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Search results

1000 results found for “enterokinase”

Name

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  • View Data Sheet

    Name :

    CK2a Zea Mays

    Description:

    Casein Kinase 2 alpha Zea Mays Recombinant

    Casein kinase II subunit alpha, EC 2.7.11.1, CK II, CK2-alpha, CK2?.

    Product # :

    PKA-210

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    Description

    Casein Kinase 2 alpha Zea Mays Recombinant is a non-glycosylated polypeptide having a molecular mass of 39.2 kDa. Casein Kinase 2 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    CK2a is supplied in 50% glycerol.

    Purity

    Greater than 99% as determined by SDS-PAGE.

    More Info

    • Introduction

      The Casein kinase 2 (EC2.7.11.1) is a serine/threonine-selective protein kinasethat is a tetramer of two alpha subunits and two beta subunits. The alpha subunits have the catalytic kinase domain. Casein kinase 2 has been implicated in cell cyclecontrol, DNA repair, regulation of the circadian rhythmand other cellular processes.
      Casein kinase 2 activity has been reported to be activated following Wnt signaling pathwayactivation. A Pertussis toxin-sensitive G proteinand Disheveled appear to be an intermediary between Wnt-mediated activation of the Frizzled receptor and activation of casein kinase 2.

    • Synonyms

      Casein kinase II subunit alpha, EC 2.7.11.1, CK II, CK2-alpha, CK2?.

    • 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.

    • Unit Definition

      No protease activity detectable, specific activity > 1U/mg (1U = 1µmol/min at 37 degree C) using the synthetic peptide RRRDDDSDDD.

    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.

    Ck2A Zea Mays
  • View Data Sheet

    Name :

    PCK1 Human

    Description:

    Phosphoenolpyruvate Carboxykinase 1 Human Recombinant

    Phosphoenolpyruvate carboxykinase 1 (soluble), PEPCK-C, PEPCK1, PEP carboxykinase, phosphoenolpyruvate carboxykinase cytosolic [GTP], EC 4.1.1.32.

    Product # :

    PKA-018

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    Description

    PCK1 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 646 amino acids (1-622) and having a molecular mass of 71.7kDa.PCK1 is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    The PCK1 solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 100mM NaCl, 1mM DTT and 10% glycerol.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    More Info

    • Introduction

      PCK1 is a central regulating point for the regulation of gluconeogenesis. PCK1 has a vital part in this process by stimulating hepatic glucose production. The expression of PCK1 is controlled by cAMP, glucocorticoids, diet etc. Modulation of the signals controlling PCK1 levels offers a possible therapeutic tactic to the treatment of Diabetes and subsequently obesity.

    • Synonyms

      Phosphoenolpyruvate carboxykinase 1 (soluble), PEPCK-C, PEPCK1, PEP carboxykinase, phosphoenolpyruvate carboxykinase cytosolic [GTP], EC 4.1.1.32.

    • 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 MGSHMPPQLQ NGLNLSAKVV QGSLDSLPQA VREFLENNAE LCQPDHIHIC DGSEEENGRL LGQMEEEGIL RRLKKYDNCW LALTDPRDVA RIESKTVIVT QEQRDTVPIP KTGLSQLGRW MSEEDFEKAF NARFPGCMKG RTMYVIPFSM GPLGSPLSKI GIELTDSPYV VASMRIMTRM GTPVLEALGD GEFVKCLHSV GCPLPLQKPL VNNWPCNPEL TLIAHLPDRR EIISFGSGYG GNSLLGKKCF ALRMASRLAK EEGWLAEHML VLGITNPEGE KKYLAAAFPS ACGKTNLAMM NPSLPGWKVE CVGDDIAWMK FDAQGHLRAI NPENGFFGVA PGTSVKTNPN AIKTIQKNTI FTNVAETSDG GVYWEGIDEP LASGVTITSW KNKEWSSEDG EPCAHPNSRF CTPASQCPII DAAWESPEGV PIEGIIFGGR RPAGVPLVYE ALSWQHGVFV GAAMRSEATA AAEHKGKIIM HDPFAMRPFF GYNFGKYLAH WLSMAQHPAA KLPKIFHVNW FRKDKEGKFL WPGFGENSRV LEWMFNRIDG KASTKLTPIG YIPKEDALNL KGLGHINMME LFSISKEFWE KEVEDIEKYL EDQVNADLPC EIEREILALK QRISQM.

    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.

    Pck1 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 :

    MAPK1 Human, Active

    Description:

    Mitogen-Activated Protein Kinase 1 Human Recombinant, Active

    Mitogen-activated protein kinase 1, EC 2.7.11.24, Extracellular signal-regulated kinase 2, ERK-2, Mitogen-activated protein kinase 2, MAP kinase 2, MAPK 2, p42-MAPK, ERT1, ERK, p38, p40, p41, ERK2, MAPK2, PRKM1, PRKM2, P42MAPK, p41mapk.

    Product # :

    PKA-214

    Price :

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    Description

    MAPK1 Human Recombinant is a non-glycosylated full length chain containing amino acids Met1-Ser360 and having a calculated molecular mass of 41,762 Dalton. MAPK1 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    MAPK1 protein solution is supplied in 50mM HEPES pH 7.5, 100mM NaCl, 5mM DTT and 20% glycerol.

    Purity

    The purity is greater than 95%.

