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Search results

1000 results found for “Sulfatase”

Name

Description

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  • View Data Sheet

    Name :

    RRM2 Human

    Description:

    Ribonucleotide Reductase M2 Human Recombinant

    EC 1.17.4.1, RR2M, RR2, Ribonucleotide Reductase M2, R2, RRM2.

    Product # :

    ENZ-523

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    Description

    RRM2 Recombinant Human produced in E.Coli is a single, non-glycosylated polypeptide chain containing 409 amino acids (1-389 a.a.) and having a molecular mass of 47 kDa. The RRM2 is fused to a 20 amino acids His-Tag at N-terminus and purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The RRM2 protein solution (1mg/ml) contains 20mM Tris-HCl pH-8, 0.1M NaCl, & 10% glycerol.

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      RRM2 catalyzes the formation of deoxyribonucleotides from ribonucleotides. Synthesis RRM2 is regulated in a cell-cycle dependent method. RRM2 supplies the precursors essential for DNA synthesis. RRM2 catalyzes the biosynthesis of deoxyribonucleotides from the corresponding ribonucleotides. RRM2 Inhibits Wnt signaling.

    • Synonyms

      EC 1.17.4.1, RR2M, RR2, Ribonucleotide Reductase M2, R2, RRM2.

    • 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 MLSLRVPLAP ITDPQQLQLS PLKGLSLVDK ENTPPALSGT RVLASKTARR IFQEPTEPKT KAAAPGVEDE PLLRENPRRF VIFPIEYHDI WQMYKKAEAS FWTAEEVDLS KDIQHWESLK PEERYFISHV LAFFAASDGI VNENLVERFS QEVQITEARC FYGFQIAMEN IHSEMYSLLI DTYIKDPKER EFLFNAIETM PCVKKKADWA LRWIGDKEAT YGERVVAFAA VEGIFFSGSF ASIFWLKKRG LMPGLTFSNE LISRDEGLHC DFACLMFKHL VHKPSEERVR EIIINAVRIE QEFLTEALPV KLIGMNCTLM KQYIEFVADR LMLELGFSKV FRVENPFDFM ENISLEGKTN FFEKRVGEYQ RMGVMSSPTE NSFTLDADF.

    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.

    Rrm2 Human
  • View Data Sheet

    Name :

    MIF Human, GST

    Description:

    Macrophage Migration Inhibitor Factor Human Recombinant, GST tag

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

    Product # :

    CYT-401

    Price :

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    Description

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

    Source

    Escherichia Coli.

    Formulation

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

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

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

    • Synonyms

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

    • Physical Appearance

      Sterile Filtered clear solution.

    • Stability

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

    • Amino Acid Sequence

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

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

    Mif Human Gst
  • View Data Sheet

    Name :

    SAT1 Human

    Description:

    Spermidine/Spermine N1-Acetyltransferase 1 Human Recombinant

    Diamine acetyltransferase 1, Spermidine/spermine N(1)-acetyltransferase 1, Putrescine acetyltransferase, Polyamine N-acetyltransferase 1, SSAT-1, SSAT, SAT1, SAT, DC21, KFSD, KFSDX.

    Product # :

    ENZ-433

    Price :

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    Description

    SAT1 Human Recombinant fused with a 20 amino acid His tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 191 amino acids (1-171 a.a.) and having a molecular mass of 22.1kDa.The SAT1 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The SAT1 solution contains 20mM Tris-HCl buffer (pH8.0) and 10% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      SAT-1 is a member the acetyltransferase family, and is a rate-limiting enzyme in the catabolic pathway of polyamine metabolism. SAT1 catalyzes the acetylation of spermidine and spermine, and is involved in the regulation of the intracellular concentration of polyamines and their transport out of cells. Therefore, SAT-1’s role is essential in polyamine homoeostasis, given that acetylated products are either excreted from the cell or oxidized by acetylpolyamine oxidase. Increased SAT1 activity causes variety of other effects which include pancreatic cells death, obstruction of regenerative tissue growth, behavioral changes, keratosis follicularis spinulosa decalvans (KFSD), and hair loss.
      Defects in the SAT1 gene are linked to KFSD (keratosis follicularis spinulosa decalvans), which is a rare X-linked disorder affecting the skin and the eye. The KFSD affected men show thickening of the skin of the neck, ears, and extremities, particularly the palms and soles, loss of eyebrows, eyelashes and beard, thickening of the eyelids with blepharitis and ectropion, and corneal degeneration. Even though the majority of the affected families are compatible with an X-linked inheritance, KFSD are found to be clinically and genetically heterogeneous.

    • Synonyms

      Diamine acetyltransferase 1, Spermidine/spermine N(1)-acetyltransferase 1, Putrescine acetyltransferase, Polyamine N-acetyltransferase 1, SSAT-1, SSAT, SAT1, SAT, DC21, KFSD, KFSDX.

    • 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 MAKFVIRPAT AADCSDILRL IKELAKYEYM EEQVILTEKD LLEDGFGEHP FYHCLVAEVP KEHWTPEGHS IVGFAMYYFT YDPWIGKLLY LEDFFVMSDY RGFGIGSEIL KNLSQVAMRC RCSSMHFLVA EWNEPSINFY KRRGASDLSS EEGWRLFKID KEYLLKMATE 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.

    Sat1 Human
  • View Data Sheet

    Name :

    DMGO

    Description:

    Dimethylglycine Oxidase Recombinant

    DMGO, Dimethylglycine Oxidase.

    Product # :

    ENZ-318

    Price :

    Quantity :

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    Description

    Dimethylglycine oxidase Recombinant originated from Arthrobacter globifomis fused to His Tag at N-terminal produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 850 amino acids and having a molecular mass of 92.1 kDa. The DMGO is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The Recombinant Dimethylglycine Oxidase solution contains 20mM Tris-HCl pH7.5 and 20% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      Dimethylglycine oxidase (DMGO) is a covalent flavoenzyme from Arthrobacter globiformis that catalyzes the oxidative demethylation of dimethylglycine to yield sarcosine, formaldehyde, and hydrogen peroxide. The N-terminal region binds FAD covalently so it is yellowish.

    • Synonyms

      DMGO, Dimethylglycine Oxidase.

    • Physical Appearance

      Sterile filtered liquid formulation 1 mg/ml.

