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1000 results found for “Isomerase”

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  • View Data Sheet

    Name :

    PRMT1 Mouse

    Description:

    Protein Arginine Methyltransferase 1 Mouse Recombinant

    ANM1, HCP1, HRMT1L2, IR1B4, Interferon receptor 1-bound protein 4, EC 2.1.1, Protein arginine N-methyltransferase 1, Prmt1, AW214366, 6720434D09Rik.

    Product # :

    ENZ-365

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    Description

    PRMT1 Mouse Recombinant fused with His-MBP tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 750 amino acids and having a molecular mass of 84 kDa.The PRMT1 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The PRMT1 solution (1mg/ml) contains 40mM Tris-HCl pH 8.0, 100mM NaCl, 4mM MgCl2, 2mM DTT and 40% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    Biological Activity

    Specific activity is defined as the amount of enzyme that transfer 1.0nmole of methyl group per minute at 37C and was found to be > 30nmol/min/mg.

    More Info

    • Introduction

      PRMT1 Methylates (mono & asymmetric dimethylation) the guanidino nitrogens of arginyl residues present in a glycine and arginine-rich domain (may methylate HNRNPA1 and histones). Methylates SUPT5H.
      The PRMT1 protein functions as a histone methyltransferase specific for H4.
      PRMT1 is an essential factor in oncogenesis and is a potential novel therapeutic target in cancer.
      PRMT1-mediated methylation serves as a positive modulator of IR/IRS-1/PI3K pathway and glucose uptake in skeletal muscle cells.
      CAF1 is a new regulator of PRMT1-dependent arginine methylation.
      PRMT1 arginine-methylates MRE11 therefore it regulates the activity of MRE11-RAD50-NBS1 complex during the intra-S-phase DNA damage checkpoint response.
      PRMT1 plays a post-translationally part in regulating the transcriptional activity.
      PRMT1is found predominantly in the cytoplasma though a fraction of PRMT1 is located in the nucleus.

    • Synonyms

      ANM1, HCP1, HRMT1L2, IR1B4, Interferon receptor 1-bound protein 4, EC 2.1.1, Protein arginine N-methyltransferase 1, Prmt1, AW214366, 6720434D09Rik.

    • 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

      MHHHHHHMKI EEGKLVIWIN GDKGYNGLAE VGKKFEKDTG IKVTVEHPDK LEEKFPQVAA TGDGPDIIFW AHDRFGGYAQ SGLLAEITPD KAFQDKLYPF TWDAVRYNGK LIAYPIAVEA LSLIYNKDLL PNPPKTWEEI PALDKELKAK GKSALMFNLQ EPYFTWPLIA ADGGYAFKYE NGKYDIKDVG VDNAGAKAGL TFLVDLIKNK HMNADTDYSI AEAAFNKGET AMTINGPWAW SNIDTSKVNY GVTVLPTFKG QPSKPFVGVL SAGINAASPN KELAKEFLEN YLLTDEGLEA
      VNKDKPLGAV ALKSYEEELA KDPRIAATME NAQKGEIMPN IPQMSAFWYA VRTAVINAAS GRQTVDEALK DAQTNSSSNN NNNNNNNNLG IEGRGSHMAA AEAANCIMEV SCGQAESSEK PNAEDMTSKD YYFDSYAHFG IHEEMLKDEV RTLTYRNSMF HNRHLFKDKV VLDVGSGTGILCMFAAKAGA RKVIGIECSS ISDYAVKIVK ANKLDHVVTI IKGKVEEVEL PVEKVDIIIS EWMGYCLFYE SMLNTVLHAR DKWLAPDGLI FPDRATLYVT AIEDRQYKDY KIHWWENVYG
      FDMSCIKDVA IKEPLVDVVD PKQLVTNACL IKEVDIYTVK VEDLTFTSPF CLQVKRNDYVHALVAYFNIE FTRCHKRTGF STSPESPYTH WKQTVFYMED YLTVKTGEEI FGTIGMRPNA KNNRDLDFTI DLDFKGQLCE LSCSTDYRMR.

    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.

    Prmt1 Mouse
  • View Data Sheet

    Name :

    L-Asparaginase

    Description:

    L-Asparaginase

    Product # :

    ENZ-287

    Price :

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    Description

    L-asparaginase was purified from E.coli ASI.357.

    Source

    Escherichia Coli.

    Formulation

    The enzyme was lyophilized with no additives.

    Purity

    Greater than 96.0% as determined by SDS-PAGE.

    Biological Activity

    One IU of L- Asparaginase is defined as that amount of enzyme required to generate 1 µmol of ammonia per minute at pH 7.3 and 37°C.

    More Info

    • Introduction

      L-Asparaginase is an enzyme that depletes L-Asparagine "an important nutrient for cancer cells" resulting in cancer/tumor cell starvation. L-asparaginase is an anti-tumor agent derived from E.coli.,which can inhibit the growth of malignant cells. It is used mainly for the induction of remission in acute lymphoblastic leukaemia. Because of the lymph node origin of malignant B cells in Multiple Myeloma, L-Asparagine is an essential amino acid for their cell metabolism, and, consequently, L-Asparaginase may be of value in managing the disease.
      The rationale behind asparaginase is that it takes advantage of the fact that ALL cellsare unable to synthesize the non-essential amino acidasparaginewhereas normal cells are able to make their own asparagine. These leukemic cells depend on circulating asparagine. Asparaginase however catalyzes the conversion of L-asparagine to aspartic acidand ammonia. This deprives the leukemic cell of circulating asparagine.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized L-Asparaginase although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution L-Asparaginase 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 L-Asparaginase in 18M-cm H2O at 1mg/ml.

    • Background

      L-Asparaginase Enzyme: Unraveling Its Therapeutic Potential in Cancer Treatment

      Abstract: L-Asparaginase is an enzyme that plays a crucial role in cancer therapy by depleting the levels of asparagine in the blood, thereby inhibiting the growth of cancer cells.

      This research paper provides a comprehensive analysis of L-Asparaginase, including its biochemical properties, mechanisms of action, therapeutic applications, and clinical implications.

      The paper explores the significance of L-Asparaginase as a key enzyme in cancer treatment and highlights its potential for improving patient outcomes.

      1. Introduction L-Asparaginase is an enzyme widely used in cancer therapy, particularly in the treatment of acute lymphoblastic leukemia (ALL). This section introduces L-Asparaginase and its role in cancer treatment, emphasizing its importance in medical research and clinical practice.
      2. Biochemical Properties of L-Asparaginase L-Asparaginase belongs to the class of enzymes known as hydrolases and catalyzes the hydrolysis of asparagine to aspartic acid and ammonia. This section discusses the biochemical properties of L-Asparaginase, including its structure, catalytic mechanism, and factors influencing its activity and stability.
      3. Mechanisms of Action L-Asparaginase exerts its anti-cancer effects by depleting circulating asparagine, an essential amino acid for cancer cell survival. This section delves into the mechanisms of action of L-Asparaginase, including its ability to selectively target cancer cells and induce metabolic stress, leading to cell death. The impact of asparagine deprivation on cancer cell metabolism and survival is also explored.
      4. Therapeutic Applications of L-Asparaginase L-Asparaginase has demonstrated therapeutic efficacy in the treatment of various malignancies, including ALL and certain solid tumors. This section provides an overview of the therapeutic applications of L-Asparaginase, highlighting its use as a first-line treatment in ALL and its potential in other cancer types. The challenges and limitations associated with L-Asparaginase therapy are also discussed.
      5. Clinical Implications and Future Perspectives L-Asparaginase therapy has shown promising results in improving patient outcomes, but it is not without side effects and challenges. This section discusses the clinical implications of L-Asparaginase treatment, including its impact on patient survival, toxicity profile, and the development of resistance. Additionally, the future prospects of L-Asparaginase therapy, such as the development of novel formulations and combination strategies, are explored.
      6. Conclusion L-Asparaginase is a vital enzyme in cancer treatment, particularly in the management of ALL. This research paper has provided a comprehensive analysis of L-Asparaginase, highlighting its biochemical properties, mechanisms of action, therapeutic applications, and clinical implications. Further research on L-Asparaginase and its optimization in cancer therapy will enhance our understanding and pave the way for improved treatments.

