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1000 results found for “Enolase”
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Name :
KARS HumanDescription:
Lysyl-tRNA Synthetase Human Recombinant
Lysine--tRNA ligase, Lysyl-tRNA synthetase, LysRS, KARS, KIAA0070, KRS, KARS2, CMTRIB.
Product # :
ENZ-161Price :
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Description
KARS Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 558 amino acids (63-597 a.a.) and having a molecular mass of 63.7kDa.KARS is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
KARS protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH8.0), 20% glycerol, 0.1M NaCl and 1mM DTT.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
Lysyl-tRNA synthetase (KARS) is a member of the class-II aminoacyl-tRNA synthetase family. KARS exists as both mitochondrial and cytoplasmic isoforms produced by alternative splicing, and believed to have a role in autoimmune diseases, such as polymyositis or dermatomyositis. The KARS protein functions to catalyze the aminoacylation of tRNAs by their corresponding amino acids, so linking amino acids with tRNA-contained nucleotide triplets.
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Synonyms
Lysine--tRNA ligase, Lysyl-tRNA synthetase, LysRS, KARS, KIAA0070, KRS, KARS2, CMTRIB.
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Physical Appearance
Sterile Filtered colorless solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSGVGPEEE SVDPNQYYKI RSQAIHQLKV NGEDPYPHKF HVDISLTDFI QKYSHLQPGD HLTDITLKVA GRIHAKRASG GKLIFYDLRG EGVKLQVMAN SRNYKSEEEF IHINNKLRRG DIIGVQGNPG KTKKGELSII PYEITLLSPC LHMLPHLHFG LKDKETRYRQ RYLDLILNDF VRQKFIIRSK IITYIRSFLD ELGFLEIETP MMNIIPGGAV AKPFITYHNE LDMNLYMRIA PELYHKMLVV GGIDRVYEIG RQFRNEGIDL THNPEFTTCE FYMAYADYHD LMEITEKMVS GMVKHITGSY KVTYHPDGPE GQAYDVDFTP PFRRINMVEE LEKALGMKLP ETNLFETEET RKILDDICVA KAVECPPPRT TARLLDKLVG EFLEVTCINP TFICDHPQIM SPLAKWHRSK EGLTERFELF VMKKEICNAY TELNDPMRQR QLFEEQAKAK AAGDDEAMFI DENFCTALEY GLPPTAGWGM GIDRVAMFLT DSNNIKEVLL FPAMKPEDKK ENVATTDTLE STTVGTSV.
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.
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Name :
LHPP HumanDescription:
Phospholysine Phosphohistidine Inorganic Pyrophosphate Phosphatase Human Recombinant
Phospholysine phosphohistidine inorganic pyrophosphate phosphatase, hLHPP, LHPP, HDHD2B.
Product # :
ENZ-575Price :
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Description
LHPP Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 307 amino acids (1-270) and having a molecular mass of 33.5kDa.LHPP is fused to a 37 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The LHPP solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 1mM DTT, 10% glycerol and 0.1M NaCl.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
Phospholysine phosphohistidine inorganic pyrophosphate phosphatase (LHPP) belongs to the HAD-like hydrolase superfamily. LHPP is an exceptional enzyme which hydrolyzes not only oxygen-phosphorus bonds in inorganic pyrophosphate but also nitrogen-phosphorus bonds in phospholysine, phosphohistidine and imidodiphosphate in vitro. LHPP is expressed in the liver, kidney and moderately in the brain.
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Synonyms
Phospholysine phosphohistidine inorganic pyrophosphate phosphatase, hLHPP, LHPP, HDHD2B.
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Physical Appearance
Sterile Filtered colorless solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MRGSHHHHHP WYASMTGGQQ MGRDLYDDDD KDRWGSHMAP WGKRLAGVRG VLLDISGVLY DSGAGGGTAI AGSVEAVARL KRSRLKVRFC TNESQKSRAE LVGQLQRLGF DISEQEVTAP APAACQILKE QGLRPYLLIH DGVRSEFDQI DTSNPNCVVI ADAGESFSYQ NMNNAFQVLM ELEKPVLISL GKGRYYKETS GLMLDVGPYM KALEYACGIK AEVVGKPSPE FFKSALQAIG VEAHQAVMIG DDIVGDVGGA QRCGMRALQV RTGKFRPSDE HHPEVKADGY VDNLAEAVDL LLQHADK.
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.
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Name :
CES2E MouseDescription:
Carboxylesterase 2E Mouse Recombinant
9030624L02Rik, Ces5, Ces2e.
Product # :
ENZ-1141Price :
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Description
CES2E Mouse produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 541 amino acids ( 27-559 aa) and having a molecular mass of 60.5kDa.CES2E is fused to a 8 amino acid His tag at C-terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
The CES2E solution (0.25 mg/ml) contains 10% Glycerol and Phosphate-Buffered Saline (pH 7.4).
Purity
Greater than 95.0% as determined by SDS-PAGE.
Biological Activity
Specific activity is > 30unit/mg, and is defined as the amount of enzyme that hydrolyze 1.0 umole of pnitrophenyl acetate to p-nitrophenol per minute at pH 7.5 at 25C˚.
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Introduction
Carboxylesterase 2E or CES2E is an enzyme that hydrolyzes various carboxylic acid esters. This enzyme can be found mainly in mammalian liver cells. CES2E is taking part in chemical reactions, especially in carboxylic ester and water catalyzation to alcohol & carboxylate.
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Synonyms
9030624L02Rik, Ces5, Ces2e.
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Physical Appearance
Sterile Filtered colorless solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
QDSASPIRNT HTGQVRGSLV HVKDTDIAVH TFLGIPFAKP PVGPLRFAPP EAPEPWSGVR DGTSHPNMCL QNDNLMGSED LKMMNLILPP ISMSEDCLYL NIYVPAHAHE GSNLPVMVWI HGGALTVGMA SMYDGSMLAA TEDVVVVAIQ YRLGVLGFFS TGDQHAKGNW GYLDQVAALR WVQQNIVHFG GNPDRVTIFG ESAGGTSVSS HVVSPMSQGL FHGAIMESGV AVLPDLISSS
SEMVHRIVAN LSGCAAVNSE TLMCCLRGKN EAEMLAINKV FKIIPGVVDG EFLPKHPQEL MASKDFHPVP SIIGINNDEY GWILPTIMDP AQKIEEITRK TLPAVLKSTA LKMMLPPECG DLLMEEYMGD TEDPETLQAQ FREMKGDFMF VIPALQVAHF QRSHAPVYFY EFQHRPSFFK DFRPPYVKAD HGDEIFLVFG YQFGNIKLPY TEEEEQLSRR IMKYWANFAR HGNPNSEGLP YWPVMDHDEQ YLQLDIQPSV GRALKARRLQ FWTKTLPQKI QELKGSQERH KELLEHHHHH H
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.
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Name :
RNMT HumanDescription:
RNA (guanine-7-) Methyltransferase Human Recombinant
mRNA cap guanine-N7 methyltransferase, RG7MT1, mRNA (guanine-N(7)-)-methyltransferase, mRNA cap methyltransferase, hCMT1, hMet, hcm1p, RNMT, KIAA0398, MET, RG7MT1, hCMT1c, DKFZp686H1252.