    • 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 MASTPRIVII GAGIVGTNLA DELVTRGWNN ITVLDQGPLN MPGGSTSHAP GLVFQTNPSK TMASFAKYTVEKLLSLTEDG VSCFNQVGGL EVATTETRLA DLKRKLGYAA AWGIEGRLLS PAECQELYPL LDGENILGGL HVPSDGLASA ARAVQLLIKRTESAGVTYRG STTVTGIEQS GGRVTGVQTA DGVIPADIVV SCAGFWGAKI GAMIGMAVPL LPLAHQYVKT TPVPAQQGRN DQPNGARLPILRHQDQDLYY REHGDRYGIG SYAHRPMPVD VDTLGAYAPE TVSEHHMPSR LDFTLEDFLP AWEATKQLLP ALADSEIEDG FNGIFSFTPDGGPLLGESKE LDGFYVAEAV WVTHSAGVAK AMAELLTTGR SETDLGECDI TRFEDVQLTP EYVSETSQQN FVEIYDVLHP LQPRLSPRNLRVSPFHARHK ELGAFFLEAG GWERPYWFEA NAALLKEMPA EWLPPARDAW SGMFSSPIAA AEAWKTRTAV AMYDMTPLKR LEVSGPGALKLLQELTTADL AKKPGAVTYT LLLDHAGGVR SDITVARLSE DTFQLGANGN IDTAYFERAA RHQTQSGSAT DWVQVRDTTG GTCCIGLWGPLARDLVSKVS DDDFTNDGLK YFRAKNVVIG GIPVTAMRLS YVGELGWELY TSADNGQRLW DALWQAGQPF GVIAAGRAAF SSLRLEKGYRSWGTDMTTEH DPFEAGLGFA VKMAKESFIG KGALEGRTEE ASARRLRCLT IDDGRSIVLG KEPVFYKEQA VGYVTSAAYG YTVAKPIAYSYLPGTVSVGD SVDIEYFGRR ITATVTEDPL YDPKMTRLRG.

    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.

    Dimethylglycine Oxidase
  • View Data Sheet

    Name :

    IDNK E.Coli

    Description:

    Thermosensitive Gluconokinase E.Coli Recombinant

    Thermosensitive gluconokinase, Gluconate kinase 1, idnK.

    Product # :

    PKA-060

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    Description

    IDNK E.Coli Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 210 amino acids (1-187 a.a) and having a molecular mass of 23.4kDa. IDNK is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

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

    Purity

    Greater than 95% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      Thermosensitive Gluconokinase, also known as IDNK is a 187 a.a protein which is a member of the gluconokinase gntK/gntV family. IDNK catalyzes theconversion of ATP and D-gluconate to ADP and 6-phospho-D-gluconate. In addition, IDNK is considered to take part in gender determination, deletion of the distal portion of 9p is able to lead to a development of male to female sex reversal, the phenotype of a female with a male X, Y genotype.

    • Synonyms

      Thermosensitive gluconokinase, Gluconate kinase 1, idnK.

    • 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 MGSMAGESFI LMGVSGSGKT LIGSKVAALL SAKFIDGDDL HPAKNIDKMS QGIPLSDEDR LPWLERLNDA SYSLYKKNET GFIVCSSLKK QYRDILRKGS PHVHFLWLDG DYETILARMQ RRAGHFMPVA LLKSQFEALE RPQADEQDIV RIDINHDIAN VTEQCRQAVL AIRQNRICAK EGSASDQRCE.

    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.

    Idnk Ecoli
  • View Data Sheet

    Name :

    NMT1 Human

    Description:

    N-Myristoyltransferase 1 Human Recombinant

    N-Myristoyltransferase 1, NMT, Myristoyl-CoA:Protein N-Myristoyltransferase 1, Type I N-Myristoyltransferase, EC 2.3.1.97, Myristoyl-CoA:Protein,N- Myristoyltransferase, Glycylpeptide N-Tetradecanoyltransferase 1,Peptide N-Myristoyltransferase 1,Alternative, Short Form NMT-S, Short Form NMT-S,Long Form, NMT-L, Alternative, Long Form, NMT-L, NMT 1.

    Product # :

    ENZ-842

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    Description

    NMT1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 519 amino acids (1-496 a.a) and having a molecular mass of 59.2kDa.NMT1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    NMT1 protein solution (1mg/ml) containing Phosphate buffered saline (pH7.4).

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      Myristate, a rare 14-carbon saturated fatty acid, is co-translationally attached by an amide linkage to the N-terminal glycine residue of cellular & viral proteins with various functions. N-Myristoyltransferase 1, also known as NMT1 catalyzes the transfer of myristate from CoA to proteins. NMT1 seems to be irreversible and is essential for full expression of the biologic activities of several N-myristoylated proteins, as well as the alpha subunit of the signal-transducing guanine nucleotide-binding protein, G protein.

    • Synonyms

      N-Myristoyltransferase 1, NMT, Myristoyl-CoA:Protein N-Myristoyltransferase 1, Type I N-Myristoyltransferase, EC 2.3.1.97, Myristoyl-CoA:Protein,N- Myristoyltransferase, Glycylpeptide N-Tetradecanoyltransferase 1,Peptide N-Myristoyltransferase 1,Alternative, Short Form NMT-S, Short Form NMT-S,Long Form, NMT-L, Alternative, Long Form, NMT-L, NMT 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 MGSMADESET AVKPPAPPLP QMMEGNGNGH EHCSDCENEE DNSYNRGGLS PANDTGAKKK KKKQKKKKEK GSETDSAQDQ PVKMNSLPAE RIQEIQKAIE LFSVGQGPAK TMEEASKRSY QFWDTQPVPK LGEVVNTHGP VEPDKDNIRQ EPYTLPQGFT WDALDLGDRG VLKELYTLLN ENYVEDDDNM FRFDYSPEFL LWALRPPGWL PQWHCGVRVV SSRKLVGFIS AIPANIHIYD TEKKMVEINF LCVHKKLRSK RVAPVLIREI TRRVHLEGIF QAVYTAGVVL PKPVGTCRYW HRSLNPRKLI EVKFSHLSRN MTMQRTMKLY RLPETPKTAG LRPMETKDIP VVHQLLTRYL KQFHLTPVMS QEEVEHWFYP QENIIDTFVV ENANGEVTDF LSFYTLPSTI MNHPTHKSLK AAYSFYNVHT QTPLLDLMSD ALVLAKMKGF DVFNALDLME NKTFLEKLKF GIGDGNLQYY LYNWKCPSMG AEKVGLVLQ.

    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.

    Nmt1 Human
  • View Data Sheet

    Name :

    UBA3 Human

    Description:

    Ubiquitin-Like Modifier Activating Enzyme 3 Human Recombinant

    NEDD8-activating enzyme E1 catalytic subunit, NEDD8-activating enzyme E1C, Ubiquitin-activating enzyme E1C, Ubiquitin-like modifier-activating enzyme 3, Ubiquitin-activating enzyme 3, UBA3, UBE1C, hUBA3.

