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Search results

1000 results found for “Chitinase”

Name

Description

Product #

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  • View Data Sheet

    Name :

    GATM Human

    Description:

    Glycine Amidinotransferase Human Recombinant

    Glycine amidinotransferase, mitochondrial, L-arginine:glycine amidinotransferase, Transamidinase, GATM, AGAT, AT.

    Product # :

    ENZ-583

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    Description

    GATM Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 410 amino acids (38-423) and having a molecular mass of 46.9kDa (Molecular size on SDS-PAGE will appear higher).GATM is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    The GATM solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 2mM DTT, 10% glycerol and 200mM NaCl.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    More Info

    • Introduction

      Glycine amidinotransferase mitochondrial (GATM) is a mitochondrial enzyme which is a member of the amidinotransferase family. The GATM enzyme is involved in creatine biosynthesis, where it catalyzes the transfer of a guanido group from L-arginine to glycine, resulting in guanidinoacetic acid, the immediate precursor of creatine, which has an imperative role in energy metabolism in muscle tissues. GATM is significant in embryonic and central nervous system development. GATM gene mutations cause arginine:glycine amidinotransferase deficiency, an inborn error of creatine synthesis characterized by mental retardation, language impairment, and behavioral disorders.

    • Synonyms

      Glycine amidinotransferase, mitochondrial, L-arginine:glycine amidinotransferase, Transamidinase, GATM, AGAT, AT.

    • 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 MGSMSTQAAT ASSRNSCAAD DKATEPLPKD CPVSSYNEWD PLEEVIVGRA ENACVPPFTI EVKANTYEKY WPFYQKQGGH YFPKDHLKKA VAEIEEMCNI LKTEGVTVRR PDPIDWSLKY KTPDFESTGL YSAMPRDILI VVGNEIIEAP MAWRSRFFEY
      RAYRSIIKDY FHRGAKWTTA PKPTMADELY NQDYPIHSVE DRHKLAAQGK FVTTEFEPCF DAADFIRAGR DIFAQRSQVT NYLGIEWMRR HLAPDYRVHI ISFKDPNPMH IDATFNIIGP GIVLSNPDRP CHQIDLFKKA GWTIITPPTP IIPDDHPLWM SSKWLSMNVL MLDEKRVMVD
      ANEVPIQKMF EKLGITTIKV NIRNANSLGG GFHCWTCDVR RRGTLQSYLD.

    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.

    Gatm Human
  • View Data Sheet

    Name :

    AKR1C3 Human, His

    Description:

    Aldo-Keto Reductase Family 1 Member C3 Human Recombinant, His Tag

    DD3, DDX, HAKRB, HAKRe, HA1753, HSD17B5, hluPGFS, KIAA0119, AKR1C3, Aldo-keto reductase family 1 member C3, 3-alpha-HSD type 2, 17-beta-HSD 5, PGFS, DD-3.

    Product # :

    ENZ-406

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    Description

    AKR1C3 Human Recombinant fused to 20 amino acid His Tag at N-terminal produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 343 amino acids (1-323 a.a.) and having a molecular mass of 39 kDa. The AKR1C3 is fused to a 20 amino acid His tag purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The AKR1C3 solution contains 20mM Tris-HCl pH-8 and 10% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Biological Activity

    Specific activity: approximately < 0.1 units/mg.
    Enzymatic activity was confirmed by measuring the amount of enzyme catalyzing the oxidation of 1 micromole NADPH per minute at 25C. Specific activity was expressed as units/mg protein.

    More Info

    • Introduction

      AKR1C3 is part of the aldo/keto reductase superfamily, which has at least 40 identified proteins. AKR1C3 catalyzes the conversion of aldehydes and ketones to their corresponding alcohols by utilizing NADH and/or NADPH as cofactors. AKR1C3 displays overlapping but distinct substrate specificity. AKR1C3 catalyzes the reduction of prostaglandin (PG) D2, PGH2 and phenanthrenequinone (PQ), and the oxidation of 9alpha,11beta-PGF2 to PGD2. AKR1C3 is involved in the pathogenesis of allergic diseases such as asthma. AKR1C3 controls cell growth and/or differentiation. AKR1C3 takes part in adrenal testosterone production. AKR1C3 expression is affected by metabolic disease, and its levels are considerably reduced in response to diet-induced weight loss and correlate with leptin levels.

    • Synonyms

      DD3, DDX, HAKRB, HAKRe, HA1753, HSD17B5, hluPGFS, KIAA0119, AKR1C3, Aldo-keto reductase family 1 member C3, 3-alpha-HSD type 2, 17-beta-HSD 5, PGFS, DD-3.

    • 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 MDSKHQCVKL NDGHFMPVLG FGTYAPPEVP RSKALEVTKL AIEAGFRHID SAHLYNNEEQ VGLAIRSKIA DGSVKREDIF YTSKLWSTFH RPELVRPALE NSLKKAQLDY VDLYLIHSPM SLKPGEELSP TDENGKVIFD IVDLCTTWEA MEKCKDAGLA KSIGVSNFNR RQLEMILNKPGLKYKPVCNQ VECHPYFNRS KLLDFCKSKD IVLVAYSALG SQRDKRWVDP NSPVLLEDPV LCALAKKHKR TPALIALRYQ LQRGVVVLAK SYNEQRIRQN VQVFEFQLTA EDMKAIDGLD RNLHYFNSDS FASHPNYPYS DEY.

    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.

    Akr1C3 Human
  • View Data Sheet

    Name :

    PHPT1 Human

    Description:

    Phosphohistidine Phosphatase 1 Human Recombinant

    PHP14, CGI-202, HSPC141, Phosphohistidine Phosphatase 1, Phosphohistidine Phosphatase 14kDa, Protein janus-A homolog, Sex-regulated protein Janus-a.

    Product # :

    ENZ-012

    Price :

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    Description

    PHPT1 produced in E.Coli is a single, non-glycosylated polypeptide chain containing 145 amino acids (1-125a.a.) and having a molecular mass of 15.9kDa.PHPT1 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The PHPT1 protein solution (0.5mg/1ml) is formulated in 20 mM Tris-HCl buffer (pH8.0) 0.2M NaCl, 2mM DTT and 10% glycerol.

    Purity

    Greater than 95% as determined by SDS-PAGE.

    More Info

    • Introduction

      PHPT1 is a member of the Janus protein familyand is 125 amino acid long. PHPT1 appears as a monomer in the cytoplasm and is an EDTA-insensitive phosphohistidine phosphatase. Overexpression of PHPT1 resolts in specific phosphohistidine phosphatase activity towards phosphopeptide I, with no activity detected towards phosphotyrosine, phosphothreonine and phosphoserine peptides.

