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Search results

1000 results found for “asparaginase”

Name

Description

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  • View Data Sheet

    Name :

    KLK5 Human, Sf9

    Description:

    Kallikrein-5 Human Recombinant, Sf9

    Kallikrein-5, Kallikrein-like protein 2, KLK-L2, Stratum corneum tryptic enzyme, KLK5, SCTE, UNQ570/PRO1132, KLKL2.

    Product # :

    ENZ-1021

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    Description

    Kallikrein-5 Human Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 236 amino acids (67-293 a.a.) and having a molecular mass of 26.2kDa (Migrates at 28-40kDa on SDS-PAGE under reducing conditions).KLK5 is expressed with a 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    KLK5 protein solution (0.5mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 10% glycerol.

    Purity

    Greater than 95% as determined by SDS-PAGE.

    More Info

    • Introduction

      Kallikrein-5 (KLK5) is a member of the serine protease family of proteolytic enzymes. KLK5 is expressed in various tissues including the salivary gland, stomach, uterus, lung, thymus, prostate, colon, brain, thyroid, and trachea. KLK5 expression is up-regulated by estrogens and progestins. KLK5 is secreted and may be involved in desquamation in the epidermis. Kallikreins which are a subgroup of serine proteases, have distinct physiological functions. Many kallikreins are associated with carcinogenesis and some have potential as novel cancer and other disease biomarkers. The KLK5 gene is one of the 15 kallikrein subfamily members located in a cluster on chromosome 19.

    • Synonyms

      Kallikrein-5, Kallikrein-like protein 2, KLK-L2, Stratum corneum tryptic enzyme, KLK5, SCTE, UNQ570/PRO1132, KLKL2.

    • 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

      ADLIINGSDC DMHTQPWQAA LLLRPNQLYC GAVLVHPQWL LTAAHCRKKV FRVRLGHYSL SPVYESGQQM FQGVKSIPHP GYSHPGHSND LMLIKLNRRI RPTKDVRPIN VSSHCPSAGT KCLVSGWGTT KSPQVHFPKV LQCLNISVLS QKRCEDAYPR QIDDTMFCAG DKAGRDSCQG DSGGPVVCNG SLQGLVSWGD YPCARPNRPG VYTNLCKFTK WIQETIQANS 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.

    Klk5 Human Sf9
  • View Data Sheet

    Name :

    UBE2Q2 Human

    Description:

    Ubiquitin Conjugating Enzyme E2Q2 Human Recombinant

    Ubiquitin-conjugating enzyme E2 Q2, UBE2Q2, E2 ubiquitin-conjugating enzyme Q2, Ubiquitin carrier protein Q2, Ubiquitin-protein ligase Q2, Ubiquitin Conjugating Enzyme E2Q2, Ubiquitin-conjugating enzyme E2 Q2 isoform1.

    Product # :

    ENZ-885

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    Description

    UBE2Q2 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 398 amino acids (1-375a.a.) and having a molecular mass of 45.2kDa.UBE2Q2 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    UBE2Q2 protein solution (0.5mg/ml) containing Phosphate Buffer Saline (pH7.4), 30% glycerol and 1mM DTT.

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Ubiquitin Conjugating Enzyme E2Q2 (UBE2Q2) is a protein coding gene which receives ubiquitin from the E1 complex and catalyzes its covalent attachment to various proteins. UBE2Q2 which is a part of the ubiquitin-conjugating enzyme family is detected in hypopharyngeal head and neck squamous cell carcinoma and in tumor masses.

    • Synonyms

      Ubiquitin-conjugating enzyme E2 Q2, UBE2Q2, E2 ubiquitin-conjugating enzyme Q2, Ubiquitin carrier protein Q2, Ubiquitin-protein ligase Q2, Ubiquitin Conjugating Enzyme E2Q2, Ubiquitin-conjugating enzyme E2 Q2 isoform1.

    • 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 MGSMSVSGLK AELKFLASIF DKNHERFRIV SWKLDELHCQ FLVPQQGSPH SLPPPLTLHC NITESYPSSS PIWFVDSEDP NLTSVLERLE DTKNNNLLRQ QLKWLICELC SLYNLPKHLD VEMLDQPLPT GQNGTTEEVT SEEEEEEEEM AEDIEDLDHY EMKEEEPISG KKSEDEGIEK ENLAILEKIR KTQRQDHLNG AVSGSVQASD RLMKELRDIY RSQSYKTGIY SVELINDSLY DWHVKLQKVD PDSPLHSDLQ ILKEKEGIEY ILLNFSFKDN FPFDPPFVRV VLPVLSGGYV LGGGALCMEL LTKQGWSSAY SIESVIMQIN ATLVKGKARV QFGANKNQYN LARAQQSYNS IVQIHEKNGW YTPPKEDG.

    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.

    Ube2Q2 Human
  • View Data Sheet

    Name :

    SPINK1 Human

    Description:

    Serine Peptidase Inhibitor Kazal Type 1 Human Recombinant

    Serine Peptidase Inhibitor Kazal Type 1, Pancreatic Secretory Trypsin Inhibitor, Tumor-Associated Trypsin Inhibitor, PCTT, TATI, Spink3, Serine Protease Inhibitor Kazal Type 1, TCP, PSTI.

    Product # :

    ENZ-724

    Price :

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    Description

    SPINK1 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 79 amino acids (24-79) and having a molecular mass of 8.6kDa.SPINK1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The SPINK1 solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 1mM DTT and 20% glycerol.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    More Info

    • Introduction

      Trypsin inhibitor SPINK1 is secreted from pancreatic acinar cells into pancreatic fluid. SPINK1 has a role in inhibition of trypsin-catalyzed premature initiation of zymogens in the pancreas and the pancreatic duct. Alterations in SPINK1 gene are the cause for tropical calcific and pancreatitis hereditary pancreatitis.