    Product # :

    ENZ-576

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    Description

    UBA3 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 487 amino acids (1-463) and having a molecular mass of 54.4kDa.UBA3 is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The UBA3 solution (1mg/ml) contains 20mM Tris-HCl buffer (pH8.0), 20% glycerol and 1mM DTT.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      NEDD8-activating enzyme E1 catalytic subunit (UBA3) is the catalytic subunit of the dimeric UBA3-NAE1 E1 enzyme, which belongs to the E1 ubiquitin-activating enzyme family. E1 activates NEDD8 by initially adenylating its C-terminal glycine residue with ATP, afterwards linking this residue to the side chain of the catalytic cysteine, generating a NEDD8-UBA3 thioester and free AMP. E1 at last transfers NEDD8 to the catalytic cysteine of UBE2M. The UBA3 enzyme connects with AppBp1, an amyloid beta precursor protein binding protein, to form a heterodimer, and at that point the enzyme complex activates NEDD8, a ubiquitin-like protein, which controls cell division, signaling and embryogenesis.

    • Synonyms

      NEDD8-activating enzyme E1 catalytic subunit, NEDD8-activating enzyme E1C, Ubiquitin-activating enzyme E1C, Ubiquitin-like modifier-activating enzyme 3, Ubiquitin-activating enzyme 3, UBA3, UBE1C, hUBA3.

    • 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 MGSHMADGEE PERKRRRIEE LLAEKMAVDG GCGDTGDWEG RWNHVKKFLE RSGPFTHPDF EPSTESLQFL LDTCKVLVIG AGGLGCELLK NLALSGFRQI HVIDMDTIDV SNLNRQFLFR PKDIGRPKAE VAAEFLNDRV PNCNVVPHFN KIQDFNDTFY RQFHIIVCGL DSIIARRWIN GMLISLLNYE DGVLDPSSIV PLIDGGTEGF KGNARVILPG MTACIECTLE LYPPQVNFPM CTIASMPRLP EHCIEYVRML QWPKEQPFGE GVPLDGDDPE HIQWIFQKSL ERASQYNIRG VTYRLTQGVV KRIIPAVAST NAVIAAVCAT EVFKIATSAY IPLNNYLVFN DVDGLYTYTF EAERKENCPA CSQLPQNIQF SPSAKLQEVL DYLTNSASLQ MKSPAITATL EGKNRTLYLQ SVTSIEERTR PNLSKTLKEL GLVDGQELAV ADVTTPQTVL FKLHFTS.

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    Uba3 Human
  • View Data Sheet

    Name :

    GNPDA1 Human

    Description:

    Glucosamine-6-Phosphate Deaminase 1 Human Recombinant

    GNP1, GNPDA, GNPI, GPI, HLN, Oscillin.

    Product # :

    ENZ-554

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    Description

    GNPDA1 Recombinant Human produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 309 amino acids (1-289) and having a molecular mass of 34.8 kDa.GNPDA1 is fused to a 20 amino macid His-Tag at N-terminus and purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    1 mg/ml solution containing 20mM Tris Hcl buffer pH-8, 1mM DTT, 50mM NaCl and 20% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      GNPDA1, catalyzes the conversion of glucosamine-6-phosphate to fructose-6-phosphate, a reaction that under physiological conditions proceeds to the formation of fructose-6-phosphate. GNPDA1 is widely expressed with highest expression in testes, ovary and heart. GNPDA1 triggers calcium oscillations in mammalian eggs. These oscillations are as the necessary trigger for egg activation and early development of the embryo.

    • Synonyms

      GNP1, GNPDA, GNPI, GPI, HLN, Oscillin.

    • Physical Appearance

      Sterile filtered colorless solution.

    • Stability

      GNPDA1 Human Recombinant although stable at 4°C for 1 week, should be stored below -18°C.Please prevent freeze-thaw cycles.

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MKLIILEHYS QASEWAAKYI RNRIIQFNPG PEKYFTLGLP TGSTPLGCYK KLIEYYKNGD LSFKYVKTFN MDEYVGLPRD HPESYHSFMW NNFFKHIDIH PENTHILDGN AVDLQAECDA FEEKIKAAGG IELFVGGIGP DGHIAFNEPG SSLVSRTRVK TLAMDTILAN ARFFDGELTK VPTMALTVGV GTVMDAREVM ILITGAHKAF ALYKAIEEGV NHMWTVSAFQ QHPRTVFVCD EDATLELKVK TVKYFKGLML VHNKLVDPLY SIKEKETEKS QSSKKPYSD.

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    Gnpda1 Human
  • View Data Sheet

    Name :

    RPP30 Human

    Description:

    Ribonuclease P/MRP 30kDa Subunit Human Recombinant

    Ribonuclease P protein subunit p30, RNaseP protein p30, RNase P subunit 2, RPP30, RNASEP2, TSG15, FLJ38491, RP11-320F15.1.

    Product # :

    ENZ-040

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    Description

    RPP30 Human Recombinant fused with a 23 amino acid His tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 291 amino acids (1-268 a.a.) and having a molecular mass of 31.8kDa. The RPP30 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The RPP30 solution (0.5 mg/ml) contains 20mM Tris-HCl buffer (pH8.0), 20% glycerol, 5mM DTT, 200mM NaCl and 1mM EDTA.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      Ribonuclease P protein subunit p30 (RPP30) is a member of the eukaryotic/archaeal RNase P protein component 3 family. RPP30 is component of ribonuclease P, which is a protein complex that generates mature tRNA molecules by cleaving their 5'-ends. Ribonuclease P (RNase P) is small nuclear ribonucleoprotein (snRNPs) which acts on RNA substrates in vitro. In addition, RNase P which accumulate in the nucleolus, have a similar RNA component and several protein subunits in common.

    • Synonyms

      Ribonuclease P protein subunit p30, RNaseP protein p30, RNase P subunit 2, RPP30, RNASEP2, TSG15, FLJ38491, RP11-320F15.1.

    • 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 MGSMAVFADL DLRAGSDLKA LRGLVETAAH LGYSVVAINH IVDFKEKKQE IEKPVAVSEL FTTLPIVQGK SRPIKILTRL TIIVSDPSHC NVLRATSSRA RLYDVVAVFP KTEKLFHIAC THLDVDLVCI TVTEKLPFYF KRPPINVAID RGLAFELVYS PAIKDSTMRR YTISSALNLM QICKGKNVII SSAAERPLEI RGPYDVANLG LLFGLSESDA KAAVSTNCRA ALLHGETRKT AFGIISTVKK PRPSEGDEDC LPASKKAKCE G.

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    Rpp30 Human
  • View Data Sheet

    Name :

    UNG

    Description:

    Uracil DNA Glycosilase

    Uracil DNA Glycosilase, Uracil DNA Glycosylase, UNG.