    • Unit Definition

      One unit of enzyme catalyzes hydrolyzation of 10 nanomoles of dUTP to dUMP in one hour at 85 Centigrade.

    • Specific Activity

      250IU/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.

    L Asparaginase
  • View Data Sheet

    Name :

    POLR2I Human

    Description:

    Polymerase II Polypeptide I Human Recombinant

    hRPB14.5, RPB9, DNA-directed RNA polymerase II subunit RPB9, DNA-directed RNA polymerase II subunit I, RNA polymerase II 14.5 kDa subunit, RPB14.5.

    Product # :

    ENZ-669

    Price :

    Quantity :

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    Description

    POLR2I Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 148 amino acids (1-125 a.a.) and having a molecular mass of 17.0kDa.POLR2I is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    POLR2I protein solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.2M NaCl, 20% glycerol and 1mM DTT.

    Purity

    Greater than 85% as determined by SDS-PAGE.

    More Info

    • Introduction

      Polymerase II Polypeptide I (POLR2I) is a member of the archaeal RpoM/eukaryotic RPA12/RPB9/RPC11 RNA polymerase family. POLR2I is a subunit of RNA polymerase II, which is a polymerase responsible for synthesizing messenger RNA in eukaryotes. DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the 4 ribonucleoside triphosphates as substrates. In addition POLR2I synthesizes mRNA precursors and numerous functional non-coding RNAs.

    • Synonyms

      hRPB14.5, RPB9, DNA-directed RNA polymerase II subunit RPB9, DNA-directed RNA polymerase II subunit I, RNA polymerase II 14.5 kDa subunit, RPB14.5.

    • 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

      MGSSHHHHHH SSGLVPRGSH MGSMEPDGTY EPGFVGIRFC QECNNMLYPK EDKENRILLY ACRNCDYQQE ADNSCIYVNK ITHEVDELTQ IIADVSQDPT LPRTEDHPCQ KCGHKEAVFF QSHSARAEDA MRLYYVCTAP HCGHRWTE.

    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.

    Polr2I Human
  • View Data Sheet

    Name :

    Carbonic Anhydrase 2 Human

    Description:

    Carbonic Anhydrase 2 Human Recombinant

    Carbonic anhydrase 2, Carbonate dehydratase 2, Carbonic Anhydrase II, CA-II, Carbonic anhydrase C, CAC, CA2, CAII, Car2.

    Product # :

    ENZ-420

    Price :

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    • More Info

    Description

    Carbonic anhydrase 2 Human Recombinant protein produced in E.Coli containing 260 amino acids (1-260) and having a molecular mass of 29.2 kDa. The Carbonic anhydrase 2 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Carbonic Anhydrase 2 protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 1mM DTT, 50mM NaCl and 10% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Biological Activity

    Specific activity is 50-70 nmoles/min/µg and was obtained by measuring the increase in the amount of p-nitrophenol by its esterase activity. Specific activity is defined as the amount of 
    p-nitrophenol that 1ug of enzyme can reduce at 25C for 1 minute.

    More Info

    • Introduction

      The enzyme Carbonic anhydrase II having an accession number of NP_414668 is also called carbonate dehydratase which is part of the enzyme family that catalyses rapid inter-conversion of carbon dioxide & water to bicarbonate, carbonic acid and protons (CO2 + H2O ? HCO3? + H+), a reaction that occurs rather slowly in the absence of a catalyst. The majority of carbonic anhydrases enclose a zinc ion in their active site and therefore is classified as metalloenzymes.
      The most important function of Carbonic anhydrase is known to preserve acid-base balance in blood and other tissues, and to help transport carbon dioxide of tissues. Carbonic anhydrases have been found in all kingdoms of life. Carbonic anhydrase has 3 different classes: alpha, beta and gamma which share very little sequence or structural similarity, thus far they all perform the same function and require a zinc ion at the active site. Mammalian carbonic anhydrase is monomeric and belongs to the alpha class. Plant carbonic anhydrase is dimeric and belongs to the beta class.
      Methane-producing bacteria carbonic anhydrase is trimeric and grows in hot springs which forms the gamma class.

    • Synonyms

      Carbonic anhydrase 2, Carbonate dehydratase 2, Carbonic Anhydrase II, CA-II, Carbonic anhydrase C, CAC, CA2, CAII, Car2.

    • 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

      MSHHWGYGKH NGPEHWHKDF PIAKGERQSP VDIDTHTAKY DPSLKPLSVS YDQATSLRIL NNGHAFNVEF DDSQDKAVLK GGPLDGTYRL IQFHFHWGSL DGQGSEHTVD KKKYAAELHL VHWNTKYGDF GKAVQQPDGL AVLGIFLKVG SAKPGLQKVV DVLDSIKTKG KSADFTNFDP RGLLPESLDY WTYPGSLTTP PLLECVTWIV LKEPISVSSE QVLKFRKLNF NGEGEPEELM VDNWRPAQPL KNRQIKASFK

    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.

    Carbonic Anhydrase 2 Human
  • View Data Sheet

    Name :

    ICOS Human

    Description:

    Inducible T Cell Costimulator 4 Human Recombinant

    Inducible T Cell Costimulator, Activation-Inducible Lymphocyte Immunomediatory Molecule, Inducible T-Cell Costimulator, AILIM, Inducible T-Cell Co-Stimulator, Inducible Costimulator, CD278 Antigen, CD278, CVID1.   

    Product # :

    PRO-2534

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    Description

    ICOS produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 362 amino acids (21-140a.a.) and having a molecular mass of 40.8kDa. (Molecular size on SDS-PAGE will appear at approximately 40-57kDa). ICOS is expressed with an 242 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    ICOS protein solution (0.25mg/ml) contains 20mM MES buffer (pH 5.5), 40% glycerol, 2mM DTT and 1mM EDTA 0.1M NaCl.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      ICOS (inducible T-cell costimulatory) belongs to the CD28 family of immune-assisted stimulatory receptors. ICOS forms homodimers and takes a significant part in immune responses, cell-cell signaling, as well as regulation of cell proliferation. The interaction of B7-H2 / ICOS takes a vital role in T-cell differentiation, T-B cell interaction in addition to humoral immune response is essential for the formation of reproductive centers as well as the production of cytokine IL-4. Moreover, ICOS is more effective in inducing IL-10 production, a cytokine which is important for the inhibitory function of T regulatory cells. The ICOS-B7RP-1 and B7-1 / B7-2-CD28 / CTLA-4 pathways offer a significant second signal which can regulate the inhibition, activation and fine regulation of T-lymphocyte responses. ICOS stimulates the production of Th1 and Th2 cytokines, however it can also participate in the generation of Th2 cells.