    • Synonyms

      PHP14, CGI-202, HSPC141, Phosphohistidine Phosphatase 1, Phosphohistidine Phosphatase 14kDa, Protein janus-A homolog, Sex-regulated protein Janus-a.

    • 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 MAVADLALIP DVDIDSDGVF KYVLIRVHSA PRSGAPAAES KEIVRGYKWA EYHADIYDKV SGDMQKQGCD CECLGGGRIS HQSQDKKIHV YGYSMAYGPA QHAISTEKIK AKYPDYEVTW ANDGY

    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.

    Phpt1 Human
  • View Data Sheet

    Name :

    CES1G Mouse

    Description:

    Carboxylesterase 1G Mouse Recombinant

    Liver carboxylesterase 1, Acyl-coenzyme A:cholesterol acyltransferase, Carboxylesterase 1G, ES-x, CES1G.

    Product # :

    ENZ-947

    Price :

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    • description
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    • More Info

    Description

    CES1G produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 556 amino acids (19-565 a.a.) and having a molecular mass of 61.9kDa (Migrates at 50-70kDa on SDS-PAGE under reducing conditions). CES1G is expressed with a 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    CES1G protein solution (0.5mg/ml) containing Phosphate Buffered Saline (pH 7.4) and 10% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    Biological Activity

    Specific activity is > 2,000 pmol/min/ug and is defined as the amount of enzyme that hydrolyze 1pmole of p-nitrophenyl acetate to p-nitrophenol per minute at pH 7.5 at 37C.

    More Info

    • Introduction

      Carboxylesterase 1 (CES1G) belongs to a large family of carboxylesterases that are liable for the hydrolysis of ester and amide bonds. CES1G is also participates in the detoxification of xenobiotics prodrugs. CES1G shares the serine hydrolase fold observed in other esterases. CES1G found in rats and mice and is expressed mainly in liver, but also in kidney and lung.

    • Synonyms

      Liver carboxylesterase 1, Acyl-coenzyme A:cholesterol acyltransferase, Carboxylesterase 1G, ES-x, CES1G.

    • 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

      ADPHPSLPPV VHTVHGKVLG KYVTLEGFSQ PVAVFLGVPF AKPPLGSLRF APPEPAEPWS FVKHTTSYPP LCYQNPEAAL RLAELFTNQR KIIPHKFSED CLYLNIYTPA DLTQNSRLPV MVWIHGGGLV IDGASTYDGV PLAVHENVVV VVIQYRLGIW GFFSTEDEHS RGNWGHLDQV AALHWVQDNI ANFGGNPGSV TIFGESAGGE SVSVLVLSPL AKNLFHRAIA QSSVIFNPCL FGRAARPLAK KIAALAGCKT TTSAAMVHCL RQKTEDELLE VSLKMKFGTV DFLGDPRESY PFLPTVIDGV LLPKAPEEIL AEKSFNTVPY MVGINKHEFG WIIPMFLDFP LSERKLDQKT AASILWQAYP ILNISEKLIP AAIEKYLGGT EDPATMTDLF LDLIGDIMFG VPSVIVSRSH RDAGAPTYMY EYQYRPSFVS DDRPQELLGD HADELFSVWG APFLKEGASE EEINLSKMVM KFWANFARNG NPNGEGLPHW PEYDQKEGYL QIGVPAQAAH RLKDKEVDFW TELRAKETAE RSSHREHVEL 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.

    Ces1 Mouse
  • View Data Sheet

    Name :

    ELAC1 Human

    Description:

    ElaC Ribonuclease Z 1 Human Recombinant

    ElaC Ribonuclease Z 1, D29, ElaC Homolog Protein 1, TRNA 3 Endonuclease 1, TRNA Z (Short Form), Ribonuclease Z 1, Deleted In Ma29, EC 3.1.26.11, TRNase Z 1, RNaseZ(S), RNase Z 1, Zinc Phosphodiesterase ELAC Protein 1, TRNA 3 Processing Endoribonuclease, ElaC (E. Coli) Homolog 1, ElaC Homolog 1 (E. Coli), ElaC Homolog 1, TRNase ZS, ELAC1.

    Product # :

    ENZ-883

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    Description

    ELAC1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 386 amino acids (1-363 a.a) and having a molecular mass of 42.4 kDa.ELAC1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    ELAC1 protein solution (0.5mg/ml) containing Phosphate buffered saline (pH7.4), 10% glycerol and 1mM DTT.

    Purity

    Greater than 80.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      ElaC Ribonuclease Z 1, also known as ELAC1 is a member of the RNase Z family. Zinc phosphodiesterase, which shows some tRNA 3'-processing endonuclease activity. In addition, ELAC1 is implicated in tRNA maturation, by removing a 3'-trailer from precursor tRNA.

    • Synonyms

      ElaC Ribonuclease Z 1, D29, ElaC Homolog Protein 1, TRNA 3 Endonuclease 1, TRNA Z (Short Form), Ribonuclease Z 1, Deleted In Ma29, EC 3.1.26.11, TRNase Z 1, RNaseZ(S), RNase Z 1, Zinc Phosphodiesterase ELAC Protein 1, TRNA 3 Processing Endoribonuclease, ElaC (E. Coli) Homolog 1, ElaC Homolog 1 (E. Coli), ElaC Homolog 1, TRNase ZS, ELAC1.

    • 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 MGSMSMDVTF LGTGAAYPSP TRGASAVVLR CEGECWLFDC GEGTQTQLMK SQLKAGRITK IFITHLHGDH FFGLPGLLCT ISLQSGSMVS KQPIEIYGPV GLRDFIWRTM ELSHTELVFH YVVHELVPTA DQCPAEELKE FAHVNRADSP PKEEQGRTIL LDSEENSYLL FDDEQFVVKA FRLFHRIPSF GFSVVEKKRP GKLNAQKLKD LGVPPGPAYG KLKNGISVVL ENGVTISPQD VLKKPIVGRK ICILGDCSGV VGDGGVKLCF EADLLIHEAT LDDAQMDKAK EHGHSTPQMA ATFAKLCRAK RLVLTHFSQR YKPVALAREG ETDGIAELKK QAESVLDLQE VTLAEDFMVI SIPIKK

    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.

    Elac1 Human
  • View Data Sheet

    Name :

    REXO1 Human

    Description:

    RNA Exonuclease 1 Human Recombinant

    RNA exonuclease 1 homolog, Elongin-A-binding protein 1, EloA-BP1, Transcription elongation factor B polypeptide 3-binding protein 1, REXO1, ELOABP1, KIAA1138, TCEB3BP1.