    Product # :

    ENZ-352

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    Description

    E.Coli Uracil DNA Glycosilase (UNG) catalyses the release of free Uracil from Uracil-containing DNA. UNG efficiently hydrolyzes uracil from signle-stranded or double-stranded DNA, but not from oligomers (6 fewer bases).

    Source

    Escherichia Coli strain that carries the UNG gene from E.coli.

    Formulation

    UNG solution in 10mM Tris-HCl (pH-7.4 at 25°C), 50mM KCl, 1mM DTT, 0.1mM EDTA, 0.1 mg/ml BSA and 50% glycerol.

    Citations

    More Info

    • Synonyms

      Uracil DNA Glycosilase, Uracil DNA Glycosylase, UNG.

    • Physical Appearance

      Sterile Filtered colorless solution.

    • Stability

      Uracil DNA Glycosilase although stable at 15°C for 1 week, should be stored below -18°C. Please prevent freeze-thaw cycles.

    • Reaction Conditions

      1X UNG Reaction Buffer, incubate at 37°C.UNG is active over a broad pH rabge with an optimum at pH-8.0, doesn't require divalent cation, and is inhibited by high ionic strength (>200mM). The abasic sites formed in DNA by UNG may be cleaved by heat, alkali-treatment or endonucleases that cleave specifically at abasic sites.

    • Inactivation

      Inactivated by heating at 95°C for 10min. Enzyme activity is partially restored at temperatures lower than 55°C.

    • Unit Definition

      1 Unit of the enzyme catalyzes the release of 1 nanomole of uracil-containing DNA template in 60 min at 37°C.

    • Specific Activity

      The Specific Activity was found to be 5U/µl.

    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.

    Uracil Dna Glycosylase Enzyme
  • View Data Sheet

    Name :

    F9 Human

    Description:

    Coagulation Factor IX Human

    Coagulation factor IX, EC 3.4.21.22, Christmas factor, Plasma thromboplastin component, PTC, F9, FIX, HEMB, MGC129641, MGC129642, GLA domain, Factor IX.

    Product # :

    PRO-353

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    Description

    Human Factor-IX produced from fresh frozen human plasma is a glycosylated polypeptide chain having a molecular mass of 56 kDa.

    Source

    Human Plasma.

    Formulation

    The Factor-IX is provided in a sterile solution containing 20mM Tris-HCl pH-7.4, 100mM NaCl and 1mM Benzamidine.

     

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Biological Activity

    The activity per mg was tested and found to be 380 PEU/mg.

    Citations

    More Info

    • Introduction

      Human Factor IX also called Christmas-Factor is a glycoprotein, which is synthesized in the liver and belongs to the serine proteases system and is part of the S1 peptidase family.
      Lack of Factor-IX causes Hemophilia-B meaning Christmas Disease. Factor-IX has a N-terminus region which contains 12xGla residues which asist the calcium dpendant binding of Factor-IX to the phospholipid surface. Factor-IX is activated by either factor XIa or the factor VIIa/tissue factor/phospholipid complex. Cleavage yields the intermediate IXa, which is subsequently converted to the fully active form IXab.
      Factor-IX binds initially to exosites on the factor XIa heavy chain, followed by interaction at the active site with subsequent bond cleavage. Coagulation factor IX is activated by interaction with the erythrocyte membrane, causing intrinsic coagulation. Chaperones & lectins act simultaniously to guarantee the proper folding of Factor-IX and the retention of mutant molecules. Human Factor IX, activated by either the Contact or Tissue Factor Pathway, is responsible for the activation of Factor X to Xa.

    • Synonyms

      Coagulation factor IX, EC 3.4.21.22, Christmas factor, Plasma thromboplastin component, PTC, F9, FIX, HEMB, MGC129641, MGC129642, GLA domain, Factor IX.

    • 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. Please prevent freeze-thaw cycles..

    • Human Virus Test

      Human plasma was tested and found negative for HIV-1, HIV-2, Hepatitis B Surface antigen and HCV. Donors are screened for CJD (Creutzfeldt-Jakob Disease).

    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.

    Factor Ix Human
  • View Data Sheet

    Name :

    BDH1 Human

    Description:

    3-Hydroxybutyrate Dehydrogenase, Type 1 Human Recombinant

    D-beta-hydroxybutyrate dehydrogenase, mitochondrial, BDH, 3-hydroxybutyrate dehydrogenase, BDH1, SDR9C1.

    Product # :

    ENZ-215

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    Description

    BDH1 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 318 amino acids (47-343) and having a molecular mass of 35.3kDa.BDH1 is fused to a 21 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    The BDH1 solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH8.0), 30% glycerol, 0.2M NaCl, 2mM DTT and 0.1mM PMSF.

    Purity

    Greater than 85% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      BDH1 belongs to the short-chain dehydrogenase/reductase gene family. BDH1 forms a homotetrameric lipid-requiring enzyme of the mitochondrial membrane and has a specific necessity for phosphatidylcholine for optimal enzymatic activity. BDH1 catalyzes the interconversion of acetoacetate and (R)-3-hydroxybutyrate, the 2 main ketone bodies formed during fatty acid catabolism.

    • Synonyms

      D-beta-hydroxybutyrate dehydrogenase, mitochondrial, BDH, 3-hydroxybutyrate dehydrogenase, BDH1, SDR9C1.

    • 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 MASAAEPVGS KAVLVTGCDS GFGFSLAKHL HSKGFLVFAG CLMKDKGHDG VKELDSLNSD RLRTVQLNVC SSEEVEKVVE IVRSSLKDPE KGMWGLVNNA GISTFGEVEF TSLETYKQVA EVNLWGTVRM TKSFLPLIRR AKGRVVNISS MLGRMANPAR SPYCITKFGV EAFSDCLRYE MYPLGVKVSV VEPGNFIAAT SLYSPESIQA IAKKMWEELP EVVRKDYGKK YFDEKIAKME TYCSSGSTDT SPVIDAVTHA LTATTPYTRY HPMDYYWWLR MQIMTHLPGA ISDMIYIR.

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    Bdh1 Human
  • View Data Sheet

    Name :

    CDC25A Human

    Description:

    Cell Division Cycle 25A Human Recombinant

    M-phase inducer phosphatase 1, Dual specificity phosphatase Cdc25A, CDC25A, CDC25A2.

    Product # :

    ENZ-091

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    Description

    CDC25A Human Recombinant fused with a 36 amino acid His tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 560 amino acids (1-524 a.a.) and having a molecular mass of 63.2kDa. The CDC25A is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The CDC25A solution (0.25 mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 5mM DTT, 20% glycerol, 0.2M NaCl and 1mM EDTA.