    More Info

    • Introduction

      Mitogen-activated protein kinase 1 (MAPK1) is also known as "extracellular signal-regulated kinase 2" (ERK2). Two similar (85% sequence identity) protein kinases were originally called ERK1 and ERK2. They were found during a search for protein kinases that are rapidly phosphorylated after activation of cell surface tyrosine kinasessuch as the epidermal growth factor receptor. Phosphorylation of ERKs leads to the activation of their kinase activity.
      The molecular events linking cell surface receptors to activation of ERKs are complex. It was found that RasGTP-binding proteins are involved in the activation of ERKs. Another protein kinase, Raf-1, was shown to phosphorylate a "MAPK kinase", thus qualifying as a "MAPK kinase kinase". The MAPK kinase was named "MAPK/ERK kinase" (MEK).
      Receptor-linked tyrosine kinases, Ras, Raf, MEK and MAPK could be fitted into a signaling cascade linking an extracellular signal to MAPK activation.
      Transgenic gene knockoutmice lacking MAPK1 have major defects in early development.

    • Synonyms

      Mitogen-activated protein kinase 1, EC 2.7.11.24, Extracellular signal-regulated kinase 2, ERK-2, Mitogen-activated protein kinase 2, MAP kinase 2, MAPK 2, p42-MAPK, ERT1, ERK, p38, p40, p41, ERK2, MAPK2, PRKM1, PRKM2, P42MAPK, p41mapk.

    • Physical Appearance

      Sterile Filtered clear solution.

    • Stability

      Store vial at -20°C to -80°C.Avoid multiple freeze-thaw cycles.

    • Amino Acid Sequence

      maaaaaagag pemvrgqvfd vgprytnlsy igegaygmvc saydnvnkvr vaikkispfe hqtycqrtlr eikillrfrh eniigindii raptieqmkd vyivqdlmet dlykllktqh lsndhicyfl yqilrglkyi hsanvlhrdl kpsnlllntt cdlkicdfgl arvadpdhdh tgflteyvat rwyrapeiml nskgytksid iwsvgcilae mlsnrpifpg khyldqlnhi lgilgspsqe dlnciinlka rnyllslphk nkvpwnrlfp nadskaldll dkmltfnphk rieveqalah pyleqyydps depiaeapfk fdmelddlpk eklkelifee tarfqpgyrs.

    • Specific Activity

      386 pmol/µgxmin ATP-KM: 1.7µM

    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.

    Mapk1 Human Active
  • View Data Sheet

    Name :

    ELANE Mouse

    Description:

    Elastase-2 Mouse Recombinant

    Elane, Ela2, F430011M15Rik, NE, Neutrophil elastase, Elastase-2, Leukocyte elastase.

    Product # :

    ENZ-1105

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    Description

    ELANE Mouse produced in Sf9 Insect cells is a single, glycosylated polypeptide chain (27-265a.a.) fused to a 6 aa His Tag at C-terminus containing 245 amino acids and having a molecular mass of 26.8kDa.ELANE shows multiple bands between 28-40kDa on SDS-PAGE, reducing conditions and purified by proprietary chromatographic techniques.

    Source

    Sf9, Insect cells.

    Formulation

    ELANE protein solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 30% Glycerol and 0.1M NaCl.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Elastase-2 (ELANE) is a serine protease that belongs to the chymotrypsin family. ELANE breaks down elastin, an elastic fiber together with collagen and controls the mechanical properties of connective tissue. The neutrophil form breaks down the Outer membrane protein A (OmpA) of E. coli and other Gram-negative bacteria. ELANEis inhibited by the acute-phase protein alpha 1-antitrypsin (A1AT), which binds almost irreversibly to the active site of elastase and trypsin.A1AT is usually secreted by the liver cells into the serum. A1AD leads to uninhibited destruction of elastic fiber by elastase.

    • Synonyms

      Elane, Ela2, F430011M15Rik, NE, Neutrophil elastase, Elastase-2, Leukocyte elastase.

    • 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

      SEIVGGRPAR PHAWPFMASL QRRGGHFCGA TLIARNFVMS AAHCVNGLNF RSVQVVLGAH
      DLRRQERTRQ TFSVQRIFEN GFDPSQLLND IVIIQLNGSA TINANVQVAQ LPAQGQGVGD
      RTPCLAMGWG RLGTNRPSPS VLQELNVTVV TNMCRRRVNV CTLVPRRQAG ICFGDSGGPL
      VCNNLVQGID SFIRGGCGSG LYPDAFAPVA EFADWINSII RSHNDHLLTH PKDREGRTNH HHHHH

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    Elastase 2 Mouse
  • View Data Sheet

    Name :

    CKBB Human His

    Description:

    Creatine Kinase Brain Human Recombinant, His Tag

    EC 2.7.3.2, Creatine kinase B chain, Creatine kinase B type, CKB, CKBBB, B-CK, Creatine Kinase Brain.

    Product # :

    CKI-274

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    Description

    CKBB Recombinant Human produced in E.Coli is a single, non-glycosylated polypeptide chain containing 401 amino acids (1-381 a.a.) and having a molecular mass of 44.8 kDa. The CKB is fused to 20 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    CKBB Human solution containing 20mM Trsi pH-8, 1mM DTT, & 10% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      CKB is a cytoplasmic enzyme that takes part in energy homeostasis. CKB enzyme reversibly catalyzes the transfer of phosphate among ATP and various phosphogens such as creatine phosphate. CKB functions as a homodimer in the brain as well as in different tissues, and as a heterodimer with a similar muscle isozyme in heart. Creatine kinases supply the energy of phosphate hydrolysis essential to drive the normal role of many cellular systems including muscle, tumor and cancer cells.

    • Synonyms

      EC 2.7.3.2, Creatine kinase B chain, Creatine kinase B type, CKB, CKBBB, B-CK, Creatine Kinase Brain.

