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Search results

1000 results found for “Adenylate Kinase”

Name

Description

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  • View Data Sheet

    Name :

    AMT Human

    Description:

    Aminomethyltransferase Human Recombinant

    GCE, GCST, GCVT, NKH, Aminomethyltransferase, mitochondrial, Glycine cleavage system T protein, GCVT.

    Product # :

    ENZ-900

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    Description

    AMT Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 398 amino acids (29-403 a.a) and having a molecular mass of 43.3kDa.AMT is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    AMT protein solution (1mg/ml) in Phosphate Buffered Saline, 30% glycerol and 1mM DTT.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      Aminomethyltransferase, mitochondrial isoform 1 (AMT) is a component of the glycine cleavage system termed T-protein. AMT reversibly catalyzes the degradation of the aminomethyl moiety of glycine attached to the lipoate cofactor of H-protein, leading to the production of ammonia, 5,10-methylenetetrahydrofolate, and dihydrolipoate-bearing H-protein in the presence of tetrahydrofolate.

    • Synonyms

      GCE, GCST, GCVT, NKH, Aminomethyltransferase, mitochondrial, Glycine cleavage system T protein, GCVT.

    • 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 MGSAQEVLRR TPLYDFHLAH GGKMVAFAGW SLPVQYRDSH TDSHLHTRQH CSLFDVSHML QTKILGSDRV KLMESLVVGD IAELRPNQGT LSLFTNEAGG ILDDLIVTNT SEGHLYVVSN AGCWEKDLAL MQDKVRELQN QGRDVGLEVL DNALLALQGP TAAQVLQAGV ADDLRKLPFM TSAVMEVFGV SGCRVTRCGY TGEDGVEISV PVAGAVHLAT AILKNPEVKL AGLAARDSLR LEAGLCLYGN DIDEHTTPVE GSLSWTLGKR RRAAMDFPGA KVIVPQLKGR VQRRRVGLMC EGAPMRAHSP ILNMEGTKIG TVTSGCPSPS LKKNVAMGYV PCEYSRPGTM LLVEVRRKQQ MAVVSKMPFV PTNYYTLK.

    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.

    Amt Human
  • View Data Sheet

    Name :

    NDUFV2 Human

    Description:

    NADH Dehydrogenase Flavoprotein 2 Human Recombinant

    CI-24k, NADH dehydrogenase [ubiquinone] flavoprotein 2, mitochondrial, NADH-ubiquinone oxidoreductase 24 kDa subunit, NDUFV2.

    Product # :

    ENZ-743

    Price :

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    Description

    NDUFV2 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 240 amino acids (33-249 a.a) and having a molecular mass of 26.1kDa.NDUFV2 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    NDUFV2 protein solution (1mg/ml) containing 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

      NADH Dehydrogenase Flavoprotein 2 (NDUFV2) is a 24 kDa Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) which is a part of the minimal assembly required for catalysisthe. NDUFV2 is aslo involved in electron transfer. Mutations in NDUFV2 are implicated in Parkinson's disease, bipolar disorder, schizophrenia, and have been discovered in one case of early onset hypertrophic cardiomyopathy and encephalopathy.

    • Synonyms

      CI-24k, NADH dehydrogenase [ubiquinone] flavoprotein 2, mitochondrial, NADH-ubiquinone oxidoreductase 24 kDa subunit, NDUFV2.

    • 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 MGSGAGGALF VHRDTPENNP DTPFDFTPEN YKRIEAIVKN YPEGHKAAAV LPVLDLAQRQ NGWLPISAMN KVAEVLQVPP MRVYEVATFY TMYNRKPVGK YHIQVCTTTP CMLRNSDSIL EAIQKKLGIK VGETTPDKLF TLIEVECLGA CVNAPMVQIN DNYYEDLTAK DIEEIIDELK AGKIPKPGPR SGRFSCEPAG GLTSLTEPPK GPGFGVQAGL.

    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.

    Ndufv2 Human
  • View Data Sheet

    Name :

    ARL1 Human

    Description:

    ADP-Ribosylation Factor-Like 1 Human Recombinant

    ARFL1.

    Product # :

    PRO-508

    Price :

    Quantity :

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    • description
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    Description

    ARL1 Recombinant Human produced in E.Coli is a single, non-glycosylated polypeptide chain containing 201 amino acids (1-181 a.a.) and having a molecular mass of 22.5 kDa. The ARL1 is fused to a 20 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The ARL1 solution (0.25mg/ml) containing 20mM Tris-HCl pH-8, 2mM DTT, 100mM NaCl and 40% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      ARL1 is part of the ARL (ADP-ribosylation factor-like) family of proteins, which are structurally associated to ADP-ribosylation factors (ARFs). ARFs, described as activators of cholera toxin (CT) ADP-ribosyltransferase activity, control intracellular vesicular membrane trafficking, and stimulate a phospholipase D (PLD) isoform.
      ARL1 is a weak stimulator of PLD and CT in a phospholipid dependent manner.
      ARL1 is a GTP-binding protein that has low efficiency as allosteric activator of the cholera toxin catalytic subunit, an ADP-ribosyltransferase. ARL1 is involved in the Golgi apparatus.

    • Synonyms

      ARFL1.

    • 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 MGGFFSSIFS SLFGTREMRI LILGLDGAGK TTILYRLQVG EVVTTIPTIG FNVETVTYKN LKFQVWDLGG QTSIRPYWRC YYSNTDAVIY VVDSCDRDRI GISKSELVAM LEEEELRKAI LVVFANKQDM EQAMTSSEMA NSLGLPALKD RKWQIFKTSA TKGTGLDEAM EWLVETLKSR Q.

    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.

    Arl1 Human
  • View Data Sheet

    Name :

    ARL2 Human

    Description:

    ADP-Ribosylation Factor-Like 2 Human Recombinant

    ADP-ribosylation factor-like protein 2, ARL2, ARFL2.

    Product # :

    PRO-074

    Price :

    Quantity :

    Shipping Method :

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    • description
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    • Citations

    Description

    ARL2 Human Recombinant fused with a 20 amino acid His tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 204 amino acids (1-184 a.a.) and having a molecular mass of 23kDa. The ARL2 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The ARL2 solution (0.25 mg/ml) contains 20mM Tris-HCl buffer (pH8.0), 0.1mM PMSF, 1mM DTT and 40% Glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      ARL2 is a member of the ADP-ribosylation factor (ARF) family. ARL2 functions as a component of a secretory pathway which is involved in the Ca2-dependent release of acetylcholine. ARL2 has a role in the folding of tubule proteins, thus playing a significant role in microtubule dynamics and cell cycle progression. Unlike other members of the ARF family, ARL2 doesn’t act as an activator of the catalytic subunit of cholera toxin.