Product # :
ENZ-114Price :
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Description
RNMT produced in E.Coli is a single, non-glycosylated polypeptide chain containing 496 amino acids (1-476 a.a.) and having a molecular mass of 57kDa.RNMT is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
RNMT solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH 8.0) 2mM DTT, 20% glycerol and 100mM NaCl.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
RNMT is a widely expressed nuclear protein which is a member of the mRNA cap methyltransferase family. Cap-dependent mRNA translation requires the methylation of the mRNA guanosine cap by RNMT. RNMT catalyzes the transfer of a methyl group from AdoMet (S-adenosylmethionine) to the GpppN end of the growing mRNA at the N-7 position, thus producing AdoHyc (S-adenosylhomocysteine) and m7GpppN terminated RNA.
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Synonyms
mRNA cap guanine-N7 methyltransferase, RG7MT1, mRNA (guanine-N(7)-)-methyltransferase, mRNA cap methyltransferase, hCMT1, hMet, hcm1p, RNMT, KIAA0398, MET, RG7MT1, hCMT1c, DKFZp686H1252.
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Physical Appearance
Sterile filtered colorless solution.
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Stability
RNMT Human Recombinant although stable at 4°C for 1 week, should be stored below -18°C. Please prevent freeze thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MANSAKAEEY EKMSLEQAKA SVNSETESSF NINENTTASG TGLSEKTSVC RQVDIARKRK EFEDDLVKES SSCGKDTPSK KRKLDPEIVP EEKDCGDAEG NSKKRKRETE DVPKDKSSTG DGTQNKRKIA LEDVPEKQKN LEEGHSSTVA AHYNELQEVG LEKRSQSRIF YLRNFNNWMK SVLIGEFLEK VRQKKKRDIT VLDLGCGKGG DLLKWKKGRI NKLVCTDIAD VSVKQCQQRY EDMKNRRDSE YIFSAEFITA DSSKELLIDK FRDPQMCFDI CSCQFVCHYS FESYEQADMM LRNACERLSP GGYFIGTTPN SFELIRRLEA SETESFGNEI YTVKFQKKGD YPLFGCKYDF NLEGVVDVPE FLVYFPLLNE MAKKYNMKLV YKKTFLEFYE EKIKNNENKM LLKRMQALEP YPANESSKLV SEKVDDYEHA AKYMKNSQVR LPLGTLSKSE WEATSIYLVF AFEKQQ.
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.
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Name :
T5 ExonucleaseDescription:
T5 Exonuclease Recombinant
T5 Exonuclease
Product # :
ENZ-1184Price :
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Description
T5 Exonuclease T5 phage D15 gene Recombinant produced in E.Coli is a single, non-glycosylated polypeptide. T5 Exonuclease is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
10U/ul, 50mM Tris-HCl (25℃, pH 7.5), 100mM NaCl, 0.1mM EDTA, 1mM DTT, 0.1% Triton X-100 and 50% glycerol.
Purity
Greater than 95% as determined by SDS-PAGE.
More Info
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Introduction
T5 Exonuclease is an important enzyme that belongs to the family of exonucleases and plays a vital role in DNA metabolism and genetic engineering. This research paper aims to provide an overview of T5 Exonuclease, including its structure, function, and diverse applications in molecular biology.
T5 Exonuclease is derived from the bacteriophage T5, and it possesses a remarkable ability to selectively degrade single-stranded DNA in a 5' to 3' direction. It is a highly processive enzyme, meaning it can cleave multiple nucleotides consecutively without dissociating from the DNA substrate. The enzyme exhibits high specificity for single-stranded DNA, making it a valuable tool for various molecular biology applications.
The primary function of T5 Exonuclease is to remove nucleotides from the 5' ends of single-stranded DNA molecules. By digesting DNA in a processive manner, T5 Exonuclease is involved in DNA repair mechanisms, such as the removal of damaged or mismatched nucleotides. It is also widely utilized in molecular cloning techniques to generate DNA fragments with precise ends for subsequent DNA ligation reactions.
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Synonyms
T5 Exonuclease
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Physical Appearance
Sterile Filtered colorless solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA). Avoid multiple freeze-thaw cycles.
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Applications
Gibson Assembly
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Background
The structural features of T5 Exonuclease play a crucial role in its enzymatic activity. The enzyme consists of distinct functional domains, including an N-terminal domain responsible for DNA binding and a C-terminal domain containing the exonuclease active site. Understanding the three-dimensional structure of T5 Exonuclease provides insights into its catalytic mechanism and substrate specificity.
The versatility of T5 Exonuclease extends beyond DNA repair and cloning applications. It has been employed in various molecular biology techniques, such as site-directed mutagenesis, DNA sequencing, and preparation of DNA templates for in vitro transcription. Additionally, T5 Exonuclease has found utility in research areas like next-generation sequencing library preparation, restriction fragment length polymorphism (RFLP) analysis, and gene expression studies.
In recent years, the use of T5 Exonuclease in genome editing technologies, such as CRISPR-Cas9, has gained attention. T5 Exonuclease can be employed to remove unwanted DNA sequences or overhangs, enabling precise and efficient genome editing. This application highlights the significance of T5 Exonuclease in advancing genetic engineering and synthetic biology research.
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Unit Definition
1 unit of T5 Exonuclease is defined as the amount of enzyme required to cause the change of 0.00032 A260nm/min at 37° C in 1xReaction Buffer: 20mM Tris-acetate (pH 7.9 @ 25°C), 50mM Potassium Acetate, 10mM Magnesium Acetate and 1mM DTT.
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.
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Name :
PON1 Human, HEKDescription:
Paraoxonase-1 Human Recombinant, HEK
Serum paraoxonase/arylesterase 1, Serum aryldialkylphosphatase 1, Aromatic esterase 1, A-esterase 1 , Serum aryldialkylphosphatase 1, paraoxonase 1, K-45, ESA, PON, MVCD5
Product # :
ENZ-1154Price :
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Description
PON1 Human Recombinant produced in HEK cells is a single, glycosylated, polypeptide chain (16-355 a.a) containing a total of 346 amino acids, having a molecular mass of 39.0kDa. PON1 is fused to a 6 amino acid His-tag at C-terminus,and is purified by proprietary chromatographic techniques.
Source
HEK293 Cells.
Formulation
The PON1 solution (0.25mg/ml) contains 20% Glycerol and Phosphate-Buffered Saline (pH 7.4).
Purity
Greater than 90.0% as determined by SDS-PAGE.
Biological Activity
Specific activity is > 2,500 pmol/min/ug. Defined by the amount of enzyme that hydrolyzes 1pmole of pnitrophenyl acetate to p-nitrophenol per minute at pH 7.5 at 37˚C.
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Introduction
Paraoxonase-1 or PON1 is part of the paraoxonase group of proteins. PON1 is an enzyme, responsible to the toxic metabolites of a different of organophosphorus insecticides hydrolyzation. Furthermore, PON1 is a dominant anti-atherosclerotic part of HDL. The enzyme needs PPAR-gamma for activation, leading to synthesis and release of paraoxonase 1 from the liver tissue, resulting in atherosclerosis reduction. PON1 has many qualities for atheroprotective through inflammatory lipid peroxides metabolism. This enzyme can hydrolyze a large number of substrates, for example cyclic carbonates, lactones, nerve gases etc.
