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1000 results found for “dehydrogenase”
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Name :
NANA E.ColiDescription:
N-Acetylneuraminate Lyase E.Coli Recombinant
N-acetylneuraminate lyase, N-acetylneuraminate pyruvate-lyase, N-acetylneuraminic acid aldolase, NALase, Sialate lyase, Sialic acid aldolase, Sialic acid lyase, nanA, npl, b3225, JW3194.
Product # :
ENZ-128Price :
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Description
NANA produced in E.Coli is a single, non-glycosylated polypeptide chain containing 317 amino acids (1-297 a.a.) and having a molecular mass of 34.7kDa.NANA is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The NANA protein solution (1mg/ml) 20mM Tris-HCl buffer (pH8.0) and 20% glycerol.
Purity
Greater than 95% as determined by SDS-PAGE.
More Info
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Introduction
N-acetylneuraminate lyase (NanA) is a member of a family of lyases, specifically the oxo-acid-lyases, which cleave carbon-carbon bonds. NanA catalyzes the cleavage of N-acetylneuraminic acid (sialic acid) to form pyruvate and N-acetyl-D-mannosamine. NanA is inhibited by reduction with NaBH4 in the presence of the substrate, which indicates that it belongs to the Schiff-base-forming Class I aldolases. NanA is strongly inhibited by Cu2+ ions, p-chloromercuribenzoate and N-bromosuccinimide, it is also inhibited competitively by the reaction product, pyruvate, and its structurally related compounds, dihydroxyacetone and DL-glyceraldehyde.
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Synonyms
N-acetylneuraminate lyase, N-acetylneuraminate pyruvate-lyase, N-acetylneuraminic acid aldolase, NALase, Sialate lyase, Sialic acid aldolase, Sialic acid lyase, nanA, npl, b3225, JW3194.
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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). Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MATNLRGVMA ALLTPFDQQQ ALDKASLRRL VQFNIQQGID GLYVGGSTGE AFVQSLSERE QVLEIVAEEA KGKIKLIAHV GCVSTAESQQ LAASAKRYGF DAVSAVTPFY YPFSFEEHCD HYRAIIDSAD GLPMVVYNIP ALSGVKLTLD QINTLVTLPG
VGALKQTSGD LYQMEQIRRE HPDLVLYNGY DEIFASGLLA GADGGIGSTY NIMGWRYQGI VKALKEGDIQ TAQKLQTECN KVIDLLIKTG VFRGLKTVLH YMDVVSVPLC RKPFGPVDEK YLPELKALAQ QLMQERG.
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 :
ECH1 HumanDescription:
Enoyl CoA Hydratase 1, Peroxisomal Human Recombinant
peroxisomal, enoyl Coenzyme A hydratase 1.
Product # :
ENZ-562Price :
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Description
ECH1 produced in E.Coli is a single, non-glycosylated polypeptide chain containing 316 amino acids (34-328a.a.) and having a molecular mass of 34.4kDa.ECH1 is fused to a 21 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The ECH1 protein solution (1mg/1ml) is formulated in 20mM Tris-HCl buffer (pH8.0) 1mM DTT, 50mM NaCl, and 10% glycerol.
Purity
Greater than 90% as determined by SDS-PAGE.
More Info
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Introduction
ECH1 is a member of the hydratase/isomerase superfamily. ECH1 demonstrates high sequence similarity to enoyl-coenzyme A (CoA) hydratases of more than a few species, mostly within a conserved domain characteristic of these proteins. ECH1 contains a C-terminal peroxisomal targeting sequence, localizes to both the peroxisome and the mitochondria. peroxisomal takes part in the auxiliary step of the fatty acid beta-oxidation pathway specifically functioning to catalyze the isomerization of 3-trans, 5-cis-dienoyl-CoA to 2-trans, 4-transdienoyl-CoA.
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Synonyms
peroxisomal, enoyl Coenzyme A hydratase 1.
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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).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MTGSSAQEAA SGVALGEAPD HSYESLRVTS AQKHVLHVQL NRPNKRNAMN KVFWREMVEC FNKISRDADC RAVVISGAGK MFTAGIDLMD MASDILQPKG DDVARISWYL RDIITRYQET FNVIERCPKP VIAAVHGGCI GGGVDLVTAC DIRYCAQDAF FQVKEVDVGL AADVGTLQRL PKVIGNQSLV NELAFTARKM MADEALGSGL VSRVFPDKEV MLDAALALAA EISSKSPVAV QSTKVNLLYS RDHSVAESLN YVASWNMSML QTQDLVKSVQ ATTENKELKT VTFSKL.
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 :
UBE2D1 HumanDescription:
Ubiquitin Conjugating Enzyme E2D1 Human Recombinant
Ubiquitin-conjugating enzyme E2 D1, Stimulator of Fe transport, SFT, UBC4/5 homolog, UbcH5, Ubiquitin carrier protein D1, Ubiquitin-conjugating enzyme E2(17)KB 1, Ubiquitin-conjugating enzyme E2-17 kDa 1, Ubiquitin-protein ligase D1, UBE2D1, SFT, UBC5A, UBCH5A, E2(17)KB1.
Product # :
ENZ-116Price :
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Description
UBE2D1 produced in E.Coli is a single, non-glycosylated polypeptide chain containing 170 amino acids (1-147 a.a.) and having a molecular mass of 19kDa.UBE2D1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
UBE2D1 solution (1mg/ml) containing 20mM Tris-HCl buffer (pH8.0), 40% glycerol and 0.1M NaCl.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
UBE2D1 is a member of the ubiquitin-conjugating enzyme family. Ubiquitination involves at least 3 classes of enzymes: ubiquitin-activating enzymes (E1s), ubiquitin-conjugating enzymes (E2s) and ubiquitin-protein ligases (E3s). UBE2D1 is strongly related to a stimulator of iron transport (SFT), and is up-regulated in hereditary hemochromatosis. In addition, UBE2D1 functions in the ubiquitination of the tumor-suppressor protein p53 and the hypoxia-inducible transcription factor HIF1alpha by interacting with the E1 ubiquitin-activating enzyme and the E3 ubiquitin-protein ligases.
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Synonyms
Ubiquitin-conjugating enzyme E2 D1, Stimulator of Fe transport, SFT, UBC4/5 homolog, UbcH5, Ubiquitin carrier protein D1, Ubiquitin-conjugating enzyme E2(17)KB 1, Ubiquitin-conjugating enzyme E2-17 kDa 1, Ubiquitin-protein ligase D1, UBE2D1, SFT, UBC5A, UBCH5A, E2(17)KB1.