    • Synonyms

      Serine Peptidase Inhibitor Kazal Type 1, Pancreatic Secretory Trypsin Inhibitor, Tumor-Associated Trypsin Inhibitor, PCTT, TATI, Spink3, Serine Protease Inhibitor Kazal Type 1, TCP, PSTI.

    • 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 MGSDSLGREA KCYNELNGCT KIYDPVCGTD GNTYPNECVL CFENRKRQTS ILIQKSGPC.

    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.

    Spink1 Human
  • View Data Sheet

    Name :

    Placental Lactogen Ovine

    Description:

    Placental Lactogen Ovine Recombinant

    Chorionic Somatomammotropin Hormone 1, CSH1, CS-1, hCS, PL.

    Product # :

    CYT-512

    Price :

    Quantity :

    Shipping Method :

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

    Description

    Placental Lactogen Ovine 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 97.0% as determined by:
    (a) Analysis gel filtration.
    (b) Analysis by SDS-PAGE.

    Biological Activity

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

    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 Ovine is also capable of activating human and other heterologous GH receptors but not ruminat GH receptors.

    • Synonyms

      Chorionic Somatomammotropin Hormone 1, CSH1, CS-1, hCS, PL.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized Placental Lactogen Ovine 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 five N-terminal amino acids was determined and was found to be Ala-Gln-His-Pro-Pro.

    • Protein content

      UV spectroscopy at 280 nm using the absorbency value of 0.85 as the extinction coefficient for a 0.1% (1mg/ml) solution. This value is calculated by the PC GENE computer analysis program of protein sequences (IntelliGenetics).

    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 Ovine
  • View Data Sheet

    Name :

    NDUFV3 Human

    Description:

    NADH Dehydrogenase Flavoprotein 3 Human Recombinant

    NADH Dehydrogenase (Ubiquinone) Flavoprotein 3 10kDa, Renal Carcinoma Antigen NY-REN-4, NADH-Ubiquinone Oxidoreductase 9 KDa Subunit, EC 1.6.5.311, CI-10k, Complex I 10kDa

    Product # :

    ENZ-749

    Price :

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    Description

    NDUFV3 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 97 amino acids (35-108) and having a molecular mass of 10.8kDa.NDUFV3 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The NDUFV3 solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH8.0), 0.2M NaCl, 2mM DTT, 2mM EDTA and 50% glycerol.

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      NDUFV3 is one of no less than 41 subunits which form the NADH-ubiquinone oxidoreductase complex that is involved in the mitochondrial respiratory chain and assists in catalyzing the rotenone-sensitive oxidation of NADH and the reduction of ubiquinone. NDUFV3 is 1 of 3 proteins found in the flavoprotein fraction of the complex but it exact function is unknown. Two transcript variants encoding altered isoforms are known for this gene.

    • Synonyms

      NADH Dehydrogenase (Ubiquinone) Flavoprotein 3 10kDa, Renal Carcinoma Antigen NY-REN-4, NADH-Ubiquinone Oxidoreductase 9 KDa Subunit, EC 1.6.5.311, CI-10k, Complex I 10kDa

    • 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 MGSSAESGKS EKGQPQNSKK QSPPKKPAPV PAEPFDNTTY KNLQHHDYST YTFLDLNLEL SKFRMPQPSS GRESPRH

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    Ndufv3 Human
  • View Data Sheet

    Name :

    IYD Human

    Description:

    Iodotyrosine Deiodinase Human Recombinant

    Iodotyrosine dehalogenase 1, IYD-1, Iodotyrosine Deiodinase, IYD, C6orf71, DEHAL1, iodotyrosine dehalogenase 1 isoform 3, dJ422F24.1, TDH4.

    Product # :

    ENZ-779

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    Description

    IYD Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 214 amino acids (24-214 a.a) and having a molecular mass of 25.1kDa.IYD is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

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

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      IYD is an enzyme that catalyzes the oxidative NADPH-dependent deiodination of both mono- and diiodotyrosine although acts more efficiently on monoiodotyrosine. The N-terminus of Iodotyrosine Deiodinase , also known as IYD, plays a role as a membrane anchor. IYD acts during the hydrolysis of thyroglobulin to liberate iodide, which then reenter the hormone-producing pathways.

    • Synonyms

      Iodotyrosine dehalogenase 1, IYD-1, Iodotyrosine Deiodinase, IYD, C6orf71, DEHAL1, iodotyrosine dehalogenase 1 isoform 3, dJ422F24.1, TDH4.

    • 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 MGSDRSMEKK KGEPRTRAEA RPWVDEDLKD SSDLHQAEED ADEWQESEEN VEHIPFSHNH YPEKEMVKRS QEFYELLNKR RSVRFISNEQ VPMEVIDNVI RTAGTAPSGA HTEPWTFVVV KDPDVKHKIR KIIEEEEEIN YMKRMGHRWV TDLKKLRTNW IKEYLDTAPI LILIFKQVHG FAANGKKKVH YYNE.

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    Iyd Human
  • View Data Sheet

    Name :

    DsbA E.Coli

    Description:

    Disulfide Oxidoreductase E.Coli Recombinant

    Disulfide oxidoreductase A, dsbA, rpbB, Disulfide oxidoreductase (DsbA) E Coli, DsDNA-binding protein A, Doublestranded DNA-binding protein, Disulfide oxidoreductase A periplasmic protein disulfide isomerase I, Thiol disulfide interchange protein dsbA.

    Product # :

    ENZ-1143

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    Description

    DsbA E.Coli Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 190 amino acids (20-208) and having a molecular mass of 21.2 kDa. DsbA E.Coli is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    DsbA E.Coli protein (1mg/ml) is formulated in 20mM Tris-HCl buffer (pH 7.5) and 2mM EDTA.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Disulfide Oxidoreductase or DsbA is a protein, found in the plasma. It is part of the thioredoxin protein family. The protein creates disulfide bonds in the target proteins by contributing disulfide bond from its Cys30-Pro31-His32-Cys33 active site to a couple of cysteine residues.