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Synonyms
Serum paraoxonase/arylesterase 1, Serum aryldialkylphosphatase 1, Aromatic esterase 1, A-esterase 1 , Serum aryldialkylphosphatase 1, paraoxonase 1, K-45, ESA, PON, MVCD5
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Physical Appearance
Sterile Filtered colorless solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
LFRNHQSSYQ TRLNALREVQ PVELPNCNLV KGIETGSEDL EILPNGLAFI SSGLKYPGIK SFNPNSPGKI LLMDLNEEDP TVLELGITGS KFDVSSFNPH GISTFTDEDN AMYLLVVNHP DAKSTVELFK FQEEEKSLLH LKTIRHKLLP NLNDIVAVGP EHFYGTNDHY FLDPYLQSWE MYLGLAWSYV VYYSPSEVRV VAEGFDFANG INISPDGKYV YIAELLAHKI HVYEKHANWT LTPLKSLDFN TLVDNISVDP ETGDLWVGCH PNGMKIFFYD SENPPASEVL RIQNILTEEP KVTQVYAENG TVLQGSTVAS VYKGKLLIGT VFHKALYCEL 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.
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Name :
UNGDescription:
Uracil DNA Glycosilase
Uracil DNA Glycosilase, Uracil DNA Glycosylase, UNG.
Product # :
ENZ-352Price :
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Description
E.Coli Uracil DNA Glycosilase (UNG) catalyses the release of free Uracil from Uracil-containing DNA. UNG efficiently hydrolyzes uracil from signle-stranded or double-stranded DNA, but not from oligomers (6 fewer bases).
Source
Escherichia Coli strain that carries the UNG gene from E.coli.
Formulation
UNG solution in 10mM Tris-HCl (pH-7.4 at 25°C), 50mM KCl, 1mM DTT, 0.1mM EDTA, 0.1 mg/ml BSA and 50% glycerol.
More Info
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Synonyms
Uracil DNA Glycosilase, Uracil DNA Glycosylase, UNG.
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Physical Appearance
Sterile Filtered colorless solution.
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Stability
Uracil DNA Glycosilase although stable at 15°C for 1 week, should be stored below -18°C. Please prevent freeze-thaw cycles.
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Reaction Conditions
1X UNG Reaction Buffer, incubate at 37°C.UNG is active over a broad pH rabge with an optimum at pH-8.0, doesn't require divalent cation, and is inhibited by high ionic strength (>200mM). The abasic sites formed in DNA by UNG may be cleaved by heat, alkali-treatment or endonucleases that cleave specifically at abasic sites.
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Inactivation
Inactivated by heating at 95°C for 10min. Enzyme activity is partially restored at temperatures lower than 55°C.
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Unit Definition
1 Unit of the enzyme catalyzes the release of 1 nanomole of uracil-containing DNA template in 60 min at 37°C.
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Specific Activity
The Specific Activity was found to be 5U/µl.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
GPI Human, ActiveDescription:
Glucose-6-Phosphate Isomerase Human Recombinant, BioActive
Glucose-6-phosphate isomerase, Autocrine motility factor, Neuroleukin, Phosphoglucose isomerase, Phosphohexose isomerase, Sperm antigen 36, GPI, AMF, GNPI, NLK, PGI, PHI, SA36, SA-36.
Product # :
ENZ-1148Price :
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Description
GPIHuman Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 578 amino acids (1-558) and having a molecular mass of 65.3 kDa.GPI is fused to a 20 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The GPI solution (1 mg/ml) contains 10% Glycerol, 1mM DTT and 20mM Tris-HCl buffer (pH 8.0).
Purity
Greater than 95.0% as determined by SDS-PAGE.
Biological Activity
Specific activity is > 400unit/mg.It is defined by the increase of NADPH in absorbance at 340 nm, resulting from the reduction of NADP. 1 unit will convert 1.0 umole of D-Fructose 6-phosphate to D-glucose 6- phosphate per minute at pH 7.4 at 37˚C.
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Introduction
GPI or Glucose-6-phosphate isomerase, is a protein, part of the multifunctional phosphoglucose isomerase family, which its members take part in energy pathways. GPI is a dimeric enzyme that enhances the isomerization of glucose-6-phosphate and fructose-6- phosphate (both reversible). In mammals, GPI acts as an angiogenic factor & tumor-secreted cytokine. The enzyme also acts as a neurotrophic factor for spinal & sensory neurons.
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Synonyms
Glucose-6-phosphate isomerase, Autocrine motility factor, Neuroleukin, Phosphoglucose isomerase, Phosphohexose isomerase, Sperm antigen 36, GPI, AMF, GNPI, NLK, PGI, PHI, SA36, SA-36.
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Physical Appearance
Sterile Filtered colorless solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MAALTRDPQF QKLQQWYREH RSELNLRRLF DANKDRFNHF SLTLNTNHGH ILVDYSKNLV TEDVMRMLVD LAKSRGVEAA RERMFNGEKI NYTEGRAVLH VALRNRSNTP ILVDGKDVMP EVNKVLDKMK SFCQRVRSGD WKGYTGKTIT DVINIGIGGS DLGPLMVTEA LKPYSSGGPR VWYVSNIDGT HIAKTLAQLN PESSLFIIAS KTFTTQETIT NAETAKEWFL QAAKDPSAVA KHFVALSTNT TKVKEFGIDP QNMFEFWDWV GGRYSLWSAI GLSIALHVGF DNFEQLLSGA HWMDQHFRTT PLEKNAPVLL ALLGIWYINC FGCETHAMLP YDQYLHRFAA YFQQGDMESN GKYITKSGTR VDHQTGPIVW GEPGTNGQHA FYQLIHQGTK MIPCDFLIPV QTQHPIRKGL HHKILLANFL AQTEALMRGK STEEARKELQ AAGKSPEDLE RLLPHKVFEG NRPTNSIVFT KLTPFMLGAL VAMYEHKIFV QGIIWDINSF DQWGVELGKQ LAKKIEPELD GSAQVTSHDA STNGLINFIK QQREARVQ
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.
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Name :
FARSB HumanDescription:
Phenylalanyl-TRNA Synthetase Beta Human Recombinant
Phenylalanyl-TRNA Synthetase, Beta Subunit, FARSLB,FRSB, Phenylalanyl-TRNA Synthetase-Like, Beta Subunit, EC 6.1.1.20, PheRS, Phenylalanine-TRNA Synthetase-Like, Beta Subunit, Phenylalanine TRNA Ligase 1, Beta, Cytoplasmic, Phenylalanyl-TRNA Synthetase Beta-Subunit, Phenylalanyl-TRNA Synthetase Beta Subunit, Phenylalanine--TRNA Ligase Beta Subunit, Phenylalanyl-TRNA Synthetase Beta Chain, Phenylalanine--TRNA Ligase Beta Chain, Phenylalanine-TRNA Ligase Beta Chain, Phenylalanine TRNA Ligase 1, Cytoplasmic, EC 6.1.1, HSPC173,PheHB,Beta,FARSB.
Product # :
ENZ-851Price :
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Description
FARSB Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 612 amino acids (1-589 a.a) and having a molecular mass of 68.5kDa.FARSB is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
FARSB protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH 8.0) and 10% glycerol.