    • Physical Appearance

      Sterile filtered colorless solution.

    • Stability

      CKBB Human although stable at 4°C for 1 week, should be stored below -18°C. Please prevent freeze thaw cycles.

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH 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.

    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.

    Ckb Human
  • View Data Sheet

    Name :

    OmpA S.Enteritidis

    Description:

    Salmonella Enteritidis Outer Membrane Protein-A Recombinant

    Outer Membrane Protein-A, OmpA.

    Product # :

    PRO-1918

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    Description

    The Recombinant Salmonella Enteritidis Outer Membrane Protein A, E.Coli derived, 330 amino acids, contains the ompA immunodominant regions. The protein is fused to a His tag at C-terminal and purified by standard chromatography techniques.

    Source

    Escherichia Coli.

    Formulation

    PBS and 25MmM Arginine.

    Purity

    Protein is >95% pure as determined by 10% PAGE (coomassie staining).

    More Info

    • Introduction

      The OmpA protein is one of the main outer-membrane proteins of a large array of Gram-negative bacteria such as A.salmonicida, Shigella dysenteriae and E.coli.OmpA’s major physiological functions include maintenance of the structural integrity and morphology of the cells and porin activity, as well as a role in conjugation and bacteriophage binding.Achromogenic atypical Aeromonas salmonicida is the causative agent of goldfish ulcer disease.Virulence of this bacterium is associated with the production of a paracrystalline outer membrane A-layer protein.The species specific structural gene for the monomeric form of A-protein was cloned into a pET-3d plasmid in order to express and produce a recombinant form of the protein in E.coli BL21(DE3). The induced protein was isolated from inclusion bodies by a simple solubilization-renaturation procedure and purified by ion exchange chromatography on Q-Sepharose to over 95% pure monomeric protein.Recombinant A-protein was compared by biochemical, immunological and molecular methods with the A-protein isolated from atypical A.salmonicida bacterial cells by the glycine and the membrane extraction methods.

    • Synonyms

      Outer Membrane Protein-A, OmpA.

    • Physical Appearance

      Sterile Filtered clear solution.

    • Stability

      OmpA S.Enteritidis Recombinant although stable at 4°C for 1 week, should be stored below -18°C. Please prevent freeze thaw cycles.

    • Applications

      Immunoassay. Outer membrane protein A (ompA) of S. Enteritidis is a protein directly exposing to outsides of this organism, In hens, the production of antibodies against outer membrane protein A (ompA) during the infection has been demonstrated by inoculating both the complete bacterium and expressed protein produced from ompA DNA vaccine. Vaccination by ompA protein to hens is a poteintail tool to control S. enteritidis contaminated eggs into market, and prevent human foodborne disease from eggs.

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    Ompa Senteritidis
  • View Data Sheet

    Name :

    ITPK1 Human

    Description:

    Inositol-Tetrakisphosphate 1-Kinase Human Recombinant

    Inositol-tetrakisphosphate 1-kinase, Inositol 1,3,4-trisphosphate 5/6-kinase, Inositol-triphosphate 5/6-kinase, Ins(1,3,4)P(3) 5/6-kinase, ITPK1, ITRPK1.

    Product # :

    PKA-040

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    Description

    ITPK1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 438 amino acids (1-414 a.a) and having a molecular mass of 48.1kDa.ITPK1 is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    ITPK1 protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.1M NaCl, 10% glycerol and 1mM EDTA.

    Purity

    Greater than 95% as determined by SDS-PAGE.

    More Info

    • Introduction

      Inositol-tetrakisphosphate 1-kinase (ITPK1) is a 414 amino acid monomer which is a member of the ITPK1 family and exists as 2 alternatively spliced isoforms. ITPK1 highest levels are found in the brain, followed by the heart, skeletal muscle, kidney, pancreas, liver, placenta and lung. ITPK1 is comprised of one ATP-grasp domain and has been shown to phosphorylate various inositol polyphosphates and modify TNFa induced apoptosis.

    • Synonyms

      Inositol-tetrakisphosphate 1-kinase, Inositol 1,3,4-trisphosphate 5/6-kinase, Inositol-triphosphate 5/6-kinase, Ins(1,3,4)P(3) 5/6-kinase, ITPK1, ITRPK1.

    • 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 MGSHMQTFLK GKRVGYWLSE KKIKKLNFQA FAELCRKRGM EVVQLNLSRP IEEQGPLDVI IHKLTDVILE ADQNDSQSLE LVHRFQEYID AHPETIVLDP LPAIRTLLDR SKSYELIRKI EAYMEDDRIC SPPFMELTSL CGDDTMRLLE KNGLTFPFIC KTRVAHGTNS HEMAIVFNQE GLNAIQPPCV VQNFINHNAV LYKVFVVGES YTVVQRPSLK NFSAGTSDRE SIFFNSHNVS KPESSSVLTE LDKIEGVFER PSDEVIRELS RALRQALGVS LFGIDIIINN QTGQHAVIDI NAFPGYEGVS EFFTDLLNHI ATVLQGQSTA MAATGDVALL RHSKLLAEPA GGLVGERTCS ASPGCCGSMM GQDAPWKAEA DAGGTAKLPH QRLGCNAGVS PSFQQHCVAS LATKASSQ.

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    Itpk1 Human
  • 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.

    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. 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.

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    Protease Enzyme
  • View Data Sheet

    Name :

    LACTB E.Coli, His Active

    Description:

    Beta Lactamase E.Coli Recombinant, His Active

    Beta-lactamase, Cephalosporinase, ampC, ampA, b4150, JW4111.