    • Synonyms

      Inducible T Cell Costimulator, Activation-Inducible Lymphocyte Immunomediatory Molecule, Inducible T-Cell Costimulator, AILIM, Inducible T-Cell Co-Stimulator, Inducible Costimulator, CD278 Antigen, CD278, CVID1.

    • 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

      ADPEINGSAN YEMFIFHNGG VQILCKYPDI VQQFKMQLLK GGQILCDLTK TKGSGNTVSI KSLKFCHSQL SNNSVSFFLY NLDHSHANYY FCNLSIFDPP PFKVTLTGGY LHIYESQLCC QLKLEPKSCD KTHTCPPCPA PELLGGPSVF LFPPKPKDTL MISRTPEVTC VVVDVSHEDP EVKFNWYVDG VEVHNAKTKP REEQYNSTYR VVSVLTVLHQ DWLNGKEYKC KVSNKALPAP IEKTISKAKG QPREPQVYTL PPSRDELTKN QVSLTCLVKG FYPSDIAVEW ESNGQPENNY KTTPPVLDSD GSFFLYSKLT VDKSRWQQGN VFSCSVMHEA LHNHYTQKSL SLSPGKHHHH
      HH

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

    Icos Human
  • View Data Sheet

    Name :

    NNMT Mouse

    Description:

    Nicotinamide N-Methyltransferase Mouse Recombinant

    Nicotinamide N-methyltransferase , Nnmt, icotinamide N-methyltransferase isoform1.

    Product # :

    ENZ-1037

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    Description

    NNMT Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 288 amino acids (1-264a.a) and having a molecular mass of 32.1kDa.NNMT is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

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

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      NNMT is part of the family of transferases, especially those transferring one-carbon group methyltransferases. NNMT is mostly expressed in the liver, and a lower expression is seen in the kidney, lung, skeletal muscle, placenta and heart. NNMT catalyzes the N-methylation of nicotinamide and other pyridines to form pyridinium ions. This activity is significant for biotransformation of many drugs and xenobiotic compounds. NNMT is accountable for the enzymatic activity which uses S-adenosyl methionine as the methyl donor. NNMT expression is related with tumor stage and DFS time in hepatocellular carcinoma cases. NNMT is a good candidate as a tumor marker of various kinds of cancers. NNMT serum levels have significance in the premature detection and in the management of patients with colorectal cancer.

    • Synonyms

      Nicotinamide N-methyltransferase , Nnmt, icotinamide N-methyltransferase isoform1.

    • 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 MGSHMESGFT SKDTYLSHFN PRDYLEKYYS FGSRHCAENE ILRHLLKNLF KIFCLGAVKG ELLIDIGSGP TIYQLLSACE SFTEIIVSDY TDQNLWELQK WLKKEPGAFD WSPVVTYVCD LEGNRMKGPE KEEKLRRAIK QVLKCDVTQS QPLGGVSLPP ADCLLSTLCL DAACPDLPAY RTALRNLGSL LKPGGFLVMV DALKSSYYMI GEQKFSSLPL GWETVRDAVE EAGYTIEQFE VISQNYSSTT SNNEGLFSLV GRKPGRSE.

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    Nnmt Mouse
  • View Data Sheet

    Name :

    DUSP26 Human

    Description:

    Dual Specificity Phosphatase 26 Human Recombinant

    Dual specificity protein phosphatase 26, Dual specificity phosphatase SKRP3, Low-molecular-mass dual-specificity phosphatase 4, DSP-4, LDP-4, Mitogen-activated protein kinase phosphatase 8, MAP kinase phosphatase 8, MKP-8, Novel amplified gene in thyroid anaplastic cancer, DUSP26, DUSP24, LDP4, MKP8, NATA1, SKRP3, Dual specificity phosphatase 26 (putative).

    Product # :

    ENZ-747

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    Description

    DUSP26 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 234 amino acids (1-211a.a) and having a molecular mass of 26.3kDa.DUSP26 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The DUSP26 solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 10% glycerol and 0.4M Urea.

    Purity

    Greater than 85% as determined by SDS-PAGE.

    More Info

    • Introduction

      Dual Specificity Phosphatase 26 (DUSP26) inhibits MAP kinase p38 by dephosphorylating it and inhibits p38-mediated apoptosis in anaplastic thyroid cancer cells. DUSP26 also induces activation of MAP kinase p38 and c-Jun N-terminal kinase. DUSP26 inactivates MAPK1 and MAPK3 which leads to dephosphorylation of heat shock factor protein 4 and a decrease in its DNA-binding activity.

    • Synonyms

      Dual specificity protein phosphatase 26, Dual specificity phosphatase SKRP3, Low-molecular-mass dual-specificity phosphatase 4, DSP-4, LDP-4, Mitogen-activated protein kinase phosphatase 8, MAP kinase phosphatase 8, MKP-8, Novel amplified gene in thyroid anaplastic cancer, DUSP26, DUSP24, LDP4, MKP8, NATA1, SKRP3, Dual specificity phosphatase 26 (putative).

    • 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 MGSMCPGNWL WASMTFMARF SRSSSRSPVR TRGTLEEMPT VQHPFLNVFE LERLLYTGKT ACNHADEVWP GLYLGDQDMA NNRRELRRLG ITHVLNASHS RWRGTPEAYE GLGIRYLGVE AHDSPAFDMS IHFQTAADFI HRALSQPGGK ILVHCAVGVS RSATLVLAYL MLYHHLTLVE AIKKVKDHRG IIPNRGFLRQ LLALDRRLRQ GLEA.

    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.

    Dusp26 Human
  • View Data Sheet

    Name :

    Enterokinase Bovine His

    Description:

    Enteropeptidase/ Enterokinase Bovine Recombinant His Tag

    Enteropeptidase, EC 3.4.21.9, Enterokinase, Serine protease 7, ENTK, MGC133046.

    Product # :

    ENZ-655

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    Description

    Enterokinase Bovine Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 241 amino acids with a 6 × His at C-terminus and having a molecular mass of 28.0kDa.The Enterokinase Bovine is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Bovine EK is supplied in 50mM Tris-HCl, pH 8.0, 0.5M NaCl and 50% glycerol.

    More Info

    • Introduction

      Enteropeptidase or enterokinase is an enzymeinvolved in human digestion. It is produced by cells in the duodenum wall, and is secreted from duodenum's glands, the crypts of Lieberk?hn, whenever ingested food enters the duodenum from the stomach. Enteropeptidase has the critical job of turning trypsinogen(a zymogen) to trypsin, indirectly activating a number of pancreaticdigestive enzymes.
      Enteropeptidase is a serine proteaseenzyme(EC3.4.21.9). Enteropeptidase is a part of the Chymotrypsin-clan of serine proteases, and is structurally similar to these proteins.

    • Synonyms

      Enteropeptidase, EC 3.4.21.9, Enterokinase, Serine protease 7, ENTK, MGC133046.

    • Physical Appearance

      Sterile liquid solution.

    • Stability

      One year when stored at -20°C. Please avoid freeze-thaw cycles.

    • Unit Definition

      One unit is defined as the amount of enzyme needed to cleave 50ug of fusion protein in 16 hours to 95% completion at 25°C in a buffer containing 25mM Tris-HCl, pH 7.6, 50mM NaCl, and 2mM CaCl2.

    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.