    • Synonyms

      Disulfide oxidoreductase A, dsbA, rpbB, Disulfide oxidoreductase (DsbA) E Coli, DsDNA-binding protein A, Doublestranded DNA-binding protein, Disulfide oxidoreductase A periplasmic protein disulfide isomerase I, Thiol disulfide interchange protein dsbA.

    • 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

      MAQYEDGKQY TTLEKPVAGA PQVLEFFSFF CPHCYQFEEV LHISDNVKKK LPEGVKMTKY HVNFMGGDLG KDLTQAWAVA MALGVEDKVT VPLFEGVQKT QTIRSASDIR DVFINAGIKG EEYDAAWNSF VVKSLVAQQE KAAADVQLRG VPAMFVNGKY QLNPQGMDTS NMDVFVQQYA DTVKYLSEKK.

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    Disulfide Oxidoreductase Enzyme
  • View Data Sheet

    Name :

    CTSA Mouse

    Description:

    Cathepsin-A Mouse Recombinant

    Lysosomal protective protein (EC:3.4.16.5), Carboxypeptidase C, Carboxypeptidase, Cathepsin A, Protective protein cathepsin A, PPCA, Protective protein for beta-galactosidase.

    Product # :

    ENZ-945

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    Description

    CTSA produced in Sf9 Insect cells is a single, glycosylated polypeptide chain containing 459 amino acids (24-474 a.a.) and having a molecular mass of 52.4kDa (Molecular size on SDS-PAGE will appear at approximately 50-70kDa).CTSA is expressed with an 8 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9 Insect cells.

    Formulation

    CTSA protein solution (0.5mg/ml) contains phosphate buffered saline (pH7.4) and 10% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Cathepsin-A (CTSA) is a protective protein which is crucial for both the activity of beta-galactosidase and neuraminidase, CTSA associates with these enzymes and exerts a protective function required for their stability and activity. The CTSA protein is also a carboxypeptidase and can deamidate tachykinins. CTSA is a component of the lysosomal multienzyme complex along with beta-galactosidase and sialidase Neu1. CTSA is a multicatalytic enzyme with deamidase and esterase in addition to carboxypeptidase activities.

    • Synonyms

      Lysosomal protective protein (EC:3.4.16.5), Carboxypeptidase C, Carboxypeptidase, Cathepsin A, Protective protein cathepsin A, PPCA, Protective protein for beta-galactosidase.

    • 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

      APDQDEIDCL PGLAKQPSFR QYSGYLRASD SKHFHYWFVE SQNDPKNSPV VLWLNGGPGC SSLDGLLTEH GPFLIQPDGV TLEYNPYAWN LIANVLYIES PAGVGFSYSD DKMYVTNDTE VAENNYEALK DFFRLFPEYK DNKLFLTGES YAGIYIPTLA VLVMQDPSMN LQGLAVGNGL ASYEQNDNSL VYFAYYHGLL GNRLWTSLQT HCCAQNKCNF YDNKDPECVN NLLEVSRIVG KSGLNIYNLY APCAGGVPGR HRYEDTLVVQ DFGNIFTRLP LKRRFPEALM RSGDKVRLDP PCTNTTAPSN YLNNPYVRKA LHIPESLPRW DMCNFLVNLQ YRRLYQSMNS QYLKLLSSQK YQILLYNGDV DMACNFMGDE WFVDSLNQKM EVQRRPWLVD YGESGEQVAG FVKECSHITF LTIKGAGHMV PTDKPRAAFT MFSRFLNKEP YVEHHHHHH.

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    Ctsa Mouse
  • View Data Sheet

    Name :

    ADH1A Human, sf9

    Description:

    Alcohol Dehydrogenase 1A, Human Recombinant, sf9

    ADH1A, Alcohol dehydrogenase 1A, Alcohol dehydrogenase 1A, Alcohol dehydrogenase subunit alpha, ADH1.

    Product # :

    ENZ-1009

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    Description

    ADH1A Human Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 381 amino acids (1-375) and having a molecular mass of 40.6kDa. ADH1A is fused to a 6 amino acid His-Tag at C-terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    ADH1A protein solution (0.5mg/ml) containing Phosphate Buffered Saline (pH 7.4) and 10% glycerol.

    Purity

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

    More Info

    • Introduction

      Alcohol dehydrogenase 1A (ADH1A) is a member of the alcohol dehydrogenase family. ADH1A has a key role in ethanol metabolism. ADH1A along with coenzyme NAD catalyzes the reversible conversion of organic alcohols to ketones or aldehydes. The physiologic function of ADH1A in the liver is the elimination of ethanol formed by microorganisms in the intestinal tract. ADH1A is monomorphic and predominant in fetal and infant livers, growing to be less active in gestation and only weakly active during adulthood.

    • Synonyms

      ADH1A, Alcohol dehydrogenase 1A, Alcohol dehydrogenase 1A, Alcohol dehydrogenase subunit alpha, ADH1.

    • 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

      MSTAGKVIKC KAAVLWELKK PFSIEEVEVA PPKAHEVRIK MVAVGICGTD DHVVSGTMVT PLPVILGHEA AGIVESVGEG VTTVKPGDKV IPLAIPQCGK CRICKNPESN YCLKNDVSNP QGTLQDGTSR FTCRRKPIHH FLGISTFSQY TVVDENAVAK IDAASPLEKV CLIGCGFSTG YGSAVNVAKV TPGSTCAVFG LGGVGLSAIM GCKAAGAARI IAVDINKDKF AKAKELGATE CINPQDYKKP IQEVLKEMTD GGVDFSFEVI GRLDTMMASL LCCHEACGTS VIVGVPPDSQ NLSMNPMLLL TGRTWKGAIL GGFKSKECVP KLVADFMAKK FSLDALITHV LPFEKINEGF DLLHSGKSIR TILMFHHHHH H.