    Product # :

    ENZ-1033

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    Description

    LACTB produced in E.Coli is a single, non-glycosylated polypeptide chain containing 379 amino acids (20-377 a.a) and having a molecular mass of 41.8kDa. LACTB is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

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

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Biological Activity

    Specific activity is >700 units/mg, in which One unit will hydrolyze 1.0umole of Nitrocefin per minute at pH 7.0 at 37°C.

    More Info

    • Introduction

      Beta-lactamase is a type of enzyme (EC 3.5.2.6) produced by some bacteria that is responsible for their resistance to beta-lactam antibiotics like penicillins, cephalosporins, cephamycins and carbapenems. These antibiotics have a common element in their molecular structure: a four-atom ring known as a beta-lactam. The lactamase enzyme breaks that ring open, deactivating the molecule's antibacterial properties.

    • Synonyms

      Beta-lactamase, Cephalosporinase, ampC, ampA, b4150, JW4111.

    • 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 MAPQQINDIV HRTITPLIEQ QKIPGMAVAV IYQGKPYYFT WGYADIAKKQ PVTQQTLFEL GSVSKTFTGV LGGDAIARGE IKLSDPTTKY WPELTAKQWN GITLLHLATY TAGGLPLQVP DEVKSSSDLL RFYQNWQPAW APGTQRLYAN SSIGLFGALA VKPSGLSFEQ AMQTRVFQPL KLNHTWINVP PAEEKNYAWG YREGKAVHVS PGALDAEAYG VKSTIEDMAR WVQSNLKPLD INEKTLQQGI QLAQSRYWQT GDMYQGLGWE MLDWPVNPDS IINGSDNKIA LAARPVKAIT PPTPAVRASW VHKTGATGGF GSYVAFIPEK ELGIVMLANK NYPNPARVDA AWQILNALQ.

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    Lactb Ecoli His Active
  • View Data Sheet

    Name :

    KLK11 Human

    Description:

    Kallikrein-11 Human Recombinant

    Kallikrein-11, hK11, Hippostasin, Serine protease 20, Trypsin-like protease, Kallikrein-11 inactive chain 1, Kallikrein-11 inactive chain 2, KLK11, PRSS20, TLSP, UNQ649/PRO1279, Kallikrein 11.

    Product # :

    ENZ-816

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    Description

    KLK11 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 226 amino acids (54-278 a.a) and having a molecular mass of 24.8kDa.

    Source

    Escherichia Coli.

    Formulation

    KLK11 protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 10% glycerol and 0.4M Urea.

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Kallikreins are a subgroup of serine proteases having various physiological functions. Numerous kallikreins are involved in carcinogenesis. Kallikrein-11 (KLK11) which is a multifunctional protease is 1 of the 15 kallikrein subfamily members found in a cluster on chromosome 19. KLK11 cleaves synthetic peptides after arginine but not lysine residues.

    • Synonyms

      Kallikrein-11, hK11, Hippostasin, Serine protease 20, Trypsin-like protease, Kallikrein-11 inactive chain 1, Kallikrein-11 inactive chain 2, KLK11, PRSS20, TLSP, UNQ649/PRO1279, Kallikrein 11.

    • 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

      MIIKGFECKP HSQPWQAALF EKTRLLCGAT LIAPRWLLTA AHCLKPRYIV HLGQHNLQKE EGCEQTRTAT ESFPHPGFNN SLPNKDHRND IMLVKMASPV SITWAVRPLT LSSRCVTAGT SCLISGWGST SSPQLRLPHT LRCANITIIE HQKCENAYPG NITDTMVCAS VQEGGKDSC GDSGGPLVCN QSLQGIISWG QDPCAITRKP GVYTKVCKYV DWIQET.

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    Klk11 Human
  • View Data Sheet

    Name :

    CSNK2A1 Human, His

    Description:

    Casein Kinase 2 alpha 1 Human Recombinant, His

    Casein kinase II subunit alpha, EC 2.7.11.1, CK II, CK2A1, CKII alpha, CSNK2A1, PKCK2, CSK21.

    Product # :

    PKA-225

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    Description

    CK2A Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain encoding the sequence of 411 amino acids and having a molecular mass of 47.3 kDa.Casein Kinase 2 alpha subunit is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    CSNK2A1 is supplied in 20mM Tris pH-8.0 , 500mM NaCl, 1mM DTT and 50% glycerol.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    More Info

    • Introduction

      The Casein kinase 2 (EC2.7.11.1) is a serine/threonine-selective protein kinasethat is a tetramer of two alpha subunits and two beta subunits. The alpha subunits have the catalytic kinase domain. Casein kinase 2 has been implicated in cell cyclecontrol, DNA repair, regulation of the circadian rhythmand other cellular processes.
      Casein kinase 2 activity has been reported to be activated following Wnt signaling pathwayactivation. A Pertussis toxin-sensitive G proteinand Disheveled appear to be an intermediary between Wnt-mediated activation of the Frizzled receptor and activation of casein kinase 2.
      Mice that lack casein kinase 2 alpha prime have a defect in the morphology of developing sperm.

    • Synonyms

      Casein kinase II subunit alpha, EC 2.7.11.1, CK II, CK2A1, CKII alpha, CSNK2A1, PKCK2, CSK21.

    • Physical Appearance

      Sterile Filtered clear solution.