    • Synonyms

      ADP-ribosylation factor-like protein 2, ARL2, ARFL2.

    • 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 MGLLTILKKM KQKERELRLL MLGLDNAGKT TILKKFNGED IDTISPTLGF NIKTLEHRGF KLNIWDVGGQ KSLRSYWRNY FESTDGLIWV VDSADRQRMQ DCQRELQSLL VEERLAGATL LIFANKQDLP GALSSNAIRE ALELDSIRSH HWCIQGCSAV TGENLLPGID WLLDDISSRI FTAD.

    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.

    Arl2 Human
  • View Data Sheet

    Name :

    ASMT Human

    Description:

    Acetylserotonin O-Methyltransferase Human Recombinant

    HIOMT, HIOMTY, Acetylserotonin O-methyltransferase , Hydroxyindole O-methyltransferase , ASMT.

    Product # :

    ENZ-664

    Price :

    Quantity :

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    • description
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    • Citations

    Description

    ASMT Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 318 amino acids (1-298 a.a) and having a molecular mass of 35.3kDa.ASMT is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

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

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      ASMT is a member of the methyltransferase superfamily. ASMT participates in melatonin biosynthesis. ASMT Expressed in brain, retina and pineal gland, ASMT utilities to catalyze the final reaction in the synthesis of melatonin, particularly the conversion of S-adenosyl-L-methionine and N-acetylserotonin to S-adenosyl-Lhomocysteine and melatonin.

    • Synonyms

      HIOMT, HIOMTY, Acetylserotonin O-methyltransferase , Hydroxyindole O-methyltransferase , ASMT.

    • 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 MGSSEDQAYR LLNDYANGFM VSQVLFAACE LGVFDLLAEA PGPLDVAAVA AGVRASAHGT ELLLDICVSL KLLKVETRGG KAFYRNTELS SDYLTTVSPT SQCSMLKYMG RTSYRCWGHL ADAVREGRNQ YLETFGVPAE ELFTAIYRSE GERLQFMQAL QEVWSVNGRS VLTAFDLSVF PLMCDLGGDF FKDPLPEADL YILARVLHDW ADGKCSHLLE RIYHTCKPGG GILVIESLLD EDRRGPLLTQ LYSLNMLVQT EGQERTPTHY HMLLSSAGFR DFQFKKTGAI YDAILARK

    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.

    Asmt Human
  • View Data Sheet

    Name :

    OSGEP Human

    Description:

    O-Sialoglycoprotein Endopeptidase Human Recombinant

    O-Sialoglycoprotein Endopeptidase, T(6)A37 Threonylcarbamoyladenosine Biosynthesis Protein OSGEP, TRNA Threonylcarbamoyladenosine Biosynthesis Protein OSGEP, N6-L-Threonylcarbamoyladenine Synthase, T(6)A Synthase, HOSGEP, GCPL1, Probable TRNA Threonylcarbamoyladenosine Biosynthesis Protein OSGEP, Probable TRNA N6-Adenosine Threonylcarbamoyltransferase , Probable O-Sialoglycoprotein Endopeptidase, EC 3.4.24.57, EC 2.3.1.234, FLJ20411, OSGEP1, PRSMG1, KAE1, Probable tRNA N6-adenosine threonylcarbamoyltransferase.

    Product # :

    ENZ-821

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    Description

    OSGEP Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 358 amino acids (1-335 a.a) and having a molecular mass of 38.8kDa. OSGEP is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    OSGEP protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH8.0), 10% glycerol and 0.4M Urea.

    Purity

    Greater than 80.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      O-Sialoglycoprotein Endopeptidase, also known as OSGEP is a member of the KAE1 / TsaD family. OSGEP is essential for the formation of threonylcarbamoyl group on adenosine at position 37 (t6A37) in tRNAs which read codons beginning with adenine. OSGEP take a direct catalytic part in the above reaction, however other proteins of the complex are required to fulfill this activity.

    • Synonyms

      O-Sialoglycoprotein Endopeptidase, T(6)A37 Threonylcarbamoyladenosine Biosynthesis Protein OSGEP, TRNA Threonylcarbamoyladenosine Biosynthesis Protein OSGEP, N6-L-Threonylcarbamoyladenine Synthase, T(6)A Synthase, HOSGEP, GCPL1, Probable TRNA Threonylcarbamoyladenosine Biosynthesis Protein OSGEP, Probable TRNA N6-Adenosine Threonylcarbamoyltransferase , Probable O-Sialoglycoprotein Endopeptidase, EC 3.4.24.57, EC 2.3.1.234, FLJ20411, OSGEP1, PRSMG1, KAE1, Probable tRNA N6-adenosine threonylcarbamoyltransferase.

    • 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 MGSMPAVLGF EGSANKIGVG VVRDGKVLAN PRRTYVTPPG TGFLPGDTAR HHRAVILDLL QEALTESGLT SQDIDCIAYT KGPGMGAPLV SVAVVARTVA QLWNKPLVGV NHCIGHIEMG RLITGATSPT VLYVSGGNTQ VIAYSEHRYR IFGETIDIAV GNCLDRFARV LKISNDPSPG YNIEQMAKRG KKLVELPYTV KGMDVSFSGI LSFIEDVAHR MLATGECTPE DLCFSLQETV FAMLVEITER AMAHCGSQEA LIVGGVGCNV RLQEMMATMC QERGARLFAT DERFCIDNGA MIAQAGWEMF RAGHRTPLSD SGVTQRYRTD EVEVTWRD.

    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.

    Osgep Human
  • View Data Sheet

    Name :

    LCAT Human

    Description:

    Lecithin-Cholesterol Acyltransferase Human Recombinant

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

    Product # :

    ENZ-380

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    Description

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

    Source

    Escherichia Coli.

    Formulation

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

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

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

    • Synonyms

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

    • Physical Appearance

      Sterile filtered colorless solution.

    • Stability

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

    • Amino Acid Sequence

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

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

    Lcat Human
  • View Data Sheet

    Name :

    CDA Human

    Description:

    Cytidine Deaminase Human Recombinant

    Cytidine deaminase, Cytidine aminohydrolase, CDA, CDD.