Purity
Greater than 85.0% as determined by SDS-PAGE.
More Info
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Introduction
FARSB, also known as Phenylalanyl-TRNA Synthetase Beta is a member of the phenylalanyl-tRNA synthetase beta subunit family. FARSB is composed tetramer of two alpha and two beta subunits. In the presence of ATP, this tetramer is accountable for attaching L-phenylalanine to the terminal adenosine of the appropriate tRNA.
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Synonyms
Phenylalanyl-TRNA Synthetase, Beta Subunit, FARSLB,FRSB, Phenylalanyl-TRNA Synthetase-Like, Beta Subunit, EC 6.1.1.20, PheRS, Phenylalanine-TRNA Synthetase-Like, Beta Subunit, Phenylalanine TRNA Ligase 1, Beta, Cytoplasmic, Phenylalanyl-TRNA Synthetase Beta-Subunit, Phenylalanyl-TRNA Synthetase Beta Subunit, Phenylalanine--TRNA Ligase Beta Subunit, Phenylalanyl-TRNA Synthetase Beta Chain, Phenylalanine--TRNA Ligase Beta Chain, Phenylalanine-TRNA Ligase Beta Chain, Phenylalanine TRNA Ligase 1, Cytoplasmic, EC 6.1.1, HSPC173,PheHB,Beta,FARSB.
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Physical Appearance
Sterile Filtered colorless solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSMPTVSVK RDLLFQALGR TYTDEEFDEL CFEFGLELDE ITSEKEIISK EQGNVKAAGA SDVVLYKIDV PANRYDLLCL EGLVRGLQVF KERIKAPVYK RVMPDGKIQK LIITEETAKI RPFAVAAVLR NIKFTKDRYD SFIELQEKLH QNICRKRALV AIGTHDLDTL SGPFTYTAKR PSDIKFKPLN KTKEYTACEL MNIYKTDNHL KHYLHIIENK PLYPVIYDSN GVVLSMPPII NGDHSRITVN TRNIFIECTG TDFTKAKIVL DIIVTMFSEY CENQFTVEAA EVVFPNGKSH TFPELAYRKE MVRADLINKK VGIRETPENL AKLLTRMYLK SEVIGDGNQI EIEIPPTRAD IIHACDIVED AAIAYGYNNI QMTLPKTYTI ANQFPLNKLT ELLRHDMAAA GFTEALTFAL CSQEDIADKL GVDISATKAV HISNPKTAEF QVARTTLLPG LLKTIAANRK MPLPLKLFEI SDIVIKDSNT DVGAKNYRHL CAVYYNKNPG FEIIHGLLDR IMQLLDVPPG EDKGGYVIKA SEGPAFFPGR CAEIFARGQS VGKLGVLHPD VITKFELTMP CSSLEINVGP FL
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.
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Name :
HAO1 HumanDescription:
Hydroxyacid Oxidase 1 Human Recombinant
Hydroxyacid oxidase 1, HAOX1, Glycolate oxidase, GOX, HAO1, GOX1.
Product # :
ENZ-162Price :
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Description
HAO1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 406 amino acids (1-370 a.a.) and having a molecular mass of 45kDa.HAO1 is fused to a 36 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
HAO1 protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH8.0), 20% glycerol and 0.5M NaCl.
Purity
Greater than 95% as determined by SDS-PAGE.
More Info
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Introduction
Glycolate oxidase (HAO1) belongs to the superfamily of the alpha hydroxy acid oxidases (HAO) enzymes. HAO1 catalyzes the FMN mediated oxidation of glycolate to glyoxylate and glyoxylate to oxalate with reduction of oxygen to hydrogen peroxide. HAO1 is most abundantly expressed in the liver and pancreas and is most active on twocarbon substrates such as glycolate. Lately, HAO1 has been identified as a key contributor to hyperoxaluria, a disorder in which large deposits of calcium oxalate form kidney stones.
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Synonyms
Hydroxyacid oxidase 1, HAOX1, Glycolate oxidase, GOX, HAO1, GOX1.
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Physical Appearance
Sterile filtered colorless solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MRGSHHHHHH GMASMTGGQQ MGRDLYDDDD KDRWGSMLPR LICINDYEQH AKSVLPKSIY DYYRSGANDE ETLADNIAAF SRWKLYPRML RNVAETDLST SVLGQRVSMP ICVGATAMQR MAHVDGELAT VRACQSLGTG MMLSSWATSS IEEVAEAGPE ALRWLQLYIY KDREVTKKLV RQAEKMGYKA IFVTVDTPYL GNRLDDVRNR FKLPPQLRMK NFETSTLSFS PEENFGDDSG LAAYVAKAID PSISWEDIKW LRRLTSLPIV AKGILRGDDA REAVKHGLNG ILVSNHGARQ LDGVPATIDV LPEIVEAVEG KVEVFLDGGV RKGTDVLKAL ALGAKAVFVG RPIVWGLAFQ GEKGVQDVLE ILKEEFRLAM ALSGCQNVKV IDKTLVRKNP LAVSKI.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
NDUFV2 HumanDescription:
NADH Dehydrogenase Flavoprotein 2 Human Recombinant
CI-24k, NADH dehydrogenase [ubiquinone] flavoprotein 2, mitochondrial, NADH-ubiquinone oxidoreductase 24 kDa subunit, NDUFV2.
Product # :
ENZ-743Price :
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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.
More Info
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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.
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Synonyms
CI-24k, NADH dehydrogenase [ubiquinone] flavoprotein 2, mitochondrial, NADH-ubiquinone oxidoreductase 24 kDa subunit, NDUFV2.
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Physical Appearance
Sterile Filtered colorless solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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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.
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Name :
MSRA E.ColiDescription:
Methionine Sulfoxide Reductase A E.Coli Recombinant
Peptide methionine sulfoxide reductase MsrA, Protein-methionine-S-oxide reductase, Peptide-methionine (S)-S-oxide reductase, Peptide Met(O) reductase, msrA, pms, b4219, JW4178.
Product # :
ENZ-129Price :
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Description
MSRA produced in E.Coli is a single, non-glycosylated polypeptide chain containing 232 amino acids (1-212 a.a.) and having a molecular mass of 25.4kDa.MSRA is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
MSRA protein solution (0.5mg/ml) 20mM Tris-HCl buffer (pH 8.0), 1mM DTT, 10% glycerol and 0.1M NaCl.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
Peptide methionine sulfoxide reductase A (msrA) is an enzyme which catalyzes the reversible oxidation-reduction of methionine sulfoxide in proteins to methionine. MSRA may have a significant function as a repair enzyme for proteins which have been inactivated by oxidation.
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Synonyms
Peptide methionine sulfoxide reductase MsrA, Protein-methionine-S-oxide reductase, Peptide-methionine (S)-S-oxide reductase, Peptide Met(O) reductase, msrA, pms, b4219, JW4178.
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Physical Appearance
Sterile filtered colorless solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks.Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MSLFDKKHLV SPADALPGRN TPMPVATLHA VNGHSMTNVP DGMEIAIFAM GCFWGVERLF WQLPGVYSTA AGYTGGYTPN PTYREVCSGD TGHAEAVRIV YDPSVISYEQ LLQVFWENHD PAQGMRQGND HGTQYRSAIY PLTPEQDAAA RASLERFQAA
MLAADDDRHI TTEIANATPF YYAEDDHQQY LHKNPYGYCG IGGIGVCLPP EA.
