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655 results found for “superoxide dismutase”
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Name :
ANSA E.coliDescription:
Cytoplasmic L-asparaginase I E.Coli Recombinant
L-asparaginase 1, L-asparaginase I, L-ASNase I, L-asparagine amidohydrolase I, ansA, b1767, JW1756.
Product # :
ENZ-119Price :
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Description
ANSA produced in E.Coli is a single, non-glycosylated polypeptide chain containing 358 amino acids (1-338 a.a.) and having a molecular mass of 39.3kDa.ANSA is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The ANSA solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 10% glycerol and 2mM DTT.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
AnsA is a cytoplasmic asparaginase from E.coli involved in intracellular asparagine utilization. E.coli has 2 L-asparaginases: the cytoplasmic type I form (ansA) and the periplasmic type II form (ansB). AnsA (Type L asparaginase) is constitutively expressed and is obligatory for the growth of the bacteria on asparagine as the sole nitrogen source.
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Synonyms
L-asparaginase 1, L-asparaginase I, L-ASNase I, L-asparagine amidohydrolase I, ansA, b1767, JW1756.
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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 MQKKSIYVAY TGGTIGMQRS EQGYIPVSGH LQRQLALMPE FHRPEMPDFT IHEYTPLMDS SDMTPEDWQH IAEDIKAHYD DYDGFVILHG TDTMAYTASA LSFMLENLGK PVIVTGSQIP LAELRSDGQI NLLNALYVAA NYPINEVTLF FNNRLYRGNR TTKAHADGFD AFASPNLPPL LEAGIHIRRL NTPPAPHGEG ELIVHPITPQ PIGVVTIYPG ISADVVRNFL RQPVKALILR SYGVGNAPQN KAFLQELQEA SDRGIVVVNL TQCMSGKVNM GGYATGNALA HAGVIGGADM TVEATLTKLH YLLSQELDTE TIRKAMSQNL RGELTPDD.
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 :
NDUFAF1 HumanDescription:
NADH Dehydrogenase 1 Alpha Subcomplex, Assembly Factor 1 Human Recombinant
Complex I intermediate-associated protein 30, mitochondrial, NADH dehydrogenase [ubiquinone] 1 alpha subcomplex assembly factor 1, NDUFAF1, CIA30, CGI-65, CGI65.
Product # :
ENZ-661Price :
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Description
NDUFAF1 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 326 amino acids (25-327) and having a molecular mass of 37kDa.NDUFAF1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The NDUFAF1 solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 10% glycerol and 1mM DTT.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
NADH dehydrogenase [ubiquinone] 1 alpha subcomplex assembly factor 4 (NDUFAF4) is involved in the compilation of mitochondrial NADH: ubiquinone oxidoreductase complex (complex I). In addition, NDUFAF4 is involved in cell proliferation and survival of hormone-dependent tumor cells. NDUFAF4 may also be a regulator of breast tumor cell invasion. NDUFAF4 gene mutations cause the mitochondrial complex I deficiency.
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Synonyms
Complex I intermediate-associated protein 30, mitochondrial, NADH dehydrogenase [ubiquinone] 1 alpha subcomplex assembly factor 1, NDUFAF1, CIA30, CGI-65, CGI65.
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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 MGSYPFLGIR FAEYSSSLQK PVASPGKASS QRKTEGDLQG DHQKEVALDI TSSEEKPDVS FDKAIRDEAI YHFRLLKDEI VDHWRGPEGH PLHEVLLEQA KVVWQFRGKE DLDKWTVTSD KTIGGRSEVF LKMGKNNQSA LLYGTLSSEA PQDGESTRSG YCAMISRIPR GAFERKMSYD WSQFNTLYLR VRGDGRPWMV NIKEDTDFFQ RTNQMYSYFM FTRGGPYWQE VKIPFSKFFF SNRGRIRDVQ HELPLDKISS IGFTLADKVD GPFFLEIDFI GVFTDPAHTE EFAYENSPEL NPRLFK.
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 :
ATOX1 HumanDescription:
Copper Transport Protein ATOX1 Human Recombinant
Antioxidant protein 1, ATX1, HAH1, Copper transport protein ATOX1, Metal transport protein ATX1, ATOX1, MGC138453, MGC138455.
Product # :
PRO-754Price :
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Description
ATOX1 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 88 amino acids (1-68 a.a.) and having a molecular mass of 9.5kDa. ATOX1 is fused to a 20 amino acid His Tag at N-terminus and purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
ATOX1 solution containing 20mM Tris pH-8, 1mM DTT and 10% glycerol.
Purity
Greater than 95% as determined by SDS-PAGE.
More Info
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Introduction
ATOX1 is a metal transport protein that is part of the ATX1 family. ATOX1 is a copper chaperone that takes part in cellular antioxidant defense and can bind and deliver cytosolic copper to the copper ATPase proteins in the trans-Golgi network for later incorporation to the ceruloplasmin. ATOX1 plays a role as an antioxidant against superoxide and hydrogen peroxide, and consequently, takes an important part in cancer carcinogenesis. Because of ATOX1 cytogenetic location, the gene can be a good a candidate gene for 5q-syndrome.
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Synonyms
Antioxidant protein 1, ATX1, HAH1, Copper transport protein ATOX1, Metal transport protein ATX1, ATOX1, MGC138453, MGC138455.
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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).Please prevent freeze thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MPKHEFSVDM TCGGCAEAVS RVLNKLGGVK YDIDLPNKKV CIESEHSMDT LLATLKKTGK TVSYLGLE.
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 :
IMPA1 HumanDescription:
Inositol Monophosphatase 1 Human Recombinant
Inositol monophosphatase 1, IMP 1, IMPase 1, Inositol-1(or 4)-monophosphatase 1, Lithium-sensitive myo-inositol monophosphatase A1, IMPA1, IMPA, IMP.