    • Stability

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

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MSGPVPSRAR VYTDVNTHRP REYWDYESHV VEWGNQDDYQLVRKLGRGKY SEVFEAINIT NNEKVVVKIL KPVKKKKIKR EIKILENLRG GPNIITLADI VKDPVSRTPA LVFEHVNNTD FKQLYQTLTD YDIRFYMYEI LKALDYCHSM GIMHRDVKPH NVMIDHEHRK LRLIDWGLAE FYHPGQEYNV RVASRYFKGP ELLVDYQMYD YSLDMWSLGC MLASMIFRKE PFFHGHDNYD QLVRIAKVLG TEDLYDYIDK YNIELDPRFN DILGRHSRKRWERFVHSENQ HLVSPEALDF LDKLLRYDHQ SRLTAREAME HPYFYTVVKD QARMGSSSMP GGSTPVSSAN MMSGISSVPT PSPLGPLAGS PVIAAANPLG MPVPAAAGAQ Q.

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    Csnk2A1 Human His
  • View Data Sheet

    Name :

    SENP8 Human

    Description:

    Sentrin Specific Peptidase Family Member 8 Human Recombinant

    SUMO/sentrin specific peptidase family member 8, DEN1, NEDP1, Protease cysteine 2 (NEDD8 specific), PRSC2, NEDD8-specific protease 1, HsT17512, Deneddylase-1, NEDD8 specific-protease cysteine 2, Sentrin/SUMO-specific protease SENP8.

    Product # :

    ENZ-146

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    Description

    SENP8 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 232 amino acids (1-212) and having a molecular mass of 26.2 kDa.The SENP8 is fused to a 20 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    SENP8 protein 1mg/ml is supplied in 20mM Tris-HCL, pH-8, 0.1M NaCl, 1mM DTT and 10% Glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      SENP8 is a cysteine protease which belongs to the sentrin-specific protease family. SENP8 takes part in processing and deconjugation of the ubiquitin-like protein labeled, neural precursor cell expressed developmentally downregulated 8(NEDD8).

    • Synonyms

      SUMO/sentrin specific peptidase family member 8, DEN1, NEDP1, Protease cysteine 2
      (NEDD8 specific), PRSC2, NEDD8-specific protease 1, HsT17512, Deneddylase-1, NEDD8 specific-protease cysteine 2, Sentrin/SUMO-specific protease SENP8.

    • Physical Appearance

      SENP8 is supplied as a 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 MDPVVLSYMD SLLRQSDVSL LDPPSWLNDH IIGFAFEYFA NSQFHDCSDH VSFISPEVTQ FIKCTSNPAE IAMFLEPLDL PNKRVVFLAI NDNSNQAAGG THWSLLVYLQ DKNSFFHYDS HSRSNSVHAK QVAEKLEAFL GRKGDKLAFV EEKAPAQQNS YDCGMYVICN TEALCQNFFR QQTESLLQLL TPAYITKKRG EWKDLITTLA KK

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    Senp8 Human
  • View Data Sheet

    Name :

    Chitinase Protein

    Description:

    Chitinase Clostridium Paraputrificum Recombinant

    Product # :

    ENZ-031

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    Description

    Chitinase Clostridium Paraputrificum Recombinant fused with a His tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 582 amino acids and having a molecular mass of 64.2kDa. The Chitinase is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Chitinase lyophilized from a 0.2µm filtered concentrated solution in PBS.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Chitinase is a digestive enzyme which breaks down glycosidic bonds in chitin. Due to chitin being a component of the cell walls of fungi and exoskeletal elements of some animals (including worms and arthropods), chitinases are usually found in organisms that either need to remake their own chitin or to dissolve and digest the chitin of fungi or animals. Chitinivorous organisms include many bacteria genuses such as Aeromonas, Bacillus, Vibrio, among others, which may be pathogenic or detritivorous. Chitinase expression is mediated by the NPR1 gene and the salicylic acid pathway, both of which are involved in resisting fungal and insect attack. Human chitinases appear in gastric juices. They are likely to be digestive chitinases, for catabolic activity. Chitinase activity is identified systemically in humans, in the blood, and possibly cartilage. Chitinase has been related to allergies, asthma in particular has been linked to enhanced chitinase expression levels, also dust mites and mold spores which are both chitin covered.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Amino Acid Sequence

      MRGSGSHHHH HHMYYGDWSI WGGQGNFYPK DIPADKLTHL NFAFMDFNSS GELIYCDKDA AIGHPLGNLG VTYGDVNGGI LNAFQVLKSE NPNLKIGVSL GGWSKSGDFS TIAATPSIRA KFVENVMKFI KYTNMDFVDI DWEYPGDYRE PDKTDNINDE GTPNASAGDK ENYILLLQDL KEALNKQGKE LGKVYELSVA LPAGVSKIEK GIDVDKLFNI VDFANIMTYD MAGAWSTTSG HQTALYTNPN APEEYKGLSV DESVKYYISQ GAEREKIVVG AAYYTRGWEQ VSDKGTDPNN PGLFGEAAVV NKDADLSPTP GALNEAPMKN GEGGRAGGVW GYNALDKLKS KYTGLKEYWD DSAKAPYLYN SETGAFFTYD NIRSIQEKAK YVKENNLGGI IGWMASQDAT TNSTKRDELT TATKESLFGK EDLPKYEIKY TENDITCTVT PVKQSWGSGG VLKMSITNNE KLDESGEVLS TVETSAKTVK NMKVYIKTDG IAITGSQYPA GPVTKEGDYY VIDFGKISDG KLMKAGITFT FDLNLDKAIE DTNNIISIEV SQRMYQTSPE FNRQTIWENT NS.

    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.

    Chitinase
  • View Data Sheet

    Name :

    LCAT Human

    Description:

    Lecithin-Cholesterol Acyltransferase Human Recombinant

    Phosphatidylcholine-sterol acyltransferase, Lecithin-cholesterol acyltransferase, Phospholipid-cholesterol acyltransferase, LCAT.