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Physical Appearance
Sterile filtered colorless solution.
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Stability
UBE2D1 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 MGSMALKRIQ KELSDLQRDP PAHCSAGPVG DDLFHWQATI MGPPDSAYQG GVFFLTVHFP TDYPFKPPKI AFTTKIYHPN INSNGSICLD ILRSQWSPAL TVSKVLLSIC SLLCDPNPDD PLVPDIAQIY KSDKEKYNRH AREWTQKYAM.
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 :
NNMT HumanDescription:
Nicotinamide N-Methyltransferase Human Recombinant
Nicotineamide N-methyltransferase, NNMT.
Product # :
ENZ-418Price :
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Description
NNMT Human Recombinant fused with a 20 amino acid His-Tag tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing a total of 284 amino acids (1-264 a.a.) and having a molecular mass of 31.7 kDa.The NNMT is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The NNMT solution contains 20mM Tris pH 8.0 & 20% glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
NNMT is part of the family of transferases, especially those transferring one-carbon group methyltransferases. NNMT is mostly expressed in the liver, and a lower expression is seen in the kidney, lung, skeletal muscle, placenta and heart. NNMT catalyzes the N-methylation of nicotinamide and other pyridines to form pyridinium ions. This activity is significant for biotransformation of many drugs and xenobiotic compounds. NNMT is accountable for the enzymatic activity which uses S-adenosyl methionine as the methyl donor. NNMT expression is related with tumor stage and DFS time in hepatocellular carcinoma cases. NNMT is a good candidate as a tumor marker of various kinds of cancers. NNMT serum levels have significance in the premature detection and in the management of patients with colorectal cancer.
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Synonyms
Nicotineamide N-methyltransferase, NNMT.
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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 MESGFTSKDT YLSHFNPRDY LEKYYKFGSR HSAESQILKH LLKNLFKIFC LDGVKGDLLI DIGSGPTIYQLLSACESFKE IVVTDYSDQN LQELEKWLKK EPEAFDWSPV VTYVCDLEGN RVKGPEKEEK LRQAVKQVLK CDVTQSQPLG AVPLPPADCV LSTLCLDAAC PDLPTYCRAL RNLGSLLKPG GFLVIMDALK SSYYMIGEQK FSSLPLGREA VEAAVKEAGY TIEWFEVISQ SYSSTMANNEGLFSLVARKL SRPL.
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 :
ACP5 Human, HisDescription:
Acid Phosphatase-5 Human Recombinant, His Tag
Acid Phosphatase 5, Tartrate Resistant, Tartrate-Resistant Acid ATPase, EC 3.1.3.2, TrATPase, SPENCDI, Tartrate-Resistant Acid Phosphatase Type 5, Tartrate-Resistant Acid Phosphatase, Type 5 Acid Phosphatase, TR-AP, TRAP, ACP5.
Product # :
ENZ-913Price :
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Description
ACP5 Human Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 310 amino acids (22-325 a.a) and having a molecular mass of 35.1kDa.ACP5 is fused to a 6 amino acid His-tag at C-terminus & purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
ACP5 protein solution (0.5mg/ml) containing Phosphate Buffered Saline (pH 7.4) and 10% glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Biological Activity
Specific activity is > 5,000 units/mg, and is defined as the amount of enzyme that hydrolyze 1.0 nmoles of p-nitrophenyl phosphate (pNPP) per minute at pH 5.0 at 37C.More Info
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Introduction
Acid Phosphatase-5, also known as ACP5 is a member of the Purple acid phosphatase family. ACP5 is implicated in osteopontin as well as bone sialoprotein dephosphorylation. ACP5 expression appears to increase in certain pathological states for instance Gaucher & Hodgkin diseases, the hairy cell, the B-cell, as well as the T-cell leukemias.
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Synonyms
Acid Phosphatase 5, Tartrate Resistant, Tartrate-Resistant Acid ATPase, EC 3.1.3.2, TrATPase, SPENCDI, Tartrate-Resistant Acid Phosphatase Type 5, Tartrate-Resistant Acid Phosphatase, Type 5 Acid Phosphatase, TR-AP, TRAP, ACP5.
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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
ATPALRFVAV GDWGGVPNAP FHTAREMANA KEIARTVQIL GADFILSLGD NFYFTGVQDI NDKRFQETFE DVFSDRSLRK VPWYVLAGNH DHLGNVSAQI AYSKISKRWN FPSPFYRLHF KIPQTNVSVA IFMLDTVTLC GNSDDFLSQQ PERPRDVKLA RTQLSWLKKQ LAAAREDYVL VAGHYPVWSI AEHGPTHCLV KQLRPLLATY GVTAYLCGHD HNLQYLQDEN GVGYVLSGAG NFMDPSKRHQ RKVPNGYLRF HYGTEDSLGG FAYVEISSKE MTVTYIEASG KSLFKTRLPR RARPHHHHHH.
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 :
FUT3 HumanDescription:
Fucosyltransferase 3 Human Recombinant
Galactoside 3(4)-L-fucosyltransferase, Blood group Lewis alpha-4-fucosyltransferase, Lewis FT, Fucosyltransferase 3, Fucosyltransferase III, FucT-III, FUT3, FT3B, LE, CD174, Les.
Product # :
ENZ-745Price :
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Description
FUT3 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 350 amino acids (35-361 a.a) and having a molecular mass of 40.6kDa.FUT3 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The FUT3 solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.4M urea and 10% glycerol.
Purity
Greater than 80% as determined by SDS-PAGE.
More Info
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Introduction
Fucosyltransferase 3 (FUT3) catalyzes alpha-1, 3 and alpha-1, 4 glycosidic linkages which take part in the expression of Vim-2, Lewis A, Lewis B, sialyl Lewis X and Lewis X/SSEA-1 antigens. FUT3 takes part in blood group Lewis determination; Lewis-positive (Le+) individuals have an active enzyme while Lewis-negative (Le-) individuals have an inactive enzyme. FUT3 also operates on the corresponding 1, 4-galactosyl derivative, creating1, 3-L-fucosyl links.
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Synonyms
Galactoside 3(4)-L-fucosyltransferase, Blood group Lewis alpha-4-fucosyltransferase, Lewis FT, Fucosyltransferase 3, Fucosyltransferase III, FucT-III, FUT3, FT3B, LE, CD174, Les.
