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Search results

1000 results found for “Phosphatase”

Name

Description

Product #

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  • View Data Sheet

    Name :

    DARS Human

    Description:

    Aspartyl-tRNA Synthetase Human Recombinant

    Aspartyl-tRNA synthetase, Cell proliferation-inducing gene 40 protein, AspRS, aspartate tRNA ligase 1 cytoplasmic, EC 6.1.1.12.

    Product # :

    ENZ-591

    Price :

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    Description

    DARS Recombinant produced in E. coli is a single polypeptide chain containing 521 amino acids (1-501) and having a molecular mass of 59.3kDa.DARS is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    The DARS solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 150mM Nacl, 1mM DTT and 40% glycerol.

    Purity

    Greater than 85% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      DARS uses a 2 step reaction to catalyze the specific attachment of an amino acid to its cognate tRNA: the amino acid (AA) is first activated by ATP to form AA-AMP and then transferred to the acceptor end of the tRNA.

    • Synonyms

      Aspartyl-tRNA synthetase, Cell proliferation-inducing gene 40 protein, AspRS, aspartate tRNA ligase 1 cytoplasmic, EC 6.1.1.12.

    • 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 MPSASASRKS QEKPREIMDA AEDYAKERYG ISSMIQSQEK PDRVLVRVRD LTIQKADEVV WVRARVHTSR AKGKQCFLVL RQQQFNVQAL VAVGDHASKQ MVKFAANINK ESIVDVEGVV RKVNQKIGSC TQQDVELHVQ KIYVISLAEP RLPLQLDDAV RPEAEGEEEG RATVNQDTRL DNRVIDLRTS TSQAVFRLQS GICHLFRETL INKGFVEIQT PKIISAASEG GANVFTVSYF KNNAYLAQSP QLYKQMCICA DFEKVFSIGP VFRAEDSNTH RHLTEFVGLD IEMAFNYHYH EVMEEIADTM VQIFKGLQER FQTEIQTVNK QFPCEPFKFL EPTLRLEYCE ALAMLREAGV EMGDEDDLST PNEKLLGHLV KEKYDTDFYI LDKYPLAVRP FYTMPDPRNP KQSNSYDMFM RGEEILSGAQ RIHDPQLLTE RALHHGIDLE KIKAYIDSFR FGAPPHAGGG IGLERVTMLF LGLHNVRQTS MFPRDPKRLT P.

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

    Dars Human
  • View Data Sheet

    Name :

    ANSA E.coli

    Description:

    Cytoplasmic L-asparaginase I E.Coli Recombinant

    L-asparaginase 1, L-asparaginase I, L-ASNase I, L-asparagine amidohydrolase I, ansA, b1767, JW1756.

    Product # :

    ENZ-119

    Price :

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    Description

    ANSA produced in E.Coli is a single, non-glycosylated polypeptide chain containing 358 amino acids (1-338 a.a.) and having a molecular mass of 39.3kDa.ANSA is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The ANSA solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 10% glycerol and 2mM DTT.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      AnsA is a cytoplasmic asparaginase from E.coli involved in intracellular asparagine utilization. E.coli has 2 L-asparaginases: the cytoplasmic type I form (ansA) and the periplasmic type II form (ansB). AnsA (Type L asparaginase) is constitutively expressed and is obligatory for the growth of the bacteria on asparagine as the sole nitrogen source.

    • Synonyms

      L-asparaginase 1, L-asparaginase I, L-ASNase I, L-asparagine amidohydrolase I, ansA, b1767, JW1756.

    • 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 MQKKSIYVAY TGGTIGMQRS EQGYIPVSGH LQRQLALMPE FHRPEMPDFT IHEYTPLMDS SDMTPEDWQH IAEDIKAHYD DYDGFVILHG TDTMAYTASA LSFMLENLGK PVIVTGSQIP LAELRSDGQI NLLNALYVAA NYPINEVTLF FNNRLYRGNR TTKAHADGFD AFASPNLPPL LEAGIHIRRL NTPPAPHGEG ELIVHPITPQ PIGVVTIYPG ISADVVRNFL RQPVKALILR SYGVGNAPQN KAFLQELQEA SDRGIVVVNL TQCMSGKVNM GGYATGNALA HAGVIGGADM TVEATLTKLH YLLSQELDTE TIRKAMSQNL RGELTPDD.

    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.

    Ansa Ecoli
  • View Data Sheet

    Name :

    ATP1B2 Human

    Description:

    ATPaseTransporting Beta 2 Human Recombinant

    ATPase Na+/K+ Transporting Beta 2 Polypeptide, Sodium-Potassium ATPase Subunit Beta 2 (Non-Catalytic), Sodium/Potassium-Dependent ATPase Beta-2 Subunit, Sodium/Potassium-Transporting ATPase Beta-2 Chain, Adhesion Molecule On Glia, Na K-ATPase Beta-2 Polypeptide, Sodium Pump Subunit Beta-2, AMOG.

    Product # :

    PRO-1647

    Price :

    Quantity :

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    Description

    ATP1B2 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 246 amino acids (68-290) and having a molecular mass of 27.8kDa. ATP1B2 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The ATP1B2 solution contains 20mM Tris-HCl buffer (pH 8.0), 0.4M Urea and 10% glycerol.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      ATPaseTransporting Beta 2 (ATP1B2) is the non-catalytic component of the active enzyme, which catalyzes the hydrolysis of ATP coupled with the exchange of Na+ and K+ ions across the plasma membrane. The precise function of the beta-2 subunit is not known. The ATP1B2 protein is composed of 3 subunits: alpha (catalytic), beta and gamma.

    • Synonyms

      ATPase Na+/K+ Transporting Beta 2 Polypeptide, Sodium-Potassium ATPase Subunit Beta 2 (Non-Catalytic), Sodium/Potassium-Dependent ATPase Beta-2 Subunit, Sodium/Potassium-Transporting ATPase Beta-2 Chain, Adhesion Molecule On Glia, Na K-ATPase Beta-2 Polypeptide, Sodium Pump Subunit Beta-2, AMOG.

    • 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 MGSDHTPKYQ DRLATPGLMI RPKTENLDVI VNVSDTESWD QHVQKLNKFL EPYNDSIQAQ KNDVCRPGRY YEQPDNGVLN YPKRACQFNR TQLGNCSGIG DSTHYGYSTG QPCVFIKMNR VINFYAGANQ SMNVTCAGKR DEDAENLGNF VMFPANGNID LMYFPYYGKK FHVNYTQPLV AVKFLNVTPN VEVNVECRIN AANIATDDER DKFAGRVAFK LRINKT

    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.