    Enterokinase Bovine His
  • View Data Sheet

    Name :

    PCOLCE Human

    Description:

    Procollagen C-Endopeptidase Enhancer Human Recombinant

    Procollagen C-Endopeptidase Enhancer, Procollagen C-Proteinase Enhancer 1, Type I Procollagen COOH-Terminal Proteinase Enhancer, Type 1 Procollagen C-Proteinase Enhancer Protein, Procollagen COOH-Terminal Proteinase Enhancer 1, PCPE-1, PCPE1, Procollagen, Type 1, COOH-Terminal Proteinase Enhancer, Procollagen C-Endopeptidase Enhancer 1, COOH-Terminal Proteinase Enhancer, Procollagen, Type 1, PCPE, Procollagen C-endopeptidase enhancer 1.

    Product # :

    ENZ-863

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    Description

    PCOLCE Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 447 amino acids (26-449 a.a) and having a molecular mass of 47.9kDa. PCOLCE is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    PCOLCE protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH 8.0) and 10% glycerol.

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Procollagen C-endopeptidase enhancer 1, also known as PCOLCE binds to the C-terminal propeptide of type I procollagen and enhances procollagen C-proteinase activity. In addition, C-terminal processed part of PCPE (CT-PCPE) has a metalloproteinase inhibitory activity. Among the diseases which are associated with PCOLCE: bone fracture & oculopharyngeal muscular dystrophy.

    • Synonyms

      Procollagen C-Endopeptidase Enhancer, Procollagen C-Proteinase Enhancer 1, Type I Procollagen COOH-Terminal Proteinase Enhancer, Type 1 Procollagen C-Proteinase Enhancer Protein, Procollagen COOH-Terminal Proteinase Enhancer 1, PCPE-1, PCPE1, Procollagen, Type 1, COOH-Terminal Proteinase Enhancer, Procollagen C-Endopeptidase Enhancer 1, COOH-Terminal Proteinase Enhancer, Procollagen, Type 1, PCPE, Procollagen C-endopeptidase enhancer 1.

    • Physical Appearance

      Sterile filtered colorless solution.

    • Stability

      Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MGSQTPNYTR PVFLCGGDVK GESGYVASEG FPNLYPPNKE CIWTITVPEG QTVSLSFRVF DLELHPACRY DALEVFAGSG TSGQRLGRFC GTFRPAPLVA PGNQVTLRMT TDEGTGGRGF LLWYSGRATS GTEHQFCGGR LEKAQGTLTT PNWPESDYPP GISCSWHIIA PPDQVIALTF EKFDLEPDTY CRYDSVSVFN GAVSDDSRRL GKFCGDAVPG SISSEGNELL VQFVSDLSVT ADGFSASYKT LPRGTAKEGQ GPGPKRGTEP KVKLPPKSQP PEKTEESPSA PDAPTCPKQC RRTGTLQSNF CASSLVVTAT VKSMVREPGE GLAVTVSLIG AYKTGGLDLP SPPTGASLKF YVPCKQCPPM KKGVSYLLMG QVEENRGPVL PPESFVVLHR PNQDQILTNL SKRKCPSQPV RAAASQD.

    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.

    Pcolce Human
  • View Data Sheet

    Name :

    AASDHPPT Human

    Description:

    Aminoadipate-Semialdehyde Dehydrogenase-Phosphopantetheinyl Transferase Human Recombinant

    L-aminoadipate-semialdehyde dehydrogenase-phosphopantetheinyl transferase, 4'-phosphopantetheinyl transferase, Alpha-aminoadipic semialdehyde dehydrogenase-phosphopantetheinyl transferase, AASD-PPT, LYS5 ortholog, AASDHPPT, LYS2, LYS5, CGI-80, DKFZp566E2346.

    Product # :

    ENZ-008

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    Description

    AASDHPPT Human Recombinant fused with a 21 amino acid His tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 316 amino acids (14-309 a.a.) and having a molecular mass of 36.4kDa. The AASDHPPT is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

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

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      AASDHPPT is a member of the P-Pant transferase superfamily. AASDHPPT catalyzes the post-translational modification of target proteins by phosphopantetheine and can transfer the 4'-phosphopantetheine moiety from coenzyme A to a serine residue of a broad range of acceptors, such as the acyl carrier domain of FASN (in vitro). AASDHPPT is similar to Saccharomyces cerevisiae LYS5, which is required for the activation of the alpha-aminoadipate dehydrogenase in the biosynthetic pathway of lysine. AASDHPPT is found in the heart, skeletal muscle, placenta, testis, brain, pancreas, liver and kidney. It’s been suggested that defects in the human AASDHPPT gene result in pipecolic acidemia.

    • Synonyms

      L-aminoadipate-semialdehyde dehydrogenase-phosphopantetheinyl transferase, 4'-phosphopantetheinyl transferase, Alpha-aminoadipic semialdehyde dehydrogenase-phosphopantetheinyl transferase, AASD-PPT, LYS5 ortholog, AASDHPPT, LYS2, LYS5, CGI-80, DKFZp566E2346.

    • 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 MEGVRWAFSC GTWLPSRAEW LLAVRSIQPE EKERIGQFVF ARDAKAAMAG RLMIRKLVAE KLNIPWNHIR LQRTAKGKPV LAKDSSNPYP NFNFNISHQG DYAVLAAEPE LQVGIDIMKT SFPGRGSIPE FFHIMKRKFT NKEWETIRSF KDEWTQLDMF YRNWALKESF IKAIGVGLGF ELQRLEFDLS PLNLDIGQVY KETRLFLDGE EEKEWAFEES KIDEHHFVAV ALRKPDGSRH QDVPSQDDSK PTQRQFTILN FNDLMSSAVP MTPEDPSFWD CFCFTEEIPI RNGTKS.

    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.

    Aasdhppt Human
  • View Data Sheet

    Name :

    KEL Mouse

    Description:

    Kell Metallo-Endopeptidase Mouse Recombinant

    kell blood group antigen, kell blood group glycoprotein, Kell blood group, Kell blood group glycoprotein homolog, KEL, Kell, CD238 antigen, CD238, ECE3, Kell blood group-metalloendopeptidase, Kell blood group-metalloendopeptidase.

    Product # :

    ENZ-1158

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    Description

    KEL Mouse produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 674 amino acids (49-713 aa) and having a molecular mass of 76.3kDa.KEL is fused to a 9 amino acid His tag at C-terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    The KEL solution (0.25mg/ml) contains 10% Glycerol and Phosphate-Buffered Saline (pH 7.4).

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Kell blood group glycoprotein homolog or KEL, is an enzyme, part of the zinc endopeptidase of the neprilysin (NEP) group of proteins. KEL has a crucial part in the production of the potent bioactive ET-3, which also includes enzymes that are endothelin convertingenzymes (PEX, XCE, DINE &various NEP-like proteins). KEL uses a single disulfide bond to XK, a gated membranal transporter. The Kell antigen system that includes two proteins, is very crucial among blood group systems.

    • Synonyms

      kell blood group antigen, kell blood group glycoprotein, Kell blood group, Kell blood group glycoprotein homolog, KEL, Kell, CD238 antigen, CD238, ECE3, Kell blood group-metalloendopeptidase, Kell blood group-metalloendopeptidase.