    Product # :

    ENZ-767

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    Description

    REXO1 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 198 amino acids (1060-1221a.a) and having a molecular mass of 22.3kDa. REXO1 is fused to a 36 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The REXO1 solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 10% glycerol and 1mM DTT.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    More Info

    • Introduction

      REXO1 is an exonuclease domain-containing protein which binds to Elongin. The Elongin complex stimulates the rate of transcription elongation by RNA polymerase II by suppressing the transient pausing of the polymerase at many sites along the DNA template. REXO1 is composed of 1221 amino acids and its mRNA is ubiquitously expressed. REXO1 is a putative stem cell marker and is highly expressed in embryonic and adult stem cells.

    • Synonyms

      RNA exonuclease 1 homolog, Elongin-A-binding protein 1, EloA-BP1, Transcription elongation factor B polypeptide 3-binding protein 1, REXO1, ELOABP1, KIAA1138, TCEB3BP1.

    • Physical Appearance

      Sterile Filtered colorless solution.

    • Stability

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

    • Amino Acid Sequence

      MRGSHHHHHH GMASMTGGQQ MGRDLYDDDD KDRWGSIYAL DCEMSYTTYG LELTRVTVVD TDVHVVYDTF VKPDNEIVDY NTRFSGVTEA DLADTSVTLR DVQAVLLSMF SADTILIGHS LESDLLALKV IHSTVVDTSV LFPHRLGLPY KRSLRNLMAD YLRQIIQDNV DGHSSSEDAG ACMHLVIWKV REDAKTKR.

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    Rexo1 Human
  • View Data Sheet

    Name :

    MMP 3 Human, HEK

    Description:

    Matrix Metalloproteinase-3 Human Recombinant, HEK

    Stromelysin-1, EC 3.4.24.17, Matrix metalloproteinase-3, MMP-3, Transin-1, SL-1, STMY, STR1, STMY1, MGC126102, MGC126103, MGC126104.

    Product # :

    ENZ-284

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    • sds-page

    Description

    MMP-3 Human Recombinant produced in HEK293 cells is a proform of the Human MMP3 [Tyr18-Cys477 (Lys45Glu)] and fused with a ployhistide tag at the C-terminus, having an Mw of 52kDa. MMP-3 is purified by proprietary chromatographic techniques.

    Source

    HEK293 cells.

    Formulation

    The MMP-3 is supplied as a 0.2µm filtered solution in 20mM Tris-HCl, 150mM NaCl and 0.05% Brij35, pH 7.5.

    Purity

    Greater than 95% as determined by SDS-PAGE.

    Biological Activity

    The activity was measured by its ability to cleave the fluorogenic peptide substrate, Mca-RPKPVE-Nval-WRK(Dnp)-NH2. The specific activity is > 150 pmoles/min/µg.
    Recombinant Human MMP-3 protein pro form needs to be activated with Chymotrypsin.
    Activation Protocol:
    1. Dilute MMP3 to 20µg/ml in the Assay Buffer: 50mM Tris, 10mM CaCl2, 150mM NaCl, 0.05% (w/v) and Brij 35, pH 7.5.
    2. Activate MMP3 by adding Chymotrypsin(Sigma, Catalog#C­3142,1mg/ml stock in 1mM HCl) to a final concentration of 5ug/ml.
    3. Incubate at 37°C for 30 minutes.
    4. Stop activation with 2mM PMSF. Pre-warm the PMSF to 37°C prior to adding to sample.

    sds-page

    mmp-3 human hek sds-page - Product image 1

    More Info

    • Introduction

      MMP-3 enzyme is also known as Stromelysin-1or as Transin-1 which hydrolyzes natural collagen at physiological pH and temperature. It dissolves the intervertebral nucleus pulposus and annulus fibrosus of Herniated Lumbar Intervertebral Disk . MMP-3 hydrolyzes components of the extracellular matrix like proteoglycan, laminin, fibronectin, gelatin and collagen types III, IV and IX. It also activates pro-MMP-9 and pro-MMP-8 and superactivates plasmin activated MMP-1. MMP-3 is secreted as a latent proenzyme and is activated by a variety of proteinases, e.g. plasmin, trypsin, chymotrypsin, cathepsin G or human neutrophil elastase. MMP-3 was found to be capable of activating the precursor of IL1-beta.

    • Synonyms

      Stromelysin-1, EC 3.4.24.17, Matrix metalloproteinase-3, MMP-3, Transin-1, SL-1, STMY, STR1, STMY1, MGC126102, MGC126103, MGC126104.

    • Physical Appearance

      Sterile Filtered colorless solution.

    • Stability

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

    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.

    Mmp3 Human
  • View Data Sheet

    Name :

    TKT Human

    Description:

    Transketolase Human Recombinant

    Transketolase, TK, TKT1, EC 2.2.1.1.

    Product # :

    ENZ-588

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    Description

    TKT Human Recombinant produced in E. coli is a single polypeptide chain containing 643 amino acids (1-623) and having a molecular mass of 70.0kDa.TKT is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    The TKT solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 100mM Nacl, 1mM DTT and 10% glycerol.

    Purity

    Greater than 85% as determined by SDS-PAGE.

    More Info

    • Introduction

      TKT is a thiamine-dependent enzyme that takes part in the channeling of leftover sugar phosphates to glycolysis in the pentose phosphate pathway. Multiple alternatively spliced variants are known that encode the same protein.

    • Synonyms

      Transketolase, TK, TKT1, EC 2.2.1.1.

    • Physical Appearance

      Sterile Filtered colorless solution.

    • Stability

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

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MESYHKPDQQ KLQALKDTAN RLRISSIQAT TAAGSGHPTS CCSAAEIMAV LFFHTMRYKS QDPRNPHNDR FVLSKGHAAP ILYAVWAEAG FLAEAELLNL RKISSDLDGH PVPKQAFTDV ATGSLGQGLG AACGMAYTGK YFDKASYRVY CLLGDGELSE GSVWEAMAFA SIYKLDNLVA ILDINRLGQS DPAPLQHQMD IYQKRCEAFG WHAIIVDGHS VEELCKAFGQ AKHQPTAIIA KTFKGRGITG VEDKESWHGK PLPKNMAEQI IQEIYSQIQS KKKILATPPQ EDAPSVDIAN IRMPSLPSYK VGDKIATRKA YGQALAKLGH ASDRIIALDG DTKNSTFSEI FKKEHPDRFI ECYIAEQNMV SIAVGCATRN RTVPFCSTFA AFFTRAFDQI RMAAISESNI NLCGSHCGVS IGEDGPSQMA LEDLAMFRSV PTSTVFYPSD GVATEKAVEL AANTKGICFI RTSRPENAII YNNNEDFQVG QAKVVLKSKD DQVTVIGAGV TLHEALAAAE LLKKEKINIR VLDPFTIKPL DRKLILDSAR ATKGRILTVE DHYYEGGIGE AVSSAVVGEP GITVTHLAVN RVPRSGKPAE LLKMFGIDRD AIAQAVRGLI TKA.