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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).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSRVSRDDA TGSPRAPSGS SRQDTTPTRP TLLILLWTWP FHIPVALSRC SEMVPGTADC HITADRKVYP QADTVIVHHW DIMSNPKSRL PPSPRPQGQR WIWFNLEPPP NCQHLEALDR YFNLTMSYRS DSDIFTPYGW LEPWSGQPAH PPLNLSAKTE LVAWAVSNWK PDSARVRYYQ SLQAHLKVDV YGRSHKPLPK GTMMETLSRY KFYLAFENSL HPDYITEKLW RNALEAWAVP VVLGPSRSNY ERFLPPDAFI HVDDFQSPKD LARYLQELDK DHARYLSYFR WRETLRPRSF SWALDFCKAC WKLQQESRYQ TVRSIAAWFT.
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 :
TOP1 HumanDescription:
DNA Topoisomerase-I Human Recombinant
DNA topoisomerase 1, EC 5.99.1.2, DNA topoisomerase I, TOP1, Scl-70.
Product # :
ENZ-306Price :
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Description
DNA Topoisomerase-I Human Recombinant produced in SF9 is a glycosylated, polypeptide chain having a molecular mass of 102 kDa. The TOP1 is expressed with a -6xHis tag and purified by proprietary chromatographic techniques.
Source
Sf9 insect cells.
Formulation
TOP1 is supplied in 16mM HEPES buffer pH-7.5, 400mM sodium chloride, and 20% glycerol.
Purity
Greater than 95% as determined by SDS-PAGE.
More Info
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Introduction
DNA toposisomerase I is a key nuclear enzyme that interconverts supercoiled DNA to the required topological conformations for normal DNA replication and transcription. This enzyme is the target antigen for the so-called Scl-70 autoantibodies. Scl-70 antibodies are a specific marker in Scleroderma patients (specificity 98-100%) and are associated with the presence of diffuse skin involvement and pulmonary fibrosis.
In human tissues the DNA topoisomerase I is initially synthesized as a protein with 100 kDa molecular weight. Most of this precursor is then proteolytically processed to a species with 70 kDa molecular weight from which the Scl-70 antigen has derived its name. -
Synonyms
DNA topoisomerase 1, EC 5.99.1.2, DNA topoisomerase I, TOP1, Scl-70.
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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. 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.
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Name :
METTL1 HumanDescription:
Methyltransferase Like 1 Human Recombinant
Methyltransferase-Like 1, TRM8, tRNA(m7G46)-methyltransferase, tRNA (guanine-N(7)-)-methyltransferase , C12orf1, YDL201w, D1075-like gene product, FLJ95748, EC 2.1.1.33.
Product # :
ENZ-054Price :
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Description
Recombinant Human METTL1 produced in E.Coli is a single, non-glycosylated polypeptide chain containing 296 amino acids (1-276a.a.) and having a molecular mass of 33.6kDa.METTL1 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The METTL1 protein solution (0.5mg/1ml) is formulated in 20mM Tris-HCl buffer (pH8.0)
1mM DTT, 50mM NaCl and 10% glycerol.Purity
Greater than 90% as determined by SDS-PAGE.
More Info
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Introduction
METTL1 is recognized as tRNA (guanine-N(7)-)-methyltransferase that is a part of the methyltransferase superfamily. METTL1 displays high sequence similarity to yeast ORF YDL201w and can be inactivated by phosphorylation. METTL1 protein has a conserved S-adenosylmethionine-binding motif and ccatalyzes the formation of N(7)-methylguanine at position 46 (m7G46) in tRNA.
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Synonyms
Methyltransferase-Like 1, TRM8, tRNA(m7G46)-methyltransferase, tRNA (guanine-N(7)-)-methyltransferase , C12orf1, YDL201w, D1075-like gene product, FLJ95748, EC 2.1.1.33.
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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).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MAAETRNVAG AEAPPPQKRY YRQRAHSNPM ADHTLRYPVK PEEMDWSELY PEFFAPLTQN QSHDDPKDKK EKRAQAQVEF ADIGCGYGGL LVELSPLFPD TLILGLEIRV KVSDYVQDRI RALRAAPAGG FQNIACLRSN AMKHLPNFFY KGQLTKMFFL FPDPHFKRTK HKWRIISPTL LAEYAYVLRV GGLVYTITDV LELHDWMCTH FEEHPLFERV PLEDLSEDPV VGHLGTSTEE GKKVLRNGGK NFPAIFRRIQ DPVLQAVTSQ TSLPGH
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 :
ABO HumanDescription:
ABO Blood Group Human Recombinant
Histo-blood group ABO system transferase, Fucosylglycoprotein 3-alpha-galactosyltransferase, Fucosylglycoprotein alpha-N-acetylgalactosaminyltransferase, Glycoprotein-fucosylgalactoside alpha-N-acetylgalactosaminyltransferase, Glycoprotein-fucosylgalactoside alpha-galactosyltransferase, Histo-blood group A transferase, A transferase, Histo-blood group B transferase, B transferase, NAGAT, ABO, GTB, A3GALNT, A3GALT1.
Product # :
ENZ-167Price :
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Description
ABO Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 322 amino acids (54-354 a.a) and having a molecular mass of 37.4kDa.ABO is fused to a 21 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
ABO protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 2mM DTT, 20% glycerol and 200mM NaCl.
Purity
Greater than 85.0% as determined by SDS-PAGE.
More Info
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Introduction
NAGAT (ABO) is a member of the glycosyltransferase 6 family. The ABO protein is the basis of the ABO blood group system and related to the first discovered blood group system, ABO. The allele that is present in an individual determines the blood group. The histo-blood group ABO is comprised of 3 carbohydrate antigens: A, B, and H. A, B, and AB individuals express a glycosyltransferase activity which converts the H antigen to the A antigen (by addition of UDP-GalNAc) or to the B antigen (by addition of UDP-Gal), whereas O individuals are deficient of such activity.
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Synonyms
Histo-blood group ABO system transferase, Fucosylglycoprotein 3-alpha-galactosyltransferase, Fucosylglycoprotein alpha-N-acetylgalactosaminyltransferase, Glycoprotein-fucosylgalactoside alpha-N-acetylgalactosaminyltransferase, Glycoprotein-fucosylgalactoside alpha-galactosyltransferase, Histo-blood group A transferase, A transferase, Histo-blood group B transferase, B transferase, NAGAT, ABO, GTB, A3GALNT, A3GALT1.