    Purity

    Greater than 80.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      M-phase inducer phosphatase 1 (CDC25A) belongs to the CDC25 family of phosphatases. CDC25A is essential for progression from G1 to the S phase of the cell cycle. CDC25A activates the cyclin-dependent kinase CDC2 by eliminating 2 phosphate groups. CDC25A is specifically degraded in reaction to DNA damage, which inhibits cells with chromosomal abnormalities from progressing in the course of cell division. CDC25A is an oncogene, though its exact function in oncogenesis has not been determined.

    • Synonyms

      M-phase inducer phosphatase 1, Dual specificity phosphatase Cdc25A, CDC25A, CDC25A2.

    • 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

      MRGSHHHHHH GMASMTGGQQ MGRDLYDDDD KDRWGSMELG PEPPHRRRLL FACSPPPASQ PVVKALFGAS AAGGLSPVTN LTVTMDQLQG LGSDYEQPLE VKNNSNLQRM GSSESTDSGF CLDSPGPLDS KENLENPMRR IHSLPQKLLG CSPALKRSHS DSLDHDIFQL IDPDENKENE AFEFKKPVRP VSRGCLHSHG LQEGKDLFTQ RQNSAPARML SSNERDSSEP GNFIPLFTPQ SPVTATLSDE DDGFVDLLDG ENLKNEEETP SCMASLWTAP LVMRTTNLDN RCKLFDSPSL CSSSTRSVLK RPERSQEESP PGSTKRRKSM SGASPKESTN PEKAHETLHQ SLSLASSPKG TIENILDNDP RDLIGDFSKG YLFHTVAGKH QDLKYISPEI MASVLNGKFA NLIKEFVIID CRYPYEYEGG HIKGAVNLHM EEEVEDFLLK KPIVPTDGKR VIVVFHCEFS SERGPRMCRY VRERDRLGNE YPKLHYPELY VLKGGYKEFF MKCQSYCEPP SYRPMHHEDF KEDLKKFRTK SRTWAGEKSK REMYSRLKKL.

    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.

    Cdc25A Human
  • View Data Sheet

    Name :

    HAO1 Human, Active

    Description:

    Hydroxyacid Oxidase 1 Human Recombinant, Active

    Hydroxyacid oxidase 1, HAOX1, Glycolate oxidase, GOX, HAO1, GOX1.

    Product # :

    ENZ-1094

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    Description

    HAO1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 406 amino acids (1-370 a.a) and having a molecular mass of 45.0kDa. HAO1 is fused to a 36 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    HAO1 protein solution (1mg/ml) contains 20% glycerol, 20mM Tris-Hcl (pH8.0) and 0.5M NaCl.

    Purity

    Greater than 95% as determined by SDS-PAGE.

    Biological Activity

    Specific activity is > 3000 pmol/min/ug, and defined as the amount of enzyme that oxidize glyoxylate at pH 8.0 at 25C.

    Citations

    More Info

    • Introduction

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

    • Synonyms

      Hydroxyacid oxidase 1, HAOX1, Glycolate oxidase, GOX, HAO1, GOX1.

    • Physical Appearance

      Sterile filtered yellowish 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

      MRGSHHHHHH GMASMTGGQQ MGRDLYDDDD KDRWGSMLPR LICINDYEQH AKSVLPKSIY DYYRSGANDE ETLADNIAAF SRWKLYPRMLRNVAETDLST SVLGQRVSMP ICVGATAMQR MAHVDGELAT VRACQSLGTG MMLSSWATSS IEEVAEAGPE ALRWLQLYIY KDREVTKKLVRQAEKMGYKA IFVTVDTPYL GNRLDDVRNR FKLPPQLRMK NFETSTLSFS PEENFGDDSG LAAYVAKAID PSISWEDIKW LRRLTSLPIVAKGILRGDDA REAVKHGLNG ILVSNHGARQ LDGVPATIDV LPEIVEAVEG KVEVFLDGGV RKGTDVLKAL ALGAKAVFVG RPIVWGLAFQGEKGVQDVLE ILKEEFRLAM ALSGCQNVKV IDKTLVRKNP LAVSKI.

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

    Hao1 Protein
  • View Data Sheet

    Name :

    N6AMT1 Human

    Description:

    N-6 Adenine-Specific DNA Methyltransferase 1 Human Recombinant

    N-6 Adenine-Specific DNA Methyltransferase 1 (Putative), N(6)-Adenine-Specific DNA Methyltransferase 1, HemK Methyltransferase Family Member 2, M.HsaHemK2P, C21orf127, HEMK2, Chromosome 21 Open Reading Frame 127, N6-DNA-Methyltransferase, EC 2.1.1.- , PRED28, N6AMT, MTQ2, HemK methyltransferase family member 2.

    Product # :

    ENZ-834

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    Description

    N6AMT1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 237 amino acids (1-214 a.a) and having a molecular mass of 25.3kDa. N6AMT1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    N6AMT1 protein solution (0.25 mg/ml) containing Phosphate buffered saline (pH7.4), 20% glycerol and 1mM DTT.

    Purity

    Greater than 85% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      N-6 Adenine-Specific DNA Methyltransferase 1, also known as N6AMT1 is part of the methyltransferase family. N6AMT1 is implicated in the methylation of release factor I during translation termination. In addition, N6AMT1 is involved in converting the arsenic metabolite monomethylarsonous acid to the less toxic dimethylarsonic acid.

    • Synonyms

      N-6 Adenine-Specific DNA Methyltransferase 1 (Putative), N(6)-Adenine-Specific DNA Methyltransferase 1, HemK Methyltransferase Family Member 2, M.HsaHemK2P, C21orf127, HEMK2, Chromosome 21 Open Reading Frame 127, N6-DNA-Methyltransferase, EC 2.1.1.- , PRED28, N6AMT, MTQ2, HemK methyltransferase family member 2.

    • Physical Appearance

      Sterile Filtered colorless solution.

    • Stability

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

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MGSMAGENFA TPFHGHVGRG AFSDVYEPAE DTFLLLNALE AAAAELAGVE ICLEVGSGSG VVSAFLASMI GPQALYMCTD INPEAAACTL ETARCNKVHI QPVITDLVKG LLPRLTEKVD LLVFNPPYVV TPPQEVGSHG IEAAWAGGRN GREVMDRFFP LVPDLLSPRG LFYLVTIKEN NPEEILKIMK TKGLQGTTAL SRQAGQETLS VLKFTKS.

    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.

    N6Amt1 Human
  • View Data Sheet

    Name :

    Taq Plus DNA

    Description:

    Taq Plus DNA Polymerase Recombinant

    Taq Plus DNA Polymerase, Taq Plus DNA, TaqPDNA.