    Product # :

    ENZ-007

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    Description

    CDA Human Recombinant fused with a 20 amino acid His tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 166 amino acids (1-146 a.a.) and having a molecular mass of 18.3kDa. The CDA is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The CDA solution (0.5mg/ml) contains 20mM Tris-HCl Buffer (pH 8.0), 1mM DTT, 2mM EDTA, 100mM NaCl and 40% Glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    Biological Activity

    Specific activity is > 10,000pmol/min/ug, and is defined as the amount of required to deaminate 1.0pmole of cytidine per min at pH 7.5 at 25C.

    Citations

    More Info

    • Introduction

      Cytidine deaminase (CDA) is an enzyme that scavenges exogenous and endogenous cytidine and 2'-deoxycytidine for UMP synthesis. CDA is one of several deaminases responsible for maintaining the cellular pyrimidine pool. CDA also catalyzes the deamination of chemotherapeutic cytosine nucleoside analogs such as Ara-C and 5-azacytidine, which results in the loss of their cytotoxic and antitumor function. CDA can form homotetramers and is generally expressed in granulocytes. Mutations in the CDA gene are linked to decreased sensitivity to the cytosine nucleoside analogue cytosine arabinoside used in the treatment of certain childhood leukemias.

    • Synonyms

      Cytidine deaminase, Cytidine aminohydrolase, CDA, CDD.

    • 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 MAQKRPACTL KPECVQQLLV CSQEAKQSAY CPYSHFPVGA ALLTQEGRIF KGCNIENACY PLGICAERTA IQKAVSEGYK DFRAIAIASD MQDDFISPCG ACRQVMREFG TNWPVYMTKP DGTYIVMTVQ ELLPSSFGPE DLQKTQ.

    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.

    Cda Human
  • View Data Sheet

    Name :

    UMPS Human

    Description:

    Uridine Monophosphate Synthetase Human Recombinant

    OPRT, Uridine 5'-monophosphate synthase, UMP synthase, Orotate phosphoribosyltransferase , OPRT, OPRTase, Orotidine 5'-phosphate decarboxylase , ODC, OMPdecase.

    Product # :

    ENZ-663

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    Description

    UMPS Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 500 amino acids (1-480 a.a) and having a molecular mass of 54.3kDa.UMPS is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The UMPS solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 2M Urea and 20% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      Uridine 5'-monophosphate synthase (UMPS), is a bifunctional enzyme that catalyzes the ultimate two steps of the de novo pyrimidine biosynthetic pathway. UMPS in eukaryotes links the orotate phosphoribosyltransferase and the orotidine-5’-monophosphate (OMP) decarboxylase activities into a single protein. The harmony of these 2 enzymes is assumed to be stabilized the catalytic centers as a result of the low molar concentration of the protein in mammalian cells.mutations in this gene are the reason of inherited orotic aciduria disease.

    • Synonyms

      OPRT, Uridine 5'-monophosphate synthase, UMP synthase, Orotate phosphoribosyltransferase , OPRT, OPRTase, Orotidine 5'-phosphate decarboxylase , ODC, OMPdecase.

    • 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 MAVARAALGP LVTGLYDVQA FKFGDFVLKS GLSSPIYIDL RGIVSRPRLL SQVADILFQT AQNAGISFDT VCGVPYTALP LATVICSTNQ IPMLIRRKET KDYGTKRLVE GTINPGETCL IIEDVVTSGS SVLETVEVLQ KEGLKVTDAI VLLDREQGGK DKLQAHGIRL HSVCTLSKML EILEQQKKVD AETVGRVKRF IQENVFVAAN HNGSPLSIKE APKELSFGAR AELPRIHPVA SKLLRLMQKK ETNLCLSADV SLARELLQLA DALGPSICML KTHVDILNDF TLDVMKELIT LAKCHEFLIF EDRKFADIGN TVKKQYEGGI FKIASWADLV NAHVVPGSGV VKGLQEVGLP LHRGCLLIAE MSSTGSLATG DYTRAAVRMA EEHSEFVVGF ISGSRVSMKP EFLHLTPGVQ LEAGGDNLGQ QYNSPQEVIG KRGSDIIIVG RGIISAADRL EAAEMYRKAA WEAYLSRLGV.

    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.

    Umps Human
  • View Data Sheet

    Name :

    ADH5 Human

    Description:

    Alcohol Dehydrogenase 5 Human Recombinant

    Alcohol dehydrogenase 5 (class III) chi polypeptide, Alcohol dehydrogenase class chi chain, Glutathione-dependent formaldehyde dehydrogenase, S-(hydroxymethyl) glutathione dehydrogenase, FDH, ADHX, ADH-3, FALDH, GSH-FDH, GSNOR, EC 1.1.1.1, EC 1.1.1.284.

    Product # :

    ENZ-595

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    Description

    ADH5 Recombinant produced in E. coli is a single polypeptide chain containing 398 amino acids (1-374) and having a molecular mass of 42.3kDa.ADH5 is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    The ADH5 solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 100mM NaCl, 1mM DTT and 20% glycerol.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      ADH5 belongs to the alcohol dehydrogenase family which metabolizes a large selection of substrates, such as retinol, ethanol, other aliphatic alcohols, hydroxysteroids, and lipid peroxidation products. ADH5 has practically no activity for ethanol oxidation, but displays high activity for oxidation of long-chain primary alcohols and for oxidation of S-hydroxymethyl-glutathione, a spontaneous adduct between glutathione and formaldehyde. ADH5 enzyme is a key factor of cellular metabolism for the removal of formaldehyde, a powerful aggravating and alerting mediator which causes pharyngitis, lacrymation, rhinitis and contact dermatitis.

    • Synonyms

      Alcohol dehydrogenase 5 (class III) chi polypeptide, Alcohol dehydrogenase class chi chain, Glutathione-dependent formaldehyde dehydrogenase, S-(hydroxymethyl) glutathione dehydrogenase, FDH, ADHX, ADH-3, FALDH, GSH-FDH, GSNOR, EC 1.1.1.1, EC 1.1.1.284.

    • 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 MGSHMANEVI KCKAAVAWEA GKPLSIEEIE VAPPKAHEVR IKIIATAVCH TDAYTLSGAD PEGCFPVILG HEGAGIVESV GEGVTKLKAG DTVIPLYIPQ CGECKFCLNP KTNLCQKIRV TQGKGLMPDG TSRFTCKGKT ILHYMGTSTF SEYTVVADIS VAKIDPLAPL DKVCLLGCGI STGYGAAVNT AKLEPGSVCA VFGLGGVGLA VIMGCKVAGA SRIIGVDINK DKFARAKEFG ATECINPQDF SKPIQEVLIE MTDGGVDYSF ECIGNVKVMR AALEACHKGW GVSVVVGVAA SGEEIATRPF QLVTGRTWKG TAFGGWKSVE SVPKLVSEYM SKKIKVDEFV THNLSFDEIN KAFELMHSGK SIRTVVKI

    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.