    Atp1B2 Human
  • View Data Sheet

    Name :

    Placental Lactogen Bovine

    Description:

    Placental Lactogen Bovine Recombinant

    Chorionic Somatomammotropin Hormone 1, CSH1, CSB, CS-1, hCS-B, BPL, BPLP-I.

    Product # :

    CYT-511

    Price :

    Quantity :

    Shipping Method :

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

    Description

    Placental Lactogen Bovine Recombinant, is a single polypeptide chain containing 199 amino acids and an additional Ala at the N-terminus having a molecular mass of 23 kDa. Placental Lactogen Recombinant is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The protein was lyophilized from a concentrated (1mg/ml) solution with 0.02-0.03% NaHCO3.

    Purity

    Greater than 99.0% as determined by:
    (a) Analysis by SEC-HPLC.
    (b) Analysis by SDS-PAGE.

    Biological Activity

    Placental Lactogen Bovine is biologically active as evidenced by inducing proliferation of Nb2 cells.

    Citations

    More Info

    • Introduction

      Placental Lactogen is a polypeptide hormone that is produced by the Syncytiotrophoblasts of the Placenta, also known as chorionic somatomammotropin. It has both Growth Hormone and Prolactin activities on growth, lactation, and luteal steroid production. In women, placental lactogen secretion begins soon after implantation and increases to 1 g or more a day in late pregnancy. Placental lactogen is also an insulin antagonist.
      Placental Lactogen Bovine is also capable of activating human and other heterologous GH receptors but not ruminat GH receptors.

    • Synonyms

      Chorionic Somatomammotropin Hormone 1, CSH1, CSB, CS-1, hCS-B, BPL, BPLP-I.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Amino Acid Sequence

      The sequence of the first six N-terminal amino acids was determined and was found to be Ala-Glu-Asp-Tyr-Ala-Pro.

    • Protein content

      UV spectroscopy at 280 nm using the absorbency value of 0.86 as the extinction coefficient for a 0.1% (1mg/ml) solution at pH 8. This value is calculated by the DNAman computer analysis program of protein sequences.

    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.

    Placental Lactogen Bovine
  • View Data Sheet

    Name :

    GDA Human, His

    Description:

    Guanine Deaminase Human Recombinant, His Tag

    CYPIN, GUANASE, NEDASIN, Guanine aminase, Guanine aminohydrolase, GAH, p51-nedasin.

    Product # :

    ENZ-682

    Price :

    Quantity :

    Shipping Method :

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    Description

    GDA Human Recombinant produced in E. coli is a single polypeptide chain containing 477 amino acids (1-454) and having a molecular mass of 53kDa. GDA is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

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

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      GDA is a member of the ATZ/TRZ family and is in charge for the hydrolytic deamination of guanine. GDA takes part in microtubule assembly. Multiple transcript variants encoding different isoforms have been found for GDA.

    • Synonyms

      CYPIN, GUANASE, NEDASIN, Guanine aminase, Guanine aminohydrolase, GAH, p51-nedasin.

    • 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 MGSMCAAQMP PLAHIFRGTF VHSTWTCPME VLRDHLLGVS DSGKIVFLEE ASQQEKLAKE WCFKPCEIRE LSHHEFFMPG LVDTHIHASQ YSFAGSSIDL PLLEWLTKYT FPAEHRFQNI DFAEEVYTRV VRRTLKNGTT TACYFATIHT DSSLLLADIT DKFGQRAFVG KVCMDLNDTF PEYKETTEES IKETERFVSE MLQKNYSRVK PIVTPRFSLS CSETLMGELG NIAKTRDLHI QSHISENRDE VEAVKNLYPS YKNYTSVYDK NNLLTNKTVM AHGCYLSAEE LNVFHERGAS IAHCPNSNLS LSSGFLNVLE VLKHEVKIGL GTDVAGGYSY SMLDAIRRAV MVSNILLINK VNEKSLTLKE VFRLATLGGS QALGLDGEIG NFEVGKEFDA ILINPKASDS PIDLFYGDFF GDISEAVIQK FLYLGDDRNI EEVYVGGKQV VPFSSSV.

    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.

    Gda Human
  • View Data Sheet

    Name :

    GGH Human

    Description:

    Gamma-Glutamyl Hydrolase Human Recombinant

    Gamma-glutamyl hydrolase (conjugase, folylpolygammaglutamyl hydrolase), Gamma-Glu-X carboxypeptidase, gamma-glutamyl hydrolase, Conjugase, GH, EC 3.4.19.9.

    Product # :

    ENZ-242

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    Description

    GGH Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 315 amino acids (25-318) and having a molecular mass of 35.9kDa.GGH is fused to a 21 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

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

    Purity

    Greater than 95% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      GGH is a homodimeric protein which catalyzes the cleavage of the gamma-glutamyl chain of folylpoly-gamma-glutamyl substrates. GGH is a vital enzyme in folyl and antifolyl poly-gamma-glutamate metabolism and it has a significant part in the bioavailability of dietary pteroylpolyglutamates and in the metabolism of antifolates and pteroylpolyglutamates.

    • Synonyms

      Gamma-glutamyl hydrolase (conjugase, folylpolygammaglutamyl hydrolase), Gamma-Glu-X carboxypeptidase, gamma-glutamyl hydrolase, Conjugase, GH, EC 3.4.19.9.

    • 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 MRPHGDTAKK PIIGILMQKC RNKVMKNYGR YYIAASYVKY LESAGARVVP VRLDLTEKDY EILFKSINGI LFPGGSVDLR RSDYAKVAKI FYNLSIQSFD DGDYFPVWGT CLGFEELSLL ISGECLLTAT DTVDVAMPLN FTGGQLHSRM FQNFPTELLL SLAVEPLTAN FHKWSLSVKN FTMNEKLKKF FNVLTTNTDG KIEFISTMEG YKYPVYGVQW HPEKAPYEWK NLDGISHAPN AVKTAFYLAE FFVNEARKNN HHFKSESEEE KALIYQFSPI YTGNISSFQQ CYIFD

    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.

    Ggh Human
  • View Data Sheet

    Name :

    GIMAP6 Human

    Description:

    GTPase, IMAP Family Member 6 Human Recombinant

    GTPase IMAP Family Member 6, Immune Associated Nucleotide 2, Immune Associated Nucleotide 6, IAN6, IAN2, hIAN2, hIAN6.

    Product # :

    PRO-1628

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    Description

    GIMAP6 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 315 amino acids (1-292) and having a molecular mass of 35.0kDa.GIMAP6 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The GIMAP6 solution contains 20mM Tris-HCl buffer (pH 8.0), 0.2M NaCl, 1mM DTT and 30% glycerol.