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.
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Name :
GALT HumanDescription:
Galactose-1-Phosphate Uridylyltransferase Human Recombinant
Galactose-1-phosphate uridylyltransferase, Gal-1-P uridylyltransferase, UDP-glucose--hexose-1-phosphate uridylyltransferase, GALT.
Product # :
ENZ-358Price :
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Description
GALT Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 403 amino acids (1-379) and having a molecular mass of 45.9kDa.GALT is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The GALT solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH 8.5), 0.2M NaCl and 10% glycerol.
Purity
Greater than 85.0% as determined by SDS-PAGE.
More Info
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Introduction
Galactose-1-Phosphate Uridylyltransferase (GALT) catalyzes the 2nd step of the “Leloir pathway” of galactose metabolism, specifically the conversion of UDP-glucose + galactose-1-phosphate to glucose-1-phosphate + UDP-galactose. The deficiency of the GALT enzyme results in typical galactosemia in humans and may be fatal in the newborn stage if lactose is not eliminated from the diet. Galactosemia pathophysiology has not been clearly defined.
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Synonyms
Galactose-1-phosphate uridylyltransferase, Gal-1-P uridylyltransferase, UDP-glucose--hexose-1-phosphate uridylyltransferase, GALT.
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Physical Appearance
Sterile filtered colorless solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA). Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSHMSRSGT DPQQRQQASE ADAAAATFRA NDHQHIRYNP LQDEWVLVSA HRMKRPWQGQ VEPQLLKTVP RHDPLNPLCP GAIRANGEVN PQYDSTFLFD NDFPALQPDA PSPGPSDHPL FQAKSARGVC KVMCFHPWSD VTLPLMSVPE IRAVVDAWAS VTEELGAQYP WVQIFENKGA MMGCSNPHPH CQVWASSFLP DIAQREERSQ QAYKSQHGEP LLMEYSRQEL LRKERLVLTS EHWLVLVPFW ATWPYQTLLL PRRHVRRLPE LTPAERDDLA SIMKKLLTKY DNLFETSFPY SMGWHGAPTG SEAGANWNHW QLHAHYYPPL LRSATVRKFM VGYEMLAQAQ RDLTPEQAAE RLRALPEVHY HLGQKDRETA TIA.
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.
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Name :
UGP2 HumanDescription:
UDP-Glucose Pyrophosphorylase 2 Human Recombinant
UDP-Glucose Pyrophosphorylase 2,UDP-Glucose Pyrophosphorylase 1, EC 2.7.7.9, UGPP2, UDPGP, UGP1, UTP--Glucose-1-Phosphate Uridylyltransferase 2Uridyl Diphosphate Glucose Pyrophosphorylase-1, Uridyl Diphosphate Glucose Pyrophosphorylase 2, UTP--Glucose-1-Phosphate Uridylyltransferase , UTP-Glucose-1-Phosphate, Uridyltransferase, UDP-Glucose Pyrophosphorylase , UDP-Glucose Diphosphorylase, UGPase 2, UDPGP2, PHC379, UGPase, UGPP1, UDPG.
Product # :
ENZ-832Price :
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Description
UGP2 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 531 amino acids (1-508 a.a) and having a molecular mass of 59.3kDa.UGP2 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
UGP2 protein solution (0.25mg/ml) containing Phosphate buffered saline (pH7.4) 30% glycerol and 1mM DTT.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
UDP-Glucose Pyrophosphorylase 2, also known as UGP2 is an essential intermediary in mammalian carbohydrate inter conversions. UGP2 transfers a glucose moiety from glucose-1-phosphate to MgUTP and forms UDP-glucose and MgPPi. UDP-glucose is a direct precursor of glycogen in the liver and muscle tissue, moreover in lactating mammary gland it is converted to UDP-galactose which is next converted to lactose.
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Synonyms
UDP-Glucose Pyrophosphorylase 2,UDP-Glucose Pyrophosphorylase 1, EC 2.7.7.9, UGPP2, UDPGP, UGP1, UTP--Glucose-1-Phosphate Uridylyltransferase 2Uridyl Diphosphate Glucose Pyrophosphorylase-1, Uridyl Diphosphate Glucose Pyrophosphorylase 2, UTP--Glucose-1-Phosphate Uridylyltransferase , UTP-Glucose-1-Phosphate, Uridyltransferase, UDP-Glucose Pyrophosphorylase , UDP-Glucose Diphosphorylase, UGPase 2, UDPGP2, PHC379, UGPase, UGPP1, UDPG.
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Physical Appearance
Sterile filtered colorless solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSMSRFVQD LSKAMSQDGA SQFQEVIRQE LELSVKKELE KILTTASSHE FEHTKKDLDG FRKLFHRFLQ EKGPSVDWGK IQRPPEDSIQ PYEKIKARGL PDNISSVLNK LVVVKLNGGL GTSMGCKGPK SLIGVRNENT FLDLTVQQIE HLNKTYNTDV PLVLMNSFNT DEDTKKILQK YNHCRVKIYT FNQSRYPRIN KESLLPVAKD VSYSGENTEA WYPPGHGDIY ASFYNSGLLD TFIGEGKEYI FVSNIDNLGA TVDLYILNHL MNPPNGKRCE FVMEVTNKTR ADVKGGTLTQ YEGKLRLVEI AQVPKAHVDE FKSVSKFKIF NTNNLWISLA AVKRLQEQNA IDMEIIVNAK TLDGGLNVIQ LETAVGAAIK SFENSLGINV PRSRFLPVKT TSDLLLVMSN LYSLNAGSLT MSEKREFPTV PLVKLGSSFT KVQDYLRRFE SIPDMLELDH LTVSGDVTFG KNVSLKGTVI IIANHGDRID IPPGAVLENK IVSGNLRILD H.
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.
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Name :
DNase HumanDescription:
Deoxyribonuclease I Human Recombinant
EC 3.1.21.1, Deoxyribonuclease I, DNase I, DNL1, DRNI, FLJ38093, DNASE1.
Product # :
ENZ-319Price :
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Description
Deoxyribonuclease I Human Recombinant produced in CHO is a glycosylated, polypeptide chain containing 260 amino acids and having a total molecular mass of 37,000 Dalton with a molecular formula of C1321H1999N339O396S9. DNase is purified by proprietary chromatographic techniques.
Source
Chinese Hamster Ovary Cells.
Formulation
Each mg contains 150 µg calcium chloride dehydrate and 8.77 mg NaCl.
More Info
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Introduction
Deoxyribonuclease I Human Recombinant (rhDNase), an enzyme which selectively cleaves DNA. Recombinant Human Dnase is an endonuclease enzyme which splits phosphodiester linkages within polynucleotides, acting primarely on single stranded DNA (ssDNA), double stranded DNA (ddDNA) and chromatin. Dnase is activated by bivalent metals such as Mg+2 and Ca+2 .