    Adh5 Human
  • View Data Sheet

    Name :

    NAA30 Human

    Description:

    N Alpha-Acetyltransferase 30, NatC Catalytic Subunit Human Recombinant

    N(Alpha)-Acetyltransferase 30, NatC Catalytic Subunit, C14orf35, NAT12, N-Acetyltransferase 12 (GCN5-Related, Putative), N-Acetyltransferase 12, NatC Catalytic Subunit, MAK3, N-Acetyltransferase MAK3 Homolog, Chromosome 14 Open Reading Frame 35, Mak3p, NAT12P, N-Alpha-Acetyltransferase 30, N-Alpha-Acetyltransferase 30, NatC Catalytic Subunit, Putative N-Acetyltransferase, EC 2.3.1.88.

    Product # :

    ENZ-720

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    Description

    NAA30 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 385 amino acids (1-362 a.a) and having a molecular mass of 41.7kDa.NAA30 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    NAA30 protein solution (0.25mg/ml) containing 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

      N-alpha-acetyltransferase 30 (NAA30) is catalytic subunit of the N-terminal acetyltransferase C (NatC) complex. NAA30 catalyzes acetylation of the N-terminal methionine residues of peptides beginning with Met-Leu-Ala and Met-Leu-Gly. In addition, NAA30 is essential for the lysosomal localization and function of ARL8B. The disease Eastern equine encephalitis has been associated with NAA30.

    • Synonyms

      N(Alpha)-Acetyltransferase 30, NatC Catalytic Subunit, C14orf35, NAT12, N-Acetyltransferase 12 (GCN5-Related, Putative), N-Acetyltransferase 12, NatC Catalytic Subunit, MAK3, N-Acetyltransferase MAK3 Homolog, Chromosome 14 Open Reading Frame 35, Mak3p, NAT12P, N-Alpha-Acetyltransferase 30, N-Alpha-Acetyltransferase 30, NatC Catalytic Subunit, Putative N-Acetyltransferase, EC 2.3.1.88.

    • 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 MGSMAEVPPG PSSLLPPPAP PAPAAVEPRC PFPAGAALAC CSEDEEDDEE HEGGGSRSPA GGESATVAAK GHPCLRCPQP PQEQQQLNGL ISPELRHLRA AASLKSKVLS VAEVAATTAT PDGGPRATAT KGAGVHSGER PPHSLSSNAR TAVPSPVEAA AASDPAAARN GLAEGTEQEE EEEDEQVRLL SSSLTADCSL RSPSGREVEP GEDRTIRYVR YESELQMPDI MRLITKDLSE PYSIYTYRYF IHNWPQLCFL AMVGEECVGA IVCKLDMHKK MFRRGYIAML AVDSKYRRNG IGTNLVKKAI YAMVEGDCDE VVLETEITNK SALKLYENLG FVRDKRLFRY YLNGVDALRL KLWLR

    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.

    Naa30 Human
  • View Data Sheet

    Name :

    NARS Human

    Description:

    Asparaginyl-TRNA Synthetase Human Recombinant

    NARS, Asparaginyl-TRNA Synthetase, AsnRS, EC 6.1.1.22, Asparaginyl-TRNA Synthetase, Cytoplasmic, Asparagine TRNA Ligase 1, Cytoplasmic, Asparagine--TRNA Ligase, Cytoplasmic, Asparagine TRNA Ligase 1, Cytoplasmic, NARS1.

    Product # :

    ENZ-915

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    Description

    NARS Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 571 amino acids (1-548 a.a) and having a molecular mass of 65.3kDa. NARS is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    NARS protein solution (0.25mg/ml) containing Phosphate Buffered Saline (pH7.4) and 10% glycerol.

    Purity

    Greater than 80.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      Aminoacyl-tRNA synthetases are a class of enzymes which charge tRNAs with their cognate amino acids. Asparaginyl-tRNA synthetase (NARS) is localized to the cytoplasm and is a member of the class II family of tRNA synthetases. The N-terminal domain characterizes the signature sequence for the eukaryotic asparaginyl-tRNA synthetases.

    • Synonyms

      NARS, Asparaginyl-TRNA Synthetase, AsnRS, EC 6.1.1.22, Asparaginyl-TRNA Synthetase, Cytoplasmic, Asparagine TRNA Ligase 1, Cytoplasmic, Asparagine--TRNA Ligase, Cytoplasmic, Asparagine TRNA Ligase 1, Cytoplasmic, NARS1.

    • 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

      GSSHHHHHH SSGLVPRGSH MGSMVLAELY VSDREGSDAT GDGTKEKPFK TGLKALMTVG KEPFPTIYVD SQKENERWNV ISKSQLKNIK KMWHREQMKS ESREKKEAED SLRREKNLEE AKKITIKNDP SLPEPKCVKI GALEGYRGQR VKVFGWVHRL RRQGKNLMFL VLRDGTGYLQ CVLADELCQC YNGVLLSTES SVAVYGMLNL TPKGKQAPGG HELSCDFWEL IGLAPAGGAD NLINEESDVD VQLNNRHMMI RGENMSKILK ARSMVTRCFR DHFFDRGYYE VTPPTLVQTQ VEGGATLFKL DYFGEEAFLT QSSQLYLETC LPALGDVFCI AQSYRAEQSR TRRHLAEYTH VEAECPFLTF DDLLNRLEDL VCDVVDRILK SPAGSIVHEL NPNFQPPKRP FKRMNYSDAI VWLKEHDVKK EDGTFYEFGE DIPEAPERLM TDTINEPILL CRFPVEIKSF YMQRCPEDSR LTESVDVLMP NVGEIVGGSM RIFDSEEILA GYKREGIDPT PYYWYTDQRK YGTCPHGGYG LGLERFLTWI LNRYHIRDVC LYPRFVQRCT 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.

    Human Nars
  • View Data Sheet

    Name :

    ECI1 Human

    Description:

    Enoyl-CoA Delta Isomerase 1 Human Recombinant

    Enoyl-CoA delta isomerase 1, mitochondrial, 3,2-trans-enoyl-CoA isomerase, Enoyl-CoA Delta Isomerase 1, Delta(3),Delta(2)-enoyl-CoA isomerase, D3,D2-enoyl-CoA isomerase, Dodecenoyl-CoA isomerase, ECI1, DCI.