    Purity

    Greater than 85% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      GIMAP6 is a member of the GTPases of immunity-associated proteins (GIMAP) family. GIMAP proteins contain GTP-binding and coiled-coil motifs, and may play roles in the regulation of cell survival. Decreased expression of this gene may play a role in non-small cell lung cancer. Alternatively spliced transcript variants encoding multiple isoforms have been observed for this gene, which is found in a cluster with seven additional GIMAP genes on the long arm of chromosome 7.

    • Synonyms

      GTPase IMAP Family Member 6, Immune Associated Nucleotide 2, Immune Associated Nucleotide 6, IAN6, IAN2, hIAN2, hIAN6.

    • 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 MGSMEEEEYE QIPQENPPEE LSQDPVLELS GGLREKEQKT PRRLRLILMG KTGSGKSATG NSILGRDVFE SKLSTRPVTK TSQRRSREWA GKELEVIDTP NILSPQVSPE VADAICQAIV LSAPGPHAVL LVTQLGRFTD EDQQVVRRLQ EVFGVGVLGH TILVFTRKED LAGGSLEDYV RETNNQALAW LDVTLARRHC GFNNRAQGEE QEAQLRELME KVEAIMWENE GDYYSNKAYQ YTQQNFRLKE LQERQVSQGQ GSEDVPGEES WLEGLSQIQK ESEEAHRCLL GKADL

    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.

    Gimap6 Human
  • View Data Sheet

    Name :

    PRKACB Human

    Description:

    Protein Kinase CAMP-Dependent Catalytic Beta Human Recombinant

    Protein Kinase CAMP-Dependent Catalytic Beta, PKA C-Beta, EC 2.7.11.11, PKACB, CAMP-Dependent Protein Kinase Catalytic Beta Subunit Isoform 4ab, CAMP-Dependent Protein Kinase Catalytic Subunit Beta, Protein Kinase A Catalytic Subunit Beta, EC 2.7.11, PRKACB.

    Product # :

    PKA-366

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    Description

    PRKACB Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 421 amino acids (1-398) and having a molecular mass of 48.6kDa. PRKACB is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

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

    Purity

    Greater than 80.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      Protein Kinase CAMP-Dependent Catalytic Beta (PRKACB) belongs to the Ser/Thr protein kinase family and is a catalytic subunit of cAMP-dependent protein kinase. cAMP is a signaling molecule imperative for various cellular functions. cAMP activates the cAMP-dependent protein kinase, which transduces the signal by way of phosphorylation of different target proteins. The inactive kinase holoenzyme is a tetramer composed of 2 regulatory and 2 catalytic subunits. cAMP triggers the dissociation of the inactive holoenzyme into a dimer of regulatory subunits bound to 4 cAMP and 2 free monomeric catalytic subunits. PRKACB mediates cAMP-dependent signaling initiated by receptor binding to GPCRs. PKA activation regulates various cellular processes such as cell proliferation, the cell cycle, differentiation and regulation of microtubule dynamics, chromatin condensation and decondensation, nuclear envelope disassembly and reassembly, in addition to regulation of intracellular transport mechanisms and ion flux. PRKACB regulates the abundance of compartmentalized pools of its regulatory subunits via phosphorylation of PJA2 which binds and ubiquitinates these subunits, leading to their consequent proteolysis.

    • Synonyms

      Protein Kinase CAMP-Dependent Catalytic Beta, PKA C-Beta, EC 2.7.11.11, PKACB, CAMP-Dependent Protein Kinase Catalytic Beta Subunit Isoform 4ab, CAMP-Dependent Protein Kinase Catalytic Subunit Beta, Protein Kinase A Catalytic Subunit Beta, EC 2.7.11, PRKACB.

    • 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 MGSMAAYREP PCNQYTGTTT ALQKLEGFAS RLFHRHSKGT AHDQKTALEN DSLHFSEHTA LWDRSMKEFL AKAKEDFLKK WENPTQNNAG LEDFERKKTL GTGSFGRVML VKHKATEQYY AMKILDKQKV VKLKQIEHTL NEKRILQAVN FPFLVRLEYA FKDNSNLYMV MEYVPGGEMF SHLRRIGRFS EPHARFYAAQ IVLTFEYLHS LDLIYRDLKP ENLLIDHQGY IQVTDFGFAK RVKGRTWTLC GTPEYLAPEI ILSKGYNKAV DWWALGVLIY EMAAGYPPFF ADQPIQIYEK IVSGKVRFPS HFSSDLKDLL RNLLQVDLTK RFGNLKNGVS DIKTHKWFAT TDWIAIYQRK VEAPFIPKFR GSGDTSNFDD YEEEDIRVSI TEKCAKEFGE F.

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    Prkacb Human
  • View Data Sheet

    Name :

    PSMD9 Human

    Description:

    Proteasome 26S Subunit, Non-ATPase 9 Human Recombinant

    p27, Rpn4, 26S proteasome non-ATPase regulatory subunit 9, 26S proteasome regulatory subunit p27, PSMD9.

    Product # :

    ENZ-666

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    Description

    PSMD9 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 246 amino acids (1-223) and having a molecular mass of 27.1kDa. PSMD9 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The PSMD9 solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 10% glycerol and 1mM DTT.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      PSMD9 is a multicatalytic proteinase complex with a highly ordered structure composed of 2 complexes, a 20S core and a 19S regulator. PSMD9 acts as a chaperone through the assembly of the 26S proteasome, specifically of the base subcomplex of the PA700/19S regulatory complex (RC). During the base subcomplex compilation, PSMD9 is part of an intermediate PSMD9:PSMC6:PSMC3 module, also called modulator trimer complex. PSMD9 is released during the further base assembly process.

    • Synonyms

      p27, Rpn4, 26S proteasome non-ATPase regulatory subunit 9, 26S proteasome regulatory subunit p27, PSMD9.

    • 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 MGSMSDEEAR QSGGSSQAGV VTVSDVQELM RRKEEIEAQI KANYDVLESQ KGIGMNEPLV DCEGYPRSDV DLYQVRTARH NIICLQNDHK AVMKQVEEAL HQLHARDKEK QARDMAEAHK EAMSRKLGQS ESQGPPRAFA KVNSISPGSP ASIAGLQVDD EIVEFGSVNT QNFQSLHNIG SVVQHSEGKP LNVTVIRRGE KHQLRLVPTR WAGKGLLGCN IIPLQR.