Product # :
ENZ-006Price :
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Description
IMPA1 Human Recombinant fused with a 20 amino acid His tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 297 amino acids (1-277 a.a.) and having a molecular mass of 32.3kDa. The IMPA1 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The IMPA1 solution (1mg/ml) contains 20mM Tris-HCl Buffer (pH 8.0) and 10% Glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
Inositol monophosphatase1 (IMPA1) is responsible for the provision of inositol essential for synthesis of phosphatidylinositol and polyphosphoinositides. IMPA1 has a central role in the phosphatidylinositol signaling pathway by catalyzing the hydrolysis of inositol monophosphates. IMPA1 has been recognized as the pharmacological target for lithium action in the brain. The IMPA1 enzyme has a magnesium-dependent phosphatase activity and is inhibited by therapeutic concentrations of lithium. Inhibition of inositol monophosphate hydroylosis and ensuing depletion of inositol for phosphatidylinositol synthesis may perhaps explain the anti-manic and anti-depressive effects of lithium administered to treat bipolar disorder.
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Synonyms
Inositol monophosphatase 1, IMP 1, IMPase 1, Inositol-1(or 4)-monophosphatase 1, Lithium-sensitive myo-inositol monophosphatase A1, IMPA1, IMPA, IMP.
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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 MADPWQECMD YAVTLARQAG EVVCEAIKNE MNVMLKSSPV DLVTATDQKV EKMLISSIKE KYPSHSFIGE ESVAAGEKSI LTDNPTWIID PIDGTTNFVH RFPFVAVSIG FAVNKKIEFG VVYSCVEGKM YTARKGKGAF CNGQKLQVSQ QEDITKSLLV TELGSSRTPE TVRMVLSNME KLFCIPVHGI RSVGTAAVNM CLVATGGADA YYEMGIHCWD VAGAGIIVTE AGGVLMDVTG GPFDLMSRRV IAANNRILAE RIAKEIQVIP LQRDDED.
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 :
LDHA HumanDescription:
Lactate Dehydrogenase A Human Recombinant
LDH-A, GSD11, LDH1, LDHM, PIG19, EC 1.1.1.27, lactate dehydrogenase M, LDH-M, LDH-1, L-lactate dehydrogenase A chain, LDH muscle subunit, Renal carcinoma antigen NY-REN-59, Cell proliferation-inducing gene 19 protein, LDHA.
Product # :
ENZ-491Price :
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Description
LDHA Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 352 amino acids (1-332 a.a.) and having a molecular mass of 38.8 kDa. The LDHA is fused to a 20 amino acid his tag at N-terminus and purified by conventional chromatography.
Source
Escherichia Coli.
Formulation
The LDHA protein solution (0.5mg/ml) contains 20mM Tris-HCl pH-8.0, 100mM NaCl and 20% glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Biological Activity
Specific activity is > 20 units/mg. in which one unit will convert 1.0 umole of pyruvate to L-lactate and beta-NAD per minute at pH 7.5 at 37°C.More Info
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Introduction
LDHA catalyzes the conversion of L-lactate and NAD to pyruvate and NADH in the final step of anaerobic glycolysis. LDHA is localized primarily in muscle tissue and is part of the lactate dehydrogenase family. Mutations in LDHA have been linked to exertional myoglobinuria. LDH1 is decreased in essential thrombocythemia. LDHA is induced through a non-genomic pathway of estrogen action. Reduction in LDH-A activity results in stimulation of mitochondrial respiration and decrease of mitochondrial membrane potential.
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Synonyms
LDH-A, GSD11, LDH1, LDHM, PIG19, EC 1.1.1.27, lactate dehydrogenase M, LDH-M, LDH-1, L-lactate dehydrogenase A chain, LDH muscle subunit, Renal carcinoma antigen NY-REN-59, Cell proliferation-inducing gene 19 protein, LDHA.
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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 MATLKDQLIY NLLKEEQTPQ NKITVVGVGA VGMACAISIL MKDLADELAL VDVIEDKLKG EMMDLQHGSL FLRTPKIVSG KDYNVTANSK LVIITAGARQ QEGESRLNLV QRNVNIFKFI IPNVVKYSPN CKLLIVSNPV DILTYVAWKI SGFPKNRVIG SGCNLDSARF RYLMGERLGV HPLSCHGWVL GEHGDSSVPV WSGMNVAGVS LKTLHPDLGT DKDKEQWKEV HKQVVESAYE VIKLKGYTSW AIGLSVADLA ESIMKNLRRV HPVSTMIKGL YGIKDDVFLS VPCILGQNGI SDLVKVTLTS EEEARLKKSA DTLWGIQKEL QF.
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 :
GSTP2 MouseDescription:
Glutathione S-Transferase pi 2 Mouse Recombinant
Glutathione S-transferase P 2, Gst P2, GST YF-YF, GST class-pi, GST-piA.
Product # :
ENZ-943Price :
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Description
GSTP2 Mouse Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 210 amino acids (1-210 a.a.) and having a molecular mass of 23.5kDa. The GSTP2 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The GSTP2 protein solution (0.5mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 20% glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
Gltathione S-transferase PI 2, also known as GSTP2 is multifunctional enzyme which is involved in the protection of cellular components against anti-cancer drugs or peroxidative stress. Furthermore, down regulation of GSTP2 induces an increase of oxidative damage in the pyramidal cells of the CA1&CA3 regions as well as in the granular layer of the dentate gyrus, which at the end leads to structural and functional damage.
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Synonyms
Glutathione S-transferase P 2, Gst P2, GST YF-YF, GST class-pi, GST-piA.
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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
MPPYTIVYFP SPGRCEAMRM LLADQGQSWK EEVVTIDTWM QGLLKPTCLY GQLPKFEDGD LTLYQSNAIL RHLGRSLGLY GKNQREAAQV DMVNDGVEDL RGKYGTMIYR NYENGKNDYV KALPGHLKPF ETLLSQNQGG KAFIVGDQIS FADYNLLDLL LIHQVLAPGC LDNFPLLSAY VARLSARPKI KAFLSSPEHV NRPINGNGKQ.