    Product # :

    ENZ-758

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    Description

    ECI1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 284 amino acids (42-302 a.a.) and having a molecular mass of 31.1kDa. ECI1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    ECI1 protein solution (0.25mg/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

      Enoyl-CoA Delta Isomerase 1 (ECI1) is a main mitochondrial enzyme which takes part in beta-oxidation of unsaturated fatty acids. ECI1 is a member of the hydratase/isomerase superfamily. ECI1 catalyzes the transformation of 3-cis and 3-trans-enoyl-CoA esters to the 2-trans-enoylCoA intermediates.

    • Synonyms

      Enoyl-CoA delta isomerase 1, mitochondrial, 3,2-trans-enoyl-CoA isomerase, Enoyl-CoA Delta Isomerase 1, Delta(3),Delta(2)-enoyl-CoA isomerase, D3,D2-enoyl-CoA isomerase, Dodecenoyl-CoA isomerase, ECI1, DCI.

    • 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 MGSFGSQRVL VEPDAGAGVA VMKFKNPPVN SLSLEFLTEL VISLEKLEND KSFRGVILTS DRPGVFSAGL DLTEMCGRSP AHYAGYWKAV QELWLRLYQS NLVLVSAING ACPAGGCLVA LTCDYRILAD NPRYCIGLNE TQLGIIAPFW LKDTLENTIG HRAAERALQL GLLFPPAEAL QVGIVDQVVP EEQVQSTALS AIAQWMAIPD HARQLTKAMM RKATASRLVT QRDADVQNFV SFISKDSIQK SLQMYLERLK EEKG.

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    Eci1 Human
  • View Data Sheet

    Name :

    ENO2 Mouse

    Description:

    Enolase-2 Mouse Recombinant

    AI837106, D6Ertd375e, Eno-2, NSE, 2-phospho-D-glycerate hydro-lyase, Enolase 2, Neural enolase, Neuron-specific enolase.

    Product # :

    ENZ-1028

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    • biological activity
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    Description

    ENO2 Mouse Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 457 amino acids (1-434) and having a molecular mass of 49.7kDa.ENO2 is fused to a 23 amino acid His-tag at N-terminus& purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The ENO2 solution (1mg/ml) contains Phosphate Buffered Saline (pH7.4) and 10% glycerol.

    Purity

    Greater than 95% as determined by SDS-PAGE.

    Biological Activity

    Specific activity is > 10,000 pmol/min/µg, and was obtained by measuring the decrease of NAD in absorbance at 340nm resulting from NADH at pH 6.5 at 37°C.

    Citations

    More Info

    • Introduction

      Neuron-specificenolase also caled NSE is a glycolytic isoenzyme which is situated in central and peripheral neurons and neuroendocrine cells. Enolase-2 is released into the CSF when neural tissue is injured. Neoplasms derived from neural or neuroendocrine tissue release Enolase-2 into the blood. Enolase-2 is a useful substance that has been detected in patients with certain tumors, such as neuroblastoma, small cell lung cancer, medullary thyroid cancer, carcinoid tumors, pancreatic endocrine tumors, and melanoma. ENO2 is 1 of the 3 enolase isoenzymes found in mammals. ENO2 isoenzyme, is found in mature neurons and cells of neuronal origin. An exchange from alpha enolase to gamma enolase occurs in neural tissue during development in rats and primates.

    • Synonyms

      AI837106, D6Ertd375e, Eno-2, NSE, 2-phospho-D-glycerate hydro-lyase, Enolase 2, Neural enolase, Neuron-specific enolase.

    • Physical Appearance

      Sterile Filtered clear 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 MGSMSIEKIW AREILDSRGN PTVEVDLYTA KGLFRAAVPS GASTGIYEAL ELRDGDKQRY LGKGVLKAVD HINSRIAPAL ISSGISVVEQ EKLDNLMLEL DGTENKSKFG ANAILGVSLA VCKAGAAERD LPLYRHIAQL AGNSDLILPV PAFNVINGGS HAGNKLAMQE FMILPVGAES FRDAMRLGAE VYHTLKGVIK DKYGKDATNV GDEGGFAPNI LENSEALELV KEAIDKAGYT EKMVIGMDVA ASEFYRDGKY DLDFKSPADP SRYITGDQLG ALYQDFVRNY PVVSIEDPFD QDDWAAWSKF TANVGIQIVG DDLTVTNPKR IERAVEEKAC NCLLLKVNQI GSVTEAIQAC KLAQENGWGV MVSHRSGETE DTFIADLVVG LCTGQIKTGA PCRSERLAKY NQLMRIEEEL GDEARFAGHN FRNPSVL.

    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.

    Eno2 Mouse
  • View Data Sheet

    Name :

    PNPT1 Human

    Description:

    Polyribonucleotide Nucleotidyltransferase 1 Human Recombinant

    Polyribonucleotide Nucleotidyltransferase 1, Polynucleotide Phosphorylase-Like Protein, Polynucleotide Phosphorylase 1, 3-5 RNA Exonuclease OLD35, PNPase Old-35, EC 2.7.7.8, PNPase 1, COXPD13, DFNB70, PNPASE, OLD35, Polyribonucleotide Nucleotidyltransferase 1, Mitochondrial, Deafness, Autosomal Recessive 70, Polynucleotide Phosphorylase, 3-5 RNA Exonuclease, EC 2.7.7, Old-35, Polyribonucleotide nucleotidyltransferase 1, mitochondrial, 3'-5' RNA exonuclease OLD35, PNPase old-35.

    Product # :

    ENZ-888

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    Description

    PNPT1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 761 amino acids (46-783 a.a) and having a molecular mass of 83.3kDa. PNPT1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    PNPT1 protein solution (0.25mg/ml) containing Phosphate buffered saline (pH7.4), 10% glycerol and 1mM DTT.

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      Polyribonucleotide nucleotidyltransferase 1, also known as PNPT1 is predominantly localized in the mitochondrial intermembrane space and is implicated in the import of RNA to mitochondria. Mutations in PNPT1 have been connected with combined oxidative phosphorylation deficiency-13 as well as autosomal recessive nonsyndromic deafness-70. Related pseudogenes have been found on chromosomes 3 & 7.