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    Psmd9 Human
  • View Data Sheet

    Name :

    REV1 Human

    Description:

    REV1 Polymerase Human Recombinant

    REV1 Polymerase (DNA Directed), REV1L, Alpha Integrin-Binding Protein 80, Rev1-Like Terminal Deoxycytidyl Transferase, AIBP80, REV1 (Yeast Homolog)- Like, REV1 Homolog (S. Cerevisiae) , REV1-Like (Yeast) , DNA Repair Protein REV1, REV1 Homolog, REV1- Like, EC 2.7.7.-.

    Product # :

    ENZ-796

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    Description

    REV1 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 227 amino acids (51-256) and having a molecular mass of 25.2kDa.REV1 is fused to a 21 amino acid His-tag at N-terminus.

    Source

    Escherichia Coli.

    Formulation

    The REV1 solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.4M Urea and 10% glycerol.

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      REV1 Polymerase (REV1) contains a BRCT domain, which is imperative in protein-protein interactions. REV1 is a deoxycytidyl transferase involved in DNA repair. REV1 assists in the 1st step in the bypass of abasic lesions by the incorporation of a nucleotide opposite the lesion. REV1 is essential for normal generation of mutations by physical and chemical agents. REV1 transfers a dCMP residue from dCTP to the 3'-end of a DNA primer in a template-dependent reaction. A role for the human Rev1-like protein has been suggested as a scaffold which recruits DNA polymerases involved in translesion synthesis (TLS) of damaged DNA.

    • Synonyms

      REV1 Polymerase (DNA Directed), REV1L, Alpha Integrin-Binding Protein 80, Rev1-Like Terminal Deoxycytidyl Transferase, AIBP80, REV1 (Yeast Homolog)- Like, REV1 Homolog (S. Cerevisiae) , REV1-Like (Yeast) , DNA Repair Protein REV1, REV1 Homolog, REV1- Like, EC 2.7.7.-.

    • 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 MGVAIYVNGY TDPSAEELRK LMMLHGGQYH VYYSRSKTTH IIATNLPNAK IKELKGEKVI RPEWIVESIK AGRLLSYIPY QLYTKQSSVQ KGLSFNPVCR PEDPLPGPSN IAKQLNNRVN HIVKKIETEN EVKVNGMNSW NEEDENNDFS FVDLEQTSPG RKQNGIPHPR GSTAIFNGHT PSSNGALKTQ DCLVPMVNSV ASRLSPA.

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    Rev1 Human
  • View Data Sheet

    Name :

    SORD Human, His

    Description:

    Sorbitol Dehydrogenase Human Recombinant, His Tag

    EC 1.1.1.14, SORD1,SORD, L-iditol 2-dehydrogenase, DHSO, Sorbitol Dehydrogenase.

    Product # :

    ENZ-520

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    Description

    SORD Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 377 amino acids (1-357 a.a.) and having a molecular mass of 40.4 kDa. SORD protein is fused to a 20 amino acid His tag at N-terminus and is purified by standard chromatography.

    Source

    Escherichia Coli.

    Formulation

    SORD protein solution (0.5mg/ml) is formulated in 20mM Tris-HCl pH-8, 0.2M NaCl, 5mM DTT & 20% glycerol.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    Biological Activity

    Specific activity is > 0.2 units/mg, in which one unit will convert 1.0 umole of D-fructose to D-sorbitol per minute at pH 7.5 at 25°C.

    Citations

    More Info

    • Introduction

      SORD enzyme is part of of the zinc-containing alcohol dehydrogenase family that is broadly expressed in kidney and in the lens eye. SORD enzymatically catalyzes the zinc-dependent interconversion of polyols, such as sorbitol and xylitol, to their respective ketoses.

    • Synonyms

      EC 1.1.1.14, SORD1,SORD, L-iditol 2-dehydrogenase, DHSO, Sorbitol Dehydrogenase.

    • 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 MAAAAKPNNL SLVVHGPGDL RLENYPIPEP GPNEVLLRMH SVGICGSDVH YWEYGRIGNF IVKKPMVLGH EASGTVEKVG SSVKHLKPGD RVAIEPGAPR ENDEFCKMGR YNLSPSIFFC ATPPDDGNLC RFYKHNAAFC YKLPDNVTFE EGALIEPLSV GIHACRRGGV TLGHKVLVCG AGPIGMVTLL VAKAMGAAQV VVTDLSATRL SKAKEIGADL VLQISKESPQ EIARKVEGQL GCKPEVTIEC TGAEASIQAG IYATRSGGTL VLVGLGSEMT TVPLLHAAIR EVDIKGVFRY CNTWPVAISM LASKSVNVKP LVTHRFPLEK ALEAFETFKK GLGLKIMLKC DPSDQNP.

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    Sord Human
  • View Data Sheet

    Name :

    Cyclophilin B Mouse

    Description:

    Cyclophilin-B Mouse Recombinant

    Peptidyl-prolyl cis-trans isomerase B, PPIase B, CYP-S1, Cyclophilin B, Rotamase B, S-cyclophilin, SCYLP.

    Product # :

    ENZ-1039

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    Description

    Cyclophilin B Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 207 amino acids (34-216 a.a) and having a molecular mass of 22.7kDa.Cyclophilin B is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

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

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Biological Activity

    Specific activity is > 1,000 nmol/min/mg, and is defined as the amount of enzyme that cleaves 1nmole of suc-AAFP-PNA per minute at 37C in Tris–HCl pH 8.0 using chymotrypsin.

    Citations

    More Info

    • Introduction

      Cyclophilin B (also known as PPIB, peptidylpropyl isomerase B) is a cyclosporine-binding protein and is mainly located within the endoplasmic reticulum. It is associated with the secretory pathway and released in biological fluids. This protein can bind to cells derived from T- and B-lymphocytes, and may regulate cyclosporine A-mediated immunosuppression.

    • Synonyms

      Peptidyl-prolyl cis-trans isomerase B, PPIase B, CYP-S1, Cyclophilin B, Rotamase B, S-cyclophilin, SCYLP.

    • 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 MGSMNDKKKG PKVTVKVYFD LQIGDESVGR VVFGLFGKTV PKTVDNFVAL ATGEKGFGYK NSKFHRVIKD FMIQGGDFTR GDGTGGKSIY GERFPDENFK LKHYGPGWVS MANAGKDTNG SQFFITTVKT SWLDGKHVVF GKVLEGMDVV RKVESTKTDS
      RDKPLKDVII VDSGKIEVEK PFAIAKE.

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    Cyclophilin B Mouse
  • View Data Sheet

    Name :

    AK5 Human

    Description:

    Adenylate Kinase 5 Human Recombinant

    Adenylate kinase isoenzyme 5, AK 5, ATP-AMP transphosphorylase 5, AK5, AK6.