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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 MAVREPDHLQ RVSLPRMVYP QPKVLTPCRK DVLVVTPWLA PIVWEGTFNI DILNEQFRLQ NTTIGLTVFA IKKYVAFLKL FLETAEKHFM VGHRVHYYVF TDQPAAVPRV TLGTGRQLSV LEVRAYKRWQ DVSMRRMEMI SDFCERRFLS EVDYLVCVDV DMEFRDHVGV EILTPLFGTL HPGFYGSSRE AFTYERRPQS QAYIPKDEGD FYYLGGFFGG SVQEVQRLTR ACHQAMMVDQ ANGIEAVWHD ESHLNKYLLR HKPTKVLSPE YLWDQQLLGW PAVLRKLRFT AVPKNHQAVR NP.
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 :
GNMT Human, ActiveDescription:
Glycine N-Methyltransferase Human Recombinant , Active
Glycine N-methyltransferase, GNMT, Glycine N-Methyltransferase, EC 2.1.1.20Epididymis Secretory Sperm Binding Protein Li 182mP, HEL-S-182mP.
Product # :
ENZ-1059Price :
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Description
GNMT Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 315 amino acids (1-295 a.a) and having a molecular mass of 34.9kDa.GNMT is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
GNMT protein solution (1mg/ml) containing 20 mM Tris-HCl buffer (pH 8.0) and 20% glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Biological Activity
Specific activity is > 100 nmol/min/mg, and is defined as the amount of enzyme that transfer 1.0 nmole of methyl group per minute at 37C.
More Info
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Introduction
GNMT is an enzyme that catalyzes the conversion of S-adenosyl-L-methionine with glycine to S-adenosyl-L-homocysteine and sarcosine. GNMT is located in the cytoplasm and acts as a homotetramer. Defects in the GNMT gene causes of GNMT deficiency (hypermethioninemia). GNMT affects DNA methylation by regulating the ratio of S-adenosylmethionine to S-adenosylhomocystine and is involved in the detoxification pathway in liver cells. GNMT expression is diminished in human hepatocellular carcinoma (HCC). GNMT catalyzes the methylation of glycine by using s- adenosylmethionine (adomet) to form n-methylglycine (sarcosine) with the concomitant production of s-adenosylhomocysteine (adohcy). GNMT plays an essential role in the regulation of tissue concentration of adomet and of metabolism of methionine.
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Synonyms
Glycine N-methyltransferase, GNMT, Glycine N-Methyltransferase, EC 2.1.1.20
Epididymis Secretory Sperm Binding Protein Li 182mP, HEL-S-182mP. -
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 MVDSVYRTRS LGVAAEGLPD QYADGEAARV WQLYIGDTRS RTAEYKAWLL GLLRQHGCQR VLDVACGTGV DSIMLVEEGF SVTSVDASDK MLKYALKERW NRRHEPAFDK WVIEEANWMT LDKDVPQSAE GGFDAVICLG NSFAHLPDCK GDQSEHRLAL KNIASMVRAG GLLVIDHRNY DHILSTGCAP PGKNIYYKSD LTKDVTTSVL IVNNKAHMVT LDYTVQVPGA GQDGSPGLSK FRLSYYPHCL ASFTELLQAA FGGKCQHSVL GDFKPYKPGQ TYIPCYFIHV LKRTD.
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 :
NMNAT2 HumanDescription:
Nicotinamide Nucleotide Adenylyltransferase 2 Human Recombinant
Nicotinamide Nucleotide Adenylyltransferase 2, C1orf15, Nicotinate-Nucleotide Adenylyltransferase 2, NaMN Adenylyltransferase 2, NMN Adenylyltransferase 2, PNAT2, KIAA0479, Chromosome 1 Open Reading Frame 15, Nicotinamide Mononucleotide Adenylyltransferase 2, Pyridine Nucleotide Adenylyltransferase 2, EC 2.7.7.1, EC 2.7.7.18.
Product # :
ENZ-509Price :
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Description
NMNAT2 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 327 amino acids (1-307 a.a) and having a molecular mass of 36.6kDa.NMNAT2 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
NMNAT2 protein solution (0.25mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 20% glycerol and 1mM DTT.
Purity
Greater than 85.0% as determined by SDS-PAGE.
Biological Activity
Specific activity: > 500 pmol/min/ug. One unit will convert 1.0 pmole of beta-NADH per minute to beta-NAD at PH 8.0 at 37°C.More Info
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Introduction
Nicotinamide Nucleotide Adenylyltransferase 2, also known as NMNAT2 is a member of the nicotinamide mononucleotide adenylyltransferase (NMNAT) enzyme family, members of which catalyze a vital step in NAD (NADP) biosynthetic pathway. Unlike the other human family member, which is localized to the nucleus, and is ubiquitously expressed; NMNAT2 is cytoplasmic, and is predominantly expressed in the brain. Two transcript variants encoding different isoforms have been found for NMNAT2. Among the diseases associated with NMNAT2 are tauopathy, and systemic lupus erythematosus.
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Synonyms
Nicotinamide Nucleotide Adenylyltransferase 2, C1orf15, Nicotinate-Nucleotide Adenylyltransferase 2, NaMN Adenylyltransferase 2, NMN Adenylyltransferase 2, PNAT2, KIAA0479, Chromosome 1 Open Reading Frame 15, Nicotinamide Mononucleotide Adenylyltransferase 2, Pyridine Nucleotide Adenylyltransferase 2, EC 2.7.7.1, EC 2.7.7.18.
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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).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MTETTKTHVI LLACGSFNPI TKGHIQMFER ARDYLHKTGR FIVIGGIVSP VHDSYGKQGL VSSRHRLIMC QLAVQNSDWI RVDPWECYQD TWQTTCSVLE HHRDLMKRVT GCILSNVNTP SMTPVIGQPQ NETPQPIYQN SNVATKPTAA KILGKVGESL SRICCVRPPV ERFTFVDENA NLGTVMRYEE IELRILLLCG SDLLESFCIP GLWNEADMEV IVGDFGIVVV PRDAADTDRI MNHSSILRKY KNNIMVVKDD INHPMSVVSS TKSRLALQHG DGHVVDYLSQ PVIDYILKSQ LYINASG
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 :
L-AsparaginaseDescription:
L-Asparaginase
Product # :
ENZ-287Price :
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Description
L-asparaginase was purified from E.coli ASI.357.