    • 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

      ADPIFRNCGP CPCETPVCME LLDHYLASGN RSVAPCTDFF SFACEKANGT SDSFQALTEE NKSRLWRLLE APGSWHLGSG EEKAFQFYNS CMDTDAIEAS GSGPLIQIIE ELGGWNITGN WTSLDFNQNL RLLMSQYGHF PFFRAYLRPH PAPPHTPIIQ IDQPEFDILL QQEQEQKVYA QILREYVTYL NRLGTLLGSN PQEAQQHASW SIVFTSRLFQ FLRPQQQQQA QDKLFHVVTI DELQEMAPAI DWLSCLQAIF TPMSLNSSQT LVVHDLDYLR NMSQLVEEGL LNHRESIQSY MILGLVDTLS PALDTKFQEA RRELIQELRK LKERPPLPAY PRWMKCVEQT GAFFEPTLAA LFVREAFGPS IQSAAMELFA EIKDAVIIRL KKLSWISEET QKEALNKLAQ LQVEMGAPKR AVKPDIATQE YNDIQLGPSF LQSFLSCVRS LRARNVQSFL QPFPYHRWQK SPWEVNAYYS ISDHMVVFPA GLLQPPFFHP GYPRAVNFGA AGSIMAHELL HIFYQLLLPG GCPACDTHVL QEALLCLERH YAAFPLPSIS SFNGSHTLLE NAADIGGVAI AFQAYSKRIV EHTGELTLPN LDLSPYQLFF RSYAQVMCRG LSSQDPQDPH SPPSLRVHGP LSNTPDFAKH FHCPRGTLLN PSARCKLWHH HHHH.

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

    Cd238 Mouse
  • View Data Sheet

    Name :

    GSTA1 Human

    Description:

    Glutathione S-Transferase Alpha-1 Human Recombinant

    GST2, GSTA1-1, GTH1, GSTA-1, GSTAI, GSTA-I, EC 2.5.1.18, Glutathione S-transferase A1, GST HA subunit 1, GST-epsilon, GST class-alpha member 1, GSTA1, MGC131939.

    Product # :

    ENZ-469

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    Description

    GSTA1 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 222 amino acids (1-222 a.a.) and having a molecular mass of 25.6 kDa. The GSTA1 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The GSTA1 solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 1mM DTT and 10% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    Biological Activity

    Specific activity is 35,000 pmol/min/ug, and is defined as the amount of enzyme that conjugate 1.0 u mole of 1-chloro-2,4-dinitrobenzene (CDNB) with reduced glutathione per minute at pH 6.5 at 25°C.

    More Info

    • Introduction

      Membrane-bound & Cytosolic forms of GST are encoded by 2 separate supergene families. These enzymes function in the detoxification of electrophilic compounds, including carcinogens, therapeutic drugs, environmental toxins and products of oxidative stress, by conjugation with glutathione. There are 8 different classes of soluble cytoplasmic mammalian GST: alpha, kappa, mu, omega, pi, sigma, theta and zeta. The GSTA1 is found in a cluster mapped to chromosome 6, and is highly expressed in the liver. GSTA1 protects the cells from reactive oxygen species.

    • Synonyms

      GST2, GSTA1-1, GTH1, GSTA-1, GSTAI, GSTA-I, EC 2.5.1.18, Glutathione S-transferase A1, GST HA subunit 1, GST-epsilon, GST class-alpha member 1, GSTA1, MGC131939.

    • 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

      MAEKPKLHYF NARGRMESTR WLLAAAGVEF EEKFIKSAED LDKLRNDGYL MFQQVPMVEI DGMKLVQTRA ILNYIASKYN LYGKDIKERA LIDMYIEGIA DLGEMILLLP VCPPEEKDAK LALIKEKIKN RYFPAFEKVL KSHGQDYLVG NKLSRADIHL VELLYYVEEL DSSLISSFPL LKALKTRISN LPTVKKFLQP GSPRKPPMDE KSLEEARKIF RF.

    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.

    Gsta1 Human
  • View Data Sheet

    Name :

    QDPR Human

    Description:

    Quinoid Dihydropteridine Reductase Human Recombinant

    Dihydropteridine reductase, HDHPR, Quinoid dihydropteridine reductase, QDPR, DHPR, PKU2, SDR33C1.

    Product # :

    ENZ-163

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    Description

    QDPR Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 267 amino acids (1-244 a.a.) and having a molecular mass of 28.2kDa.QDPR is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    QDPR protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 10% glycerol and 2mM DTT.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      QDPR belongs to the short-chain dehydrogenases/reductase (SDR) family of enzymes. Operating as a homodimer, QDPR has an imperative role in the recycling of tetrahydrobiopterin (BH4), a vital cofactor for the hydroxylation of the aromatic amino acids (tryptophan, tyrosine and phenylalanine). More precisely, QDPR catalyzes the regeneration of BH4 from quinonoid dihydrobiopterin (qBH2), the product generated from the hydroxylation reactions. Mutations in the QDPR gene may lead to phenylketonuria II.

    • Synonyms

      Dihydropteridine reductase, HDHPR, Quinoid dihydropteridine reductase, QDPR, DHPR, PKU2, SDR33C1.

    • 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 MGSMAAAAAA GEARRVLVYG GRGALGSRCV QAFRARNWWV ASVDVVENEE ASASIIVKMT DSFTEQADQV TAEVGKLLGE EKVDAILCVA GGWAGGNAKS KSLFKNCDLM WKQSIWTSTI SSHLATKHLK EGGLLTLAGA KAALDGTPGM IGYGMAKGAV HQLCQSLAGK NSGMPPGAAA IAVLPVTLDT PMNRKSMPEA DFSSWTPLEF LVETFHDWIT GKNRPSSGSL IQVVTTEGRT ELTPAYF.

    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.

    Qdpr Human
  • View Data Sheet

    Name :

    IFNG Mouse

    Description:

    IFN-Gamma Mouse Recombinant

    Immune IFN, type II IFN, T cell IFN, MAF, IFNG, IFG, IFI, IFN-gamma.

    Product # :

    CYT-358

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    Description

    IFN-gamma Mouse Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 134 amino acids and having a molecular mass of 15.6kDa.The IFN-gamma is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Lyophilized from a 0.2µm filtered concentrated (1mg/ml) solution in PBS, pH 7.4 and 5% trehalose.

    Purity

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

    Biological Activity

    The specific activity as determined in a viral resistance assay is < 0.1 ng/ml, corresponding to a specific activity of 10,000,000 IU/mg

     

    More Info

    • Introduction

      IFN-gamma produced by lymphocytes activated by specific antigens or mitogens.
      IFN-gamma, in addition to having antiviral activity, has important immunoregulatory functions, it is a potent activator of macrophages, and has antiproliferative effects on transformed cells and it can potentiate the antiviral and antitumor effects of the type I IFNs.

    • Synonyms

      Immune IFN, type II IFN, T cell IFN, MAF, IFNG, IFG, IFI, IFN-gamma.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized IFN-gamma although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IFN-gamma 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 IFN-gamma in sterile distilled water or 20mM AcOH at concentrations ranging between 0.1mg-0.5mg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      MHGTVIESLE SLNNYFNSSG IDVEEKSLFL DIWRNWQKDG DMKILQSQII SFYLRLFEVL KDNQAISNNI SVIESHLITT FFSNSKAKKD AFMSIAKFEV NNPQVQRQAF NELIRVVHQL LPESSLRKRK RSRC.

    • Background

      What is the molecular weight/Mw of IFNG MOUSE Protein?
      IFNG MOUSE Protein has a total Mw of 15.6kDa.

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

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

      What is the Biological Activity of IFNG MOUSE Protein?
      The specific activity as determined in a viral resistance assay is < 0.1 ng/ml, corresponding to a specific activity of 10,000,000 IU/mg


      What is the amino acid sequence of IFNG MOUSE Protein?
      MHGTVIESLE SLNNYFNSSG IDVEEKSLFL DIWRNWQKDG DMKILQSQII SFYLRLFEVL KDNQAISNNI SVIESHLITT FFSNSKAKKD AFMSIAKFEV NNPQVQRQAF NELIRVVHQL LPESSLRKRK RSRC.