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 :
CASP3 Human, Sf9Description:
Caspase 3 Apoptosis-Related Cysteine Peptidase Human Recombinant, Sf9
CASP3, CPP32, CPP32B, SCA-1, CASP-3, Apopain, Cysteine protease CPP32, CPP-32, Protein Yama, SREBP cleavage activity 1.
Product # :
ENZ-1106Price :
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Description
CASP3 Human produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 256 amino acids (29-277 a.a.) and having a molecular mass of 29.4kDa (Migrates at 13.5-18kDa on SDS-PAGE under reducing conditions). CASP3 is expressed with a 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
CASP3 protein solution (0.5mg/ml) containing 20mM HEPES buffer (pH 7.5), 0.1M NaCl, 1mM EDTA, 20% Glycerol and 1mM DTT.
Purity
Greater than 90.0% as determined by SDS-PAGE.
Biological Activity
Specific activity is greater than 5,000 pmol/min/ug. One unit will liberate 1 pmoles of Ac-DEVD-AFC to Ac-DEVD and AFC per minute at pH7.5 at 25C.
More Info
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Introduction
Caspase 3 Apoptosis-Related Cysteine Peptidase (CASP3) belongs to the cysteine-aspartic acid protease (caspase) family. Sequential activation of caspases plays a key role in the execution-phase of cell apoptosis. Caspases exist as inactive proenzymes which undergo proteolytic processing at conserved aspartic residues to generate 2 subunits, large and small, that dimerize to create the active enzyme. CASP3 protein cleaves and activates caspases 6, 7 and 9, and the protein itself is processed by caspases 8, 9 and 10. CASP3 is the leading caspase involved in the cleavage of amyloid-beta 4A precursor protein, which is linked with neuronal death in Alzheimer's disease. In addition, CASP3 is involved in the cleavage of huntingtin. CASP3 also cleaves and activates sterol regulatory element binding proteins (SREBPs) between the basic helix-loop-helix leucine zipper domain and the membrane attachment domain. CASP3 initiates cell adhesion in sympathetic neurons through RET cleavage.
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Synonyms
CASP3, CPP32, CPP32B, SCA-1, CASP-3, Apopain, Cysteine protease CPP32, CPP-32, Protein Yama, SREBP cleavage activity 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
MSGISLDNSY KMDYPEMGLC IIINNKNFHK STGMTSRSGT DVDAANLRET FRNLKYEVRN
KNDLTREEIV ELMRDVSKED HSKRSSFVCV LLSHGEEGII FGTNGPVDLK KITNFFRGDR
CRSLTGKPKL FIIQACRGTE LDCGIETDSG VDDDMACHKI PVEADFLYAY STAPGYYSWR
NSKDGSWFIQ SLCAMLKQYA DKLEFMHILT RVNRKVATEF ESFSFDATFH AKKQIPCIVS MLTKELYFYH 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 :
ALDH6A1 HumanDescription:
Aldehyde Dehydrogenase 6 A1 Human Recombinant
MMSADHA, MMSDH , Aldehyde Dehydrogenase 6 Family, Member A1, Methylmalonate-Semialdehyde Dehydrogenase [Acylating], Mitochondrial, Mitochondrial Acylating Methylmalonate-Semialdehyde Dehydrogenase, Malonate-Semialdehyde Dehydrogenase [Acylating], Aldehyde Dehydrogenase Family 6 Member A1, Malonate-Semialdehyde Dehydrogenase, EC 1.2.1.18, EC 1.2.1.27.
Product # :
ENZ-907Price :
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Description
ALDH6A1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 525 amino acids (34-535 a.a) and having a molecular mass of 56.8kDa. ALDH6A1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
ALDH6A1 protein solution (0.25mg/ml) containing Phosphate buffered saline (pH7.4), 10% glycerol and 1mM DTT.
Purity
Greater than 85.0% as determined by SDS-PAGE.
More Info
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Introduction
ALDH6A1 or Methylmalonate-semialdehyde dehydrogenase [acylating], mitochondrial is a mitochondrial methylmalonate semialdehyde dehydrogenase. ALDH6A1 participates in the valine and pyrimidine catabolic pathways. ALDH6A1 catalyzes the irreversible oxidative decarboxylation of malonate, propionyl-CoA and methylmalonate semialdehydes to acetyl. ALDH6A1 deficiency is distinguished by high levels of beta-alanine, 3-hydroxypropionic acid, and the two isomers of 3-amino and 3-hydroxyisobutyric acids in urine organic acids.
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Synonyms
MMSADHA, MMSDH , Aldehyde Dehydrogenase 6 Family, Member A1, Methylmalonate-Semialdehyde Dehydrogenase [Acylating], Mitochondrial, Mitochondrial Acylating Methylmalonate-Semialdehyde Dehydrogenase, Malonate-Semialdehyde Dehydrogenase [Acylating], Aldehyde Dehydrogenase Family 6 Member A1, Malonate-Semialdehyde Dehydrogenase, EC 1.2.1.18, EC 1.2.1.27.
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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 MGSSSSVPTV KLFIGGKFVE SKSDKWIDIH NPATNEVIGR VPQATKAEMD AAIASCKRAF PAWADTSVLS RQQVLLRYQQ LIKENLKEIA KLITLEQGKT LADAEGDVFR GLQVVEHACS VTSLMMGETM PSITKDMDLY SYRLPLGVCA GIAPFNFPAM IPLWMFPMAM VCGNTFLMKP SERVPGATML LAKLLQDSGA PDGTLNIIHG QHEAVNFICD HPDIKAISFV GSNKAGEYIF ERGSRHGKRV QANMGAKNHG VVMPDANKEN TLNQLVGAAF GAAGQRCMAL STAVLVGEAK KWLPELVEHA KNLRVNAGDQ PGADLGPLIT PQAKERVCNL IDSGTKEGAS ILLDGRKIKV KGYENGNFVG PTIISNVKPN MTCYKEEIFG PVLVVLETET LDEAIQIVNN NPYGNGTAIF TTNGATARKY AHLVDVGQVG VNVPIPVPLP MFSFTGSRSS FRGDTNFYGK QGIQFYTQLK TITSQWKEED ATLSSPAVVM PTMGR.