    Product # :

    PKA-011

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    Description

    AK5 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 586 amino acids (1-562 a.a.) and having a molecular mass of 65.9kDa.AK5 is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    AK5 protein solution (0.25mg/ml) containing 20mM Tris-HCl buffer (pH8.0), 20% glycerol and 1mM DTT.

    Purity

    Greater than 85% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      Adenylate kinase isoenzyme 5 (AK5) belongs to the adenylate kinase family, which is involved in regulating the adenine nucleotide composition within a cell by catalyzing the reversible transfer of phosphate groups among adenine nucleotides. AK5 is related to the UMP/CMP kinase of several species. AK5 is located in the cytosol and expressed exclusively in the brain.

    • Synonyms

      Adenylate kinase isoenzyme 5, AK 5, ATP-AMP transphosphorylase 5, AK5, AK6.

    • 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 MGSHMNTNDA KEYMARREIP QLFESLLNGL MCSKPEDPVE YLESCLQKVK ELGGCDKVKW DTFVSQEKKT LPPLNGGQSR RSFLRNVMPG NSNFPYRRYD RLPPIHQFSI ESDTDLSETA ELIEEYEVFD PTRPRPKIIL VIGGPGSGKG TQSLKIAERY GFQYISVGEL LRKKIHSTSS NRKWSLIAKI ITTGELAPQE TTITEIKQKL MQIPDEEGIV IDGFPRDVAQ ALSFEDQICT PDLVVFLACA NQRLKERLLK RAEQQGRPDD NVKATQRRLM NFKQNAAPLV KYFQEKGLIM TFDADRDEDE VFYDISMAVD NKLFPNKEAA AGSSDLDPSM ILDTGEIIDT GSDYEDQGDD QLNVFGEDTM GGFMEDLRKC KIIFIIGGPG SGKGTQCEKL VEKYGFTHLS TGELLREELA SESERSKLIR DIMERGDLVP SGIVLELLKE AMVASLGDTR GFLIDGYPRE VKQGEEFGRR IGDPQLVICM DCSADTMTNR LLQRSRSSLP VDDTTKTIAK RLEAYYRASI PVIAYYETKT QLHKINAEGT PEDVFLQLCT AIDSIF.

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    Ak5 Human
  • View Data Sheet

    Name :

    IDO1 Human, Active

    Description:

    Indoleamine 2,3-Dioxygenase 1 Human Recombinant, Active

    IDO, IDO-1, INDO, Indoleamine 2,3-dioxygenase 1, Indoleamine-pyrrole 2,3-dioxygenase.

    Product # :

    ENZ-1012

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    Description

    IDO1 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 426 amino acids (1-403a.a) and having a molecular mass of 47.7kDa. IDO1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The IDO1 solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 20% glycerol and 1mM DTT.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    Biological Activity

    Specific activity is > 300 pmol/min/ug, and is defined as the amount of enzyme that hydrolyze 1.0 pmole of L-Tryptophan to N-formyl-Lkynurenine per minute at pH 6.5 at 25C.

    Citations

    More Info

    • Introduction

      Indoleamine 2,3-Dioxygenase 1 (IDO1) catalyzes the primary and rate-limiting stage in tryptophan catabolism to N-formyl-kynurenine. IDO1 affects on various tryptophan substrates including D-tryptophan, and serotonin and is expressed in dendritic cells, monocytes, and macrophages. IDO1 takes part in a range of pathophysiological processes like neuropathology, antimicrobial and antitumor defense, immunoregulation, and antioxidant activity. IDO1 regulates T-cell behavior by its pericellular catabolization of the necessary amino acid tryptophan.

    • Synonyms

      IDO, IDO-1, INDO, Indoleamine 2,3-dioxygenase 1, Indoleamine-pyrrole 2,3-dioxygenase.

    • 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 MGSMAHAMEN SWTISKEYHI DEEVGFALPN PQENLPDFYN DWMFIAKHLP DLIESGQLRE RVEKLNMLSI DHLTDHKSQR LARLVLGCIT MAYVWGKGHG DVRKVLPRNI AVPYCQLSKK LELPPILVYA DCVLANWKKK DPNKPLTYEN MDVLFSFRDG DCSKGFFLVS LLVEIAAASA IKVIPTVFKA MQMQERDTLL KALLEIASCL EKALQVFHQI HDHVNPKAFF SVLRIYLSGW KGNPQLSDGL VYEGFWEDPK EFAGGSAGQS SVFQCFDVLL GIQQTAGGGH AAQFLQDMRR YMPPAHRNFL CSLESNPSVR EFVLSKGDAG LREAYDACVK ALVSLRSYHL QIVTKYILIP ASQQPKENKT SEDPSKLEAK GTGGTDLMNF LKTVRSTTEK SLLKEG.

    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.

    Ido1 Human Active
  • View Data Sheet

    Name :

    STAT1 Human

    Description:

    Signal Transducer and Activator of Transcription 1 Human Recombinant

    Signal transducer and activator of transcription 1-alpha/beta, Transcription factor ISGF-3 components p91/p84, STAT1, ISGF-3, STAT91, DKFZp686B04100.

    Product # :

    PKA-315

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    Description

    STAT1 Recombinant Human produced in E.Coli is a single, non-glycosylated polypeptide chain containing 732 amino acids (1-712 a.a.) and having a molecular mass of 85.2 kDa. The STAT1 is fused to a 20 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    STAT1 0.5mg/ml protein solution contains 20mM Tris-HCl buffer pH-8, 0.1M NaCl, 1mM DTT and 10% glycerol.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      STAT1 is a member of the Signal Transducers and Activators of Transcriptionfamily of transcription factors. STAT1 is involved in upregulating genes due to a signal by either type Ior type IIinterferons. In response to IFN-?stimulation, STAT1 forms homodimers or heterodimers with STAT3that bind to the GAS (Interferon-Gamma Activated Sequence) promoter element; in response to either IFN-? or IFN-?stimulation, STAT1 forms a heterodimer with STAT2that can bind the ISRE (Interferon Stimulated Response Element) promoter element. In either case, binding of the promoter element leads to an increased expression of ISG (Interferon Stimulated Genes).

    • Synonyms

      Signal transducer and activator of transcription 1-alpha/beta, Transcription factor ISGF-3 components p91/p84, STAT1, ISGF-3, STAT91, DKFZp686B04100.