Dnase enzymes are common reagents used in biochemical methods requiring diestion of DNA and recovery of RNA, or where DNA is to be removed without affecting structural proteins or enzymes. Dnase enzymes are also used in tissue culture to digest DNA from damaged cells, resulting in reduced viscosity, and for removal of membrane-bound DNA fragments. -
Synonyms
EC 3.1.21.1, Deoxyribonuclease I, DNase I, DNL1, DRNI, FLJ38093, DNASE1.
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Physical Appearance
Sterile liquid colorless solution at a concentration of 1mg/ml.
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Stability
2 years when stored at 4°C, three weeks at 15°C, pH-6.3.
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Unit Definition
Dnase is generally assayed according to the photometric method developed by Kunitz. One Dnase unit results in an increase in absorbance at 260nm of 0.001/minute at 25°C when acting upon highly polymerized solution of DNA at pH-5. Also 0.005 Kunitz unit digests 1µgof lambda phage DNA in 10 minutes at 37°C in50mM Tris, 1mMMg++, pH 7.8 in a 50ul reaction.
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Specific Activity
1000IU/1mg.
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.
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Name :
NAA10 HumanDescription:
N Alpha-Acetyltransferase 10, NatA Catalytic Subunit Human Recombinant
N-alpha-acetyltransferase 10, N-terminal acetyltransferase complex ARD1 subunit homolog A, NatA catalytic subunit, NAA10, ARD1, ARD1A, TE2, NATD, DXS707.
Product # :
ENZ-158Price :
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Description
NAA10 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 255 amino acids (1-235 a.a.) and having a molecular mass of 28.6kDa (the molecular weight on SDS-PAGE will appear higher).NAA10 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
NAA10 protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 5mM DTT, 10% glycerol and 200mM NaCl.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
NAA10 is a member of the acetyltransferase family. NAA10 interacts with NAA15, HIF-1 and with the ribosome. In its binding to HIF-1, NAA10 functions as a protein acetyltransferase by regulating its stability. In various cell lines, NAA10 is downregulated in response to hypoxia. NAA10 is expressed during the course of the development of the brain.
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Synonyms
N-alpha-acetyltransferase 10, N-terminal acetyltransferase complex ARD1 subunit homolog A, NatA catalytic subunit, NAA10, ARD1, ARD1A, TE2, NATD, DXS707.
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Physical Appearance
Sterile Filtered colorless solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MNIRNARPED LMNMQHCNLL CLPENYQMKY YFYHGLSWPQ LSYIAEDENG KIVGYVLAKM EEDPDDVPHG HITSLAVKRS HRRLGLAQKL MDQASRAMIE NFNAKYVSLH VRKSNRAALH LYSNTLNFQI SEVEPKYYAD GEDAYAMKRD LTQMADELRR HLELKEKGRH VVLGAIENKV ESKGNSPPSS GEACREEKGL AAEDSGGDSK DLSEVSETTE STDVKDSSEA SDSAS.
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.
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Name :
RNASE1 HumanDescription:
Ribonuclease 1 Human Recombinant
RNASE1, ribonuclease A family member 1, pancreatic, RAC1, RIB1, RNS1, ribonuclease pancreatic, HP-RNase, RIB-1, RNase UpI-1, RNase 1, Ribonuclease A, RNase A, Ribonuclease 1.
Product # :
ENZ-1168Price :
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Description
RNASE1 Human Recombinant produced in HEK cells is a single, glycosylated, polypeptide chain (29-156 a.a) containing a total of 134 amino acids, having a molecular mass of 15.3kDa. RNASE1 is fused to a 6 amino acid His-tag at C-terminus,and is purified by proprietary chromatographic techniques.
Source
HEK293 Cells.
Formulation
The RNASE1 solution (1mg/ml) contains 10% Glycerol and Phosphate-Buffered Saline (pH 7.4).
Purity
Greater than 90.0% as determined by SDS-PAGE.
Biological Activity
Specific activity is > 3 X 10^6 unit/mg. Defined by the amount of enzyme that hydrolyzes 1nmole of RNA per minute at 25˚C.
More Info
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Introduction
Ribonuclease 1R (NASE1) is a small protein which is a part of pancreatic ribonuclease enzyme family. NASE1 has 4 disulfide bonds in its native state and cleaves speciallyafter pyrimidine nucleotides.Cleavage takes place in 2 steps: first, the 3’,5’-phosphodiester bond is cleaved to craete a 2’,3’-cyclic phosphodiester intermediate; than, the cyclic phosphodiester is hydrolyzed to a 3’-monophosphate. NASE1is activated the most with single stranded RNA.NASE1inhibited by alkylation of His12 and His119 and activated by potassium and sodium salts.NASE1hydrolyzes RNA from protein samples.
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Synonyms
RNASE1, ribonuclease A family member 1, pancreatic, RAC1, RIB1, RNS1, ribonuclease pancreatic, HP-RNase, RIB-1, RNase UpI-1, RNase 1, Ribonuclease A, RNase A, Ribonuclease 1.
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Physical Appearance
Sterile Filtered colorless solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks.Store, frozen at -20°C for longer periods of time.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
KESRAKKFQR QHMDSDSSPS SSSTYCNQMM RRRNMTQGRC KPVNTFVHEP LVDVQNVCFQ EKVTCKNGQG NCYKSNSSMH ITDCRLTNGS RYPNCAYRTS PKERHIIVAC EGSPYVPVHF DASVEDSTHH 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.
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Name :
ACO1 HumanDescription:
Aconitase-1 Human Recombinant
Onitase 1 Soluble, IRP1, IREB1, IREBP, Citrate hydro-lyase, Iron regulatory protein 1, Ferritin repressor protein, Iron-responsive element-binding protein 1, ACONS, Aconitate Hydratase, EC 4.2.1.3, Aconitase.
Product # :
ENZ-056Price :
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Description
ACO1 produced in E.Coli is a single, non-glycosylated polypeptide chain containing 912 amino acids (1-889a.a.) and having a molecular mass of 100.8kDa.ACO1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The ACO1 protein solution (0.5mg/1ml) is formulated in 20mM Tris-HCl buffer (pH8.0)
2mM DTT, 100mM NaCl and 10% glycerol.Purity
Greater than 90% as determined by SDS-PAGE.
More Info
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Introduction
ACO1 has a part in an iron sensor. ACO1 catalyzes the stereo-specific isomerization of citrate to isocitrate via cis-aconitate in the tricarboxylic acid cycle, a non-redox-active process.
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Synonyms
Onitase 1 Soluble, IRP1, IREB1, IREBP, Citrate hydro-lyase, Iron regulatory protein 1, Ferritin repressor protein, Iron-responsive element-binding protein 1, ACONS, Aconitate Hydratase, EC 4.2.1.3, Aconitase.
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Physical Appearance
Sterile Filtered clear solution.