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    Tkt Human
  • View Data Sheet

    Name :

    AKR7A3, Human

    Description:

    Aldo-Keto Reductase Family 7 Member A3 Human Recombinant

    AFAR2, Aflatoxin B1 aldehyde reductase member 3, AFB1 aldehyde reductase 2, AFB1-AR 2, AKR7A3.

    Product # :

    ENZ-1129

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    Description

    AKR7A3 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 331 amino acids (1-331) and having a molecular mass of 37.7 kDa.AKR7A3 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The AKR7A3 solution (1mg/ml) contains 10% Glycerol and 20mM Tris-HCl buffer (pH 8.5).

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    Biological Activity

    Specific activity is > 800pmol/min/ug. It is defined by the amount of enzyme that catalyzes the reduction 1.0pmole of 1,2-Naphthoquinone presence of NADPH per minute at pH 7.0 at 25˚C.

    More Info

    • Introduction

      Aldo-Keto Reductase Family 7 Member A3 or AKR7A3, is an enzyme, it is part of the detoxification of aldehydes and ketones process. AKR7A3 diminishes the dialdehyde protein-binding form of aflatoxin B1 to the non-binding AFB1 dialcohol. The enzyme takes partin protection of liver from toxic and carcinogenic effects of AFB1, a potent hepatocarcinogen.

    • Synonyms

      AFAR2, Aflatoxin B1 aldehyde reductase member 3, AFB1 aldehyde reductase 2, AFB1-AR 2, AKR7A3.

    • 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

      MSRQLSRARP ATVLGAMEMG RRMDAPTSAA VTRAFLERGH TEIDTAFVYS EGQSETILGG LGLRLGGSDC RVKIDTKAIP LFGNSLKPDS LRFQLETSLK RLQCPRVDLF YLHMPDHSTP VEETLRACHQ LHQEGKFVEL GLSNYAAWEV AEICTLCKSN GWILPTVYQG MYNAITRQVE TELFPCLRHF GLRFYAFNPL AGGLLTGKYK YEDKDGKQPV GRFFGNTWAE MYRNRYWKEH HFEGIALVEK ALQAAYGASA PSMTSATLRW MYHHSQLQGA HGDAVILGMS SLEQLEQNLA AAEEGPLEPA VVDAFNQAWH LVAHECPNYF R

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    Akr7A3 Enzyme
  • View Data Sheet

    Name :

    B3GNT2 Human

    Description:

    Beta-1,3-N-Acetylglucosaminyltransferase 2 Human Recombinant

    B3GNT2, B3GN-T2, B3GNT, B3GNT-2, B3GNT1, BETA3GNT, BGnT-2, BGNT2, N-acetyllactosaminide beta-1,3-N-acetylglucosaminyltransferase 2, Beta-1,3-N-acetylglucosaminyltransferase 1, BGnT-1, Beta-1,3-Gn-T1, Beta3Gn-T1, Beta-1,3-galactosyltransferase 7, Beta-1,3-GalTase 7, Beta3Gal-T7, Beta3GalT7, b3Gal-T7, Beta-3-Gx-T7, beta-GlcNAc beta-1,3-galactosyltransferase 7, betaGal beta-1,3-N-acetylglucosaminyltransferase 2, BGnT-2, Beta-1,3-Gn-T2, Beta-1,3-N-acetylglucosaminyltransferase 2, Beta3Gn-T2, beta-N-acetylglucosamine beta-1,3-galactosyltransferase 7.

    Product # :

    ENZ-973

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    Description

    B3GNT2 produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 375 amino acids (29-397a.a.) and having a molecular mass of 43.5kDa (Molecular size on SDS-PAGE will appear at approximately 40-57kDa). B3GNT2 is expressed with a 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    B3GNT2 protein solution (0.5mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 10% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Beta-1,3-N-Acetylglucosaminyltransferase 2 (B3GNT2) is a part of the beta-1,3-N-acetylglucosaminyltransferase family which takes part in the synthesis of poly-N-acetyllactosamine. B3GNT2 is a type II transmembrane protein which prefers the substrate of lacto-N-neotetraose. B3GNT2 catalyzes the initiation and elongation of poly-N-acetyllactosamine chains and comprises the main polylactosamine synthase.

    • Synonyms

      B3GNT2, B3GN-T2, B3GNT, B3GNT-2, B3GNT1, BETA3GNT, BGnT-2, BGNT2, N-acetyllactosaminide beta-1,3-N-acetylglucosaminyltransferase 2, Beta-1,3-N-acetylglucosaminyltransferase 1, BGnT-1, Beta-1,3-Gn-T1, Beta3Gn-T1, Beta-1,3-galactosyltransferase 7, Beta-1,3-GalTase 7, Beta3Gal-T7, Beta3GalT7, b3Gal-T7, Beta-3-Gx-T7, beta-GlcNAc beta-1,3-galactosyltransferase 7, betaGal beta-1,3-N-acetylglucosaminyltransferase 2, BGnT-2, Beta-1,3-Gn-T2, Beta-1,3-N-acetylglucosaminyltransferase 2, Beta3Gn-T2, beta-N-acetylglucosamine beta-1,3-galactosyltransferase 7.

    • Physical Appearance

      Sterile Filtered colorless solution.

    • Stability

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

    • Amino Acid Sequence

      ADPKSSSQEK NGKGEVIIPK EKFWKISTPP EAYWNREQEK LNRQYNPILS MLTNQTGEAG RLSNISHLNY CEPDLRVTSV VTGFNNLPDR FKDFLLYLRC RNYSLLIDQP DKCAKKPFLL LAIKSLTPHF ARRQAIRESW GQESNAGNQT VVRVFLLGQT PPEDNHPDLS DMLKFESEKH QDILMWNYRD TFFNLSLKEV LFLRWVSTSC PDTEFVFKGD DDVFVNTHHI LNYLNSLSKT KAKDLFIGDV IHNAGPHRDK KLKYYIPEVV YSGLYPPYAG GGGFLYSGHL ALRLYHITDQ VHLYPIDDVY TGMCLQKLGL VPEKHKGFRT FDIEEKNKNN ICSYVDLMLV HSRKPQEMID IWSQLQSAHL KCHHHHHH.

    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.