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 :
POR (43-677) HumanDescription:
P450 Oxidoreductase Human Recombinant
P450 (Cytochrome) Oxidoreductase, EC 1.6.2.4, CYPOR, P450R, CPR, NADPH-Dependent Cytochrome P450 Reductase, NADPH--Cytochrome P450 Reductase, NADPH--cytochrome P450 reductase.
Product # :
ENZ-1186Price :
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Description
POR Human Recombinant produced in Sf9 Insect cells is a single, glycosylated, polypeptide chain (43-677 a.a) containing a total of 642 amino acids, having a molecular mass of 73.0 kDa. POR is fused to a 6 amino acid His-tag at C-terminus,and is purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
POR protein solution (0.5mg/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 > 1,500 pmol/min/mg. Defined by the amount of enzyme that reduction of 1 pmole cytochrome-C by NADPH/min. at pH-8 25C.
More Info
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Synonyms
P450 (Cytochrome) Oxidoreductase, EC 1.6.2.4, CYPOR, P450R, CPR, NADPH-Dependent Cytochrome P450 Reductase, NADPH--Cytochrome P450 Reductase, NADPH--cytochrome P450 reductase.
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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
MLFRKKKEEV PEFTKIQTLT SSVRESSFVE KMKKTGRNII VFYGSQTGTA EEFANRLSKD AHRYGMRGMS ADPEEYDLAD LSSLPEIDNA LVVFCMATYG EGDPTDNAQD FYDWLQETDV DLSGVKFAVF GLGNKTYEHF NAMGKYVDKR LEQLGAQRIF ELGLGDDDGN LEEDFITWRE QFWPAVCEHF GVEATGEESS IRQYELVVHT DIDAAKVYMG EMGRLKSYEN QKPPFDAKNP FLAAVTTNRK LNQGTERHLM HLELDISDSK IRYESGDHVA VYPANDSALV NQLGKILGAD LDVVMSLNNL DEESNKKHPF PCPTSYRTAL TYYLDITNPP RTNVLYELAQ YASEPSEQEL LRKMASSSGE GKELYLSWVV EARRHILAIL QDCPSLRPPI DHLCELLPRL QARYYSIASS SKVHPNSVHI CAVVVEYETK AGRINKGVAT NWLRAKEPAG ENGGRALVPM FVRKSQFRLP FKATTPVIMV GPGTGVAPFI GFIQERAWLR QQGKEVGETL LYYGCRRSDE DYLYREELAQ FHRDGALTQL NVAFSREQSH KVYVQHLLKQ DREHLWKLIE GGAHIYVCGD ARNMARDVQN TFYDIVAELG AMEHAQAVDY IKKLMTKGRY SLDVWSHHHH HH.
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Background
P450 Oxidoreductase (POR) is a vital enzyme that plays a crucial role in the electron transfer system, specifically in the cytochrome P450 (CYP) enzyme family. POR acts as an electron donor for various CYP enzymes involved in drug metabolism, steroid biosynthesis, and detoxification processes. This research aims to explore the function, regulation, and significance of POR protein in human cells, shedding light on its role in maintaining cellular homeostasis and drug metabolism.
Function of POR Protein:
POR protein serves as an essential component in the redox reactions of the CYP enzymes. It transfers electrons from NADPH to the CYP enzymes, allowing them to catalyze a wide range of reactions involved in the metabolism of endogenous compounds, drugs, and toxins. Through its electron transfer function, POR enables the activation or inactivation of substrates, contributing to the regulation of cellular processes such as hormone synthesis, drug clearance, and xenobiotic detoxification.
Regulation of POR Protein:
The expression and activity of POR protein are tightly regulated to ensure proper functioning of the CYP enzymes. Several factors influence POR expression, including genetic variations, environmental stimuli, and hormonal signals. Transcriptional regulation of POR involves binding of specific transcription factors to its promoter region. Additionally, post-translational modifications, such as phosphorylation and protein-protein interactions, modulate POR activity, influencing its electron transfer efficiency and interaction with CYP enzymes.
Role of POR Protein in Drug Metabolism:
One of the prominent functions of POR protein is its involvement in drug metabolism. POR collaborates with CYP enzymes in the biotransformation of a wide array of drugs, converting them into more soluble and easily excretable forms. The interplay between POR and CYP enzymes determines the pharmacokinetics and therapeutic efficacy of numerous drugs. Understanding the role of POR in drug metabolism is crucial for predicting drug-drug interactions, optimizing drug dosing, and minimizing the risk of adverse reactions.
Significance of POR Protein in Disease States:
Emerging evidence suggests that POR protein dysregulation can contribute to various disease states. Mutations in the POR gene have been linked to disorders such as Antley-Bixler syndrome and disordered steroidogenesis, highlighting the critical role of POR in development and endocrine function. Moreover, altered POR expression and activity have been implicated in drug resistance and toxicity, as well as in the pathogenesis of certain cancers.
Conclusion:
The investigation of P450 Oxidoreductase (POR) protein in human cells provides valuable insights into its function, regulation, and significance in various physiological and pathological processes. Understanding the interplay between POR and CYP enzymes is essential for deciphering drug metabolism pathways, predicting drug interactions, and developing personalized therapeutic strategies. Further research is warranted to unravel the intricate mechanisms governing POR activity and its potential as a therapeutic target.
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.
- View Data Sheet
Name :
KXD1 HumanDescription:
KxDL Motif Containing 1 Human Recombinant
C19orf50, KXDL, MST096, MSTP096, KXD1.
Product # :
PRO-1656Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
KXD1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 199 amino acids (1-176 a.a.) and having a molecular mass of 22.1kDa.KXD1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
KXD1 protein solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 10% glycerol and 1mM DTT.
Purity
Greater than 85.0% as determined by SDS-PAGE.