    Product # :

    ENZ-380

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    Description

    LCAT Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 441 amino acids (25-440) which includes a 25 amino acid His Tag fused at N-terminus and having a total molecular mass of 49.8 kDa. LCAT Human Recombinant is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    LCAT protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.4M Urea and 10% glycerol.

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      LCAT is an extracellular cholesterol esterifying enzyme, lecithin-cholesterol acyltransferase. The esterification of cholesterol is required for cholesterol transport. LCAT is a essential enzyme in the extracellular metabolism of plasma lipoproteins.

    • Synonyms

      Phosphatidylcholine-sterol acyltransferase, Lecithin-cholesterol acyltransferase, Phospholipid-cholesterol acyltransferase, LCAT.

    • 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 MGSHMFWLLN VLFPPHTTPK AELSNHTRPV ILVPGCLGNQ LEAKLDKPDV VNWMCYRKTE DFFTIWLDLN MFLPLGVDCW IDNTRVVYNR SSGLVSNAPG VQIRVPGFGK TYSVEYLDSS KLAGYLHTLV QNLVNNGYVR DETVRAAPYD WRLEPGQQEE YYRKLAGLVE EMHAAYGKPV FLIGHSLGCL HLLYFLLRQP QAWKDRFIDG FISLGAPWGG SIKPMLVLAS GDNQGIPIMS SIKLKEEQRI TTTSPWMFPS RMAWPEDHVF ISTPSFNYTG RDFQRFFADL HFEEGWYMWL QSRDLLAGLP APGVEVYCLY GVGLPTPRTY IYDHGFPYTD PVGVLYEDGD DTVATRSTEL CGLWQGRQPQ PVHLLPLHGI QHLNMVFSNL TLEHINAILL GAYRQGPPAS PTASPEPPPP E.

    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.

    Lcat 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.

    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 :

    ASNS Mouse

    Description:

    Asparagine Synthetase Mouse Recombinant

    Glutamine-dependent asparagine synthetase, Asns, Asparagine synthetase. 

    Product # :

    ENZ-1100

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    Description

    ASNS produced in Sf9 Insect cells is a single, glycosylated polypeptide chain containing 567 amino acids (1-561a.a.) and having a molecular mass of 65.1 kDa.ASNS is expressed with a 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Insect cells.

    Formulation

    ASNS protein solution ( 0.25mg/ml ) contains PBS (pH 7.4) and 40% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Asparagine synthetase (ASNS) is a cytoplasmic enzyme that turns aspartate toasparagine and functions mostly in mammalian organs. ASNS is responsible for cell growthand its mRNA content is associated with changes in the cell cycle. ASNS may also play a role as a biomarker for ovarian cancer.

    • Synonyms

      Glutamine-dependent asparagine synthetase, Asns, Asparagine synthetase.

    • 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

      MCGIWALFGS DDCLSVQCLS AMKIAHRGPD AFRFENVNGY TNCCFGFHRL AVVDPLFGMQ PIRVRKYPYL WLCYNGEIYN HKALQQRFEF EYQTNVDGEI ILHLYDKGGI EKTICMLDGV FAFILLDTAN KKVFLGRDTY GVRPLFKAMT EDGFLAVCSE AKGLVSLKHS TTPFLKVEPF LPGHYEVLDL KPNGKVASVE MVKYHHCTDE PLHAIYDSVE KLFPGFDLET VKNNLRILFD NAIKKRLMTD RRIGCLLSGG LDSSLVAASL LKQLKEAQVQ YPLQTFAIGM EDSPDLLAAR KVANYIGSEH HEVLFNSEEG IQALDEVIFS LETYDITTVR ASVGMYLISK YIRKNTDSVV IFSGEGSDEL TQGYIYFHKA PSPEKAEEES ERLLKELYLF DVLRADRTTA AHGLELRVPF LDHRFSSYYL SLPPDMRIPK NGIEKHLLRE TFEDCNLLPK EILWRPKEAF SDGITSVKNS WFKILQDYVE HQVDDEMMSA SQKFPFNTP KTKEGYFYRQ IFERHYPGRA DWLTHYWMPK WINATDPSAR TLTHYKS AAK AHHHHHH.

    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.

    Asns Mouse
  • View Data Sheet

    Name :

    UBE2K Human

    Description:

    Ubiquitin-Conjugating Enzyme E2K Human Recombinant

    HIP2, Huntingtin Interacting protein 2, HYPG, Ubiquitin-conjugating enzyme E2-25K kDa, Ubiquitin-protein ligase, Ubiquitin carrier protein, LIG, HIP-2, E2(25K), DKFZp686J24237, OTTHUMP00000218440, EC 6.3.2.19.

    Product # :

    ENZ-339

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    Description

    UBE2K produced in E.Coli is a single, non-glycosylated polypeptide chain containing 236 amino acids (1-200a.a.) and having a molecular mass of 26.5kDa.UBE2K is fused to a 36 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The UBE2K protein solution (1mg/1ml) is formulated in 20mM Tris-HCl buffer (pH7.5) 1mM DTT, 50mM NaCl, and 10% glycerol.

    Purity

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

    More Info

    • Introduction

      UBE2K belongs to the ubiquitin-conjugating enzymes family which take part in many cellular processes such as selective protein degradation, DNA repair, cell cycle control, and sporulation. In this mechanism, the ATP-coupled activation and subsequent ligation of ubiquitin are catalyzed by separate enzymes functionally linked by ubiquitin carrier protein UBC1. In addition, UBE2K is involved in Alzheimer's disease, Huntington's disease and antigen processing through its interaction with amyloid-?, huntingtin, and MHC-heavy chain proteins.