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

      What is the endotoxin level for IFNG MOUSE Protein?
      The endotoxin level is minimal, IFNG MOUSE 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.

    Interferon Gamma Mouse
  • View Data Sheet

    Name :

    UCHL3 Mouse

    Description:

    Ubiquitin Carboxyl-Terminal Esterase L3 Mouse Recombinant

    Ubiquitin carboxyl-terminal hydrolase isozyme L3, UCH-L3, UCHL3, Ubiquitin Carboxyl-Terminal Esterase L3, Ubiquitin thioesterase L3, Uchl3, Ubiquitin carboxyl-terminal esterase L3.

    Product # :

    ENZ-978

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    Description

    UCHL3 Mouse Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 238 amino acids (1-230) and having a molecular mass of 27.2kDa (Molecular size on SDS-PAGE will appear at approximately 28-40kDa).UCHL3 is fused to 8 amino acid His-Tag at C-terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    UCHL3 protein solution (0.5mg/ml) containing Phosphate buffered saline (pH7.4) and 10% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    Biological Activity

    Specific activity is > 9,000 pmol/min/mg, and is defined as the amount of enzyme that hydrolysis 1.0 pmole of ubiquitin-AMC per minute at pH 7.5, at 37°C.

    More Info

    • Introduction

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

    • Synonyms

      Ubiquitin carboxyl-terminal hydrolase isozyme L3, UCH-L3, UCHL3, Ubiquitin Carboxyl-Terminal Esterase L3, Ubiquitin thioesterase L3, Uchl3, Ubiquitin carboxyl-terminal esterase L3.

    • 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

      MEGQRWLPLE ANPEVTNQFL KQLGLHPNWQ FVDVYGMEPE LLSMVPRPVC AVLLLFPITE KYEVFRTEEE EKIKSQGQDV TSSVYFMKQT ISNACGTIGL IHAIANNKDK MHFESGSTLK KFLEESVSMS PEERAKFLEN YDAIRVTHET SAHEGQTEAP SIDEKVDLHF IALVHVDGHL YELDGRKPFP INHGKTSDET LLEDAIEVCK KFMERDPDEL RFNAIALSAA LEHHHHHH.

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

    Uchl3 Mouse
  • View Data Sheet

    Name :

    Carbonic Anhydrase II E.coli

    Description:

    Carbonic Anhydrase II E.coli Recombinant

    Carbonic anhydrase 2, Carbonate dehydratase 2, can, cynT2, yadF, b0126, JW0122, Carbonic Anhydrase II.

    Product # :

    ENZ-373

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    Description

    Carbonic anhydrase II is an E.coli Recombinant protein produced in E.Coli containing 240 amino acids (1-220) and having a molecular mass of 27 kDa. Carbonic anhydrase is expressedwith an amino-terminal hexahistidine tag.The Carbonic anhydrase 2 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The Carbonic Anhydrase 2 enzyme is supplied in 20mM Tris pH-8 and 1mM DTT.

    Purity

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

    More Info

    • Introduction

      The enzyme Carbonic anhydrase II having an accession number of NP_414668 is also called carbonate dehydratase which is part of the enzyme family that catalyses rapid inter-conversion of carbon dioxide & water to bicarbonate, carbonic acid and protons (CO2 + H2O ? HCO3? + H+), a reaction that occurs rather slowly in the absence of a catalyst. The majority of carbonic anhydrases enclose a zinc ion in their active site and therefore is classified as metalloenzymes.
      The most important function of Carbonic anhydrase is known to preserve acid-base balance in blood and other tissues, and to help transport carbon dioxide of tissues. Carbonic anhydrases have been found in all kingdoms of life. Carbonic anhydrase has 3 different classes: alpha, beta and gamma which share very little sequence or structural similarity, thus far they all perform the same function and require a zinc ion at the active site. Mammalian carbonic anhydrase is monomeric and belongs to the alpha class. Plant carbonic anhydrase is dimeric and belongs to the beta class.
      Methane-producing bacteria carbonic anhydrase is trimeric and grows in hot springs which forms the gamma class.

    • Synonyms

      Carbonic anhydrase 2, Carbonate dehydratase 2, can, cynT2, yadF, b0126, JW0122, Carbonic Anhydrase II.

    • 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 MKDIDTLISN NALWSKMLVE EDPGFFEKLAQAQKPRFLWI GCSDSRVPAE RLTGLEPGEL FVHRNVANLV IHTDLNCLSV VQYAVDVLEV EHIIICGHYG CGGVQAAVEN PELGLINNWL HIRDIWFKH SSLLGEMPQE RRLDTLCELN VMEQVYNLGH STIMQSAWKR GQKVTIHGWA YGIHDGLLRD LDVTATNRET LEQRYRHGIS NLKLKHANHK.

    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.

    Carbonic Anhydrase Ii
  • View Data Sheet

    Name :

    MMP14 Human

    Description:

    Matrix Metalloproteinase-14 Recombinant Human

    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-1101

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    Description

    Matrix Metalloproteinase-14 Human Recombinant produced in E.Coli is a single, non- glycosylated polypeptide chain containing 264 amino acids and having a molecular mass of 29.6kDa. MMP14 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    MMP14 is supplied as a 0.2 μm filtered solution conteining 20mM Tris-HCl, pH 7.4, 30 % glycerol, 300mM NaCl, 3mM CaCl2 and 10μM ZnCl2.

    Purity

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

    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

      ALASLGSAQS SSFSPEAWLQ QYGYLPPGDL RTHTQRSPQS LSAAIAAMQK FYGLQVTGKA DADTMKAMRR PRCGVPDKFG AEIKANVRRK RYAIQGLKWQ HNEITFCIQN YTPKVGEYAT YEAIRKAFRV WESATPLRFR EVPYAYIREG HEKQADIMIF FAEGFHGDST PFDGEGGFLA HAYFPGPNIG GDTHFDSAEP WTVRNEDLNG NDIFLVAVHE LGHALGLEHS SDPSAIMAPF YQWMDTENFV LPDDDRRGIQ QLYG.

    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 Protein
  • View Data Sheet

    Name :

    POLR3K Human

    Description:

    Polymerase III Polypeptide K Human Recombinant

    DNA-directed RNA polymerase III subunit RPC10, RNA polymerase III subunit C10, DNA-directed RNA polymerase III subunit K, RNA polymerase III 12.5 kDa subunit, RPC12.5, RNA polymerase III subunit C11, HsC11p, RPC11, hRPC11, POLR3K, My010, Polymerase III Polypeptide K, C11, C11-RNP3, hRPC11, RPC10.

    Product # :

    ENZ-806

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    Description

    POLR3K Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 131 amino acids (1-108 a.a) and having a molecular mass of 14.7kDa.POLR3K is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    POLR3K protein solution (0.25mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 50% glycerol, 2mM DTT and 2mM EDTA.

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Polymerase III Polypeptide K, known as PORL3K, is a small vital subunit of RNA polymerase III. The carboxy-terminal domain of PORL3K owns a sequence which is very similar to the carboxy-terminal domain of an RNA polymerase II elongation factor. PORL3K takes part in sensing and limiting infection by intracellular bacteria and DNA viruses. PORL3K is also plays a role as nuclear and cytosolic DNA sensor which takes part in the innate immune response.