    B3Gnt2 Human
  • View Data Sheet

    Name :

    ENO2 Protein

    Description:

    Enolase-2 Human

    Gamma-enolase, EC 4.2.1.11, 2-phospho-D-glycerate hydro-lyase, Neural enolase, Neuron-specific enolase, NSE, Enolase 2, ENO2.

    Product # :

    ENZ-371

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    Description

    Human Neurone Specific Enolase produced in Human CNS having a molecular mass of 45kDa.

    Source

    Human CNS.

    Formulation

    The protein solution is in 10mM NaH2PO4 buffer pH 7.4 containing 150mM NaCl and 5mM MgSO4.

    Purity

    Greater than 96.0%.

    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

      Gamma-enolase, EC 4.2.1.11, 2-phospho-D-glycerate hydro-lyase, Neural enolase, Neuron-specific enolase, NSE, Enolase 2, ENO2.

    • Physical Appearance

      Sterile Filtered clear solution.

    • Stability

      Human NSE although stable at 4°C for 1 week, should be stored at -18°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.

    Eno2 Human
  • View Data Sheet

    Name :

    RNASE3 Human

    Description:

    Ribonuclease 3 Human Recombinant

    ECP, RNS3, Ribonuclease 3, Eosinophil cationic protein, RNASE3, RNASE3.

    Product # :

    ENZ-668

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    Description

    RNASE3 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 171 amino acids (28-160) and having a molecular mass of 19.9kDa. RNASE3 is fused to a 38 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The RNASE3 solution (1mg/ml) contains 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

      Ribonuclease 3 (RNASE3) is cytotoxin and helminthotoxin with low-efficiency ribonuclease activity. RNASE3 possesses a broad diversity of biological activities. RNASE3 protein has shown antibacterial activity such as cytoplasmic membrane depolarization of preferentially Gram-negative and Gram-positive strains and promotes E. coli outer membrane detachment, alteration of the overall cell shape and partial loss of cell content.

    • Synonyms

      ECP, RNS3, Ribonuclease 3, Eosinophil cationic protein, RNASE3, RNASE3.

    • Physical Appearance

      Sterile Filtered colorless solution.

    • Stability

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

    • Amino Acid Sequence

      MRGSHHHHHH GMASMTGGQQ MGRDLYDDDD KDRWGSHMRP PQFTRAQWFA IQHISLNPPR CTIAMRAINN YRWRCKNQNT FLRTTFANVV NVCGNQSIRC PHNRTLNNCH RSRFRVPLLH CDLINPGAQN ISNCRYADRP GRRFYVVACD NRDPRDSPRY PVVPVHLDTT I.

    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.

    Rnase3 Human
  • View Data Sheet

    Name :

    Welqut Protease

    Description:

    Welqut Protease Staphylococcus aureus Recombinant

    Product # :

    ENZ-1113

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    Description

    Welqut Protease Recombinant is a single, non-glycosylated polypeptide chain containing 204 amino acids and having a molecular mass of 22kDa. The Welqut Protease is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Welqut Protease contains 10 mM Na2HPO4, 50% glycerol, 1.8 mM KH2PO4, pH 7.3, 140 mM NaCl and 2.7 mM KCl.

    Purity

    Greater than 97.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      WELQut Protease is an extremely specific and recombinant serine protease from Staphylococcus aureus. The WELQut Protease identifies and accurately cleaves recombinant proteins that has a recognition sequence added to them, with the amino acid sequence Trp, Glu, Leu, Gln, X (any amino acid). WELQut Protease cut externally from the recognition sequence, therefor doesn’t leave extra amino acids bound to the target protein. The protease isn’t temperature sensitive (works in 4-30°C) or pH sensitive (pH 6.5-9.0), also, there is no need in any particular buffers.

    • 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.

    • Unit Definition

      Each unit is defined as the amount of enzyme required to cleave ≥99% of 100μg of a control protein in 16 h at 20°C. Enzyme activity is assayed in 100μl 100 mM Tris-HCl (pH 8.0).

    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.

    Welqut Protease
  • View Data Sheet

    Name :

    SMUG1 Human

    Description:

    Single-Strand-Selective Monofunctional Uracil-DNA Glycosylase 1 Human Recombinant

    Single-strand selective monofunctional uracil DNA glycosylase, SMUG1, FDG, UNG3, HMUDG.

    Product # :

    ENZ-674

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    Description

    SMUG1 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 293 amino acids (1-270) and having a molecular mass of 32.3kDa.SMUG1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    The SMUG1 solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.2M NaCl, 30% glycerol and 1mM DTT.

    Purity

    Greater than 95% as determined by SDS-PAGE.

    More Info

    • Introduction

      Single-strand-selective monofunctional uracil-DNA glycosylase (SMUG1) is an enzyme responsible for recognizing base lesions in the genome and initiating base excision DNA repair. SMUG1 participates in base excision repair by removing uracil from single- and double-stranded DNA. SMUG1 serves as a monofunctional DNA glycosylase specific for uracil (U) residues in DNA and has inclination for single-stranded DNA substrates. SMUG1 activity is greater against mismatches (U/G) than against matches (U/A).

    • Synonyms

      Single-strand selective monofunctional uracil DNA glycosylase, SMUG1, FDG, UNG3, HMUDG.

    • 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 MGSMPQAFLL GSIHEPAGAL MEPQPCPGSL AESFLEEELR LNAELSQLQF SEPVGIIYNP VEYAWEPHRN YVTRYCQGPK EVLFLGMNPG PFGMAQTGVP FGEVSMVRDW LGIVGPVLTP PQEHPKRPVL GLECPQSEVS GARFWGFFRN LCGQPEVFFH HCFVHNLCPL LFLAPSGRNL TPAELPAKQR EQLLGICDAA LCRQVQLLGV RLVVGVGRLA EQRARRALAG LMPEVQVEGL LHPSPRNPQA NKGWEAVAKE RLNELGLLPL LLK.

    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.

    Smug1 Human
  • 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 :

    TYMS Human

    Description:

    Thymidylate Synthetase Human Recombinant

    TMS, EC 2.1.1.45, HST422, Thymidylate synthase, TSase, TS, TYMS, MGC88736.

    Product # :

    ENZ-470

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    Description

    Thymidylate synthase Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 333 amino acids (1-313 a.a.) and having a molecular mass of 37.8 kDa. The Thymidylate synthase fused to a 20 amino acid His-Tag at N-Terminus and purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

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

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Thymidylate synthase catalyzes the methylation of deoxyuridylate to deoxythymidylate using 5,10-methylenetetrahydrofolate as a cofactor which maintains the dTMP (thymidine-5-prime monophosphate) pool vital for DNA replication and repair. Thymidylate synthase plays an important role as a cancer chemotherapeutic agent. Thymidylate synthase is the primary site of action for 5-fluoro-2-prime-deoxyuridine and several folate analogs.