    Product # :

    ENZ-309

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    Description

    Taq Plus is a mixture of Taq and Pfu. Taq Plus, which is used to improve the reliability and yield of conventional primer extension reaction. Taq Plus has two following advantages over Taq: (1) high fidelity with an error frequency 1.6/106 (or 0.0016/103) during DNA synthesis. (2) Taq Plus increases the efficiency of polymerization reaction, resulting in a great percentage of extenuation reaction completion up to 10 kb to 30 kb. Pfu has a temperature optimum between 72-78°C and remains > 95% active following 1-hour incubation at 95°C.

    Source

    Recombinant E.coli contains Thermus aquaticus polymerase gene.

    Formulation

    5U/µl.

    Citations

    More Info

    • Synonyms

      Taq Plus DNA Polymerase, Taq Plus DNA, TaqPDNA.

    • Stability

      Stable for 5 days at 10°C, for longer period of time store at -20°C.

    • Optimization of DNA Synthesis

      It is important to ad the reaction components in the following order1. H2O.2. 10 x reaction buffer.3. dNTPs.4. DNA template and primers.5. Taq Plus.

    • Reaction Conditions

      DNA synthesis is performed in 100?l of mixture containing 20-200μm dNTPs, 0.3-1μm Promers, 0.1-0.250 mg of template DNA, 10 ?l of 10 x reaction buffer and 2.5-5 units of Taq Plus. Mix the reaction gently, centrifuge briefly and then overlay with light mineral oil. Initially, denature the reaction by incubating at 95? for 5 minutes and then cool to 40-68? for 5 minutes to allow the primers to anneal to the template DNA.

    • Storage Buffer

      20mM Tris-HCl (pH 8.0), 1mM DTT, 0.1mM EDTA, 100mM KCl, Stabilizers, and 50%glycerol.

    • Note

      All reagents, including Taq Plus, should be mixed immediately before use.

    • Unit Definition

      One unit of the enzyme catalyzes the incorporation of 10nmole of deoxyribonucleotides into a polynucleotide fraction in 30 min at 74°C.

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

    Taq Plus Dna
  • View Data Sheet

    Name :

    SUMO2 Human

    Description:

    Small Ubiquitin-Related Modifier 2 Human Recombinant

    Small ubiquitin-related modifier 2, SUMO-2, Ubiquitin-like protein SMT3B, SMT3 homolog 2, Sentrin-2, HSMT3, SUMO-3, SUMO2, SMT3B, SMT3H2, MGC117191.

    Product # :

    PRO-586

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    Description

    SUMO2 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 93 amino acids and having a molecular mass of 10.6 kDa.The SUMO-2 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The SUMO2 (1mg/ml) containing 20mM Tris-HCl buffer (pH 8.0).

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      Small Ubiquitin-like Modifiers (SUMOs) are a family of small, related proteins that can be enzymatically attached to a target protein by a post-translational modification process termed sumoylation. Unlike ubiquitination, which targets proteins for degradation, sumoylation participates in a number of cellular processes, such as nuclear transport, transcriptional regulation, apoptosis, and protein stability. All SUMO proteins share the conserved ubiquitin domain and the C-terminal diglycine cleavage/attachment site. Human SUMO2, also known as Sentrin2 and SMT3B is synthesized as a 95 amino acid (aa), 11 kDa propeptide that contains a two aa C-terminal prosegment, and an 18 aa N-terminal protein interacting region (aa 33 -50). Following prosegment cleavage, the C-terminal glycine is enzymatically attached to a lysine on a target protein. Human SUMO2 shares 100% sequence identity to SUMO-2 from mouse. SUMO2 also has very high sequence homology to SUMO3 and SUMO4, 86 % and 85%, respectively. SUMO2 shares only 44% sequence identity to SUMO1.

    • Synonyms

      Small ubiquitin-related modifier 2, SUMO-2, Ubiquitin-like protein SMT3B, SMT3 homolog 2, Sentrin-2, HSMT3, SUMO-3, SUMO2, SMT3B, SMT3H2, MGC117191.

    • Physical Appearance

      Sterile filtered colorless solution.

    • Stability

      Can be stored at +4C for 1 week. For long term storage , below -20C.Please prevent freeze-thaw cycles.

    • Amino Acid Sequence

      MADEKPKEGVKTENNDHINLKVAGQDGSVVQFKIKRHTPLSKLMKAYC
      ERQGLSMRQIRFRFDGQPINETDTPAQLEMEDEDTIDVFQQQTGG.

    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.

    Sumo2 Human
  • View Data Sheet

    Name :

    HSD17B14 Human

    Description:

    Hydroxysteroid (17-beta) Dehydrogenase 14 Human Recombinant

    17-beta-hydroxysteroid dehydrogenase 14, 17-beta-HSD 14, 17-beta-hydroxysteroid dehydrogenase DHRS10, Dehydrogenase/reductase SDR family member 10, Retinal short-chain dehydrogenase/reductase retSDR3, HSD17B14, DHRS10, SDR3, SDR47C1, retSDR3.

    Product # :

    ENZ-029

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    Description

    HSD17B14 Human Recombinant fused with a 36 amino acid His tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 306 amino acids (1-270 a.a.) and having a molecular mass of 32.4kDa. The HSD17B14 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The HSD17B14 solution (1 mg/ml) contains 20mM Tris-HCl buffer (pH8.0), 20% glycerol, 0.1M NaCl and 1mM DTT.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      17-beta-hydroxysteroid dehydrogenase 14 (HSD17B14) is a member of the 17-beta-HSD family of proteins, which regulate the availability of steroids within various tissues throughout the body. 17-beta-hydroxysteroid dehydrogenases (HSD17B14) are mainly involved in metabolism of steroids at the C17 position and also of other substrates, such as fatty acids, prostaglandins, and xenobiotics. HSD17B14 exists as a homotetramer that localizes to the cytoplasm and is highly expressed in the brain, placenta, liver and kidney.

    • Synonyms

      17-beta-hydroxysteroid dehydrogenase 14, 17-beta-HSD 14, 17-beta-hydroxysteroid dehydrogenase DHRS10, Dehydrogenase/reductase SDR family member 10, Retinal short-chain dehydrogenase/reductase retSDR3, HSD17B14, DHRS10, SDR3, SDR47C1, retSDR3.