    • Synonyms

      DNA-directed RNA polymerase III subunit RPC10, RNA polymerase III subunit C10, DNA-directed RNA polymerase III subunit K, RNA polymerase III 12.5 kDa subunit, RPC12.5, RNA polymerase III subunit C11, HsC11p, RPC11, hRPC11, POLR3K, My010, Polymerase III Polypeptide K, C11, C11-RNP3, hRPC11, RPC10.

    • 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 MGSMLLFCPG CGNGLIVEEG QRCHRFACNT CPYVHNITRK VTNRKYPKLK EVDDVLGGAA AWENVDSTAE SCPKCEHPRA YFMQLQTRSA DEPMTTFYKC CNAQCGHRWR D.

    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.

    Polr3K Human
  • View Data Sheet

    Name :

    DCPS Human

    Description:

    Decapping Enzyme, Scavenger Human Recombinant

    Scavenger mRNA-decapping enzyme DcpS, DCS-1, Hint-related 7meGMP-directed hydrolase, Histidine triad protein member 5, HINT-5, DCPS, DCS1, HINT5, HSPC015, HSL1.

    Product # :

    ENZ-159

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    Description

    DCPS Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 357 amino acids (1-337 a.a.) and having a molecular mass of 40.7kDa.DCPS is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    DCPS protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH8.0), 20% glycerol and 1mM DTT.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    More Info

    • Introduction

      Scavenger mRNA-decapping enzyme (DCPS) is a member of the HIT family. DCPS is required for the complete degradation of mRNAs, both in normal mRNA turnover and in nonsense-mediated mRNA decay. It was shown that DCPS hydrolyzes the residual m7GpppN cap structure after the complete 3'–5' degradation of the mRNA by the exosome. Furthermore, DCPS releases m7GMP and is incapable of cleaving cap structures attached to a long RNA chain.

    • Synonyms

      Scavenger mRNA-decapping enzyme DcpS, DCS-1, Hint-related 7meGMP-directed hydrolase, Histidine triad protein member 5, HINT-5, DCPS, DCS1, HINT5, HSPC015, HSL1.

    • 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 MADAAPQLGK RKRELDVEEA HAASTEEKEA GVGNGTCAPV RLPFSGFRLQ KVLRESARDK IIFLHGKVNE ASGDGDGEDA VVILEKTPFQ VEQVAQLLTG SPELQLQFSN DIYSTYHLFP PRQLNDVKTT VVYPATEKHL QKYLRQDLRL IRETGDDYRN ITLPHLESQS LSIQWVYNIL DKKAEADRIV FENPDPSDGF VLIPDLKWNQ QQLDDLYLIA ICHRRGIRSL RDLTPEHLPL LRNILHQGQE AILQRYRMKG DHLRVYLHYL PSYYHLHVHF TALGFEAPGS GVERAHLLAE VIENLECDPR HYQQRTLTFA LRADDPLLKL LQEAQQS.

    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.

    Dcps Human
  • View Data Sheet

    Name :

    PHOSPHO1 Human

    Description:

    Phosphatase Orphan-1 Human Recombinant

    Phosphoethanolamine/phosphocholine phosphatase, Phosphatase, Orphan 1, EC 3.1.3.75, Phospho1.

    Product # :

    ENZ-363

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    Description

    Human Phospho1 Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 295 amino acids and having a molecular mass of 31.3 kDa. The Human Phospho1 is fused to a 14 aa His tag at N-Terminus. Human Phosphocholine Phosphatase is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Filtered (0.4µm) and lyophilized from 0.5mg/ml in 30mM acetate buffer pH-4.

    Purity

    Greater than 95% as determined by SDS-PAGE.

    More Info

    • Introduction

      PHOSPHO1 is involved in mineralization process & plays a role in bone and cartilage matrix mineralization.
      PHOSPHO1 is expressed at sites of mineralization in bone and cartilage. Highly expressed in osteoblast cell line SaOS-2 which produces a mineralized matrix.
      Orphan-1 is collagen type -2 is specific for cartilaginous tissues. Orphan1 is essential for the normal embryonic development of the skeleton, for linear growth and for the ability of cartilage to resist compressive forces.
      Phosphoethanolamine (2-O3POCH2CH2NH3) is a key intermediate in the formation of cephalins, it is formed in liver and brain by phosphorylation of ethanolamine.
      PHOSPHO2 and PHOSPHO1 suggest subtle differences in the charge distributions around the putative substrate entry site and in the location of potential H-bond donors.
      PHOSPHO1 exhibits high specific phosphoethanolamine and phosphocholine phosphatase activities PHOSPHO1 is a phosphatase enzyme for which expression is upregulated in mineralizing cells. PHOSPHO1 has been implicated in the generation of Pi for matrix mineralization, a process central to skeletal development. PHOSPHO1 is a member of the haloacid dehalogenase (HAD) superfamily of Mg2+-dependent hydrolases. PHOSPHO1 exhibits high specific activities toward phosphoethanolamine (PEA) and phosphocholine (PCho).

    • Synonyms

      Phosphoethanolamine/phosphocholine phosphatase, Phosphatase, Orphan 1, EC 3.1.3.75, Phospho1.

    • Physical Appearance

      Filtered lyophilized (freeze-dried) powder.

    • Stability

      Store lyophilized protein at -20°C. Aliquot the product after reconstitution to avoid repeated freezing/thawing cycles. Reconstituted protein can be stored at 4°C for a limited period of time.

    • Solubility

      It is recommended to add 0.1M Acetate buffer pH4 to prepare a working stock solution of approximately 0.5mg/ml and let the lyophilized pellet dissolve completely. For conversion into higher pH value, we recommend intensive dilution by relevant buffer to a concentration of 10µg/ml. In higher concentrations the solubility of this protein is limited. Product is not sterile! Please filter the product by an appropriate sterile filter before using it in the cell culture.

    • Amino Acid Sequence

      MRGSHHHHHH GMASMSGCFP VSGLRCLSRD GRMAAQGAPR FLLTFDFDET IVDENSDDSI VRAAPGQRLP ESLRATYREG FYNEYMQRVF KYLGEQGVRP RDLSAIYEAI PLSPGMSDLL QFVAKQGACF EVILISDANT FGVESSLRAA GHHSLFRRIL SNPSGPDARG LLALRPFHTH SCARCPANMC KHKVLSDYLR ERAHDGVHFE RLFYVGDGAN DFCPMGLLAG GDVAFPRRGY PMHRLIQEAQ KAEPSSFRAS VVPWETAADV RLHLQQVLKSC.

    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.

    Phospho1 Human
  • View Data Sheet

    Name :

    PHOSPHO2 Human

    Description:

    Phosphatase Orphan-2 Human Recombinant

    Pyridoxal phosphate phosphatase PHOSPHO2, PHOSPHO2.

    Product # :

    ENZ-231

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    Description

    PHOSPHO2 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 265 amino acids (1-241) and having a molecular mass of 30.3kDa.PHOSPHO2 is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The PHOSPHO2 solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 1mM DTT, 10% glycerol and 0.1M NaCl.

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Pyridoxal phosphate phosphatase PHOSPHO2, orphan 2 (PHOSPHO2) is a member of the haloacid dehalogenase (HAD) superfamily. Phosphatase has an elevated activity toward phosphoethanolamine (PEA) and phosphocholine (PCho). PHOSPHO 1, a phosphoethanolamine/phosphocholine phosphatase, is upregulated in mineralizing cells and is believed to be implicated in the production of inorganic phosphate for bone mineralization. PHOSPHO2 is a recognized phosphatase sharing a 42% sequence identity with PHOSPHO1. PHOSPHO1 and PHOSPHO2 are especially similar, however surprisingly recombinant PHOSPHO2 hydrolyses phosphoethanolamine and phosphocholine comparatively inadequately.