    • Synonyms

      TMS, EC 2.1.1.45, HST422, Thymidylate synthase, TSase, TS, TYMS, MGC88736.

    • 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 MPVAGSELPR RPLPPAAQER DAEPRPPHGE LQYLGQIQHI LRCGVRKDDR TGTGTLSVFG MQARYSLRDE FPLLTTKRVF WKGVLEELLW FIKGSTNAKE LSSKGVKIWD ANGSRDFLDS LGFSTREEGD LGPVYGFQWR HFGAEYRDME SDYSGQGVDQ LQRVIDTIKT NPDDRRIIMC AWNPRDLPLM ALPPCHALCQ FYVVNSELSC QLYQRSGDMG LGVPFNIASY ALLTYMIAHI TGLKPGDFIH TLGDAHIYLN HIEPLKIQLQ REPRPFPKLR ILRKVEKIDD FKAEDFQIEG YNPHPTIKME MAV.

    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.

    Tyms Human
  • View Data Sheet

    Name :

    GPX1 Human

    Description:

    Glutathione Peroxidase 1 Human Recombinant

    Glutathione peroxidase 1, GPx-1, GSHPx-1, Cellular glutathione peroxidase, GPX1, GPXD, GSHPX1.

    Product # :

    ENZ-186

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    Description

    GPX1 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 223 amino acids (1-203) and having a molecular mass of 24.2kDa.GPX1 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The GPX1 solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 2mM DTT, 30% glycerol and 100mM NaCl.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    More Info

    • Introduction

      Glutathione peroxidase 1 (GPX1) is a member of the glutathione peroxidase family, consisting of 8 identified glutathione peroxidases (Gpx1-8) in humans. Glutathione peroxidase serves in the detoxification of hydrogen peroxide, and is one of the most vital antioxidant enzymes in humans. The GPX1 is a component of the enzymatic antioxidant defense, preventing oxidative damage to DNA, proteins and lipids by detoxifying hydrogen and lipid peroxides which may contribute to prostate cancer development. GPX1 is one of only a small number of proteins known in higher vertebrates to contain selenocysteine, which occurs at the active site of glutathione peroxidase and is coded by the nonsense (stop) codon TGA. Furthermore, the GPX1 protein is characterized in a polyalanine sequence polymorphism in the N-terminal region, which includes 3 alleles with 5, 6 or 7 alanine (ALA) repeats in this sequence. The allele with 5 ALA repeats is significantly linked to breast cancer risk.

    • Synonyms

      Glutathione peroxidase 1, GPx-1, GSHPx-1, Cellular glutathione peroxidase, GPX1, GPXD, GSHPX1.

    • 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 MCAARLAAAA AAAQSVYAFS ARPLAGGEPV SLGSLRGKVL LIENVASLCG TTVRDYTQMN ELQRRLGPRG LVVLGFPCNQ FGHQENAKNE EILNSLKYVR PGGGFEPNFM LFEKCEVNGA GAHPLFAFLR EALPAPSDDA TALMTDPKLI TWSPVCRNDV AWNFEKFLVG PDGVPLRRYS RRFQTIDIEP DIEALLSQGP SCA.

    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.

    Gpx1 Human
  • View Data Sheet

    Name :

    AKR7A2 Human

    Description:

    Aldo-Keto Reductase Family 7 Member A2 Human Recombinant

    Aflatoxin B1 aldehyde reductase member 2, AFAR, AFAR1, AFB1-AR1, AKR7, Succinic semialdehyde reductase, SSA reductase, AFB1 aldehyde reductase 1, Aldoketoreductase 7, AKR7A2.

    Product # :

    ENZ-485

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    Description

    AKR7A2 Human Recombinant fused to a 39 amino acid His Tag at N-terminal produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 398 amino acids (1-359 a.a) and having a molecular mass of 44 kDa. The AKR7A2 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The AKR7A2 solution contains 20mM Tris-HCl pH-8, 1mM DTT and 20% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    Biological Activity

    Specific activity: approximately 0.25-0.3 units/mg.
    Enzymatic activity was confirmed by measuring the amount of enzyme catalyzing the oxidation of 1 micromole NADPH per minute at 25C. Specific activity was expressed as units/mg protein.

    More Info

    • Introduction

      AKR7A2 participates in the detoxification of aldehydes and ketones. AKR7A2 catalyzes the NADPH-dependent reduction of succinic semialdehyde to gamma-hydroxybutyrate. AKR7A2 is involved in producing the neuromodulator gamma-hydroxybutyrate (GHB). AKR7A2 has extensive substrate specificity. AKR7A2 shows NADPH-dependent aldehyde reductase activity towards 2-carboxybenzaldehyde, 2-nitrobenzaldehyde and pyridine-2-aldehyde (in vitro). AKR7A2 reduces 1,2-naphthoquinone and 9,10-phenanthrenequinone (in vitro). AKR7A2 reduces the dialdehyde protein-binding form of aflatoxin B1 (AFB1) to the non-binding AFB1 dialcohol. AKR7A2 takes part in protection of liver against the toxic and carcinogenic effects of AFB1, a potent hepatocarcinogen.

    • Synonyms

      Aflatoxin B1 aldehyde reductase member 2, AFAR, AFAR1, AFB1-AR1, AKR7, Succinic semialdehyde reductase, SSA reductase, AFB1 aldehyde reductase 1, Aldoketoreductase 7, AKR7A2.

    • 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

      MRGSHHHHHH GMASMTGGQQ MGRDLYDDDD KDRWGSELEM LSAASRVVSR AAVHCALRSP PPEARALAMS RPPPPRVASV LGTMEMGRRM DAPASAAAVR AFLERGHTEL DTAFMYSDGQ SETILGGLGL GLGGGDCRVK IATKANPWDG KSLKPDSVRS QLETSLKRLQ CPQVDLFYLH APDHGTPVEE TLHACQRLHQ EGKFVELGLS NYASWEVAEI CTLCKSNGWI LPTVYQGMYN ATTRQVETEL FPCLRHFGLR FYAYNPLAGG LLTGKYKYED KDGKQPVGRF FGNSWAETYR NRFWKEHHFE AIALVEKALQ AAYGASAPSV TSAALRWMYH HSQLQGAHGD AVILGMSSLE QLEQNLAATE EGPLEPAVVD AFNQAWHLVA HECPNYFR.

    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.