    • 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

      MRGSHHHHHH GMASMTGGQQ MGRDLYDDDD KDRWGSMATG TRYAGKVVVV TGGGRGIGAG IVRAFVNSGA RVVICDKDES GGRALEQELP GAVFILCDVT QEDDVKTLVS ETIRRFGRLD CVVNNAGHHP PPQRPEETSA QGFRQLLELN LLGTYTLTKL ALPYLRKSQG NVINISSLVG AIGQAQAVPY VATKGAVTAM TKALALDESP YGVRVNCISP GNIWTPLWEE LAALMPDPRA TIREGMLAQP LGRMGQPAEV GAAAVFLASE ANFCTGIELL VTGGAELGYG CKASRSTPVD APDIPS.

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    Hsd17B14 Human
  • View Data Sheet

    Name :

    SNCA NACP112 Human

    Description:

    Alpha Synuclein NACP112 Human Recombinant

    Alpha-synuclein, Non-A beta component of AD amyloid, Non-A4 component of amyloid precursor, NACP, PD1, PARK1, PARK4, MGC110988, a-Synuclein, SNCA.

    Product # :

    PRO-162

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    Description

    A-Synuclein NACP112 Human Recombinant which is an alternatively spliced (103-129) form of a-Synuclein, produced in E.Coli is a single, non-glycosylated polypeptide chain of 112 amino acids having a molecular mass of 11.3kDa. The Recombinant Human a-Synuclein NACP112 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The SNCA NACP112 protein solution (1mg/ml) contains 20mM Tris-HCl buffer pH 7.5 and 100mM NaCl.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      a-Synuclein (amino acids 1-140), an acidic neuronal protein of 140 amino acids, is extremely heat-resistant and is natively unfolded with an extended structure primarily composed of random coils. a-synuclein has been suggested to be implicated in the pathogenesis of Parkinson’s disease and related neurodegenerative disorders, and more recently, to be an important regulatory component of vesicular transport in neuronal cells. Moreover, recent studies have shown that a-synuclein has chaperone activity and that this activity is lost upon removing its C-terminal acidic tail (amino acids 96-140).

    • Synonyms

      Alpha-synuclein, Non-A beta component of AD amyloid, Non-A4 component of amyloid precursor, NACP, PD1, PARK1, PARK4, MGC110988, a-Synuclein, SNCA.

    • 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

      MDVFMKGLSK AKEGVVAAAE KTKQGVAEAA GKTKEGVLYV GSKTKEGVVH GVATVAEKTK EQVTNVGGAV VTGVTAVAQK TVEGAGSIAA ATGFVKKDQL GKEGYQDYEP EA.

    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.

    Snca Nacp112 Human
  • View Data Sheet

    Name :

    BDH2 Human

    Description:

    3-Hydroxybutyrate Dehydrogenase, Type 2 Human Recombinant

    3-hydroxybutyrate dehydrogenase type 2, FLJ13261, PRO20933, SDR15C1, UCPA-OR, UNQ6308, dehydrogenase/reductase (SDR family) member 6, Oxidoreductase UCPA, DHRS6, R-beta-hydroxybutyrate dehydrogenase, EFA6R, EC 1.1.1.30.

    Product # :

    ENZ-060

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    Description

    BDH2 produced in E.Coli is a single, non-glycosylated polypeptide chain containing 265 amino acids (1-245a.a.) and having a molecular mass of 28.8kDa.BDH2 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The BDH2 protein solution (1mg/1ml) is formulated in 20mM Tris-HCl buffer (pH8.0) 0.1M NaCl and 10% glycerol.

    Purity

    Greater than 95% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      BDH2 is a member of the short-chain dehydrogenases/reductases (SDR) family. BDH2 protein has a significant part in the peripheral utilization of 3-hydroxybutyrate. BDH2 can convert high levels of circulating 3-hydroxybutyrate into acetoacetate due to cytoplasmic localization in high ratio of oxidized NAD+, the NAD+ dependence and the kinetic parameters.

    • Synonyms

      3-hydroxybutyrate dehydrogenase type 2, FLJ13261, PRO20933, SDR15C1, UCPA-OR, UNQ6308, dehydrogenase/reductase (SDR family) member 6, Oxidoreductase UCPA, DHRS6, R-beta-hydroxybutyrate dehydrogenase, EFA6R, EC 1.1.1.30.

    • 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

      MGSSHHHHHH SSGLVPRGSH MGRLDGKVII LTAAAQGIGQ AAALAFAREG AKVIATDINE SKLQELEKYP GIQTRVLDVT KKKQIDQFAN EVERLDVLFN VAGFVHHGTV LDCEEKDWDF SMNLNVRSMY LMIKAFLPKM LAQKSGNIIN MSSVASSVKG VVNRCVYSTT KAAVIGLTKS VAADFIQQGI RCNCVCPGTV DTPSLQERIQ ARGNPEEARN DFLKRQKTGR FATAEEIAML CVYLASDESA YVTGNPVIID GGWSL

    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.

    Bdh2 Human
  • View Data Sheet

    Name :

    KLK3, His

    Description:

    Kallikrein-3 Human Recombinant, His Tag

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

    Product # :

    ENZ-620

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    Description

    KLK3 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 262 amino acids (25-261) and having a molecular mass of 28.8kDa.The KLK3 is fused to a 25 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    KLK3 protein solution (1mg/ml) is supplied in 20mM Tris-HCl buffer (pH8.0) and 0.4M Urea.

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      Kallikrein-3 (KLK3) belongs to the kallikrein-related peptidase family. Kallikreins are a subgroup of serine proteases having various physiological functions. Numerous kallikreins are involved in carcinogenesis and some may be prospective cancer and other disease biomarkers. Kallikrein-3 is 1 of the 15 kallikrein subfamily members located in a cluster on chromosome 19 and is a protease present in seminal plasma. KLK3 hydrolyzes semenogelin-1 consequently leading to the liquefaction of the seminal coagulum. KLK3 is assumed to act normally in the liquefaction of seminal coagulum, probably by hydrolysis of the high molecular mass seminal vesicle protein. Serum level of the KLK3 protein, called PSA in the clinical setting, is beneficial in the diagnosis and monitoring of prostatic carcinoma.

    • Synonyms

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

    • 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 MGSHMIVGGW ECEKHSQPWQ VLVASRGRAV CGGVLVHPQW VLTAAHCIRN KSVILLGRHS LFHPEDTGQV FQVSHSFPHP LYDMSLLKNR FLRPGDDSSH DLMLLRLSEP AELTDAVKVM DLPTQEPALG TTCYASGWGS IEPEEFLTPK KLQCVDLHVI SNDVCAQVHP QKVTKFMLCA GRWTGGKSTC SGDSGGPLVC NGVLQGITSW GSEPCALPER PSLYTKVVHY RKWIKDTIVA NP.

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    Klk3 Human
  • View Data Sheet

    Name :

    CDO1 Human

    Description:

    Cysteine Dioxygenase Human Recombinant

    Cysteine dioxygenase type 1, Cysteine dioxygenase type I, CDO-I, CDO, CDO1.

