, Tyrosine kinase-type cell surface receptor HER3, HER3, Receptor tyrosine-protein kinase erbB-3 isoform, c-erbB-3, ErbB-3, erbB3-S, LCCS2, MDA-BF-1, p180-ErbB3, p45-sErbB3, p85-sErbB3.

    • 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

      SEVGNSQAVC PGTLNGLSVT GDAENQYQTL YKLYERCEVV MGNLEIVLTG HNADLSFLQW IREVTGYVLV AMNEFSTLPL PNLRVVRGTQ VYDGKFAIFV MLNYNTNSSH ALRQLRLTQL TEILSGGVYI EKNDKLCHMD TIDWRDIVRD RDAEIVVKDN GRSCPPCHEV CKGRCWGPGS EDCQTLTKTI CAPQCNGHCF GPNPNQCCHD ECAGGCSGPQ DTDCFACRHF NDSGACVPRC PQPLVYNKLT FQLEPNPHTK YQYGGVCVAS CPHNFVVDQT SCVRACPPDK MEVDKNGLKM CEPCGGLCPK ACEGTGSGSR FQTVDSSNID GFVNCTKILG NLDFLITGLN GDPWHKIPAL DPEKLNVFRT VREITGYLNI QSWPPHMHNF SVFSNLTTIG GRSLYNRGFS LLIMKNLNVT SLGFRSLKEI SAGRIYISAN RQLCYHHSLN WTKVLRGPTE ERLDIKHNRP RRDCVAEGKV CDPLCSSGGC WGPGPGQCLS CRNYSRGGVC VTHCNFLNGE PREFAHEAEC FSCHPECQPM EGTATCNGSG SDTCAQCAHF RDGPHCVSSC PHGVLGAKGP IYKYPDVQNE CRPCHENCTQ GCKGPELQDC LGQTLVLIGK THLTRSPKSC DKTHTCPPCP APELLGGPSV FLFPPKPKDT LMISRTPEVT CVVVDVSHED PEVKFNWYVD GVEVHNAKTK PREEQYNSTY RVVSVLTVLH QDWLNGKEYK CKVSNKALPA PIEKTISKAK GQPREPQVYT LPPSRDELTK NQVSLTCLVK GFYPSDIAVE WESNGQPENN YKTTPPVLDS DGSFFLYSKL TVDKSRWQQG NVFSCSVMHE ALHNHYTQKS LSLSPGKHHH HHH.

    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.

    Erbb3 Human Sf9
  • View Data Sheet

    Name :

    CA12 Human

    Description:

    Carbonic Anhydrase XII Human Recombinant

    Carbonic anhydrase 12, Carbonate dehydratase XII, Carbonic anhydrase XII, CA-XII, Tumor antigen HOM-RCC-3.1.3, CA12, Carbonic Anhydrase XII, Carbonic anhydrase 12 isoform 1, CAXII, HsT18816.

    Product # :

    ENZ-886

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    • source
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    • Citations

    Description

    CA12 Human Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 283 amino acids (25-301a.a.) and having a molecular mass of 31.94kDa (Migrates at 28-40kDa on SDS-PAGE under reducing conditions).CA12 is fused to a 6 amino acid His-tag at C-terminus & purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    CA12 protein solution (0.5mg/ml) containing Phosphate Buffer Saline (pH7.4) and 10% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    Biological Activity

    Specific activity is > 300 pmol/min/ug, and is defined as the amount of enzyme that hydrolyze 1.0 pmole of 4-nitrophenyl acetate to 4-nitrophenol per minute at pH 7.5 at 37C.

    Citations

    More Info

    • Introduction

      Carbonic anhydrase 12 (CA12) is an enzyme that belongs to the Carbonic anhydrases (CAs) family. This is a large family of zinc metalloenzymes which catalyze the reversible hydration of carbon dioxide. They are involved in various biological processes, including respiration, calcification, acid-base balance, bone resorption, and the formation of aqueous humor, cerebrospinal fluid, saliva, and gastric acid. CA12 is a type I membrane protein which is highly expressed in normal tissues, such as the kidney, colon and pancreas, and is overexpressed in 10% of clear cell renal carcinomas.

    • Synonyms

      Carbonic anhydrase 12, Carbonate dehydratase XII, Carbonic anhydrase XII, CA-XII, Tumor antigen HOM-RCC-3.1.3, CA12, Carbonic Anhydrase XII, Carbonic anhydrase 12 isoform 1, CAXII, HsT18816.

    • 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

      APVNGSKWTY FGPDGENSWS KKYPSCGGLL QSPIDLHSDI LQYDASLTPL EFQGYNLSAN KQFLLTNNGH SVKLNLPSDM HIQGLQSRYS ATQLHLHWGN PNDPHGSEHT VSGQHFAAEL HIVHYNSDLY PDASTASNKS EGLAVLAVLI EMGSFNPSYD KIFSHLQHVK YKGQEAFVPG FNIEELLPER TAEYYRYRGS LTTPPCNPTV LWTVFRNPVQ ISQEQLLALE TALYCTHMDD PSPREMINNF RQVQKFDERL VYTSFSQVQV CTAAGLSHHH HHH.

    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.

    Ca12 Human
  • View Data Sheet

    Name :

    CAIII Human, His

    Description:

    Carbonic Anhydrase III Human Recombinant, His Tag

    Car3, CAIII, Carbonic anhydrase 3, EC 4.2.1.1, Carbonic anhydrase III, Carbonate dehydratase III, CA-III.

    Product # :

    ENZ-270

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    Description

    Carbonic anhydrase III Human Recombinant produced in E.Coli, and having a molecular mass of 33.9 kDa. CAIII is expressed with an amino-terminal hexahistidine tag.The CA-III is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Supplied in 10mM Tris-HCl (pH 8), 250mM NaCl, 0.5mM DTT, 1.5mM Cysteine, and 50% Glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      Carbonic anhydrase (carbonate dehydratase) is a family of metalloenzymes (enzymes that contain one or more metal atoms as a functional component of the enzyme) that catalyze the rapid (and reversible) conversion of carbon dioxide to bicarbonate and protons, a reaction that occurs rather slowly in the absence of a catalyst. Carbonic anhydrase greatly increases the rate of the reaction, with typical catalytic rates of the different forms of this enzyme ranging between 104 and 106 reactions per second. The active site of most carbonic anhydrases contains a zincion. CAIII is a cytoplasmic isoenzyme, but is released into the circulation following injury.

    • Synonyms

      Car3, CAIII, Carbonic anhydrase 3, EC 4.2.1.1, Carbonic anhydrase III, Carbonate dehydratase III, CA-III.

    • Physical Appearance

      Sterile Filtered blue 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.

    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.

    Caiii Human
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