More Info
-
Introduction
KxDL Motif Containing 1 (KXD1) is a member of the KXD1 family. KXD1 is participating in endosomal cargo sorting. KXD1 contacts with the BLOC-1 complex and Interacts with BLOC1S1. KXD1 Interacts with DTNBP1/BLOC1S7 through coiled-coil domain.
-
Synonyms
C19orf50, KXDL, MST096, MSTP096, KXD1.
-
Physical Appearance
Sterile Filtered clear solution.
-
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
-
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSMDLPDSA SRVFCGRILS MVNTDDVNAI ILAQKNMLDR FEKTNEMLLN FNNLSSARLQ QMSERFLHHT RTLVEMKRDL DSIFRRIRTL KGKLARQHPE AFSHIPEASF LEEEDEDPIP PSTTTTIATS EQSTGSCDTS PDTVSPSLSP GFEDLSHVQP GSPAINGRSQ TDDEEMTGE.
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.
- View Data Sheet
Name :
Lysozyme HumanDescription:
Lysozyme Human Recombinant
EC 3.2.1.17, LYZ, Lysozyme.
Product # :
ENZ-1159Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Recombinant Human Lysozyme produced in Plant is a non-glycosylated, polypeptide chain containing 130 amino acids and having a molecular mass of 14.7kDa. The Recombinant Human Lysozyme is purified by proprietary chromatographic techniques.
Source
Oryza sativa (rice).
Formulation
The protein (1mg/ml) was lyophilized with no additives.
Purity
Purity as determined by SDS-PAGE is greater than 90%.
Biological Activity
1.6x105 U/mg.
More Info
-
Introduction
Lysozymeis an antimicrobial enzyme produced by animals that are part of the innate immune system. Lysozyme is a glycoside hydrolase that catalyzes the hydrolysis of 1,4-beta-linkages between N-acetylmuramic acid and N-acetyl-D-glucosamine residues in peptidoglycan, which is the major component of gram-positive bacterial cell wall.Lysozymes have primarily a bacteriolytic function - those in tissues and body fluids are associated with the monocyte-macrophage system and enhance the activity of immunoagents.
-
Synonyms
EC 3.2.1.17, LYZ, Lysozyme.
-
Physical Appearance
Sterile Filtered lyophilized (freeze-dried) off white powder.
-
Stability
Store the lyophilized Lysozyme between 2-8°C, do not freeze. Upon reconstitution Lysozyme should be stored at 4°C between 2-7 days and for future use below -18°C. Please prevent freeze-thaw cycles.
-
Solubility
Stock solutions can be prepared by dissolving gently into PBS for several minutes. Recommended stock concentrations are 1mg/ml in PBS.
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.
- View Data Sheet
Name :
ASNS MouseDescription:
Asparagine Synthetase Mouse Recombinant
Glutamine-dependent asparagine synthetase, Asns, Asparagine synthetase.
Product # :
ENZ-1100Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
ASNS produced in Sf9 Insect cells is a single, glycosylated polypeptide chain containing 567 amino acids (1-561a.a.) and having a molecular mass of 65.1 kDa.ASNS is expressed with a 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Insect cells.
Formulation
ASNS protein solution ( 0.25mg/ml ) contains PBS (pH 7.4) and 40% glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
Asparagine synthetase (ASNS) is a cytoplasmic enzyme that turns aspartate toasparagine and functions mostly in mammalian organs. ASNS is responsible for cell growthand its mRNA content is associated with changes in the cell cycle. ASNS may also play a role as a biomarker for ovarian cancer.
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Synonyms
Glutamine-dependent asparagine synthetase, Asns, Asparagine synthetase.
-
Physical Appearance
Sterile Filtered colorless solution.
-
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA). Avoid multiple freeze-thaw cycles.
-
Amino Acid Sequence
MCGIWALFGS DDCLSVQCLS AMKIAHRGPD AFRFENVNGY TNCCFGFHRL AVVDPLFGMQ PIRVRKYPYL WLCYNGEIYN HKALQQRFEF EYQTNVDGEI ILHLYDKGGI EKTICMLDGV FAFILLDTAN KKVFLGRDTY GVRPLFKAMT EDGFLAVCSE AKGLVSLKHS TTPFLKVEPF LPGHYEVLDL KPNGKVASVE MVKYHHCTDE PLHAIYDSVE KLFPGFDLET VKNNLRILFD NAIKKRLMTD RRIGCLLSGG LDSSLVAASL LKQLKEAQVQ YPLQTFAIGM EDSPDLLAAR KVANYIGSEH HEVLFNSEEG IQALDEVIFS LETYDITTVR ASVGMYLISK YIRKNTDSVV IFSGEGSDEL TQGYIYFHKA PSPEKAEEES ERLLKELYLF DVLRADRTTA AHGLELRVPF LDHRFSSYYL SLPPDMRIPK NGIEKHLLRE TFEDCNLLPK EILWRPKEAF SDGITSVKNS WFKILQDYVE HQVDDEMMSA SQKFPFNTP KTKEGYFYRQ IFERHYPGRA DWLTHYWMPK WINATDPSAR TLTHYKS AAK 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.
- View Data Sheet
Name :
PGAM2 Human, ActiveDescription:
Phosphoglycerate Mutase 2 Human Recombinant, Active
Phosphoglycerate mutase 2, BPG-dependent PGAM 2, Muscle-specific phosphoglycerate mutase, Phosphoglycerate mutase isozyme M, PGAM-M, PGAM2, PGAMM, GSD10.