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    Adh1A Human Sf9
  • View Data Sheet

    Name :

    PDE6H Human

    Description:

    Phosphodiesterase 6H cGMP-Specific Cone Gamma Human Recombinant

    Phosphodiesterase 6H, CGMP-Specific, Cone, Gamma, Retinal Cone Rhodopsin-Sensitive CGMP 3',5'-Cyclic Phosphodiesterase, Subunit Gamma, EC 3.1.4.35, EC 3.1.4.17, RCD3, GMP-PDE Gamma, ACHM6, PDE6H.

    Product # :

    ENZ-819

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    Description

    PDE6H Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 106 amino acids (1-83 a.a) and having a molecular mass of 11.5 kDa. PDE6H is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    PDE6H protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.2M NaCl, 40% glycerol, 2mM DTT and 0.1mM PMSF.

    Purity

    Greater than 80% as determined by SDS-PAGE.

    More Info

    • Introduction

      PDE6H belongs to the rod/cone cGMP-PDE gamma subunit family, which selectively catalyze the hydrolysis of 3 cyclic phosphate bonds in adenosine and/or guanine 3,5 cyclic monophosphate (cAMP and/or cGMP). This family regulates the cellular levels, localization and duration of action of these second messengers by controlling the rate of their degradation. PDE6H is the inhibitory (or gamma) subunit of the cone-specific cGMP phosphodiesterase, which is atetramer composed of two catalytic chains (alpha and beta), and two inhibitory chains (gamma). PDE6H is particularly expressed in the retina, and is implicated in the transmission and amplification of the visual signal. Mutations in PDE6H have been associated with retinal cone dystrophy type 3A.

    • Synonyms

      Phosphodiesterase 6H, CGMP-Specific, Cone, Gamma, Retinal Cone Rhodopsin-Sensitive CGMP 3',5'-Cyclic Phosphodiesterase, Subunit Gamma, EC 3.1.4.35, EC 3.1.4.17, RCD3, GMP-PDE Gamma, ACHM6, PDE6H.

    • 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 MGSMSDNTTL PAPASNQGPT TPRKGPPKFK QRQTRQFKSK PPKKGVKGFG DDIPGMEGLG TDITVICPWE AFSHLELHEL AQFGII.

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    Pde6H Human
  • View Data Sheet

    Name :

    PHOSPHO2 Human

    Description:

    Phosphatase Orphan-2 Human Recombinant

    Pyridoxal phosphate phosphatase PHOSPHO2, PHOSPHO2.

    Product # :

    ENZ-231

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    Description

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

    Source

    Escherichia Coli.

    Formulation

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

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

    More Info

    • Introduction

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

    • Synonyms

      Pyridoxal phosphate phosphatase PHOSPHO2, PHOSPHO2.

    • Physical Appearance

      Sterile filtered colorless solution.

    • Stability

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

    • Amino Acid Sequence

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

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    Phospho2 Human
  • View Data Sheet

    Name :

    MSRA E.Coli

    Description:

    Methionine Sulfoxide Reductase A E.Coli Recombinant

    Peptide methionine sulfoxide reductase MsrA, Protein-methionine-S-oxide reductase, Peptide-methionine (S)-S-oxide reductase, Peptide Met(O) reductase, msrA, pms, b4219, JW4178.

    Product # :

    ENZ-129

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    Description

    MSRA produced in E.Coli is a single, non-glycosylated polypeptide chain containing 232 amino acids (1-212 a.a.) and having a molecular mass of 25.4kDa.MSRA is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

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

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Peptide methionine sulfoxide reductase A (msrA) is an enzyme which catalyzes the reversible oxidation-reduction of methionine sulfoxide in proteins to methionine. MSRA may have a significant function as a repair enzyme for proteins which have been inactivated by oxidation.

    • Synonyms

      Peptide methionine sulfoxide reductase MsrA, Protein-methionine-S-oxide reductase, Peptide-methionine (S)-S-oxide reductase, Peptide Met(O) reductase, msrA, pms, b4219, JW4178.

    • 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 MSLFDKKHLV SPADALPGRN TPMPVATLHA VNGHSMTNVP DGMEIAIFAM GCFWGVERLF WQLPGVYSTA AGYTGGYTPN PTYREVCSGD TGHAEAVRIV YDPSVISYEQ LLQVFWENHD PAQGMRQGND HGTQYRSAIY PLTPEQDAAA RASLERFQAA
      MLAADDDRHI TTEIANATPF YYAEDDHQQY LHKNPYGYCG IGGIGVCLPP EA.

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    Msra Ecoli
  • View Data Sheet

    Name :

    TPST1 Human, sf9

    Description:

    Tyrosylprotein Sulfotransferase 1, sf9 Human Recombinant

    Tyrosylprotein Sulfotransferase 1, EC 2.8.2.20, TPST-1, Transport And Golgi Organization 13 Homolog A (Drosophila), Transport And Golgi Organization 13 Homolog A, Tyrosylprotein Sulfotransferase-1, TANGO13A.

    Product # :

    ENZ-948

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    Description

    TPST1 produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 354 amino acids (26-370 a.a.) and having a molecular mass of 40.6kDa (Migrates at 40-57kDa on SDS-PAGE under reducing conditions). TPST1 is expressed with a 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    TPST1 protein solution (0.25mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 10% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Tyrosylprotein Sulfotransferase 1, also known as TPST1 is the enzyme which catalyzes the sulfation reaction of protein tyrosines, a post-translational modification of proteins. TPST1 belongs to the protein sulfotransferase family. In addition, TPST1 utilizes 3'-Phosphoadenosine-5'-phosphosulfate (PAPS) as the sulfonate donor and also binds proteins with target tyrosine residues to eventually form the tyrosine O-sulfate ester group in addition to the desulfonated 3’-phosphoadenosine-5’-phosphate.