Source
Escherichia Coli.
Formulation
The enzyme was lyophilized with no additives.
Purity
Greater than 96.0% as determined by SDS-PAGE.
Biological Activity
One IU of L- Asparaginase is defined as that amount of enzyme required to generate 1 µmol of ammonia per minute at pH 7.3 and 37°C.
More Info
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Introduction
L-Asparaginase is an enzyme that depletes L-Asparagine "an important nutrient for cancer cells" resulting in cancer/tumor cell starvation. L-asparaginase is an anti-tumor agent derived from E.coli.,which can inhibit the growth of malignant cells. It is used mainly for the induction of remission in acute lymphoblastic leukaemia. Because of the lymph node origin of malignant B cells in Multiple Myeloma, L-Asparagine is an essential amino acid for their cell metabolism, and, consequently, L-Asparaginase may be of value in managing the disease.
The rationale behind asparaginase is that it takes advantage of the fact that ALL cellsare unable to synthesize the non-essential amino acidasparaginewhereas normal cells are able to make their own asparagine. These leukemic cells depend on circulating asparagine. Asparaginase however catalyzes the conversion of L-asparagine to aspartic acidand ammonia. This deprives the leukemic cell of circulating asparagine. -
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized L-Asparaginase although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution L-Asparaginase should be stored at 4°C between 2-7 days and for future use below -18°C. Please prevent freeze-thaw cycles.
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Solubility
It is recommended to reconstitute the lyophilized L-Asparaginase in 18M-cm H2O at 1mg/ml.
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Background
L-Asparaginase Enzyme: Unraveling Its Therapeutic Potential in Cancer Treatment
Abstract: L-Asparaginase is an enzyme that plays a crucial role in cancer therapy by depleting the levels of asparagine in the blood, thereby inhibiting the growth of cancer cells.
This research paper provides a comprehensive analysis of L-Asparaginase, including its biochemical properties, mechanisms of action, therapeutic applications, and clinical implications.
The paper explores the significance of L-Asparaginase as a key enzyme in cancer treatment and highlights its potential for improving patient outcomes.
- Introduction L-Asparaginase is an enzyme widely used in cancer therapy, particularly in the treatment of acute lymphoblastic leukemia (ALL). This section introduces L-Asparaginase and its role in cancer treatment, emphasizing its importance in medical research and clinical practice.
- Biochemical Properties of L-Asparaginase L-Asparaginase belongs to the class of enzymes known as hydrolases and catalyzes the hydrolysis of asparagine to aspartic acid and ammonia. This section discusses the biochemical properties of L-Asparaginase, including its structure, catalytic mechanism, and factors influencing its activity and stability.
- Mechanisms of Action L-Asparaginase exerts its anti-cancer effects by depleting circulating asparagine, an essential amino acid for cancer cell survival. This section delves into the mechanisms of action of L-Asparaginase, including its ability to selectively target cancer cells and induce metabolic stress, leading to cell death. The impact of asparagine deprivation on cancer cell metabolism and survival is also explored.
- Therapeutic Applications of L-Asparaginase L-Asparaginase has demonstrated therapeutic efficacy in the treatment of various malignancies, including ALL and certain solid tumors. This section provides an overview of the therapeutic applications of L-Asparaginase, highlighting its use as a first-line treatment in ALL and its potential in other cancer types. The challenges and limitations associated with L-Asparaginase therapy are also discussed.
- Clinical Implications and Future Perspectives L-Asparaginase therapy has shown promising results in improving patient outcomes, but it is not without side effects and challenges. This section discusses the clinical implications of L-Asparaginase treatment, including its impact on patient survival, toxicity profile, and the development of resistance. Additionally, the future prospects of L-Asparaginase therapy, such as the development of novel formulations and combination strategies, are explored.
- Conclusion L-Asparaginase is a vital enzyme in cancer treatment, particularly in the management of ALL. This research paper has provided a comprehensive analysis of L-Asparaginase, highlighting its biochemical properties, mechanisms of action, therapeutic applications, and clinical implications. Further research on L-Asparaginase and its optimization in cancer therapy will enhance our understanding and pave the way for improved treatments.
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Unit Definition
One unit of enzyme catalyzes hydrolyzation of 10 nanomoles of dUTP to dUMP in one hour at 85 Centigrade.
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Specific Activity
250IU/mg.
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 :
MMAB HumanDescription:
Methylmalonic Aciduria Type B Human Recombinant
CBIB, Cob(I)alamin adenosyltransferase, EC 2.5.1.17.
Product # :
ENZ-248Price :
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Description
MMAB Recombinant Human produced in E.Coli is a single, non-glycosylated polypeptide chain containing 239 amino acids (33-250 a.a.) and having a molecular mass of 26.3 kDa. The MMAB is fused to 21 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
MMAB 1mg/ml protein solution contains 20mM Tris pH-7.5 & 10% glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
MMAB protein catalyzes the last step in the conversion of vitamin B(12) into adenosylcobalamin (AdoCbl), a vitamin B12 containing coenzyme for methylmalonyl-CoA mutase(MCM). Decreased MMAB activity leads to the inherited disorder vitamin B12 dependent methylmalonic aciduria linked to the cblB complementation group.
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Synonyms
CBIB, Cob(I)alamin adenosyltransferase, EC 2.5.1.17.
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Physical Appearance
Sterile Filtered clear solution.
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Stability
MMAB Human 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 MQSRGPQGVE DGDRPQPSSK TPRIPKIYTK TGDKGFSSTF TGERRPKDDQ VFEAVGTTDE LSSAIGFALE LVTEKGHTFA EELQKIQCTL QDVGSALATP CSSAREAHLK YTTFKAGPIL ELEQWIDKYT SQLPPLTAFI LPSGGKISSA LHFCRAVCRR AERRVVPLVQ MGETDANVAK FLNRLSDYLF TLARYAAMKE GNQEKIYKKN DPSAESEGL.
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 :
HRPDescription:
Horseradish Peroxidase
Horseradish Peroxidase, HRP, EC 1.11.1.7.
Product # :
ENZ-321Price :
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Description
HRP consists of the basic isoenzyme having a molecular weight of 44 kDa.The Horseradish Peroxidase is purified by affinity chromatography, which results in an enzyme of high specific activity and purity.
Source
Root extracts of horseradish.
Purity
(A403/A275) = RZ: 3.0.