Product # :
ENZ-981Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
PGAM2 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 273 amino acids (1-253) and having a molecular mass of 30.9kDa.PGAM2 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The PGAM2 solution (1mg/ml) contains 20mM Tris-HCl buffer (pH8.0), 20% glycerol, 0.1M NaCl and 1mM DTT.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Biological Activity
Specific activity is > 100units/mg, in which One unit will convert 1.0 umole of 3-phosphoglycerate to 2-phosphoglcerate per minute at pH 7.6 at 37C.More Info
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Introduction
Phosphoglycerate mutase 2 (PGAM2) is a member of the phosphoglycerate mutase family. PGAM is a dimeric enzyme which contains in separate tissues, different proportions of a slow-migrating muscle (MM) isozyme, a fast-migrating brain (BB) isozyme, and a hybrid form (MB). PGAM (Phosphoglycerate mutase) catalyzes the reversible reaction of 3-phosphoglycerate (3-PGA) to 2-phosphoglycerate (2-PGA) in the glycolytic pathway. PGAM2 gene mutations cause muscle phosphoglycerate mutase efficiency, otherwise known as glycogen storage disease X.
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Synonyms
Phosphoglycerate mutase 2, BPG-dependent PGAM 2, Muscle-specific phosphoglycerate mutase, Phosphoglycerate mutase isozyme M, PGAM-M, PGAM2, PGAMM, GSD10.
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Physical Appearance
Sterile Filtered colorless solution.
-
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
-
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MATHRLVMVR HGESTWNQEN RFCGWFDAEL SEKGTEEAKR GAKAIKDAKM EFDICYTSVL KRAIRTLWAI LDGTDQMWLP VVRTWRLNER HYGGLTGLNK AETAAKHGEE QVKIWRRSFD IPPPPMDEKH PYYNSISKER RYAGLKPGEL PTCESLKDTI ARALPFWNEE IVPQIKAGKR VLIAAHGNSL RGIVKHLEGM SDQAIMELNL PTGIPIVYEL NKELKPTKPM QFLGDEETVR KAMEAVAAQG KAK.
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.
- View Data Sheet
Name :
LDHB HumanDescription:
Lactate Dehydrogenase B Human Recombinant
Lactate Dehydrogenase B, Renal Carcinoma Antigen NY-REN-46, LDH Heart Subunit, EC 1.1.1.27, LDH-B, LDH-H, Epididymis Secretory Protein Li 281, Testicular Secretory Protein Li 25, Lactate Dehydrogenase H Chain, HEL-S-281, EC 1.1.1 , LDHBD, TRG-5.
Product # :
ENZ-967Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
LDHB Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 334 amino acids (1-334) and having a molecular mass of 36.6kDa.
Source
Escherichia Coli.
Formulation
The LDHB solution (1mg/ml) contains 20mM Tris-HCl (pH 8.0), 10% glycerol and 1mM DTT.
Purity
Greater than 90% as determined by SDS-PAGE.
Biological Activity
Specific activity is >300 units/mg, in which 1 unit will convert 1.0 umole of pyruvate to L-lactate and beta-NAD per min at pH 7.5 at 37°.
More Info
-
Introduction
LDHB is part of the lactate dehydrogenase family. LDHB is an oxidoreductase which catalyses the interconversion of pyruvate and lactate with concomitant interconversion of NADH and NAD+. LDHB catalyzes the oxidation of hydroxybutyrate, and frequently called Hydroxybutyrate Dehydrogenase (HBD). The LDH family consists of three members, LDH-A, LDH-B and LDH-C. LDHs function as powerful markers for germ cell tumors.
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Synonyms
Lactate Dehydrogenase B, Renal Carcinoma Antigen NY-REN-46, LDH Heart Subunit, EC 1.1.1.27, LDH-B, LDH-H, Epididymis Secretory Protein Li 281, Testicular Secretory Protein Li 25, Lactate Dehydrogenase H Chain, HEL-S-281, EC 1.1.1 , LDHBD, TRG-5.
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Physical Appearance
Sterile Filtered colorless solution.
-
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
-
Amino Acid Sequence
MATLKEKLIA PVAEEEATVP NNKITVVGVG QVGMACAISI LGKSLADELA LVDVLEDKLK GEMMDLQHGS LFLQTPKIVA DKDYSVTANS KIVVVTAGVR QQEGESRLNL VQRNVNVFKF IIPQIVKYSP DCIIIVVSNP VDILTYVTWK LSGLPKHRVI GSGCNLDSAR FRYLMAEKLG IHPSSCHGWI LGEHGDSSVA VWSGVNVAGV SLQELNPEMG TDNDSENWKE VHKMVVESAY EVIKLKGYTN WAIGLSVADL IESMLKNLSR IHPVSTMVKG MYGIENEVFL SLPCILNARG LTSVINQKLK DDEVAQLKKS ADTLWDIQKD LKDL.
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.
- View Data Sheet
Name :
DHPS HumanDescription:
Deoxyhypusine Synthase Human Recombinant
MIG13, EC 2.5.1.46, Deoxyhypusine synthase, DHS, DHPS, DS.
Product # :
ENZ-498Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
DHPS Human Recombinant fused to 20 amino acid His Tag at N-terminal produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 389 amino acids (1-369 a.a.) and having a molecular mass of 43.1 kDa. The DHPS is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The DHPS solution contains 20mM Tris-HCl pH-8, 0.1M NaCl and 20% glycerol.
Purity
Greater than 95% as determined by SDS-PAGE.
More Info
-
Introduction
DHPS is vital for the first step of hypusine biosynthesis. DHPS catalyzes the NAD-dependent transfer of the butylamine moiety of spermidine to the epsilon-amino group of a specific lysine residue of the EIF5A precursor protein to form the intermediate deoxyhypusine residue.
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Synonyms
MIG13, EC 2.5.1.46, Deoxyhypusine synthase, DHS, DHPS, DS.
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Physical Appearance
Sterile Filtered clear colorless solution.
-
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA). Please avoid freeze-thaw cycles.
-
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MEGSLEREAP AGALAAVLKH SSTLPPESTQ VRGYDFNRGV NYRALLEAFG TTGFQATNFG RAVQQVNAMI EKKLEPLSQD EDQHADLTQS RRPLTSCTIF LGYTSNLISS GIRETIRYLV QHNMVDVLVT TAGGVEEDLI KCLAPTYLGE FSLRGKELRE NGINRIGNLL VPNENYCKFE DWLMPILDQM VMEQNTEGVK WTPSKMIARL GKEINNPESV YYWAQKNHIP VFSPALTDGS LGDMIFFHSY KNPGLVLDIV EDLRLINTQA IFAKCTGMII LGGGVVKHHI ANANLMRNGA DYAVYINTAQ EFDGSDSGAR PDEAVSWGKI RVDAQPVKVY ADASLVFPLL VAETFAQKMD AFMHEKNED.