    • Synonyms

      Tyrosylprotein Sulfotransferase 1, EC 2.8.2.20, TPST-1, Transport And Golgi Organization 13 Homolog A (Drosophila), Transport And Golgi Organization 13 Homolog A, Tyrosylprotein Sulfotransferase-1, TANGO13A.

    • 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

      ADPQHAMECH HRIEERSQPV KLESTRTTVR TGLDLKANKT FAYHKDMPLI FIGGVPRSGT TLMRAMLDAH PDIRCGEETR VIPRILALKQ MWSRSSKEKI RLDEAGVTDE VLDSAMQAFL LEIIVKHGEP APYLCNKDPF ALKSLTYLSR LFPNAKFLLM VRDGRASVHS MISRKVTIAG FDLNSYRDCL TKWNRAIETM YNQCMEVGYK KCMLVHYEQL VLHPERWMRT LLKFLQIPWN HSVLHHEEMI GKAGGVSLSK VERSTDQVIK PVNVGALSKW VGKIPPDVLQ DMAVIAPMLA KLGYDPYANP PNYGKPDPKI IENTRRVYKG EFQLPDFLKE KPQTEQVEHH HHHH.

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    Tpst1 Human Sf9
  • View Data Sheet

    Name :

    PRDX1 Human

    Description:

    Peroxiredoxin-1 Human Recombinant

    Peroxiredoxin-1, EC 1.11.1.15, Thioredoxin peroxidase 2, Thioredoxin-dependent peroxide reductase 2, Proliferation-associated gene protein, Natural killer cell-enhancing factor A, NKEF-A, PRDX1, TDPX2, PRDX-1, PAG, PAGA, PRX1, PAGB, PRXI, MSP23, NKEFA.

    Product # :

    ENZ-372

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    Description

    Peroxiredoxin Human Recombinant fused with a 20 amino acid His tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain (1-199) containing 219 amino acids and having a molecular mass of 24 kDa. The Peroxiredoxin is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The Peroxiredoxin solution (1mg/ml) contains 20mM Tris-HCl pH-7.5 & 20% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    Biological Activity

    Enzymatic activity is defined as the amount of hydroperoxide that 1ug of enzyme can reduce at 25C for minute. Specific activity is >2,000pmol/min/ug.

    More Info

    • Introduction

      PRDX1 is part of the peroxiredoxin family of antioxidant enzymes, which reduce hydrogen peroxide and alkyl hydroperoxides. PRDX1 is an important protector of red blood cells against reactive oxygen species and in tumor prevention.
      PRDX1 is antioxidant protective in cells, and contributes to the antiviral activity of CD8(+) T-cells. PRDX1 has a proliferative effect and is involved in cancer development or progression.
      Peroxiredoxin-1 is plays a role in redox regulation of the cell. Peroxiredoxin decreases peroxides with reducing equivalents provided through the thioredoxin system but not from glutaredoxin. Peroxiredoxin is involved in eliminating peroxides generated during metabolism. Peroxiredoxin participates in the signaling cascades of growth factors and TNF-alpha by regulating the intracellular concentrations of h(2)o(2).

    • Synonyms

      Peroxiredoxin-1, EC 1.11.1.15, Thioredoxin peroxidase 2, Thioredoxin-dependent peroxide reductase 2, Proliferation-associated gene protein, Natural killer cell-enhancing factor A, NKEF-A, PRDX1, TDPX2, PRDX-1, PAG, PAGA, PRX1, PAGB, PRXI, MSP23, NKEFA.

    • 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 MSSGNAKIGH PAPNFKATAV MPDGQFKDIS LSDYKGKYVV FFFYPLDFTF VCPTEIIAFS DRAEEFKKLN CQVIGASVDS HFCHLAWVNT PKKQGGLGPM NIPLVSDPKR TIAQDYGVLK ADEGISFRGL FIIDDKGILR QITVNDLPVG RSVDETLRLV QAFQFTDKHG EVCPAGWKPG SDTIKPDVQK SKEYFSKQK.

    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.

    Prdx1 Human
  • View Data Sheet

    Name :

    NDUFAF2 Human

    Description:

    NADH Dehydrogenase 1 Alpha Subcomplex, Assembly Factor 2 Human Recombinant

    Mimitin mitochondrial, B17.2-like, B17.2L, Myc-induced mitochondrial protein, MMTN, NADH dehydrogenase [ubiquinone] 1 alpha subcomplex assembly factor 2, NDUFA12-like protein, NDUFAF2, NDUFA12L, mimitin.

    Product # :

    ENZ-150

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    Description

    NDUFAF2 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 189 amino acids (1-169 a.a.) and having a molecular mass of 22kDa.NDUFAF2 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    NDUFAF2 protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 1mM DTT, 20% glycerol and 200mM NaCl.

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Mimitin (NDUFAF2) is a member of the complex I NDUFA12 subunit family.NADH dehydrogenase is an enzyme located in the inner mitochondrial membrane, which catalyzes the transfer of electrons from NADH to coenzyme Q (CoQ). NDUFAF2 is the "entry enzyme" of oxidative phosphorylation in the mitochondria. Mimitin protein functions as a molecular chaperone for mitochondrial complex I assembly.

    • Synonyms

      Mimitin mitochondrial, B17.2-like, B17.2L, Myc-induced mitochondrial protein, MMTN, NADH dehydrogenase [ubiquinone] 1 alpha subcomplex assembly factor 2, NDUFA12-like protein, NDUFAF2, NDUFA12L, mimitin.