    • Synonyms

      Polyribonucleotide Nucleotidyltransferase 1, Polynucleotide Phosphorylase-Like Protein, Polynucleotide Phosphorylase 1, 3-5 RNA Exonuclease OLD35, PNPase Old-35, EC 2.7.7.8, PNPase 1, COXPD13, DFNB70, PNPASE, OLD35, Polyribonucleotide Nucleotidyltransferase 1, Mitochondrial, Deafness, Autosomal Recessive 70, Polynucleotide Phosphorylase, 3-5 RNA Exonuclease, EC 2.7.7, Old-35, Polyribonucleotide nucleotidyltransferase 1, mitochondrial, 3'-5' RNA exonuclease OLD35, PNPase old-35.

    • 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 MGSAVAVDLG NRKLEISSGK LARFADGSAV VQSGDTAVMV TAVSKTKPSP SQFMPLVVDY RQKAAAAGRI PTNYLRREIG TSDKEILTSR IIDRSIRPLF PAGYFYDTQV LCNLLAVDGV NEPDVLAING ASVALSLSDI PWNGPVGAVR IGIIDGEYVV NPTRKEMSSS TLNLVVAGAP KSQIVMLEAS AENILQQDFC HAIKVGVKYT QQIIQGIQQL VKETGVTKRT PQKLFTPSPE IVKYTHKLAM ERLYAVFTDY EHDKVSRDEA VNKIRLDTEE QLKEKFPEAD PYEIIESFNV VAKEVFRSIV LNEYKRCDGR DLTSLRNVSC EVDMFKTLHG SALFQRGQTQ VLCTVTFDSL ESGIKSDQVI TAINGIKDKN FMLHYEFPPY ATNEIGKVTG LNRRELGHGA LAEKALYPVI PRDFPFTIRV TSEVLESNGS SSMASACGGS LALMDSGVPI SSAVAGVAIG LVTKTDPEKG EIEDYRLLTD ILGIEDYNGD MDFKIAGTNK GITALQADIK LPGIPIKIVM EAIQQASVAK KEILQIMNKT ISKPRASRKE NGPVVETVQV PLSKRAKFVG PGGYNLKKLQ AETGVTISQV DEETFSVFAP TPSAMHEARD FITEICKDDQ EQQLEFGAVY TATITEIRDT GVMVKLYPNM TAVLLHNTQL DQRKIKHPTA LGLEVGQEIQ VKYFGRDPAD GRMRLSRKVL QSPATTVVRT LNDRSSIVMG EPISQSSSNS Q.

    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.

    Pnpt1 Human
  • View Data Sheet

    Name :

    GALNT1 Mouse

    Description:

    Polypeptide N-Acetylgalactosaminyltransferase 1 Mouse Recombinant

    Polypeptide N-acetylgalactosaminyltransferase 1, Polypeptide GalNAc transferase 1, GalNAc-T1, pp-GaNTase 1, Protein-UDP acetylgalactosaminyltransferase 1, polypeptide N-acetylgalactosaminyltransferase 1. 

    Product # :

    ENZ-1066

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    Description

    GALNT1 produced in Sf9 Insect cells is a single, glycosylated polypeptide chain containing 528 amino acids (41-559 a.a.) and having a molecular mass of 60.5kDa (Molecular size on SDS-PAGE will appear at approximately 50-70kDa).GALNT1 is expressed with an 9 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Insect cells.

    Formulation

    GALNT1 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.

    Citations

    More Info

    • Introduction

      Polypeptide N-Acetylgalactosaminyltransferase 1 (Galnt1) , is part of the UDP-N-acetyl-alpha-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase (GalNAc-T) family of enzymes. The initial reaction in O-linked oligosaccharide biosynthesis is catalyzed by Glant1, the transfer of an N-acetyl-D-galactosamine residue to a serine or threonine residue on the protein receptor. Moreover, Galnt1 is implicated in the glycosylation of proteins vital for bone formation for instance osteopontin and bone sialoprotein.

    • Synonyms

      Polypeptide N-acetylgalactosaminyltransferase 1, Polypeptide GalNAc transferase 1, GalNAc-T1, pp-GaNTase 1, Protein-UDP acetylgalactosaminyltransferase 1, polypeptide N-acetylgalactosaminyltransferase 1.

    • Physical Appearance

      Sterile filtered colorless solution.

    • Stability

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

    • Amino Acid Sequence

      ADPGLPAGDV LELVQKPHEG PGEMGKPVVI PKEDQEKMKE MFKINQFNLM ASEMIALNRS LPDVRLEGCK TKVYPDNLPT TSVVIVFHNE AWSTLLRTVH SVINRSPRHM IEEIVLVDDA SERDFLKRPL ESYVKKLKVP VHVIRMEQRS GLIRARLKGA AVSRGQVITF LDAHCECTAG WLEPLLARIK HDRRTVVCPI IDVISDDTFE YMAGSDMTYG GFNWKLNFRW YPVPQREMDR RKGDRTLPVR TPTMAGGLFS IDRDYFQEIG TYDAGMDIWG GENLEISFRI WQCGGTLEIV TCSHVGHVFR KATPYTFPGG TGQIINKNNR RLAEVWMDEF KNFFYIISPG VTKVDYGDIS SRLGLRRKLQ CKPFSWYLEN IYPDSQIPRH YFSLGEIRNV ETNQCLDNMA RKENEKVGIF NCHGMGGNQV FSYTANKEIR TDDLCLDVSK LNGPVTMLKC HHLKGNQLWE YDPVKLTLQH VNSNQCLDKA TEEDSQVPSI RDCTGSRSQQ WLLRNVTLPE IFHHHHHH .

    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.

    Galnt1 Mouse
  • View Data Sheet

    Name :

    UPP1 Salmonella

    Description:

    Uridine Phosphorylase Salmonella Typhimurium Recombinant

    Uridine phosphorylase, EC 2.4.2.3, UrdPase, UPase, StUP.

    Product # :

    ENZ-348

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    Description

    Uridine phosphorylase Salmonella typhimurium Recombinantproduced in E.Coli is a non-glycosylated, polypeptide having a total molecular mass of 163068 Dalton.

    Source

    Escherichia Coli.

    Formulation

    The UPase was lyophilized from 1mg/ml solution containing 25mM Tris-HCl, pH 8.0, 0.15M NaCl.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      Uridine phosphorylase from Salmonella typhimurium (StUP) catalyzes the reversible phosphorolysis of uridine with the formation of ribose-1-phosphate and uracil.

    • Synonyms

      Uridine phosphorylase, EC 2.4.2.3, UrdPase, UPase, StUP.