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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).Please avoid freeze thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSMSNPFAH LAEPLDPVQP GKKFFNLNKL EDSRYGRLPF SIRVLLEAAI RNCDEFLVKK QDIENILHWN VTQHKNIEVP FKPARVILQD FTGVPAVVDF AAMRDAVKKL GGDPEKINPV CPADLVIDHS IQVDFNRRAD SLQKNQDLEF ERNRERFEFL KWGSQAFHNM RIIPPGSGII HQVNLEYLAR VVFDQDGYYY PDSLVGTDSH TTMIDGLGIL GWGVGGIEAE AVMLGQPISM VLPQVIGYRL MGKPHPLVTS TDIVLTITKH LRQVGVVGKF VEFFGPGVAQ LSIADRATIA NMCPEYGATA AFFPVDEVSI TYLVQTGRDE EKLKYIKKYL QAVGMFRDFN DPSQDPDFTQ VVELDLKTVV PCCSGPKRPQ DKVAVSDMKK DFESCLGAKQ GFKGFQVAPE HHNDHKTFIY DNTEFTLAHG SVVIAAITSC TNTSNPSVML GAGLLAKKAV DAGLNVMPYI KTSLSPGSGV VTYYLQESGV MPYLSQLGFD VVGYGCMTCI GNSGPLPEPV VEAITQGDLV AVGVLSGNRN FEGRVHPNTR ANYLASPPLV IAYAIAGTIR IDFEKEPLGV NAKGQQVFLK DIWPTRDEIQ AVERQYVIPG MFKEVYQKIE TVNESWNALA TPSDKLFFWN SKSTYIKSPP FFENLTLDLQ PPKSIVDAYV LLNLGDSVTT DHISPAGNIA RNSPAARYLT NRGLTPREFN SYGSRRGNDA VMARGTFANI RLLNRFLNKQ APQTIHLPSG EILDVFDAAE RYQQAGLPLI VLAGKEYGAG SSRDWAAKGP FLLGIKAVLA ESYERIHRSN LVGMGVIPLE YLPGENADAL GLTGQERYTI IIPENLKPQM KVQVKLDTGK TFQAVMRFDT DVELTYFLNG GILNYMIRKM AK
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.
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Name :
FOLH1 HumanDescription:
Folate Hydrolase 1 Human Recombinant
Glutamate carboxypeptidase 2 isoform 1,Cell growth-inhibiting gene 27 protein, Folate hydrolase 1, Folylpolygamma-glutamate carboxypeptidase, Glutamate carboxypeptidase II, Membrane glutamate carboxypeptidase, Nacetylated-alpha-linked acidic dipeptidase I, Prostate-specific membrane antigen, Pteroylpoly-gamma glutamate carboxypeptidase, Folh1, FGCP, FOLH, GCP2, GCPII, mGCP, NAALAD1, NAALAdase, PSM, PSMA
Product # :
ENZ-1170Price :
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Description
FOLH1 produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 717 amino acids (44-750 a.a) and having a molecular mass of 80.7kDa.FOLH1 is expressed with a 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
FOLH1 protein solution (0.25mg/ml) contains Phosphate buffered saline (pH 7.4) and 20% glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
FOLH1, also known as glutamate carboxypeptidase 2 (GCPII), is a single pass type 2 membrane protein which belongs to the peptidase M28 family. FOLH1 is highly produced in prostate epithelium. FOLH1 is also found in ovary, live, stomach, small intestine colon, urinary bladder, kidney, testis, and the capillary endothelium of a variety of tumours. Therefore, it plays a role in directed imaging and therapy of recurrent of metastatic disease. FOLH1 is a zinc metalloenzyme that resides in membranes and catalyses the hydrolysis of N-acetylaspartylglutamate to glutamate and N-acetylaspartate.
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Synonyms
Glutamate carboxypeptidase 2 isoform 1,Cell growth-inhibiting gene 27 protein, Folate hydrolase 1, Folylpolygamma-glutamate carboxypeptidase, Glutamate carboxypeptidase II, Membrane glutamate carboxypeptidase, Nacetylated-alpha-linked acidic dipeptidase I, Prostate-specific membrane antigen, Pteroylpoly-gamma glutamate carboxypeptidase, Folh1, FGCP, FOLH, GCP2, GCPII, mGCP, NAALAD1, NAALAdase, PSM, PSMA
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Physical Appearance
Sterile Filtered colorless solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks.Store, frozen at -20°C for longer periods of time.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
ADPMKSSNEA TNITPKHNMK AFLDELKAEN IKKFLYNFTQ IPHLAGTEQN FQLAKQIQSQ WKEFGLDSVE LAHYDVLLSY PNKTHPNYIS IINEDGNEIF NTSLFEPPPP GYENVSDIVP PFSAFSPQGM PEGDLVYVNY ARTEDFFKLE RDMKINCSGK IVIARYGKVF RGNKVKNAQL AGAKGVILYS DPADYFAPGV KSYPDGWNLP GGGVQRGNIL NLNGAGDPLT PGYPANEYAY RRGIAEAVGL PSIPVHPIGY YDAQKLLEKM GGSAPPDSSW RGSLKVPYNV GPGFTGNFST QKVKMHIHST NEVTRIYNVI GTLRGAVEPD RYVILGGHRD SWVFGGIDPQ SGAAVVHEIV RSFGTLKKEG WRPRRTILFA SWDAEEFGLL GSTEWAEENS RLLQERGVAY INADSSIEGN YTLRVDCTPL MYSLVHNLTK ELKSPDEGFE GKSLYESWTK KSPSPEFSGM PRISKLGSGN DFEVFFQRLG IASGRARYTK NWETNKFSGY PLYHSVYETY ELVEKFYDPM FKYHLTVAQV RGGMVFELAN SIVLPFDCRD YAVVLRKYAD KIYSISMKHP QEMKTYSVSF DSLFSAVKNF TEIASKFSER LQDFDKSNPI VLRMMNDQLM FLERAFIDPL GLPDRPFYRH VIYAPSSHNK YAGESFPGIY DALFDIESKV DPSKAWGEVK RQIYVAAFTV QAAAETLSEV AHHHHHH
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.
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Name :
METTL21A HumanDescription:
Methyltransferase Like 21A Human Recombinant
Protein N-lysine methyltransferase METTL21A, HSPA lysine methyltransferase, HSPA-KMT, Hepatocellular carcinoma-associated antigen 557b, Methyltransferase-like protein 21A, METTL21A, FAM119A, HCA557B, Methyltransferase Like 21A.
Product # :
ENZ-718Price :
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Description
METTL21A Human Recombinant produced in E. coli is a single polypeptide chain containing 149 amino acids (93-218) and having a molecular mass of 17 kDa.METTL21A is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
The METTL21A solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl and 30% glycerol.
Purity
Greater than 85% as determined by SDS-PAGE.
More Info
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Introduction
METTL21A, which is a part of the methyltransferase superfamily, is a Protein-lysine methyltransferase that in vitro methylates HSPA1, HSPA5 and HSPA8.
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Synonyms
Protein N-lysine methyltransferase METTL21A, HSPA lysine methyltransferase, HSPA-KMT, Hepatocellular carcinoma-associated antigen 557b, Methyltransferase-like protein 21A, METTL21A, FAM119A, HCA557B, Methyltransferase Like 21A.
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Physical Appearance
Sterile Filtered colorless solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSTDRKVAL EFLKSNVQAN LPPHIQTKTV VKELTWGQNL GSFSPGEFDL ILGADIIYLE ETFTDLLQTL EHLCSNHSVI LLACRIRYER DNNFLAMLER QFTVRKVHYD PEKDVHIYEA QKRNQKEDL.
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.
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Name :
HARS HumanDescription:
Histidyl-tRNA Synthetase Human Recombinant
Histidyl-tRNA synthetase, EC 6.1.1.21, Histidine-tRNA ligase, HisRS, HRS, FLJ20491, JO-1, HARS.