Biological Activity
276 U/mg (25°C, guaiacol as the hydrogen donor, pH-7 and H2O2 as substrates).
More Info
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Introduction
The enzyme horseradish peroxidase, found in horseradish, is used extensively in molecular biologyand in antibody amplification and detection, among other things. For example, "In recent years the technique of marking neurons with the enzyme horseradish peroxidase (HRP) has become a major tool. In its brief history, this method has probably been used by more neurobiologists than have used the Golgi stainsince its discovery in 1870." Horseradish peroxidase is also highly used in techniques such as Western blottingand ELISAs.
HRP is widely used as an enzymatic label in immunoassays. Usually, the enzyme is coupled to antibodies, lectins or haptens. Coupling to antibodies etc. may be performed through the carbohydrate side chains of the HRP. -
Synonyms
Horseradish Peroxidase, HRP, EC 1.11.1.7.
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Physical Appearance
Sterile Filtered red-brown lyophilized powder.
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Stability
Lyophilized HRP although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution HRP should be stored at 4°C between 2-7 days and for future use below -18°C.Please prevent freeze-thaw cycles.
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Solubility
It is recommended to reconstitute the lyophilized HRP in sterile 18MΩ-cm H2O not less than 100 µg/ml.
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 :
DsbCDescription:
Disulfide-Bond Isomerase Recombinant
Disulfide-bond isomerase C, dsbC, xprA, Disulfide-bond isomerase (DsbC) E.Coli, Thiol:disulfide interchange protein dsbC, Disulfide-bond isomerase C Thiol:disulfide interchange protein dsbC .
Product # :
ENZ-291Price :
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Description
Disulfide-Bond Isomerase Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 217 amino acids (21-236) and having a molecular mass of 23.6 kDa.DsbC is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
1 mg/ml solution containing 20mM Tris-HCl buffer pH 7.5 and 2mM EDTA.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
Dsb proteins (DsbA, DsbB, DsbC, and DsbD) catalyze formation and isomerization of protein disulfide bonds in the periplasm of Escherichia coli. DsbC is periplasmic enzyme known as a disulfide isomerase and can convert aberrant disulfide bonds to correct ones.
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Synonyms
Disulfide-bond isomerase C, dsbC, xprA, Disulfide-bond isomerase (DsbC) E.Coli, Thiol:disulfide interchange protein dsbC, Disulfide-bond isomerase C Thiol:disulfide interchange protein dsbC .
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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
MDDAAIQQTL AKMGIKSSDI QPAPVAGMKT VLTNSGVLYI TDDGKHIIQG PMYDVSGTAP VNVTNKMLLK QLNALEKEMI VYKAPQEKHV ITVFTDITCG YCHKLHEQMA DYNALGITVR YLAFPRQGLD SDAEKEMKAI WCAKDKNKAF DDVMAGKSVA PASCDVDIAD HYALGVQLGV SGTPAVVLSN GTLVPGYQPP KEMKEFLDEH QKMTSGK.
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 :
SMUG1 HumanDescription:
Single-Strand-Selective Monofunctional Uracil-DNA Glycosylase 1 Human Recombinant
Single-strand selective monofunctional uracil DNA glycosylase, SMUG1, FDG, UNG3, HMUDG.
Product # :
ENZ-674Price :
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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
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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).
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Synonyms
Single-strand selective monofunctional uracil DNA glycosylase, SMUG1, FDG, UNG3, HMUDG.
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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 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.
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Name :
ENO2 HumanDescription:
Enolase-2 Human Recombinant
Gamma-enolase, EC 4.2.1.11, 2-phospho-D-glycerate hydro-lyase, Neural enolase, Neuron-specific enolase, NSE, Enolase 2, ENO2.
Product # :
ENZ-324Price :
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- sds-page
Description
ENO2 Human Recombinant expressed in E. coli contains 434 amino acids and its Mw is 47 kDa. The Enolase-2 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
ENO2 is supplied in 20mM Tris pH-7.5, 0.1M KCl, 5mM MgSO4.
Purity
Greater than 95% as determined by SDS-PAGE.
Biological Activity
> 25,000 pmol/min/ug, determined by the decrease of NAD in absorbance at 340nm resulting from NADH at pH 6.5 at 37C.sds-page
More Info
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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.
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Synonyms
Gamma-enolase, EC 4.2.1.11, 2-phospho-D-glycerate hydro-lyase, Neural enolase, Neuron-specific enolase, NSE, Enolase 2, ENO2.
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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 1-2 weeks. Store, frozen at -20°C for longer periods of time. Please prevent freeze-thaw cycles.
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Amino Acid Sequence
MSIEKIWARE ILDSRGNPTV EVDLYTAKGL FRAAVPSGAS TGIYEALELR DGDKQRYLGK GVLKAVDHIN STIAPALISS GLSVVEQEKL DNLMLELDGT ENKSKFGANA ILGVSLAVCK AGAAERELPL YRHIAQLAGN SDLILPVPAF NVINGGSHAG NKLAMQEFMI LPVGAESFRD AMRLGAEVYH TLKGVIKDKY GKDATNVGDE GGFAPNILEN SEALELVKEA IDKAGYTEKI VIGMDVAASE FYRDGKYDLD FKSPTDPSRY ITGDQLGALY QDFVRDYPVV SIEDPFDQDD WAAWSKFTAN VGIQIVGDDL TVTNPKRIER AVEEKACNCL LLKVNQIGSV TEAIQACKLA QENGWGVMVS HRSGETEDTF IADLVVGLCT GQIKTGAPCR SERLAKYNQL MRIEEELGDE ARFAGHNFRN PSVL.
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 :
PAICS HumanDescription:
Phosphoribosylaminoimidazole Carboxylase Human Recombinant
PAICS, Phosphoribosylaminoimidazole Carboxylase Phosphoribosylaminoimidazole, Succinocarboxamide Synthetase, PAIS, AIRC, ADE2, ADE2H1, AIR Carboxylase, Multifunctional Protein ADE2, Multifunctional Protein ADE2H1, SAICAR Synthetase.
Product # :
ENZ-786Price :
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Description
PAICS Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 448 amino acids (1-425) and having a molecular mass of 49.5kDa.PAICS is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
The PAICS solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH8.0), 20% glycerol, 0.1M NaCl and 1mM DTT.
Purity
Greater than 90% as determined by SDS-PAGE.