    • Physical Appearance

      Sterile Filtered white lyophilized powder.

    • Stability

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

    • Enzymatic Activity

      30 U/mg protein.

    • Unit Definition

      One unit phosphorylates 1μm of uridine within 1 min at pH 7.3.

    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.

    Uridine Phosphorylase Salmonella Typhimurium
  • View Data Sheet

    Name :

    NME2 Human

    Description:

    Non-Metastatic Cells 2 Human Recombinant

    Nucleoside diphosphate kinase B, NDPK-B, NDPKB, NM23-H2, NM23B, EC 2.7.4.6, NDP kinase B, C-myc purine-binding transcription factor PUF, NDK B, NME2, puf, MGC111212.

    Product # :

    PKA-363

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    Description

    NME2 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 152 amino acids (1-152 a.a.) and having a molecular mass of 17.2kDa. The NME2 is purified by conventional chromatography.

    Source

    Escherichia Coli.

    Formulation

    The NME2 protein solution contains 20mM Tris-HCl pH-8, 1mM DTT, and 10% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      NME2 takes an important part in the synthesis of nucleoside triphosphates other than ATP. NME2 negatively controls Rho activity by interacting with AKAP13/LBC. NME2 acts as a transcriptional activator of the MYC gene. NME2 binds DNA non-specifically. NME2 is a heterodimeric enzyme functioning as a nucleoside diphosphate kinase. NME1 and NME2 contain 152 amino acids, A and B polypeptide chains of the NM23 enzyme, respectively. NME2 is identical to the beta subunit of human erythrocyte NDP kinase. NDP kinases participate in the synthesis of nucleoside triphosphates, and NM23 is involved in the regulation of signal transduction by complexing with G proteins, causing activation/inactivation of developmental pathways.

    • Synonyms

      Nucleoside diphosphate kinase B, NDPK-B, NDPKB, NM23-H2, NM23B, EC 2.7.4.6, NDP kinase B, C-myc purine-binding transcription factor PUF, NDK B, NME2, puf, MGC111212.

    • 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

      MANLERTFIA IKPDGVQRGL VGEIIKRFEQ KGFRLVAMKF LRASEEHLKQ HYIDLKDRPF FPGLVKYMNS GPVVAMVWEG LNVVKTGRVM LGETNPADSK PGTIRGDFCI QVGRNIIHGS DSVKSAEKEI SLWFKPEELV DYKSCAHDWV YE.

    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.

    Nme2 Human
  • View Data Sheet

    Name :

    Taq Plus DNA

    Description:

    Taq Plus DNA Polymerase Recombinant

    Taq Plus DNA Polymerase, Taq Plus DNA, TaqPDNA.

    Product # :

    ENZ-309

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    Description

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

    Source

    Recombinant E.coli contains Thermus aquaticus polymerase gene.

    Formulation

    5U/µl.

    Citations

    More Info

    • Synonyms

      Taq Plus DNA Polymerase, Taq Plus DNA, TaqPDNA.

    • Stability

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

    • Optimization of DNA Synthesis

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

    • Reaction Conditions

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

    • Storage Buffer

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

    • Note

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

    • Unit Definition

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

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

    Taq Plus Dna
  • View Data Sheet

    Name :

    Adipotide

    Description:

    Adipotide

    Product # :

    HOR-060

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    Description

    Adipotide is a synthetic single, non-glycosylated polypeptide chain containing 25 amino acids, having a molecular mass of 2555 Dalton and a Molecular formula of C111H204N36O28S2.

    Formulation

    The protein was lyophilized with no additives.

    Purity

    Greater than 97.0% as determined by analysis by RP-HPLC.

    Citations

    More Info

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Amino Acid Sequence

      H-Cys-Lys-Gly-Gly-Arg-Ala-Lys-AspCys-Gly-Gly-d-Lys-d-Leu-d-Ala-d-Lys-d-Leu-d-Ala-d-Lys-d-Lys-d-Leud-Ala-d-Lys-d-Leu-d-Ala-d-Lys-OH (disulfide bond).

    • Background

      Adipotide is a proapoptotic peptidomimetic which selectively destroy the blood vessels supplying white adipose tissue. Adipotide plays a main role in translational metabolic research. Adipotide is the most potent proof-of-concept for non-hormonal, vascular-targeted fat reduction.

    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.

    Adipotide
  • View Data Sheet

    Name :

    ACTH

    Description:

    Adrenocorticotropic Hormone

    Corticotropin-lipotropin, Pro-opiomelanocortin, POMC, ACTH, LPH, MSH, NPP, POC, CLIP, Tetracosactide.

    Product # :

    HOR-279

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    Description

    The Molecular formula of Adrenocorticotropic Hormone is C136H210N40O31S and the molecular weight is 2933.5 Dalton.

    Formulation

    The ACTH hormone was lyophilized with no additives.

    Purity

    Greater than 98.0% as determined by:
    (a) Analysis by RP-HPLC.
    (b) Analysis by SDS-PAGE.

    Citations

    More Info

    • Introduction

      Adrenocorticotropic hormone, as its name implies, stimulates the adrenal cortex. More specifically, it stimulates secretion of glucocorticoids such as cortisol, and has little control over secretion of aldosterone, the other major steroid hormone from the adrenal cortex. Stimulates secretion of adrenal corticosteroids and induces growth of adrenal cortex. ACTH also called Tetracosactide directly activates G-proteins. A stimulator of adenylate cyclase and cAMP formation.

    • Synonyms

      Corticotropin-lipotropin, Pro-opiomelanocortin, POMC, ACTH, LPH, MSH, NPP, POC, CLIP, Tetracosactide.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Amino Acid Sequence

      Ser-Tyr-Ser-Met-Glu-His-Phe-Arg-Trp-Gly-Lys-Pro-Val-Gly-Lys-Lys-Arg-Arg-Pro-Val-Lys-Val-Tyr-Pro-OH.

    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.

    Acth
  • View Data Sheet

    Name :

    AIMP1 Antibody

    Description:

    Aminoacyl tRNA Synthetase Complex-Interacting Multifunctional Protein 1, Mouse Anti Human

    Aminoacyl tRNA synthase complex-interacting multifunctional protein 1, Multisynthase complex auxiliary component p43, AIMP1, EMAP2, SCYE1, p43, EMAPII.

    Product # :

    ANT-619

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    Formulation

    1mg/ml containing PBS, pH-7.4, 10% Glycerol and 0.02% Sodium Azide.