    • 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 MSQWYELQQL DSKFLEQVHQ LYDDSFPMEI RQYLAQWLEK QDWEHAANDV SFATIRFHDL LSQLDDQYSR FSLENNFLLQ HNIRKSKRNL QDNFQEDPIQ MSMIIYSCLK EERKILENAQ RFNQAQSGNI QSTVMLDKQK ELDSKVRNVK DKVMCIEHEI KSLEDLQDEY DFKCKTLQNR EHETNGVAKS DQKQEQLLLK KMYLMLDNKR KEVVHKIIEL LNVTELTQNA LINDELVEWK RRQQSACIGG PPNACLDQLQ NWFTIVAESL QQVRQQLKKL EELEQKYTYE HDPITKNKQV LWDRTFSLFQ QLIQSSFVVE RQPCMPTHPQ RPLVLKTGVQ FTVKLRLLVK LQELNYNLKV KVLFDKDVNE RNTVKGFRKF NILGTHTKVM NMEESTNGSL AAEFRHLQLK EQKNAGTRTN EGPLIVTEEL HSLSFETQLC QPGLVIDLET TSLPVVVISN VSQLPSGWAS ILWYNMLVAE PRNLSFFLTP PCARWAQLSE VLSWQFSSVT KRGLNVDQLN MLGEKLLGPN ASPDGLIPWT RFCKENINDK NFPFWLWIES ILELIKKHLL PLWNDGCIMG FISKERERAL LKDQQPGTFL LRFSESSREG AITFTWVERS QNGGEPDFHA VEPYTKKELS AVTFPDIIRN YKVMAAENIP ENPLKYLYPN IDKDHAFGKY YSRPKEAPEP MELDGPKGTG YIKTELISVS EV.

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    Stat1 Human
  • View Data Sheet

    Name :

    STIP1 Human, His

    Description:

    Stress-Induced-Phosphoprotein 1 Human Recombinant, His Tag

    HOP, P60, STI1, STI1L, IEF-SSP-3521, STIP1, Stress-induced-phosphoprotein 1, Hsc70/Hsp90-organizing protein, Transformation-sensitive protein IEF SSP 3521, Renal carcinoma antigen NY-REN-11.

    Product # :

    PRO-753

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    Description

    Recombinant Human STIP1 produced in E.Coli is a single, non-glycosylated polypeptide chain containing 563 amino acids (1-543 a.a) and having a molecular mass of 64.8kDa. STIP1 is fused to a 20 amino acid His-Tag at N-terminus and purified by conventional chromatography techniques.

    Source

    Escherichia Coli.

    Formulation

    The STIP1 protein solution (1mg/ml) contains 20mM Tris-HCl, pH-8, 1mM DTT, 1mM EDTA, 0.2mM PMSF and 20% Glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      STIP1 is an adaptor protein that mediates the functions of HSP70 & HSP90 in protein folding. STIP1 supports the transfer of proteins from HSP70 to HSP90 by binding together HSP90 and substrate-bound HSP70. STIP1 stimulates the ATPase activity of HSP70 and inhibits the ATPase activity of HSP90, suggesting that it regulates both the conformations and ATPase cycles of these chaperones. STIP1 genetic variations are involved in regulating corticosteroid response in asthmatic subjects with reduced lung function.

    • Synonyms

      HOP, P60, STI1, STI1L, IEF-SSP-3521, STIP1, Stress-induced-phosphoprotein 1, Hsc70/Hsp90-organizing protein, Transformation-sensitive protein IEF SSP 3521, Renal carcinoma antigen NY-REN-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

      MGSSHHHHHH SSGLVPRGSH MEQVNELKEK GNKALSVGNI DDALQCYSEA IKLDPHNHVL YSNRSAAYAK KGDYQKAYED GCKTVDLKPDWGKGYSRKAA ALEFLNRFEE AKRTYEEGLK HEANNPQLKE GLQNMEARLA ERKFMNPFNM PNLYQKLESD PRTRTLLSDP TYRELIEQLRNKPSDLGTKL QDPRIMTTLS VLLGVDLGSM DEEEEIATPP PPPPPKKETK PEPMEEDLPE NKKQALKEKE LGNDAYKKKD FDTALKHYDKAKELDPTNMT YITNQAAVYF EKGDYNKCRE LCEKAIEVGR ENREDYRQIA KAYARIGNSY FKEEKYKDAI HFYNKSLAEH TPDVLKKCQQAEKILKEQE RLAYINPDLA LEEKNKGNEC FQKGDYPQAM KHYTEAIKRN PKDAKLYSNR AACYTKLLEF QLALKDCEEC QLEPTFIKGYTRKAAALEA MKDYTKAMDV YQKALDLDSS CKEAADGYQR CMMAQYNRHD SPEDVKRRAM ADPEVQQIMS DPAMRLILEQ MQKDPQALSE HLKNPVIAQK IQKLMDVGLI AIR.

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    Stip1 Human
  • View Data Sheet

    Name :

    CA1 Human, Active

    Description:

    Carbonic Anhydrase-1 Human Recombinant, BioActive

    CA1, CA-I, CAB.

    Product # :

    ENZ-1137

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    Description

    CA1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 281 amino acids (1-261) and having a molecular mass of 31.0 kDa. CA1 Humanis fused to a 20 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    CA1 Human protein (1mg/ml) is formulated in 20mM Tris-HCl buffer (pH 8.0) containing 1mM DTT, 10% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Biological Activity

    Specific activity is > 300pmol/min/ug, and is defined as the amount of enzyme that hydrolyze 1.0pmole of 4-nitrophenyl acetate to 4-nitrophenol per minute at pH 8.0 at 37C.

    Citations

    More Info

    • Introduction

      CA, also known as carbonic anhydrase is an enzyme. Its main function revolves around the CO2 + H2O HCO3- + H+ (conversion of carbon dioxide to bicarbonate & protons). CA has a zinc ion in its active site. The main function of CA is to keep acid-base balance in the blood stream and various tissues. This enzyme also assists Carbonic Anhydrase I to move CO2 to and from tissues.

    • Synonyms

      CA1, CA-I, CAB.

    • 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 MASPDWGYDD KNGPEQWSKL YPIANGNNQS PVDIKTSETK HDTSLKPISV SYNPATAKEI INVGHSFHVN FEDNDNRSVL KGGPFSDSYR LFQFHFHWGS TNEHGSEHTV DGVKYSAELH VAHWNSAKYS SLAEAASKAD GLAVIGVLMK VGEANPKLQK VLDALQAIKT KGKRAPFTNF DPSTLLPSSL DFWTYPGSLT HPPLYESVTW IICKESISVS SEQLAQFRSL LSNVEGDNAV PMQHNNRPTQ PLKGRTVRAS F.