More Info
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Introduction
Phosphoribosylaminoimidazole Carboxylase (PAICS) is an enzyme involved in nucleotide biosynthesis and particularly in purine biosynthesis. PAICS is a bifunctional enzyme containing phosphoribosylaminoimidazole carboxylase activity at its N-terminal region and phosphoribosylaminoimidazole succinocarboxamide synthetase at its C-terminal region. PAICS catalyzes the conversion of 5'-phosphoribosyl-5-aminoimidazole(AIR) into 5'-phosphoribosyl-4-carboxy-5-aminoimidazole (CAIR) as described in the reaction. PAICS catalyzes steps six and seven of purine biosynthesis.
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Synonyms
PAICS, Phosphoribosylaminoimidazole Carboxylase Phosphoribosylaminoimidazole, Succinocarboxamide Synthetase, PAIS, AIRC, ADE2, ADE2H1, AIR Carboxylase, Multifunctional Protein ADE2, Multifunctional Protein ADE2H1, SAICAR Synthetase.
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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 MGSMATAEVL NIGKKLYEGK TKEVYELLDS PGKVLLQSKD QITAGNAARK NHLEGKAAIS NKITSCIFQL LQEAGIKTAF TRKCGETAFI APQCEMIPIE WVCRRIATGS FLKRNPGVKE GYKFYPPKVE LFFKDDANND PQWSEEQLIA AKFCFAGLLI GQTEVDIMSH ATQAIFEILE KSWLPQNCTL VDMKIEFGVD VTTKEIVLAD VIDNDSWRLW PSGDRSQQKD KQSYRDLKEV TPEGLQMVKK NFEWVAERVE LLLKSESQCR VVVLMGSTSD LGHCEKIKKA CGNFGIPCEL RVTSAHKGPD ETLRIKAEYE GDGIPTVFVA VAGRSNGLGP VMSGNTAYPV ISCPPLTPDW GVQDVWSSLR LPSGLGCSTV LSPEGSAQFA AQIFGLSNHL VWSKLRASIL NTWISLKQAD KKIRECNL.
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 :
CA1 HumanDescription:
Carbonic Anhydrase-1 Human Recombinant
CA-1, CA1, CAI, CA-I, Carbonate dehydratase I, Carbonic anhydrase I, Carbonic anhydrase 1, Car1.
Product # :
ENZ-462Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
Recombinant Human Carbonic anhydrase 1 produced in E.Coli is a single, non-glycosylated polypeptide chain containing 281 amino acids (1-261 a.a) and having a molecular mass of 31 kDa. Carbonic anhydrase 1 is fused to a 20 amino acids His-Tag at N-terminus and purified by conventional chromatography techniques.
Source
Escherichia Coli.
Formulation
The Carbonic Anhydrase-1 protein solution contains 20mM Tris-HCl, pH-8, 1mM DTT and 10% Glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
Carbonic anhydrase 1 is a zinc metalloenzyme that catalyses reversible hydration of CO2 (CO2 + H2O ? HCO3- + H+). Carbonic anhydrase 1 is essential to many biological processes such as cellular respiration, calcification, acid-base balance, bone resorption, and the formation of aqueous humor, cerebrospinal fluid, salvia, and gastric acid. Carbonic anhydrase 1 is abundant in erythrocytes and an early marker for erythroid differentiation.
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Synonyms
CA-1, CA1, CAI, CA-I, Carbonate dehydratase I, Carbonic anhydrase I, Carbonic anhydrase 1, Car1.
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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 MASPDWGYDD KNGPEQWSKL YPIANGNNQS PVDIKTSETK HDTSLKPISV SYNPATAKEI INVGHSFHVN FEDNDNRSVL KGGPFSDSYR LFQFHFHWGS TNEHGSEHTV DGVKYSAELH VAHWNSAKYS SLAEAASKAD GLAVIGVLMK VGEANPKLQK VLDALQAIKT KGKRAPFTNF DPSTLLPSSL DFWTYPGSLT HPPLYESVTW IICKESISVS SEQLAQFRSL LSNVEGDNAV PMQHNNRPTQ PLKGRTVRAS F.
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 :
POFUT1 HumanDescription:
Protein O-Fucosyltransferase 1 Human Recombinant
FUT12, O-Fuc-T, O-FucT-1, O-FUT, GDP-fucose protein O-fucosyltransferase 1, Peptide-O-fucosyltraferase 1,KIAA0180.
Product # :
ENZ-679Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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- description
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Description
POFUT1 Human Recombinant produced in E. coli is a single polypeptide chain containing 385 amino acids (27-388) and having a molecular mass of 43.7 kDa. POFUT1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The POFUT1 solution (1mg/1ml) contains 20mM Tris-HCl buffer (pH 8.0), 2M Urea and 10% glycerol.
Purity
Greater than 85.0% as determined by SDS-PAGE.
More Info
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Introduction
GDP-fucose protein O-fucosyltransferase 1 (POUFUT1), belongs to the glycosyltransferase O-Fuc family. POUFUT1 encodes a member of the glycosyltransferase O-Fuc family and Expressed mainly in pancreas, kidney, lung, heart, brain, liver, placenta and skeletal muscle.POUFUT1 adds O-fucose through an O-glycosidic linkage to Preserve serine or threonine residues in the epidermal growth factor-like repeats of a number of cell surface and emitted proteins. POUFUT1 is involved in ligand-induced receptor signaling. Alternative splicing of this gene results in 2 transcript variants encoding different isoforms.POFUT1 participates in Notch signaling, as Notch ligands can use as POFUT1 substrates.
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Synonyms
FUT12, O-Fuc-T, O-FucT-1, O-FUT, GDP-fucose protein O-fucosyltransferase 1, Peptide-O-fucosyltraferase 1,KIAA0180.
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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 MGSGSWDPAG YLLYCPCMGR FGNQADHFLG SLAFAKLLNR TLAVPPWIEY QHHKPPFTNL HVSYQKYFKL EPLQAYHRVI SLEDFMEKLA PTHWPPEKRV AYCFEVAAQR SPDKKTCPMK EGNPFGPFWD QFHVSFNKSE LFTGISFSAS YREQWSQRFS PKEHPVLALP GAPAQFPVLE EHRPLQKYMV WSDEMVKTGE AQIHAHLVRP YVGIHLRIGS DWKNACAMLK DGTAGSHFMA SPQCVGYSRS TAAPLTMTMC LPDLKEIQRA VKLWVRSLDA QSVYVATDSE SYVPELQQLF KGKVKVVSLK PEVAQVDLYI LGQADHFIGN CVSSFTAFVK RERDLQGRPS SFFGMDRPPK LRDEF.