    • Synonyms

      HIP2, Huntingtin Interacting protein 2, HYPG, Ubiquitin-conjugating enzyme E2-25K kDa, Ubiquitin-protein ligase, Ubiquitin carrier protein, LIG, HIP-2, E2(25K), DKFZp686J24237, OTTHUMP00000218440, EC 6.3.2.19.

    • Physical Appearance

      Sterile Filtered clear solution.

    • Stability

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

    • Amino Acid Sequence

      MRGSHHHHHH GMASMTGGQQ MGRDLYDDDD KDRWGSMANI AVQRIKREFK EVLKSEETSK NQIKVDLVDE NFTELRGEIA GPPDTPYEGG RYQLEIKIPE TYPFNPPKVR FITKIWHPNI SSVTGAICLD ILKDQWAAAM TLRTVLLSLQ ALLAAAEPDD PQDAVVANQY KQNPEMFKQT ARLWAHVYAG APVSSPEYTK KIENLCAMGF DRNAVIVALS SKSWDVETAT ELLLSN.

    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.

    Ube2K Human
  • View Data Sheet

    Name :

    SlyD E.Coli

    Description:

    FKBP-Type Peptidyl-Prolyl Cis-Trans Isomerase E.Coli Recombinant

    FKBP-Type Peptidyl-Prolyl Cis-Trans Isomerase, SlyD.

    Product # :

    ENZ-338

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    Description

    SlyD Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 196 amino acids and having a molecular mass of 21 kDa.

    Source

    Escherichia Coli.

    Formulation

    SlyD protein solution contains 20mM Tris pH-7.5.

    Purity

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

    Biological Activity

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

    More Info

    • Introduction

      SlyD accessiton#: NP_755987 is a putative folding helper protein from the Escherichia coli cytosol, which has N-terminal prolyl isomerase domain of the FKBP type and a most likely unstructured C-terminal tail. SlyD is an important factor in the biosynthesis of the metal cluster in the [NiFe]-hydrogenase enzymes, and exhibits several activities including that of a peptidyl-prolyl isomerase.

    • Synonyms

      FKBP-Type Peptidyl-Prolyl Cis-Trans Isomerase, SlyD.

    • Physical Appearance

      Sterile Filtered colorless solution.

    • Stability

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

    • Amino Acid Sequence

      MKVAKDLVVS LAYQVRTEDG VLVDESPVSA PLDYLHGHGS LISGLETALE GHEVGDKFDV AVGANDAYGQ YDENLVQRVP KDVFMGVDEL QVGMRFLAET DQGPVPVEIT AVEDDHVVVD GNHMLAGQNL KFNVEVVAIR EATEEELAHG HVHGAHDHHH DHDHDGCCGG HGHDHGHEHG GEGCCGGKGN GGCGCH.

    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.

    Slyd
  • View Data Sheet

    Name :

    PREP Human

    Description:

    Prolyl Endopeptidase Human Recombinant

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

    Product # :

    ENZ-828

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    Description

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

    Source

    Escherichia Coli.

    Formulation

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

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

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

    • Synonyms

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

    • Physical Appearance

      Sterile filtered colorless solution.

    • Stability

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

    • Amino Acid Sequence

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

    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.

    Prep Human
  • View Data Sheet

    Name :

    GLB1 E.Coli

    Description:

    Galactosidase-Beta 1 E.coli Recombinant

    lacZ, beta-gal, β-gal.

    Product # :

    ENZ-041

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    Description

    The E.Coli derived recombinant protein Beta-galactosidase (114 kDa) is enzymatically inactive and Non-reactive with human serum.

    Source

    Escherichia Coli.

    Formulation

    Beta-Galactosidase (1mg/1ml) is formulated in 8M urea, 20mM Tris-HCl pH 8.0, and 10mM beta-mercaptoethanol

    Purity

    Protein is >95% pure as determined by SDS-PAGE, by measuring optical density at 280 nm and by method of Bradford et al.

    More Info

    • Introduction

      Beta-galactosidase is a hydrolase enzyme that catalyzes the hydrolysis of Beta-galactosides into monosaccharides. Substrates of different Beta-galactosidases include ganglioside GM1, lactosylceramides, lactose, and various glycoproteins. Beta-galactosidase is produced In E. coli by activation of the lac operon as the lacZ gene.

    • Synonyms

      lacZ, beta-gal, β-gal.

    • Physical Appearance

      Sterile filtered colorless solution.

    • Stability

      Protein should be stored for Short Term at 4°C and for long term at -20°C.

    • Purification Method

      Purified by proprietary chromatographic technique.

    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.

    Glb1 Ecoli Recombinant
  • View Data Sheet

    Name :

    Lysozyme Human

    Description:

    Lysozyme Human Recombinant

    EC 3.2.1.17, LYZ, Lysozyme.

    Product # :

    ENZ-1159

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    Description

    Recombinant Human Lysozyme produced in Plant is a non-glycosylated, polypeptide chain containing 130 amino acids and having a molecular mass of 14.7kDa. The Recombinant Human Lysozyme is purified by proprietary chromatographic techniques.

    Source

    Oryza sativa (rice).

    Formulation

    The protein (1mg/ml) was lyophilized with no additives.

    Purity

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

    Biological Activity

    1.6x105 U/mg.