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.
- View Data Sheet
Name :
SOSTDC1 HumanDescription:
Sclerostin Domain Containing 1 Human Recombinant
Sclerostin domain-containing protein 1, Ectodermal BMP inhibitor, Ectodin, Uterine sensitization-associated gene 1 protein, USAG-1, SOSTDC1, USAG1, CDA019.
Product # :
PRO-426Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
SOSTDC1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 206 amino acids (24-206 a.a) and having a molecular mass of 23kDa.SOSTDC1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
SOSTDC1 protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.4M UREA and 10% glycerol.
Purity
Greater than 85.0% as determined by SDS-PAGE.
More Info
-
Introduction
Sclerostin Domain Containing 1 (SOSTDC1) belongs to the sclerostin family and an N-glycosylated, secreted protein with a C-terminal cystine knot-like domain. The SOSTDC1 protein acts as a bone morphogenetic protein (BMP) antagonist. Specifically, SOSTDC1 directly associates with BMPs, prohibiting them from binding their receptors, thus regulating BMP signaling throughout cellular proliferation, differentiation, and programmed cell death. SOSTDC1 may also be involved in the onset of endometrial receptivity for implantation/sensitization for the decidual cell reaction Enhances Wnt signaling and hinders TGF-beta signaling. In addition, SOSTDC1 directly antagonizes the activity of BMP2, BMP4, BMP6 and BMP7 in a dose-dependent manner.
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Synonyms
Sclerostin domain-containing protein 1, Ectodermal BMP inhibitor, Ectodin, Uterine sensitization-associated gene 1 protein, USAG-1, SOSTDC1, USAG1, CDA019.
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Physical Appearance
Sterile Filtered colorless solution.
-
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSFKNDATE ILYSHVVKPV PAHPSSNSTL NQARNGGRHF SNTGLDRNTR VQVGCRELRS TKYISDGQCT SISPLKELVC AGECLPLPVL PNWIGGGYGT KYWSRRSSQE WRCVNDKTRT QRIQLQCQDG STRTYKITVV TACKCKRYTR QHNESSHNFE SMSPAKPVQH HRERKRASKS SKHSMS.
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.
- View Data Sheet
Name :
BLVRA HumanDescription:
Biliverdin Reductase A Human Recombinant
Biliverdin reductase A, BVR A, Biliverdin-IX alpha-reductase, BLVRA, BLVR, BVR, BVRA.
Product # :
ENZ-446Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
BLVRA Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 295 amino acids (3-296 a.a. and Methionine at N-terminus) and having a molecular mass of 33.3kDa (molecular weight on SDS-PAGE will shift up).The BLVRA is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The BLVRA solution contains 20mM Tris-HCl buffer (pH8.0) and 10% glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
-
Introduction
Biliverdin reductase A (BLVRA) is a member of the gfo/idh/mocA family. BLVRA is an enzyme that converts biliverdin to bilirubin, converting a double-bond between the second and third pyrrole ring into a single-bond. BLVRA reduces the gamma-methene bridge of the open tetrapyrrole, biliverdin IX alpha, to bilirubin with the simultaneous oxidation of a NADH or NADPH cofactor (Bilirubin + NAD(P)+ = biliverdin + NAD(P)H ).
BLVRA is a regulator for induction of activating transcription factor-2 and heme oxygenase-1. Furthermore, BLVRA enhances the role of HO-1 in cytoprotection and provides cytoprotection independent of heme degradation. In addition, Bilirubin while acting as a cytoprotective antioxidant is itself oxidized to biliverdin and subsequently recycled by biliverdin reductase back to bilirubin. -
Synonyms
Biliverdin reductase A, BVR A, Biliverdin-IX alpha-reductase, BLVRA, BLVR, BVR, BVRA.
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Physical Appearance
Sterile Filtered colorless solution.
-
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MAEPERKFGV VVVGVGRAGS VRMRDLRNPH PSSAFLNLIG FVSRRELGSI DGVQQISLED ALSSQEVEVA YICSESSSHE DYIRQFLNAG KHVLVEYPMT LSLAAAQELW ELAEQKGKVL HEEHVELLME EFAFLKKEVV GKDLLKGSLL FTAGPLEEER FGFPAFSGIS RLTWLVSLFG
ELSLVSATLE ERKEDQYMKM TVCLETEKKS PLSWIEEKGP GLKRNRYLSF HFKSGSLENV PNVGVNKNIF LKDQNIFVQK LLGQFSEKEL AAEKKRILHC LGLAEEIQKY CCSRK.
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.
- View Data Sheet
Name :
PGAM2 HumanDescription:
Phosphoglycerate Mutase 2 Human Recombinant
Phosphoglycerate mutase 2, BPG-dependent PGAM 2, Muscle-specific phosphoglycerate mutase, Phosphoglycerate mutase isozyme M, PGAM-M, PGAM2, PGAMM, GSD10.
Product # :
ENZ-578Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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- description
- source
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- More Info
Description
PGAM2 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 273 amino acids (1-253) and having a molecular mass of 30.9kDa.PGAM2 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The PGAM2 solution (1mg/ml) contains 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
-
Introduction
Phosphoglycerate mutase 2 (PGAM2) is a member of the phosphoglycerate mutase family. PGAM is a dimeric enzyme which contains in separate tissues, different proportions of a slow-migrating muscle (MM) isozyme, a fast-migrating brain (BB) isozyme, and a hybrid form (MB). PGAM (Phosphoglycerate mutase) catalyzes the reversible reaction of 3-phosphoglycerate (3-PGA) to 2-phosphoglycerate (2-PGA) in the glycolytic pathway. PGAM2 gene mutations cause muscle phosphoglycerate mutase efficiency, otherwise known as glycogen storage disease X.