    • Synonyms

      Pyridoxal phosphate phosphatase PHOSPHO2, PHOSPHO2.

    • 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 MGSHMKILLV FDFDNTIIDD NSDTWIVQCA PNKKLPIELR DSYRKGFWTE FMGRVFKYLG DKGVREHEMK RAVTSLPFTP GMVELFNFIR KNKDKFDCII ISDSNSVFID WVLEAASFHD IFDKVFTNPA AFNSNGHLTV ENYHTHSCNR CPKNLCKKVV
      LIEFVDKQLQ QGVNYTQIVY IGDGGNDVCP VTFLKNDDVA MPRKGYTLQK TLSRMSQNLE PMEYSVVVWS SGVDIISHLQ FLIKD.

    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.

    Phospho2 Human
  • View Data Sheet

    Name :

    ASRGL1 Human

    Description:

    ASRGL1 Human Recombinant

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

    Product # :

    ENZ-837

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    Description

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

    Source

    Escherichia Coli.

    Formulation

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

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

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

    • Synonyms

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

    • Physical Appearance

      Sterile Filtered colorless solution.

    • Stability

      Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.

    • Amino Acid Sequence

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

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

    Asrgl1 Human
  • View Data Sheet

    Name :

    CHST10 Human

    Description:

    Carbohydrate Sulfotransferase 10 Human Recombinant

    Carbohydrate Sulfotransferase 10, HNK1ST, HNK-1 Sulfotransferase,HuHNK-1ST, HNK-1ST, EC 2.8.2.-, EC 2.8.2, CHST10.

    Product # :

    ENZ-894

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    Description

    CHST10 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 350 amino acids (28-356 a.a) and having a molecular mass of 41.2kDa.CHST10 is fused to a 21 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    CHST10 protein solution (0.5mg/ml) containing 20mM Tris-HCl (pH8.0) and 10% glycerol.

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Carbohydrate Sulfotransferase 10, also known as CHST10 is a member of the sulfotransferase 2 family. CHST10 was first recognized as a sulfotransferase which acts on the human natural killer-1 (HNK-1) glycan. Furthermore, CHST10 is a carbohydrate involved in neurodevelopment as well as synaptic plasticity.

    • Synonyms

      Carbohydrate Sulfotransferase 10, HNK1ST, HNK-1 Sulfotransferase,HuHNK-1ST, HNK-1ST, EC 2.8.2.-, EC 2.8.2, CHST10.

    • 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 MTFKDPDVYS AKQEFLFLTT MPEVRKLPEE KHIPEELKPT GKELPDSQLV QPLVYMERLE LIRNVCRDDA LKNLSHTPVS KFVLDRIFVC DKHKILFCQT PKVGNTQWKK VLIVLNGAFS SIEEIPENVV HDHEKNGLPR LSSFSDAEIQ KRLKTYFKFF IVRDPFERLI SAFKDKFVHN PRFEPWYRHE IAPGIIRKYR RNRTETRGIQ FEDFVRYLGD PNHRWLDLQF GDHIIHWVTY VELCAPCEIM YSVIGHHETL EDDAPYILKE AGIDHLVSYP TIPPGITVYN RTKVEHYFLG ISKRDIRRLY ARFEGDFKLF GYQKPDFLLN.

    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.

    Chst10 Human
  • View Data Sheet

    Name :

    PRMT1 Human

    Description:

    Protein Arginine Methyltransferase 1 Human Recombinant

    ANM1, HCP1, HRMT1L2, IR1B4, INF receptor 1-bound protein 4, EC 2.1.1, Protein arginine N-methyltransferase 1, PRMT1, HMT2.

    Product # :

    ENZ-364

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    Description

    PRMT1 Human Recombinant (a.a. 1-353) fused with His-MBP tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 750 amino acids and having a molecular mass of 84 kDa.The PRMT1 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The PRMT1 solution contains 40mM Tris-HCl pH 8.0, 100mM NaCl, 4mM MgCl2, 2mM DTT & 40% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      PRMT1 Methylates (mono & asymmetric dimethylation) the guanidino nitrogens of arginyl residues present in a glycine and arginine-rich domain (may methylate HNRNPA1 and histones). Methylates SUPT5H.
      The PRMT1 protein functions as a histone methyltransferase specific for H4.
      PRMT1 is an essential factor in oncogenesis and is a potential novel therapeutic target in cancer.
      PRMT1-mediated methylation serves as a positive modulator of IR/IRS-1/PI3K pathway and glucose uptake in skeletal muscle cells.
      CAF1 is a new regulator of PRMT1-dependent arginine methylation.
      PRMT1 arginine-methylates MRE11 therefore it regulates the activity of MRE11-RAD50-NBS1 complex during the intra-S-phase DNA damage checkpoint response.
      PRMT1 plays a post-translationally part in regulating the transcriptional activity.
      PRMT1 is found predominantly in the cytoplasma though a fraction of PRMT1 is located in the nucleus.

    • Synonyms

      ANM1, HCP1, HRMT1L2, IR1B4, INF receptor 1-bound protein 4, EC 2.1.1, Protein arginine N-methyltransferase 1, PRMT1, HMT2.

    • 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

      MHHHHHHMKI EEGKLVIWIN GDKGYNGLAE VGKKFEKDTG IKVTVEHPDK LEEKFPQVAA TGDGPDIIFW AHDRFGGYAQ SGLLAEITPD KAFQDKLYPF TWDAVRYNGK LIAYPIAVEA LSLIYNKDLL PNPPKTWEEI PALDKELKAK GKSALMFNLQ EPYFTWPLIA ADGGYAFKYE NGKYDIKDVG VDNAGAKAGL TFLVDLIKNK HMNADTDYSI AEAAFNKGET AMTINGPWAW SNIDTSKVNY GVTVLPTFKG QPSKPFVGVL SAGINAASPN KELAKEFLEN YLLTDEGLEA VNKDKPLGAV ALKSYEEELA KDPRIAATME NAQKGEIMPN IPQMSAFWYA VRTAVINAAS GRQTVDEALK DAQTNSSSNN NNNNNNNNLG IEGRGSHMAA AEAANCIMEV SCGQAESSEKPNAEDMTSKD YYFDSYAHFG IHEEMLKDEV RTLTYRNSMF HNRHLFKDKV VLDVGSGTGI LCMFAAKAGA RKVIGIECSS ISDYAVKIVK ANKLDHVVTI IKGKVEEVEL PVEKVDIIIS EWMGYCLFYE SMLNTVLYAR DKWLAPDGLI FPDRATLYVT AIEDRQYKDY KIHWWENVYG FDMSCIKDVA IKEPLVDVVD PKQLVTNACL IKEVDIYTVK VEDLTFTSPF CLQVKRNDYV HALVAYFNIE FTRCHKRTGF STSPESPYTH WKQTVFYMED YLTVKTGEEI FGTIGMRPNA KNNRDLDFTI DLDFKGQLCE LSCSTDYRMR.

    • Unit Definition

      One unit will transfer 1pmol of methyl group to synthetic peptide of histone H4 for 10 minutes at 37°C.

    • Specific Activity

      10,000 Units/ml.

    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.

    Prmt1 Human
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