    More Info

    • Introduction

      Lysozymeis an antimicrobial enzyme produced by animals that are part of the innate immune system. Lysozyme is a glycoside hydrolase that catalyzes the hydrolysis of 1,4-beta-linkages between N-acetylmuramic acid and N-acetyl-D-glucosamine residues in peptidoglycan, which is the major component of gram-positive bacterial cell wall.Lysozymes have primarily a bacteriolytic function - those in tissues and body fluids are associated with the monocyte-macrophage system and enhance the activity of immunoagents.

    • Synonyms

      EC 3.2.1.17, LYZ, Lysozyme.

    • Physical Appearance

      Sterile Filtered lyophilized (freeze-dried) off white powder.

    • Stability

      Store the lyophilized Lysozyme between 2-8°C, do not freeze. Upon reconstitution Lysozyme should be stored at 4°C between 2-7 days and for future use below -18°C. Please prevent freeze-thaw cycles.

    • Solubility

      Stock solutions can be prepared by dissolving gently into PBS for several minutes. Recommended stock concentrations are 1mg/ml in PBS.

    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.

    Lysozyme Human
  • View Data Sheet

    Name :

    TPA (311-562) Human

    Description:

    Tissue Plasminogen Activator (311-562 a.a.) Human Recombinant

    Tissue-type plasminogen activator, EC 3.4.21.68, tPA, t-PA, t-plasminogen activator, TPA, T-PA, DKFZp686I03148, PLAT and tPA.

    Product # :

    ENZ-1023

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    Description

    TPA Human Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 261 amino acids (311-562 a.a.) and having a molecular mass of 29.2kDa (Migrates at 28-40kDa on SDS-PAGE under reducing conditions).TPA is expressed with a 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    TPA protein solution (0.5mg/ml) contains 50mM MES (pH 5.0), 5mM CaCl2, 1mM DTT, 0.5M NaCl and 30% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Tissue plasminogen activator (abbreviated PLAT or tPA) is a secreted serine proteasewhich converts the proenzymeplasminogento plasmin, a fibrinolyticenzyme. Plasminogen is synthesized as a single chain which is cleaved by PLAT into the two chain disulfide linked plasmin.
      This enzyme plays a role in cell migrationand tissue remodeling. Increased enzymatic activity causes hyperfibrinolysis, which manifests as excessive bleeding; decreased activity leads to hypofibrinolysiswhich can result in thrombosisor embolism.

    • Synonyms

      Tissue-type plasminogen activator, EC 3.4.21.68, tPA, t-PA, t-plasminogen activator, TPA, T-PA, DKFZp686I03148, PLAT and tPA.

    • 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

      ADPIKGGLFA DIASHPWQAA IFAKHRRSPG ERFLCGGILI SSCWILSAAH CFQERFPPHH LTVILGRTYR VVPGEEEQKF EVEKYIVHKE FDDDTYDNDI ALLQLKSDSS RCAQESSVVR TVCLPPADLQ LPDWTECELS GYGKHEALSP FYSERLKEAH VRLYPSSRCT SQHLLNRTVT DNMLCAGDTR SGGPQANLHD ACQGDSGGPL VCLNDGRMTL VGIISWGLGC GQKDVPGVYT KVTNYLDWIR DNMRPHHHHH H.

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

    Tpa 311 562 Human
  • View Data Sheet

    Name :

    KLK3 Human, HEK

    Description:

    Kallikrein-3 Human Recombinant, HEK

    Prostate-specific antigen, PSA, Gamma-seminoprotein, Seminin, Kallikrein-3, P-30 antigen, Semenogelase, KLK3, APS, hK3, KLK2A1

    Product # :

    ENZ-1149

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    Quantity :

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    More Info

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

    Description

    KLK3 Human Recombinant produced in HEK cells is a single, glycosylated, polypeptide chain (18-261 a.a) containing a total of 250 amino acids, having a molecular mass of 27.6kDa.KLK3 is fused to a 6 amino acid His-tag at C-terminus,and is purified by proprietary chromatographic techniques.

    Source

    HEK293 Cells.

    Formulation

    The KLK3 solution (0.25mg/ml) contains 10% Glycerol and Phosphate-Buffered Saline (pH 7.4).

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Biological Activity

    Specific activity is  > 250pmol/min/ug. Defined by the amount of enzyme that cleaves 1pmole of Succinyl-ArgPro-Tyr-p-Nitroanilide to Succinyl-Arg-Pro-Tyr and p-Nitroanilide per minute at pH 7.5 at 37˚C.

    More Info

    • Introduction

      Kallikrein-3 or KLK3 is a serine proteases subgroup, enzymes can cleave peptide bonds. KLK3 is found in the prostate and may be hold accountable to the regulation of semen liquefaction via seminogelin hydrolysis. The protein is expressed in low concentrations in men with healthy prostates serum. When elevated quantities are found it may show prostate cancer or different prostate disorders such as prostatitis and benign prostatic hyperplasia.

    • Synonyms

      Prostate-specific antigen, PSA, Gamma-seminoprotein, Seminin, Kallikrein-3, P-30 antigen, Semenogelase, KLK3, APS, hK3, KLK2A1

    • 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

      APLILSRIVG GWECEKHSQP WQVLVASRGR AVCGGVLVHP QWVLTAAHCI RNKSVILLGR HSLFHPEDTG QVFQVSHSFP HPLYDMSLLK NRFLRPGDDS SHDLMLLRLS EPAELTDAVK VMDLPTQEPA LGTTCYASGW GSIEPEEFLT PKKLQCVDLH VISNDVCAQV HPQKVTKFML CAGRWTGGKS TCSGDSGGPL VCNGVLQGIT SWGSEPCALP ERPSLYTKVV HYRKWIKDTI VANPHHHHHH

    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.

    Kallikrein 3 Human
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