Product # :
ENZ-268Price :
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Description
Histidyl-tRNA Synthetase Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain having a molecular mass of 55 kDa.
Source
Escherichia Coli.
Formulation
The protein solution contains 500mM NaCl and 10mM Tris (pH 8.0) and 6M Urea.
Purity
Greater than 95.0% as determined by Analysis by SDS-PAGE.
More Info
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Introduction
Aminoacyl-tRNA synthetases are a class of enzymes that charge tRNAs with their cognate amino acids. The protein encoded by this gene is a cytoplasmic enzyme which belongs to the class II family of aminoacyl-tRNA synthetases. The enzyme is responsible for the synthesis of histidyl-transfer RNA, which is essential for the incorporation of histidine into proteins. The gene is located in a head-to-head orientation with HARSL on chromosome five, where the homologous genes share a bidirectional promoter. The gene product is a frequent target of autoantibodies in the human autoimmune disease polymyositis/dermatomyositis.
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Synonyms
Histidyl-tRNA synthetase, EC 6.1.1.21, Histidine-tRNA ligase, HisRS, HRS, FLJ20491, JO-1, HARS.
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Physical Appearance
Sterile Filtered clear solution.
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Stability
Histidyl-tRNA Synthetase although stable at 4°C for 3 weeks, should be stored below -18°C.Please prevent freeze-thaw cycles.
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Applications
Western Blot: Strongly reactive with human anti Histidyl-tRNA Synthetase antisera.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
ASRGL1 HumanDescription:
ASRGL1 Human Recombinant
ALP, ALP1, CRASH, ,Beta-aspartyl-peptidase, Isoaspartyl dipeptidase.
Product # :
ENZ-837Price :
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Description
ASRGL1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 331 amino acids (1-308 a.a) and having a molecular mass of 34.4kDa.ASRGL1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
ASRGL1 protein solution (0.5mg/ml) containing Phosphate buffer saline, (pH 7.4) ,10% glycerol and 1mM DTT.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
ASRGL1 is a 308 amino acid protein which is a member of the Ntn-hydrolase family. ASRGL1 is an autoantigenic protein which is present in the mid-piece of sperm after obstruction of the male reproductive tract. ASRGL1 is expressed highly in the testis, but is also expressed in the brain, kidney and gastrointestinal tissues. High levels of ASRGL1 are also detected in ovarian, uterine and mammary tumors in comparison with normal tissues of the same origin.
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Synonyms
ALP, ALP1, CRASH, ,Beta-aspartyl-peptidase, Isoaspartyl dipeptidase.
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Physical Appearance
Sterile Filtered colorless solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSMNPIVVV HGGGAGPISK DRKERVHQGM VRAATVGYGI LREGGSAVDA VEGAVVALED DPEFNAGCGS VLNTNGEVEM DASIMDGKDL SAGAVSAVQC IANPIKLARL VMEKTPHCFL TDQGAAQFAA AMGVPEIPGE KLVTERNKKR LEKEKHEKGA QKTDCQKNLG TVGAVALDCK GNVAYATSTG GIVNKMVGRV GDSPCLGAGG YADNDIGAVS TTGHGESILK VNLARLTLFH IEQGKTVEEA ADLSLGYMKS RVKGLGGLIV VSKTGDWVAK WTSTSMPWAA AKDGKLHFGI DPDDTTITDL 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.
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Name :
NCEH1 HumanDescription:
Neutral Cholesterol Ester Hydrolase 1 Human Recombinant
AADACL1, NCEH, Neutral cholesterol ester hydrolase 1, Arylacetamide deacetylase-like, KIAA1363, NCEH1.
Product # :
PRO-1393Price :
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Description
NCEH1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 298 amino acids (1-275a.a) and having a molecular mass of 33.6kDa. NCEH1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
NCEH1 protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.4M urea and 10% glycerol.
Purity
Greater than 90% as determined by SDS-PAGE.
More Info
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Introduction
Neutral cholesterol ester hydrolase 1 (NCEH1), hydrolyzes 2-acetyl monoalkylglycerol ether, the penultimate precursor of the pathway for de novo synthesis of platelet-activating factor. NCEH1 is responsible for cholesterol ester hydrolysis in macrophages, by this means contributing to the development of atherosclerosis. NCEH1 contributes also to cancer pathogenesis by promoting tumor cell migration. NCEH1 is involved in organ detoxification by hydrolyzing exogenous organophosphorus compounds.
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Synonyms
AADACL1, NCEH, Neutral cholesterol ester hydrolase 1, Arylacetamide deacetylase-like, KIAA1363, NCEH1.
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Physical Appearance
Sterile Filtered colorless solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSMAEELNA VIVSIEYRLV PKVYFPEQIH DVVRATKYFL KPEVLQKYMV DPGRICISGD SAGGNLAAAL GQQFTQDASL KNKLKLQALI YPVLQALDFN TPSYQQNVNT PILPRYVMVK YWVDYFKGNY DFVQAMIVNN HTSLDVEEAA AVRARLNWTS LLPASFTKNY KPVVQTTGNA RIVQELPQLL DARSAPLIAD QAVLQLLPKT YILTCEHDVL RDDGIMYAKR LESAGVEVTL DHFEDGFHGC MIFTSWPTNF SVGIRTRNSY IKWLDQNL.
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.
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Name :
LGMN MouseDescription:
Legumain Mouse Recombinant
Legumain, Asparaginyl endopeptidase, Protease, cysteine 1.
Product # :
ENZ-933Price :
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- sds-page
Description
LGMN produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 426 amino acids (18-435a.a.) and having a molecular mass of 48.6kDa. LGMN is expressed with an 8 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
LGMN 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.
sds-page
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Introduction
Legumain, also known as LGMN is a lysosomal cysteine protease which is found in all mouse tissues, however it was mainly abundant in the kidney as well as placenta. LGMN plays an essential role in the endosomal/lysosomal degradation system as the Legumain deficiency causes the accumulation of pro cathepsins B, H & L, another group of lysosomal cysteine proteases. Furthermore, over expression of LGMN in tumors is important for invasion/metastasis.
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Synonyms
Legumain, Asparaginyl endopeptidase, Protease, cysteine 1.
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Physical Appearance
Sterile filtered colorless solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks.Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
VPVGVDDPED GGKHWVVIVA GSNGWYNYRH QADACHAYQI IHRNGIPDEQ IIVMMYDDIA NSEENPTPGV VINRPNGTDV YKGVLKDYTG EDVTPENFLA VLRGDAEAVK GKGSGKVLKS GPRDHVFIYF TDHGATGILV FPNDDLHVKD LNKTIRYMYE HKMYQKMVFY IEACESGSMM NHLPDDINVY ATTAANPKES SYACYYDEER GTYLGDWYSV NWMEDSDVED LTKETLHKQY HLVKSHTNTS HVMQYGNKSI STMKVMQFQG MKHRASSPIS LPPVTHLDLT PSPDVPLTIL KRKLLRTNDV KESQNLIGQI QQFLDARHVI EKSVHKIVSL LAGFGETAER HLSERTMLTA HDCYQEAVTH FRTHCFNWHS VTYEHALRYL YVLANLCEAP YPIDRIEMAM DKVCLSHYLE 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.