    • 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 MGWSQDLFRA LWRSLSREVK EHVGTDQFGN KYYYIPQYKN WRGQTIREKR IVEAANKKEV DYEAGDIPTE WEAWIRRTRK TPPTMEEILK NEKHREEIKI KSQDFYEKEK LLSKETSEEL LPPPVQTQIK GHASAPYFGK EEPSVAPSST GKTFQPGSWM PRDGKSHNQ.

    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.

    Ndufaf2 Human
  • View Data Sheet

    Name :

    Pfu DNA Polymerase

    Description:

    Pfu-DNA Polymerase Recombinant

    DNA polymerase, EC 2.7.7.7, Pfu polymerase, Pfu-DNA Polymerase.

    Product # :

    ENZ-265

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    Description

    Pfu DNA Polymerase is a thermo-stable enzyme having a Mw of about 90kDa. Pfu DNA Polymerase is derived from E. coli that and cloned from Pyrococcus furiosus strain Vc1 DSM3638. Pfu DNA Polymerase replicates DNA at 75°C, catalyzing the polymerization of nucleotides into duplex DNA in the 5´ to 3´ direction in the existence of magnesium. Pfu DNA Polymerase possesses 3´ to 5´ exonuclease (proofreading) activity. Base misinsertions that take place during polymerization are swiftly removed by the proofreading activity of the polymerase. Therefore, Pfu DNA Polymerase is suggested for use in PCR and primer extension reactions that require high-fidelity synthesis. Pfu DNA Polymerase-generated PCR fragments are blunt-ended.

    Source

    Escherichia Coli.

    Formulation

    50mM Tris-HCl, pH 8.2, 1mM DTT, 0.1mM EDTA, 0.05% CHAPS and 50% glycerol.

    More Info

    • Introduction

      Pfu DNA polymeraseenzyme is found in the hyperthermophilic archaeonPyrococcus furiosus, where it functions in vivoto replicate the organism's DNA. In vitro, Pfu is used to swiftly amplify DNAin the Polymerase Chain Reaction, where the enzyme serves the central function of copying a new strand of DNA during each extension step. Pfu DNA polymerase has superior thermostability and 'proofreading' properties compared to other thermostable polymerases. Unlike Taq DNA polymerase, Pfu DNA polymerase possesses 3' to 5' exonuclease proof reading activity, meaning that it works its way along the DNA from the 5' endto the 3' endand corrects nucleotidemisin corporation errors. Pfu DNA polymerase-generated PCRfragments will have fewer errors than Taq-generated PCR inserts. As a result, Pfu is more commonly used for molecular cloning of PCR fragments than the historically popular Taq. Pfu DNA polymerase is superior for techniques that require high-fidelity DNA synthesis, but can also be used in conjunction with Taq polymerase to obtain the fidelity of Pfu with the speed of Taq polymerase activity.

    • Synonyms

      DNA polymerase, EC 2.7.7.7, Pfu polymerase, Pfu-DNA Polymerase.

    • Physical Appearance

      Sterile liquid formulation.

    • Stability

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

    • Applications

      1. Ideal for high-fidelity amplification.
      2. 3'-5' exonuclease activity provides a low error rate.
      3. One of the most thermostable DNA polymerases known.
      4. Lack of extendase activity means no unwanted 3’ overhangs.
      5. Optimal for blunt-end PCR cloning.
      6. Optimum temperature near 75°C.
      7. 95% active after 1-hour incubation at 98°C.

    • PCR Protocol

      Add the following components to amplify 1kb DNA template: 0.2µl Pfu-DNA Polymerase.4µl 2.5mM dNTPs.5µl 10x buffer with MgSO4. 1µl Primers mix (10µM each).1µl Template.38µl ddH2O. Amplify using the following cycling parameters: Heat Soak: 1 cycle at 94°C/4 min.Denaturation: 30 cycles at 94°C/30 sec.Annealing: 30 cycles at 55°C /30 sec.Extension: 30 cycles at 72°C /90 sec. Final: 1 cycle at 72°C /5 min.

    • Unit Definition

      1U of enzyme catalyzes the incorporation of 10nmol of dNTP into acid-insoluble product in 30 minutes at 75°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.

    Pfu Dna Polymerase
  • View Data Sheet

    Name :

    SIAH1 Human

    Description:

    Siah E3 Ubiquitin Protein Ligase 1 Human Recombinant

    Siah E3 ubiquitin protein ligase 1, Seven in absentia homolog 1, seven in absentia homolog 1 (Drosophila), E3 ubiquitin-protein ligase SIAH1, HUMSIAH, hSIAH1, Siah-1a, SIAH1A, EC 6.3.2.

    Product # :

    ENZ-640

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    Description

    SIAH1 Human Recombinant produced in E. coli is a single polypeptide chain containing 216 amino acids (90-282) and having a molecular mass of 24.1 kDa.SIAH1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    The SIAH1 solution (0.25mg/1ml) contains 20mM Tris-HCl buffer (pH 8.0), 100mM NaCl, 1mM DTT and 40% glycerol.

    Purity

    Greater than 95% as determined by SDS-PAGE.

    More Info

    • Introduction

      E3 ubiquitin-protein ligase SIAH1 (SIAH1) belongs to the SIAH (seven in absentia homolog) family. SIAH1 is a tumor suppressor protein, which is expressed in intestinal epithelium and activated during apoptosis. SIAH1 is involved in ubiquitination and proteasome-mediated degradation of specific proteins. SIAH1 is comprised of an N-terminal RING-finger domain (required for proteolysis) and a cystein-rich C-terminal domain (which regulates oligomerization and SIAH binding to target proteins). SIAH1 causes indirect degradation of beta-catenin by way of creation of a complex with Siah-interacting protein (SIP), Skp1 and Ebi.