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    Ca1 Enzyme
  • View Data Sheet

    Name :

    CAIII Human, His

    Description:

    Carbonic Anhydrase III Human Recombinant, His Tag

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

    Product # :

    ENZ-270

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    Description

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

    Source

    Escherichia Coli.

    Formulation

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

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

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

    • Synonyms

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

    • Physical Appearance

      Sterile Filtered blue solution.

    • Stability

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

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    Caiii Human
  • View Data Sheet

    Name :

    TK2 Human

    Description:

    Thymidine Kinase 2 Human Recombinant

    Thymidine kinase 2 mitochondrial, Mt-TK, TK2, MTTK, MTDPS2.

    Product # :

    PKA-041

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    Description

    TK2 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 257 amino acids (34-265 a.a) and having a molecular mass of 30.2kDa.TK2 is fused to a 25 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    TK2 protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer, pH8.0, 30% glycerol, 2mM DTT and 200mM NaCl.

    Purity

    Greater than 85% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      Thymidine kinase 2 mitochondrial (TK2) is a member of the DCK/DGK family. TK2 is an enzyme, a phosphotransferase (a kinase): 2'-deoxythymidine kinase, ATP-thymidine 5'-phosphotransferase. Thymidine kinase is found in most living cells. Thymidine kinase is present in 2 forms in mammalian cells, TK1 and TK2. Thymidine kinases have a central function in the synthesis of DNA and thus in cell division, since they are part of the exceptional reaction chain to introduce deoxythymidine into the DNA. TK2 is a deoxyribonucleoside kinase which specifically phosphorylates thymidine, deoxycytidine, and deoxyuridine. TK2 localizes to the mitochondria and is essential for mitochondrial DNA synthesis. TK2 gene defects are a cause of mitochondrial DNA depletion syndrome type 2 (MTDPS2).

    • Synonyms

      Thymidine kinase 2 mitochondrial, Mt-TK, TK2, MTTK, MTDPS2.

    • 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 MGSHMVQRRA WPPDKEQEKE KKSVICVEGN IASGKTTCLE FFSNATDVEV LTEPVSKWRN VRGHNPLGLM YHDASRWGLT LQTYVQLTML DRHTRPQVSS VRLMERSIHS ARYIFVENLY RSGKMPEVDY VVLSEWFDWI LRNMDVSVDL IVYLRTNPET CYQRLKKRCR EEEKVIPLEY LEAIHHLHEE WLIKGSLFPM AAPVLVIEAD HHMERMLELF EQNRDRILTP ENRKHCP.

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    Tk2 Human
  • View Data Sheet

    Name :

    CES2E Mouse

    Description:

    Carboxylesterase 2E Mouse Recombinant

    9030624L02Rik, Ces5, Ces2e.

    Product # :

    ENZ-1141

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    Description

    CES2E Mouse produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 541 amino acids ( 27-559 aa) and having a molecular mass of 60.5kDa.CES2E is fused to a 8 amino acid His tag at C-terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    The CES2E solution (0.25 mg/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 > 30unit/mg, and is defined as the amount of enzyme that hydrolyze 1.0 umole of pnitrophenyl acetate to p-nitrophenol per minute at pH 7.5 at 25C˚.

    Citations

    More Info

    • Introduction

      Carboxylesterase 2E or CES2E is an enzyme that hydrolyzes various carboxylic acid esters. This enzyme can be found mainly in mammalian liver cells. CES2E is taking part in chemical reactions, especially in carboxylic ester and water catalyzation to alcohol & carboxylate.

    • Synonyms

      9030624L02Rik, Ces5, Ces2e.

    • 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

      QDSASPIRNT HTGQVRGSLV HVKDTDIAVH TFLGIPFAKP PVGPLRFAPP EAPEPWSGVR DGTSHPNMCL QNDNLMGSED LKMMNLILPP ISMSEDCLYL NIYVPAHAHE GSNLPVMVWI HGGALTVGMA SMYDGSMLAA TEDVVVVAIQ YRLGVLGFFS TGDQHAKGNW GYLDQVAALR WVQQNIVHFG GNPDRVTIFG ESAGGTSVSS HVVSPMSQGL FHGAIMESGV AVLPDLISSS
      SEMVHRIVAN LSGCAAVNSE TLMCCLRGKN EAEMLAINKV FKIIPGVVDG EFLPKHPQEL MASKDFHPVP SIIGINNDEY GWILPTIMDP AQKIEEITRK TLPAVLKSTA LKMMLPPECG DLLMEEYMGD TEDPETLQAQ FREMKGDFMF VIPALQVAHF QRSHAPVYFY EFQHRPSFFK DFRPPYVKAD HGDEIFLVFG YQFGNIKLPY TEEEEQLSRR IMKYWANFAR HGNPNSEGLP YWPVMDHDEQ YLQLDIQPSV GRALKARRLQ FWTKTLPQKI QELKGSQERH KELLEHHHHH H

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    Ces2E Mouse
  • View Data Sheet

    Name :

    MAT1A Human

    Description:

    Methionine Adenosyltransferase I Alpha Human Recombinant

    EC 2.5.1.6, MAT, MATA1, SAMS, SAMS1, Methionine adenosyltransferase 1, S-adenosylmethionine synthase isoform type-1, AdoMet synthase 1, MAT 1, Methionine adenosyltransferase I/III, MAT-I/III, MAT1A, AMS1.

    Product # :

    ENZ-493

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    Description

    MAT1A Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 414 amino acids (1-395 a.a.) and having a molecular mass of 45.6 kDa. The MAT1A is fused to a 20 amino acid his tag at N-terminus and purified by conventional chromatography.

    Source

    Escherichia Coli.

    Formulation

    The MAT1A protein solution contains 20mM Tris-HCl pH-8, 1mM DTT, 100mM NaCl and 10% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      MAT1A catalyzes a two-step reaction that involves the transfer of the adenosyl moiety of ATP to methionine to form S-adenosylmethionine and tripolyphosphate, which is subsequently cleaved to PPi and Pi. S-adenosylmethionine is the source of methyl groups for most biological methylations. MAT1A is found as a homotetramer (MAT I) or a homodimer (MAT III) whereas a third form, MAT II (gamma), is encoded by the MAT2A gene. Mutations in MAT1A gene are associated with methionine adenosyltransferase deficiency. MAT1A expression also correlates with a differentiated phenotype, whereas liver cells expressing MAT2A present a dedifferentiated phenotype and lowered AdoMet synthesis. Likewise, NFκB and TNFα cause a switch from MAT1A to MAT2A expression in human hepatocellular carcinoma (HCC), which facilitates cancer cell growth.