    Citations

    More Info

    • Introduction

      AIMP1 (EMPA2 or p43) is a cytokine that is specifically induced by apoptosis, and it is involved in the control of angiogenesis, inflammation, and wound healing. The release of the AIMP1 cytokine renders the tumor-associated vasculature sensitive to tumor necrosis factor. Furthermore, AIMP1 is involved in the stimulation of inflammatory responses after proteolytic cleavage in tumor cells.

    • Synonyms

      Aminoacyl tRNA synthase complex-interacting multifunctional protein 1, Multisynthase complex auxiliary component p43, AIMP1, EMAP2, SCYE1, p43, EMAPII.

    • Physical Appearance

      Sterile filtered colorless solution.

    • Immunogen

      Anti-human AIMP1 mAb, is derived from hybridization of mouse F0 myeloma cells with spleen cells from BALB/c mice immunized with a recombinant human AIMP1 protein 1-336 amino acids purified from E. coli.

    • Ig Subclass

      Mouse IgG2a heavy chain and Kappa light chain.

    • Clone

      PAT6D10AT.

    • Applications

      The antibody has been tested by ELISA, Western blot analysis, Flow cytometry and ICC/IF to assure specificity and reactivity. Since application varies, however, each investigation should be titrated by the reagent to obtain optimal results.

    • Type

      Mouse Anti Human Monoclonal.

    • Storage Procedures

      For periods up to 1 month store at 4°C, for longer periods of time, store at -20°C. Prevent freeze thaw cycles.

    • Purification Method

      AIMP1 antibody was purified by protein-A affinity chromatography.

    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.

    Aimp1 Antibody
  • View Data Sheet

    Name :

    SAE1 Human

    Description:

    SUMO1 Activating Enzyme Subunit 1 Human Recombinant

    AOS1, HSPC140, SUA1, UBLE1A, SAE1, SUMO1 Activating Enzyme Subunit 1, FLJ3091.

    Product # :

    ENZ-534

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    Description

    SAE1 Recombinant Human produced in E.Coli is a single, non-glycosylated polypeptide chain containing 378 amino acids (1-346 a.a.) and having a molecular mass of 42.2 kDa. The SAE1 is fused to 32 amino acid T7-Tag at N-terminus and purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    SAE1 Human solution containing 20mM Tris pH-8, 1mM DTT & 10% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      SAE1 is part of the ubiquitin-activating E1 family of proteins and participates in the significant first step of the UBL1 conjugation pathway. Proteins conjugated to Ub are marked for progressive degradation by the 26S Proteasome. SAE1 acts as a UBLI E1 ligase mediating the ATP-dependent activation of UBL1. SAE1 binds with UBLE1A and UBLE1B to form a heterodimer which can bind UBL1. SAE1 is a dimeric enzyme that takes part as a E1 ligase for SUMO1, SUMO2, SUMO3, and probably SUMO4. SAE1 regulates ATP-dependent activation of SUMO proteins and formation of a thioester with a conserved cysteine residue on SAE2.

    • Synonyms

      AOS1, HSPC140, SUA1, UBLE1A, SAE1, SUMO1 Activating Enzyme Subunit 1, FLJ3091.

    • 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

      MHHHHHHMAS MTGGQQMGRD LYDDDDKDRW GSMVEKEEAG GGISEEEAAQ YDRQIRLWGL EAQKRLRASR VLLVGLKGLG AEIAKNLILA GVKGLTMLDH EQVTPEDPGA QFLIRTGSVG RNRAEASLER AQNLNPMVDV KVDTEDIEKK PESFFTQFDA VCLTCCSRDV IVKVDQICHK NSIKFFTGDV FGYHGYTFAN LGEHEFVEEK TKVAKVSQGV EDGPDTKRAK LDSSETTMVK KKVVFCPVKE ALEVDWSSEK AKAALKRTTS DYFLLQVLLK FRTDKGRDPS SDTYEEDSEL LLQIRNDVLD SLGISPDLLP EDFVRYCFSE MAPVCAVVGG ILAQEIVKAL SQRDPPHNNF FFFDGMKGNG IVECLGPK.

    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.

    Sae1 Human
  • View Data Sheet

    Name :

    CA13 Human

    Description:

    Carbonic Anhydrase XIII Human Recombinant

    Carbonic Anhydrase XIII, Carbonate Dehydratase XIII, EC 4.2.1.1, CA-XIII, Carbonic, Anhydrase 13, CAXIII.

    Product # :

    ENZ-902

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    More Info

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

    Description

    CA13 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 285 amino acids (1-262a.a) and having a molecular mass of 31.8kDa.CA13 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    CA13 protein solution (0.5mg/ml) containing Phosphate buffered saline (pH7.4),10% glycerol and 1mM DTT.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    Biological Activity

    Specific activity is > 2,500 pmol/min/ug, and is defined as the amount of enzyme that hydrolyze 1.0 pmole of 4-nitrophenyl acetate to 4-nitrophenol per minute at pH 7.5 at 37C.

    Citations

    More Info

    • Introduction

      Carbonic Anhydrase XIII, also known as CA13 is a member of the alpha-carbonic anhydrase family, which catalyzes the rapid interconversion of carbon dioxide and water tobicarbonate and protons, a reversible reaction which occurs relatively slowly in the absence of catalyst. Furthermore, the active siteof nearly all carbonic anhydrases contains a zinc ion; they have been classified as metalloenzymes. At least fivedistinct CA families (?, ?, ?, ? and ?) have been found. These families have no significant a.a sequence resemblance and in just about allcases are considered to be an example of convergent evolution. The ?-CAs have been demonstrated in humans.

    • Synonyms

      Carbonic Anhydrase XIII, Carbonate Dehydratase XIII, EC 4.2.1.1, CA-XIII, Carbonic, Anhydrase 13, CAXIII.

    • 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 SSGLVPRGSP MGSMSRLSWG YREHNGPIHW KEFFPIADGD QQSPIEIKTK EVKYDSSLRP LSIKYDPSSA KIISNSGHSF NVDFDDTENK SVLRGGPLTG SYRLRQVHLH WGSADDHGSE HIVDGVSYAA ELHVVHWNSD KYPSFVEAAH EPDGLAVLGV FLQIGEPNSQ LQKITDTLDS IKEKGKQTRF TNFDLLSLLP PSWDYWTYPG SLTVPPLLES VTWIVLKQPI NISSQQLAKF RSLLCTAEGE AAAFLVSNHR PPQPLKGRKV RASFH.

    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.

    Ca13 Human
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