    • Synonyms

      Siah E3 ubiquitin protein ligase 1, Seven in absentia homolog 1, seven in absentia homolog 1 (Drosophila), E3 ubiquitin-protein ligase SIAH1, HUMSIAH, hSIAH1, Siah-1a, SIAH1A, EC 6.3.2.

    • 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 MGSVANSVLF PCKYASSGCE ITLPHTEKAD HEELCEFRPY SCPCPGASCK WQGSLDAVMP HLMHQHKSIT TLQGEDIVFL ATDINLPGAV DWVMMQSCFG FHFMLVLEKQ EKYDGHQQFF AIVQLIGTRK QAENFAYRLE LNGHRRRLTW EATPRSIHEG IATAIMNSDC LVFDTSIAQL FAENGNLGIN VTISMC.

    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.

    Siah1 Human
  • View Data Sheet

    Name :

    LACTB E.coli, His

    Description:

    Beta Lactamase E.coli Recombinant, His Tag

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

    Product # :

    ENZ-088

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    Description

    Beta Lactamase is an E.coli Recombinant protein produced in E.Coli containing 379 amino acids (20-377) and having a molecular mass of 41.8kDa. Beta Lactamase is expressed with a 21 N-terminal His tag.The LACTB is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The LACTB enzyme (1mg/ml) is supplied in 20mM Tris-HCl buffer (pH8.0) and 10% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

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

    • Synonyms

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

    • Physical Appearance

      Sterile Filtered colorless solution.

    • Stability

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

    • Amino Acid Sequence

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

    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.

    Lactb Ecoli His
  • View Data Sheet

    Name :

    C.Albicans Enolase

    Description:

    Candida Albicans Enolase Recombinant

    Product # :

    PRO-2297

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    Description

    Recombinant Candida Albicans Enolase produced in SF9 is a glycosylated, polypeptide chain having a calculated molecular mass of 46kDa. C.Albicans Enolase is expressed with a 10xHis tag at N-terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9 insect cells.

    Formulation

    C.Albicans Enolase is supplied in 20mM HEPES buffer pH-8, 200mM NaCl and 20% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Candida albicans is a diploid fungus, which grows both as yeast and filamentous cells and a contributory agent of opportunistic oral and genital infections in humans, and candidal onychomycosis (an infection of the nail plate). Systemic fungal infections (fungemias) including those by C. albicans are regarded as key causes of morbidity and mortality in immunocompromised patients (e.g., AIDS, cancer chemotherapy, organ or bone marrow transplantation). C. albicans biofilms may develop on the surface of implantable medical devices. C. albicans is commensal and a constituent of the normal gut flora containing microorganisms which live in the human mouth and gastrointestinal tract. Overgrowth of the fungus leads to in candidiasis (candidosis). Candidiasis is frequently detected in immunocompromised persons, including HIV-infected patients. To infect host tissue, the habitual unicellular yeast-like form of C. albicans reacts to environmental signals and changes into an invasive, multicellular filamentous form, a phenomenon which is known as dimorphism.

    • 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.

    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.

    Calbicans Enolase
  • View Data Sheet

    Name :

    NT5C2 Human

    Description:

    5'-Nucleotidase Cytosolic II Human Recombinant

    Cytosolic purine 5'-nucleotidase, Cytosolic 5'-nucleotidase II, NT5C2, NT5B, NT5CP, PNT5, GMP, cN-II.

    Product # :

    ENZ-173

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    Description

    NT5C2 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 581 amino acids (1-561 a.a.) and having a molecular mass of 67.1kDa.NT5C2 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    NT5C2 protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH8.0), 30% glycerol, 0.1M NaCl, 1mM DTT and 0.1mM PMSF.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    More Info

    • Introduction

      NT5C2 (NT5B/PNT5) has a vital role in the maintenance of purine/pyrimidine nucleotides. NT5C2 contains a phosphotransferase active site which catalyzes the dephosphorylation of 6-hydroxypurine nucleoside 5'-monophosphates. Furthermore, NT5C2 regulates the level of inosine monophosphate (IMP) and guanosine monophosphate (GMP) pools inside cells by way of hydrolysis.

    • Synonyms

      Cytosolic purine 5'-nucleotidase, Cytosolic 5'-nucleotidase II, NT5C2, NT5B, NT5CP, PNT5, GMP, cN-II.

    • 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 MSTSWSDRLQ NAADMPANMD KHALKKYRRE AYHRVFVNRS LAMEKIKCFG FDMDYTLAVY KSPEYESLGF ELTVERLVSI GYPQELLSFA YDSTFPTRGL VFDTLYGNLL KVDAYGNLLV CAHGFNFIRG PETREQYPNK FIQRDDTERF YILNTLFNLP ETYLLACLVD FFTNCPRYTS CETGFKDGDL FMSYRSMFQD VRDAVDWVHY KGSLKEKTVE NLEKYVVKDG KLPLLLSRMK EVGKVFLATN SDYKYTDKIM TYLFDFPHGP KPGSSHRPWQ SYFDLILVDA RKPLFFGEGT VLRQVDTKTG KLKIGTYTGP LQHGIVYSGG SSDTICDLLG AKGKDILYIG DHIFGDILKS KKRQGWRTFL VIPELAQELH VWTDKSSLFE ELQSLDIFLA ELYKHLDSSS NERPDISSIQ RRIKKVTHDM DMCYGMMGSL FRSGSRQTLF ASQVMRYADL YAASFINLLY YPFSYLFRAA HVLMPHESTV EHTHVDINEM ESPLATRNRT SVDFKDTDYK RHQLTRSISE IKPPNLFPLA PQEITHCHDE DDDEEEEEEE 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.