    Product # :

    ENZ-449

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    Description

    CDO1 Human Recombinant fused with a 37 amino acids His tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 207 amino acids (1-170 a.a.) and having a molecular mass of 23.9kDa.The CDO1 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The CDO1 solution contains 20mM Tris buffer(pH 8.0), 10% glycerol and 1mM DTT.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      CDO1 (Cysteine dioxygenase) is a mammalian non-heme iron enzyme that initiates a number of significant metabolic pathways associated with pyruvate and several sulfurate compounds including sulfate, hypotaurine and taurine. CDO1 catalyzes the conversion of L-cysteine to cysteine sulfinic acid (cysteine sulfinate) by incorporation of dioxygen. CDO1 is a vital regulator of cellular cysteine concentrations and has an essential role in maintaining the hepatic concentration of intracellular free cysteine within a proper narrow range. CDO1 is able to alter intracellular cysteine levels and glutathione levels. CDO1 is highly expressed in the liver and placenta. On the other hand CDO1 has a low expression in heart, brain and pancreas. CDO1 can also be detected in hepatoblastoma HepG2 cells.

    • Synonyms

      Cysteine dioxygenase type 1, Cysteine dioxygenase type I, CDO-I, CDO, CDO1.

    • 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

      MRGSHHHHHH GMASMTGGQQ MGRDLYDDDD KDRWGSHMEQ TEVLKPRTLA DLIRILHQLF AGDEVNVEEV QAIMEAYESD PTEWAMYAKF DQYRYTRNLV DQGNGKFNLM ILCWGEGHGS SIHDHTNSHC FLKMLQGNLK ETLFAWPDKK SNEMVKKSER VLRENQCAYI NDSVGLHRVE NISHTEPAVS LHLYSPPFDT CHAFDQR.

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    Cdo1 Human
  • View Data Sheet

    Name :

    GPT Human, Active

    Description:

    Glutamic-Pyruvate Transaminase Human Recombinant, Active

    Alanine aminotransferase 1, ALT1, EC 2.6.1.2, Glutamate pyruvate transaminase 1, GPT 1, Glutamic--alanine transaminase 1, Glutamic--pyruvic transaminase 1, GPT, AAT1, GPT1.

    Product # :

    ENZ-280

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    • description
    • source
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    Description

    Alanine Aminotransferase Human Recombinant produced in E.Coli is a homodimer, non-glycosylated, polypeptide chain containing 495a.a and having a molecular mass of 54,479 Dalton. The amino acid sequence is the same as that of native form of human liver ALT.The ALT is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The protein was dialyzed against 40mM sodium acetate buffer (pH 5.5), 1mM DTT,1mM EDTA, 5mM 2-oxoglutarate and 0.1mM pyridoxal-5'-phosphate.

    Purity

    Greater than 95.0% as determined by Analysis by SDS-PAGE.

    Biological Activity

    The specific activity was found to be 839 U/mg.

    Citations

    More Info

    • Introduction

      Alanine transaminase or ALT is a transaminaseenzyme.
      ALT is found in serumand in various bodily tissues, but is most commonly associated with the liver; It catalyzes the transfer of an aminogroup from alanineto a-ketoglutarate, the products of this reversible transaminationreaction being pyruvateand glutamatealanine+ a-ketoglutarate= pyruvate+ glutamate
      It is commonly measured clinically as a part of a diagnostic liver function test, to determine liver health. It is also called serum glutamate pyruvate transaminase (SGPT) or alanine aminotransferase (ALAT). Diagnostically, it is almost always measured in units/litre (U/L).

    • Synonyms

      Alanine aminotransferase 1, ALT1, EC 2.6.1.2, Glutamate pyruvate transaminase 1, GPT 1, Glutamic--alanine transaminase 1, Glutamic--pyruvic transaminase 1, GPT, AAT1, GPT1.

    • Physical Appearance

      Sterile liquid formulation.

    • Stability

      AAT1 although stable at 10°C for 5 days, should be stored below -18°C.Please prevent freeze-thaw cycles.

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

    Alanine Aminotransferase Human
  • View Data Sheet

    Name :

    UBE2R2 Human

    Description:

    Ubiquitin Conjugating Enzyme E2R 2 Human Recombinant

    CDC34B, E2-CDC34B, UBC3B, Ubiquitin carrier protein R2, Ubiquitin-conjugating enzyme E2-CDC34B, Ubiquitin-protein ligase R2, Ubiquitin-conjugating enzyme E2 R2, EC 6.3.2.19.

    Product # :

    ENZ-511

    Price :

    Quantity :

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    • description
    • source
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    Description

    UBE2R2 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 261 amino acids (1-238 a.a) and having a molecular mass of 29.6kDa (Molecular size on SDS-PAGE will appear higher).UBE2R2 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    UBE2R2 protein solution (0.25mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 20% glycerol and 1mM DTT.

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      Ubiquitin-conjugating enzyme E2 R2 (UBE2R2) is a member of the ubiquitin-conjugating enzyme family. Protein kinase CK2 is a ubiquitous and pleiotropic Ser/Thr protein kinase implicated in cell growth andtransformation. This protein is a protein similar to the E2 ubiquitin conjugating enzyme UBC3/CDC34. Studies propose that CK2-dependent phosphorylation of this ubiquitin-conjugating enzyme functions by regulating beta-TrCP substrate recognition and induces its interaction with beta-TrCP, enhancing beta-catenin degradation. UBE2R2 receives ubiquitin from the E1 complex and catalyzes its covalent attachment to other proteins. In vitro catalyzes monoubiquitination and 'Lys-48'-linked polyubiquitination. UBE2R2 may be implicated in degradation of katenin. Among the diseases associated with UBE2R2 are cblc, and herpes simplex.

    • Synonyms

      CDC34B, E2-CDC34B, UBC3B, Ubiquitin carrier protein R2, Ubiquitin-conjugating enzyme E2-CDC34B, Ubiquitin-protein ligase R2, Ubiquitin-conjugating enzyme E2 R2, 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. 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 MGSMAQQQMT SSQKALMLEL KSLQEEPVEG FRITLVDESD LYNWEVAIFG PPNTLYEGGY FKAHIKFPID YPYSPPTFRF LTKMWHPNIY ENGDVCISIL HPPVDDPQSG ELPSERWNPT QNVRTILLSV ISLLNEPNTF SPANVDASVM FRKWRDSKGK DKEYAEIIRK QVSATKAEAE KDGVKVPTTL AEYCIKTKVP SNDNSSDLLY DDLYDDDIDD EDEEEEDADC YDDDDSGNEE S

    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.

    Ube2R2 Human
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