    • Synonyms

      EC 2.5.1.6, MAT, MATA1, SAMS, SAMS1, Methionine adenosyltransferase 1, S-adenosylmethionine synthase isoform type-1, AdoMet synthase 1, MAT 1, Methionine adenosyltransferase I/III, MAT-I/III, MAT1A, AMS1.

    • 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

      MGSSHHHHHS SGLVPRGSHM NGPVDGLCDH SLSEGVFMFT SESVGEGHPD KICDQISDAV LDAHLKQDPN AKVACETVCK TGMVLLCGEI TSMAMVDYQR VVRDTIKHIG YDDSAKGFDF KTCNVLVALE QQSPDIAQCV HLDRNEEDVG AGDQGLMFGY ATDETEECMP LTIILAHKLN ARMADLRRSG LLPWLRPDSK TQVTVQYMQD NGAVIPVRIH TIVISVQHNE DITLEEMRRA LKEQVIRAVV PAKYLDEDTV YHLQPSGRFV IGGPQGDAGV TGRKIIVDTY GGWGAHGGGA FSGKDYTKVD RSAAYAARWV AKSLVKAGLC RRVLVQVSYA IGVAEPLSIS IFTYGTSQKT ERELLDVVHK NFDLRPGVIV RDLDLKKPIY QKTACYGHFG RSEFPWEVPR KLVF.

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    Mat1A Human
  • View Data Sheet

    Name :

    NQO1 Human, Active

    Description:

    NAD(P)H Dehydrogenase Quinone 1, Active 1 Human Recombinant

    NAD(P)H dehydrogenase (quinone) 1, Quinone reductase 1, QR1, NAD(P)H:quinone oxidoreductase 1, DT-diaphorase, DTD, Azoreductase, Phylloquinone reductase, Menadione reductase, NQO1, DIA4, NMOR1, DHQU, NMORI.

    Product # :

    ENZ-1107

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    Description

    NQO1 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 294 amino acids ( 1-274aa ) and having a molecular mass of 33.0 kDa. NQO1 is fused to a 20 amino acid His tag at N-terminus and purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The NQO1 solution (1 mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 1mM DTT and 10% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Biological Activity

    Specific activity is > 1,000 pmol/min/ug. One unit will convert 1 pmoles resazurin to resorufin per minute at pH 7.5 at 25°C.

    Citations

    More Info

    • Introduction

      NQO1 belongs to the NAD(P)H dehydrogenase (quinone) family and encodes a cytoplasmic 2-electron reductase. NQO1 acts as an imperative part of cellular antioxidant defense by detoxifying quinines therefore preventing the formation of reactive oxygen species. It seems that NQO1 serves as a quinone reductase relating to conjugation reactions of hydroquinons involved in detoxification pathways in addition to biosynthetic processes such as the vitamin K-dependent gamma-carboxylation of glutamate residues in prothrombin synthesis. Altered NQO1 expression is seen in many tumors and also linked to Alzheimer’s disease. NQO1 gene mutations are linked to tardive dyskinesia which is an increased risk of hematotoxicity after exposure to benzene, and susceptibility to various forms of cancer.

    • Synonyms

      NAD(P)H dehydrogenase (quinone) 1, Quinone reductase 1, QR1, NAD(P)H:quinone oxidoreductase 1, DT-diaphorase, DTD, Azoreductase, Phylloquinone reductase, Menadione reductase, NQO1, DIA4, NMOR1, DHQU, NMORI.

    • 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 MVGRRALIVL AHSERTSFNY AMKEAAAAAL KKKGWEVVES
      DLYAMNFNPI ISRKDITGKL KDPANFQYPA ESVLAYKEGH LSPDIVAEQK KLEAADLVIF
      QFPLQWFGVP AILKGWFERV FIGEFAYTYA AMYDKGPFRS KKAVLSITTG GSGSMYSLQG
      IHGDMNVILW PIQSGILHFC GFQVLEPQLT YSIGHTPADA RIQILEGWKK RLENIWDETP
      LYFAPSSLFD LNFQAGFLMK KEVQDEEKNK KFGLSVGHHL GKSIPTDNQI KARK

    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.

    Nqo1 Enzyme
  • View Data Sheet

    Name :

    POR Human, Active

    Description:

    P450 Oxidoreductase Human Recombinant, Active

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

    Product # :

    ENZ-1176

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

    Description

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

    Source

    Sf9, Baculovirus cells.

    Formulation

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

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Biological Activity

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

    Citations

    More Info

    • Introduction

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

    • Synonyms

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

    • Physical Appearance

      Sterile filtered colorless solution.

    • Stability

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

    • Amino Acid Sequence

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

    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.

    Por Enzyme
  • View Data Sheet

    Name :

    ACY3 Human

    Description:

    AminoAcylase-3 Human Recombinant

    Aspartoacylase-2, Acylase III, Aminoacylase-3, ACY-3, Hepatitis C virus core-binding protein 1, HCBP1, ACY3, ASPA2.

    Product # :

    ENZ-153

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    • description
    • source
    • formulation
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    • Citations

    Description

    ACY3 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 342 amino acids (1-319 a.a.) and having a molecular mass of 37.6kDa.ACY3 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    ACY3 protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 1mM DTT, 10% glycerol and 0.1M NaCl.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      Aspartoacylase 3 (ACY3) belongs to the Aspartoacylase subfamily. ACY3 has a vital role in deacetylating mercapturic acids in kidney proximal tubules. Aspartoacylase 3 localizes to the cytoplasm of S2 and S3 proximal tubules and also to the apical domain of S1 proximal tubules. In addition, ACY3 protein is expressed at low levels in the stomach, testis, heart, brain, lung and liver, and can function as an HCV (Hepatitis C virus) core binding protein.

    • Synonyms

      Aspartoacylase-2, Acylase III, Aminoacylase-3, ACY-3, Hepatitis C virus core-binding protein 1, HCBP1, ACY3, ASPA2.

    • 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 MGSMCSLPVP REPLRRVAVT GGTHGNEMSG VYLARHWLHA PAELQRASFS AVPVLANPAA TSGCRRYVDHDLNRTFTSSF LNSRPTPDDP YEVTRARELN QLLGPKASGQ AFDFVLDLHN TTANMGTCLI AKSSHEVFAM HLCRHLQLQY PELSCQVFLY QRSGEESYNL DSVAKNGLGL ELGPQPQGVL RADIFSRMRT LVATVLDFIE LFNQGTAFPA FEMEAYRPVG VVDFPRTEAG HLAGTVHPQL QDRDFQPLQP GAPIFQMFSG EDLLYEGEST VYPVFINEAA YYEKGVAFVQ TEKFTFTVPA MPALTPAPSP AS.

    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.

    Acy3 Human
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