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 :
PNPO HumanDescription:
Pyridoxamine 5'-Phosphate Oxidase Human Recombinant
Pyridoxine-5'-phosphate oxidase, Pyridoxamine-phosphate oxidase, PNPO, PDXPO, FLJ10535.
Product # :
ENZ-030Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
PNPO Human Recombinant fused with a 21 amino acid His tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 226 amino acids (57-261 a.a.) and having a molecular mass of 25.9kDa. The PNPO is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The PNPO solution (0.5 mg/ml) contains 20mM Tris-HCl buffer (pH8.0), 10% glycerol, 0.1M NaCl and 0.1mM PMSF.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
Pyridoxine-5'-phosphate oxidase (PNPO) is the rate-limiting enzyme in vitamin B6 synthesis. Vitamin B6 (Pyridoxal 5-prime-phosphate or PLP) is vital for normal cellular function, and some cancer cells have notable differences in vitamin B6 metabolism compared to their normal counterparts.Vitamin B6 is an essential co-factor for enzymes involved in both homocysteine metabolism and synthesis of neurotransmitters such as catecholamine. Mutations in the PNPO gene result in PNPO deficiency, a form of neonatal epileptic encephalopathy.
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Synonyms
Pyridoxine-5'-phosphate oxidase, Pyridoxamine-phosphate oxidase, PNPO, PDXPO, FLJ10535.
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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 MDPVKQFAAW FEEAVQCPDI GEANAMCLAT CTRDGKPSAR MLLLKGFGKD GFRFFTNFES RKGKELDSNP FASLVFYWEP LNRQVRVEGP VKKLPEEEAE CYFHSRPKSS QIGAVVSHQS SVIPDREYLR KKNEELEQLY QDQEVPKPKS WGGYVLYPQV MEFWQGQTNR LHDRIVFRRG LPTGDSPLGP MTHRGEEDWL YERLAP.
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 :
CA12 HumanDescription:
Carbonic Anhydrase XII Human Recombinant
Carbonic anhydrase 12, Carbonate dehydratase XII, Carbonic anhydrase XII, CA-XII, Tumor antigen HOM-RCC-3.1.3, CA12, Carbonic Anhydrase XII, Carbonic anhydrase 12 isoform 1, CAXII, HsT18816.
Product # :
ENZ-886Price :
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Shipping Method :
Shipped with Ice Packs
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Description
CA12 Human Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 283 amino acids (25-301a.a.) and having a molecular mass of 31.94kDa (Migrates at 28-40kDa on SDS-PAGE under reducing conditions).CA12 is fused to a 6 amino acid His-tag at C-terminus & purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
CA12 protein solution (0.5mg/ml) containing Phosphate Buffer Saline (pH7.4) and 10% glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
Biological Activity
Specific activity is > 300 pmol/min/ug, and is defined as the amount of enzyme that hydrolyze 1.0 pmole of 4-nitrophenyl acetate to 4-nitrophenol per minute at pH 7.5 at 37C.More Info
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Introduction
Carbonic anhydrase 12 (CA12) is an enzyme that belongs to the Carbonic anhydrases (CAs) family. This is a large family of zinc metalloenzymes which catalyze the reversible hydration of carbon dioxide. They are involved in various biological processes, including respiration, calcification, acid-base balance, bone resorption, and the formation of aqueous humor, cerebrospinal fluid, saliva, and gastric acid. CA12 is a type I membrane protein which is highly expressed in normal tissues, such as the kidney, colon and pancreas, and is overexpressed in 10% of clear cell renal carcinomas.
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Synonyms
Carbonic anhydrase 12, Carbonate dehydratase XII, Carbonic anhydrase XII, CA-XII, Tumor antigen HOM-RCC-3.1.3, CA12, Carbonic Anhydrase XII, Carbonic anhydrase 12 isoform 1, CAXII, HsT18816.
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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).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
APVNGSKWTY FGPDGENSWS KKYPSCGGLL QSPIDLHSDI LQYDASLTPL EFQGYNLSAN KQFLLTNNGH SVKLNLPSDM HIQGLQSRYS ATQLHLHWGN PNDPHGSEHT VSGQHFAAEL HIVHYNSDLY PDASTASNKS EGLAVLAVLI EMGSFNPSYD KIFSHLQHVK YKGQEAFVPG FNIEELLPER TAEYYRYRGS LTTPPCNPTV LWTVFRNPVQ ISQEQLLALE TALYCTHMDD PSPREMINNF RQVQKFDERL VYTSFSQVQV CTAAGLSHHH HHH.
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 :
GPX3 HumanDescription:
Glutathione Peroxidase 3 Human Recombinant
Glutathione peroxidase 3, GPx-3, GSHPx-3, Extracellular glutathione peroxidase, Plasma glutathione peroxidase, GPx-P, GSHPx-P, GPX3, GPXP.
Product # :
ENZ-579Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
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- formulation
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Description
GPX3 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 227 amino acids (21-226) and having a molecular mass of 25.7kDa.GPX3 is fused to a 21 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The GPX3 solution contains 20mM Tris-HCl buffer (pH7.5), 40% glycerol, 0.15M NaCl and 1mM DTT.
Purity
Greater than 85% as determined by SDS-PAGE.
More Info
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Introduction
Glutathione peroxidase 3 (GPX3) is a member of the glutathione peroxidase family, which acts in the detoxification of hydrogen peroxide. GPX3 shields cells and enzymes from oxidative damage, by catalyzing the reduction of hydrogen peroxide, lipid peroxides and organic hydroperoxide, by glutathione. The GPX3 protein is one of only a few 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.
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Synonyms
Glutathione peroxidase 3, GPx-3, GSHPx-3, Extracellular glutathione peroxidase, Plasma glutathione peroxidase, GPx-P, GSHPx-P, GPX3, GPXP.
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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 MQSRGQEKSK MDCHGGISGT IYEYGALTID GEEYIPFKQY AGKYVLFVNV ASYCGLTGQY IELNALQEEL APFGLVILGF PCNQFGKQEP GENSEILPTL KYVRPGGGFV PNFQLFEKGD VNGEKEQKFY TFLKNSCPPT SELLGTSDRL FWEPMKVHDI RWNFEKFLVG PDGIPIMRWH HRTTVSNVKM DILSYMRRQA ALGVKRK.
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.