    Akr7A2 Human
  • View Data Sheet

    Name :

    CTSF Human, Sf9

    Description:

    Cathepsin-F Human Recombinant, Sf9

    CTSF, CATSF, CLN13.

    Product # :

    ENZ-1167

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    Description

    CTSF produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 474 amino acids (20-484.a.a) and having a molecular mass of 52.5kDa.CTSF is expressed with a 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    CTSF protein solution (0.25mg/ml) contains Phosphate buffered saline (pH7.4) and 40% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    Biological Activity

    Specific activity is > 5 pmol/min/ug, and is defined as the amount of enzyme that hydrolyze 1pmole of Z-Phe-ArgAMC to Z-Phe-Arg and AMC per minute at pH 5.0 at 37℃.

    More Info

    • Introduction

      Cathepsin F (CTSF) is a member of the peptidase C1 family. Cathepsins are papain family cysteine proteinases which are a main component of the lysosomal proteolytic system. The CTSF gene is ubiquitously expressed, and it maps to chromosome 11q13, close to the gene encoding cathepsin W. CTSF plays a role in normal protein catabolism. CTSF is involved in some degradative processes occurring in tumor progression since it is highly expressed in some cancer cell lines.

    • Synonyms

      CTSF, CATSF, CLN13.

    • 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

      ADLAPAQPRA ASFQAWGPPS PELLAPTRFA LEMFNRGRAA GTRAVLGLVR GRVRRAGQGS LYSLEATLEE PPCNDPMVCR LPVSKKTLLC SFQVLDELGR HVLLRKDCGP VDTKVPGAGE PKSAFTQGSA MISSLSQNHP DNRNETFSSV ISLLNEDPLS QDLPVKMASI FKNFVITYNR TYESKEEARW RLSVFVNNMV RAQKIQALDR GTAQYGVTKF SDLTEEEFRT IYLNTLLRKE PGNKMKQAKS VGDLAPPEWD WRSKGAVTKV KDQGMCGSCW AFSVTGNVEG WFLNQGTLL SLSEQELLDC DKMDKACMGG LPSNAYSAIK NLGGLETEDD YSYQGHMQSC NFSAEKAKVY INDSVELSQN EQKLAAWLAK RGPISVAINA FGMQFYRHGI SRPLRPLCSP WLIDHAVLLV GYGNRSDVPF WAIKNSWGTD WGEKGYYYLH RGSGACGVNT MASSAVVDHH HHHH

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

    Ctsf Protein
  • View Data Sheet

    Name :

    ARSA Mouse

    Description:

    Arylsulfatase A Mouse Recombinant

    Arylsulfatase A, ASA, Cerebroside-sulfatase.

    Product # :

    ENZ-814

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    Description

    ARSA Mouse Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 498 amino acids (18-506 a.a.) and having a molecular mass of 53.2kDa (Molecular size on SDS-PAGE will appear at approximately 50-70kDa). ARSA is expressed with a 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

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

    Purity

    Greater than 95% as determined by SDS-PAGE.

    More Info

    • Introduction

      Arylsulfatase A (ARSA) hydrolyzes cerebrosidesulfate to cerebroside and sulfate. ARSA is inhibited by phosphate. The phosphate develops a covalent bond with the active site 3-oxoalanine. ARSA gene defects cause metachromatic leucodystrophy (MLD), a progressive demyelination disease which results in various neurological symptoms and ultimately death.

    • Synonyms

      Arylsulfatase A, ASA, Cerebroside-sulfatase.

    • 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

      ADPSPPNILL IFADDLGYGD LGSYGHPSST TPNLDQLAEG GLRFTDFYVP VSLCTPSRAA LLTGRLPVRS GMYPGVLGPS SQGGLPLEEV TLAEVLAARG YLTGMAGKWH LGVGPEGAFL PPHQGFHRFL GIPYSHDQGP CQNLTCFPPD IPCKGGCDQG LVPIPLLANL TVEAQPPWLP GLEARYVSFS RDLMADAQRQ GRPFFLYYAS HHTHYPQFSG QSFTKRSGRG PFGDSLMELD GAVGALMTTV GDLGLLEETL VIFTADNGPE LMRMSNGGCS GLLRCGKGTT FEGGVREPAL VYWPGHITPG VTHELASSLD LLPTLAALTG APLPNVTLDG VDISPLLLGT GKSPRKSVFF YPPYPDEIHG VFAVRNGKYK AHFFTQGSAH SDTTSDPACH AANRLTAHEP PLLYDLSQDP GENYNVLESI EGVSPEALQA LKHIQLLKAQ YDAAMTFGPS QIAKGEDPAL QICCQPSCTP HPVCCHCPGS QSHHHHHH.

    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.

    Arsa Mouse
  • View Data Sheet

    Name :

    FDFT1 Human

    Description:

    Farnesyl-Diphosphate Farnesyltransferase 1 Human Recombinant

    Farnesyl-Diphosphate Farnesyltransferase 1, Squalene Synthase, SQS, SS, FPP:FPP Farnesyltransferase, EC 2.5.1.21, DGPT, ERG9, Presqualene-Di-Diphosphate Synthase, Squalene Synthetase, Farnesyl-Diphosphate, Farnesyltransferase, FDFT1.

    Product # :

    ENZ-820

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    Description

    FDFT1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 306 amino acids (1-283 a.a) and having a molecular mass of 35.4 kDa. FDFT1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    FDFT1 protein solution (0.25 mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 10% glycerol and 0.4M Urea.

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Farnesyl-Diphosphate Farnesyltransferase 1, also known as FDFT1 is a membrane-associated enzyme sited at a branch point in the mevalonate pathway. FDFT1belongs to the phytoene/squalene synthase family. FDFT1 is the 1st specific enzyme in cholesterol biosynthesis, which catalyzes the dimerization of 2 molecules of farnesyl diphosphate in a two-step reaction to form squalene.

    • Synonyms

      Farnesyl-Diphosphate Farnesyltransferase 1, Squalene Synthase, SQS, SS, FPP:FPP Farnesyltransferase, EC 2.5.1.21, DGPT, ERG9, Presqualene-Di-Diphosphate Synthase, Squalene Synthetase, Farnesyl-Diphosphate, Farnesyltransferase, FDFT1.

    • 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 MGSMEFVKCL GHPEEFYNLV RFRIGGKRKV MPKMDQDSLS SSLKTCYKYL NQTSRSFAAV IQALDGEMRN AVCIFYLVLR ALDTLEDDMT ISVEKKVPLL HNFHSFLYQP DWRFMESKEK DRQVLEDFPT ISLEFRNLAE KYQTVIADIC RRMGIGMAEF LDKHVTSEQE WDKYCHYVAG LVGIGLSRLF SASEFEDPLV GEDTERANSM GLFLQKTNII RDYLEDQQGG REFWPQEVWS RYVKKLGDFA KPENIDLAVQ CLNELITNAL HHIPDVITYL SRLRNQ.