    Nt5C2 Human
  • View Data Sheet

    Name :

    HARS Human

    Description:

    Histidyl-tRNA Synthetase Human Recombinant

    Histidyl-tRNA synthetase, EC 6.1.1.21, Histidine-tRNA ligase, HisRS, HRS, FLJ20491, JO-1, HARS.

    Product # :

    ENZ-268

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    Description

    Histidyl-tRNA Synthetase Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain having a molecular mass of 55 kDa.

    Source

    Escherichia Coli.

    Formulation

    The protein solution contains 500mM NaCl and 10mM Tris (pH 8.0) and 6M Urea.

    Purity

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

    More Info

    • Introduction

      Aminoacyl-tRNA synthetases are a class of enzymes that charge tRNAs with their cognate amino acids. The protein encoded by this gene is a cytoplasmic enzyme which belongs to the class II family of aminoacyl-tRNA synthetases. The enzyme is responsible for the synthesis of histidyl-transfer RNA, which is essential for the incorporation of histidine into proteins. The gene is located in a head-to-head orientation with HARSL on chromosome five, where the homologous genes share a bidirectional promoter. The gene product is a frequent target of autoantibodies in the human autoimmune disease polymyositis/dermatomyositis.

    • Synonyms

      Histidyl-tRNA synthetase, EC 6.1.1.21, Histidine-tRNA ligase, HisRS, HRS, FLJ20491, JO-1, HARS.

    • Physical Appearance

      Sterile Filtered clear solution.

    • Stability

      Histidyl-tRNA Synthetase although stable at 4°C for 3 weeks, should be stored below -18°C.Please prevent freeze-thaw cycles.

    • Applications

      Western Blot: Strongly reactive with human anti Histidyl-tRNA Synthetase antisera.

    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.

    Jo 1 Human
  • View Data Sheet

    Name :

    COMT Human

    Description:

    Catechol-O-Methyltransferase Human Recombinant

    COMT, EC 2.1.1.6, Catechol O-methyltransferase.

    Product # :

    ENZ-400

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    Description

    COMT Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 221 amino acids (51-271 a.a.) & having a molecular mass of 24.4 kDa. The COMT is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    COMT protein in 20mM Tris-HCl buffer, pH-8, 1mM MgCl2 and 10% Glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      COMT catalyzes the transfer of a methyl group from S-adenosylmethionine (SAM) to catechol substrates such as the neurotransmitters. This O-methylation results in one of the main degradative pathways of the catecholamine transmitters. COMT COMT is located in the postsynaptic neuron and is involved in the metabolism of catechol estrogen drugs used in the treatment of hypertension, asthma, Parkinson disease and the inactivation of catecholamine neurotransmitters though enzymatic degradation. COMT appears in tissues in 2 forms, a soluble form and a membrane-bound form which differ in their N-termini. COMT inhibitors increase its availability and are used in the treatment of patients with Parkinson's disease.

    • Synonyms

      COMT, EC 2.1.1.6, Catechol O-methyltransferase.

    • 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

      MGDTKEQRIL NHVLQHAEPG NAQSVLEAID TYCEQKEWAM NVGDKKGKIV DAVIQEHQPS VLLELGAYCG YSAVRMARLL SPGARLITIE INPDCAAITQ RMVDFAGVKD KVTLVVGASQ DIIPQLKKKY DVDTLDMVFL DHWKDRYLPD TLLLEECGLL RKGTVLLADN VICPGAPDFL AHVRGSSCFE CTHYQSFLEY REVVDGLEKA IYKGPGSEAG 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.

    Comt Human
  • View Data Sheet

    Name :

    T7 RNAP

    Description:

    T7 RNA Polymerase Recombinant

    T7 RNAP.

    Product # :

    ENZ-1180

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    Description

    T7 RNA polymerase Recombinant protein is produced by bacteriophage T7 DNA which is expressed in recombinant E. coli bacterial system T7 RNA Polymerase is a DNA-dependent 5'→ 3' RNA polymerase which specifically recognizes T7 promoter sequences.

    Source

    T7 Bacteriophage RNA Polymerase gene

    Formulation

    Transcription Buffer 40mM Tris-HCl (25°C, pH-8), 20mM MgCl2, 2.5mM TCEP & 2mM spermidine.

    Purity

    Greater than 95% as visualized by SDS-PAGE

    More Info

    • Introduction

      T7 RNA polymerase active enzyme synthesizes RNA at an increasing degree of that of E. coli RNA polymerase and it terminates transcription often. T7 RNA polymerase is very selective for initiation at its own promoter sequences and is resistant to antibiotics that inhibit E. coli RNA polymerase. In-vitro transcription of mRNA is achieved via bacteriophage T7 RNA polymerase using its ability to produce full-length RNA transcripts with high reliability, thoughT7 RNAP can manufacture as well immunostimulatory by products for example dsRNA which affect protein expression.

    • Synonyms

      T7 RNAP.

    • Physical Appearance

      Sterile Filtered clear solution.

    • Stability

      Two years when stored at -20°C, 2 weeks at 4°C. DO NOT STORE AT -70C.

    • Applications

      Synthesis of :

      • ssRNAs.
      • Labeled or unlabeled highly specific RNA probes.
      • Capped mRNA using cap analogues.
    • Unit Definition

      1U is defined as the amount of enzyme required to incorporate 1nmol of [3H] ATP into acid-insoluble precipitates within 1 hour at 37℃, pH-8.

    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.

    T7 Rnap
  • View Data Sheet

    Name :

    CKBB Human His

    Description:

    Creatine Kinase Brain Human Recombinant, His Tag

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

    Product # :

    CKI-274

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    Description

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

    Source

    Escherichia Coli.

    Formulation

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

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

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

    • Synonyms

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

    • Physical Appearance

      Sterile filtered colorless solution.

    • Stability

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

    • Amino Acid Sequence

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

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

    Ckb Human
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