    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.

    Fdft1 Human
  • View Data Sheet

    Name :

    GARS Human

    Description:

    Glycyl-TRNA Synthetase Human Recombinant

    Glycine--tRNA ligase, Diadenosine tetraphosphate synthetase, AP-4-A synthetase, Glycyl-tRNA synthetase, GlyRS, GARS, CMT2D, DSMAV, HMN5, SMAD1.

    Product # :

    ENZ-805

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    Description

    GARS Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 270 amino acids (43-289 a.a) and having a molecular mass of 30kDa.GARS is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    GARS protein solution (0. 5mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 10% glycerol and 1mM DTT.

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      GARS is an (alpha)2 dimer which is a member of the class II family of tRNA synthetases. GARS is a glycyl-tRNA synthetase, one of the aminoacyl-tRNA synthetases which charge tRNAs with their cognate amino acids. GARS catalyzes the attachment of glycine to tRNA(Gly). In addition, GARS is able to produce diadenosine tetraphosphate (Ap4A), which is a universal pleiotropic signaling molecule required for cell regulation pathways, by direct condensation of two ATPs. GARS has been demonstrated to be a target of autoantibodies in the human autoimmune diseases, polymyositis or dermatomyositis.

    • Synonyms

      Glycine--tRNA ligase, Diadenosine tetraphosphate synthetase, AP-4-A synthetase, Glycyl-tRNA synthetase, GlyRS, GARS, CMT2D, DSMAV, HMN5, SMAD1.

    • 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 MGSPISLPAA ASRSSMDGAG AEEVLAPLRL AVRQQGDLVR KLKEDKAPQV DVDKAVAELK ARKRVLEAKE LALQPKDDIV DRAKMEDTLK RRFFYDQAFA IYGGVSGLYD FGPVGCALKN NIIQTWRQHF IQEEQILEID CTMLTPEPVL KTSGHVDKFA DFMVKDVKNG ECFRADHLLK AHLQKLMSDK KCSVEKKSEM ESVLAQLDNY GQQELADLFV NYNVKSPITG NDLSPPVSFN LMFKTFIGPG.

    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.

    Glycyl Trna Synthetase Human
  • View Data Sheet

    Name :

    ECHS1 Human

    Description:

    Enoyl CoA Hydratase, Short chain, 1, Mitochondrial Human Recombinant

    Enoyl-CoA hydratase 1, SCEH.

    Product # :

    ENZ-556

    Price :

    Quantity :

    Shipping Method :

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    Shipped with Ice Packs

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    More Info

    • description
    • source
    • formulation
    • purity
    • More Info

    Description

    ECHS1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 284 amino acids (28-290 a.a.) and having a molecular mass of 30.6kDa.ECHS1 is fused to a 21 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The ECHS1 protein solution (1mg/ml) contains 20mM Tris-HCl buffer (pH-8), 1mM DTT,0.1M NaCl and 20% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      ECHS1 is part of the hydratase/isomerase superfamily. ECHS1 is localized in the mitochondrial matrix and Expressed in muscle, liver and fibroblasts, with low expression in kidney and spleen, ECHS1 exists as a homohexamer that takes part in the second phase of the mitochondrial fatty acid β-oxidation pathway.

    • Synonyms

      Enoyl-CoA hydratase 1, SCEH.

    • 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 MASGANFEYI IAEKRGKNNT VGLIQLNRPK ALNALCDGLI DELNQALKIF EEDPAVGAIV LTGGDKAFAA GADIKEMQNL SFQDCYSSKF LKHWDHLTQV KKPVIAAVNG YAFGGGCELA MMCDIIYAGE KAQFAQPEIL IGTIPGAGGT QRLTRAVGKS LAMEMVLTGD RISAQDAKQA GLVSKICPVE TLVEEAIQCA EKIASNSKIV VAMAKESVNA AFEMTLTEGS KLEKKLFYST FATDDRKEGM TAFVEKRKAN FKDQ.

    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.

    Echs1 Human
  • View Data Sheet

    Name :

    GLYATL2 Human

    Description:

    Glycine-N-Acyltransferase-Like 2 Human Recombinant

    BXMAS2-10, GATF-B, Glycine N-acyltransferase-like protein 2, Acyl-CoA:glycine N-acyltransferase-like protein 2, GLYATL2.

    Product # :

    ENZ-770

    Price :

    Quantity :

    Shipping Method :

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    Shipped with Ice Packs

    Add To Cart

    More Info

    • description
    • source
    • formulation
    • purity
    • More Info

    Description

    GLYATL2 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 317 amino acids (1-294a.a) and having a molecular mass of 36.7kDa. GLYATL2 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The GLYATL2 solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.1M NaCl, 50% glycerol and 2mM DTT.

    Purity

    Greater than 85% as determined by SDS-PAGE.

    More Info

    • Introduction

      Glycine-N-Acyltransferase-Like 2 (GLYATL2) is a part of the glycine N-acyltransferase family expressed mainly in salivary gland and trachea. GLYATL2 is a mitochondrial acyltransferase that transfers the acyl group to the N-terminus of glycine. GLYATL2 conjugates numerous substrates, like arachidonoyl-CoA and saturated medium and longchain acyl-CoAs ranging from chain-length C8:0-CoA to C18:0-CoA, to form a variety of N-acylglycines. GLYATL2 also shows a preference for monounsaturated fatty acid oleoyl-CoA (C18:1-CoA) as an acyl donor.

    • Synonyms

      BXMAS2-10, GATF-B, Glycine N-acyltransferase-like protein 2, Acyl-CoA:glycine N-acyltransferase-like protein 2, GLYATL2.

    • 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 MGSMLVLHNS QKLQILYKSL EKSIPESIKV YGAIFNIKDK NPFNMEVLVD AWPDYQIVIT RPQKQEMKDD QDHYTNTYHI FTKAPDKLEE VLSYSNVISW EQTLQIQGCQ EGLDEAIRKV ATSKSVQVDY MKTILFIPEL PKKHKTSSND KMELFEVDDD NKEGNFSNMF LDASHAGLVN EHWAFGKNER SLKYIERCLQ DFLGFGVLGP EGQLVSWIVM EQSCELRMGY TVPKYRHQGN MLQIGYHLEK YLSQKEIPFY FHVADNNEKS LQALNNLGFK ICPCGWHQWK CTPKKYC.

    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.

    Glyatl2 Human
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