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Synonyms
Phosphoglycerate mutase 2, BPG-dependent PGAM 2, Muscle-specific phosphoglycerate mutase, Phosphoglycerate mutase isozyme M, PGAM-M, PGAM2, PGAMM, GSD10.
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Physical Appearance
Sterile Filtered colorless solution.
-
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MATHRLVMVR HGESTWNQEN RFCGWFDAEL SEKGTEEAKR GAKAIKDAKM EFDICYTSVL KRAIRTLWAI LDGTDQMWLP VVRTWRLNER HYGGLTGLNK AETAAKHGEE QVKIWRRSFD IPPPPMDEKH PYYNSISKER RYAGLKPGEL PTCESLKDTI ARALPFWNEE IVPQIKAGKR VLIAAHGNSL RGIVKHLEGM SDQAIMELNL PTGIPIVYEL NKELKPTKPM QFLGDEETVR KAMEAVAAQG KAK.
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.
- View Data Sheet
Name :
GST S. Japonicum, HisDescription:
Glutathione S-Transferase Schistosoma Japonicum Recombinant, His
Glutathione S-Transferase class-mu 26 kDa isozyme, Sj26 antigen, SjGST, Glutathione S-Transferase class-mu 26 kDa isozyme Glutathione S Transferase.
Product # :
ENZ-1146Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
GST S. Japonicum Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 244 amino acids (1-218) and having a molecular mass of 28.3 kDa.GST S. Japonicum is fused to a 26 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
GST S. Japonicum protein solution (1mg/ml) contains Phosphate-Buffered Saline (pH 7.4) and 10% glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Biological Activity
Specific activity is > 10unit/mg, and is defined as the amount of enzyme that conjugate 1.0 umole of 1-chloro2,4-dinitrobenzene (CDNB) with reduced glutathione per minute at pH 6.5 at 25C.
More Info
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Introduction
Glutathione S-transferase or GST, stands for a large family of detoxification proteins and enzymes. Glutathione S-transferase catalyzes glutathione reaction and an acceptor molecule to create S-substituted glutathione (S stands for sulfur). By this reaction, a large variety of compounds, for example therapeutic drugs, carcinogens & oxidative stress products, transformed. Glutathione S-transferase acts as a transport protein by binding toxins and acts as a transport protein. At first, the protein was isolated from Schistosomajaponicum, nowadays it is isolated from E. coli bacteria.
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Synonyms
Glutathione S-Transferase class-mu 26 kDa isozyme, Sj26 antigen, SjGST, Glutathione S-Transferase class-mu 26 kDa isozyme Glutathione S Transferase.
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Physical Appearance
Sterile Filtered colorless solution.
-
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MSPILGYWKI KGLVQPTRLL LEYLEEKYEE HLYERDEGDK WRNKKFELGL EFPNLPYYID GDVKLTQSMA IIRYIADKHN MLGGCPKERA EISMLEGAVL DIRYGVSRIA YSKDFETLKV DFLSKLPEML KMFEDRLCHK TYLNGDHVTH PDFMLYDALD VVLYMDPMCL DAFPKLVCFK KRIEAIPQID KYLKSSKYIA WPLQGWQATF GGGDHPPKSD
LVPR
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.
- View Data Sheet
Name :
UROD HumanDescription:
Uroporphyrinogen Decarboxylase Human Recombinant
UPD, PCT, EC 4.1.1.37, URO-D, UROD, Uroporphyrinogen Decarboxylase.
Product # :
ENZ-536Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
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Description
UROD Recombinant Human produced in E.Coli is a single, non-glycosylated polypeptide chain containing 387 amino acids (1-367 a.a.) and having a molecular mass of 43 kDa. The UROD is fused to 20 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
UROD Human solution containing 20mM Tris pH-8, 1mM DTT, 0.1M NaCl, 1mM EDTA & 20% glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
UROD is the fifth enzyme in the human heme biosynthetic pathway and is in charge for the transfer of uroporphyrinogen to coproporphyrinogen through the deletion of four carboxymethyl side chains. UROD Mutations and deficiency result in 3 autosomal disorders in humans: familial porphyria cutanea tarda (f-PCT), sporadic porphyria cutanea tarda (s-PCT) and hepatoerythropoietic porphyria (HEP).
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Synonyms
UPD, PCT, EC 4.1.1.37, URO-D, UROD, Uroporphyrinogen Decarboxylase.
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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 MEANGLGPQG FPELKNDTFL RAAWGEETDY TPVWCMRQAG RYLPEFRETR AAQDFFSTCR SPEACCELTL QPLRRFPLDA AIIFSDILVV PQALGMEVTM VPGKGPSFPE PLREEQDLER LRDPEVVASE LGYVFQAITL TRQRLAGRVP LIGFAGAPWT LMTYMVEGGG SSTMAQAKRW LYQRPQASHQ LLRILTDALV PYLVGQVVAG AQALQLFESH AGHLGPQLFN KFALPYIRDV AKQVKARLRE AGLAPVPMII FAKDGHFALE ELAQAGYEVV GLDWTVAPKK ARECVGKTVT LQVNLDPCAL YASEEEIGQL VKQMLDDFGP HRYIANLGHG LYPDMDPEHV GAFVDAVHKH SRLLRQN.
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.
- View Data Sheet
Name :
GLSA1 E.ColiDescription:
Glutaminase 1 E.Coli Recombinant
Glutaminase 1, ybaS.
Product # :
ENZ-133Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
GLSA1 E.Coli Recombinant fused with a 20 amino acid His tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 330 amino acids (1-310a.a.) and having a molecular mass of 35.0kDa. The GLSA1 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The GLSA1 solution (1mg/1ml) contains 20mM Tris-HCl buffer (pH8.0), 0.1M NaCl, 1mM DTT and 10% glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
GlsA1 is a member of the great superfamily of serine-dependent beta-lactamases and penicillin-binding proteins which exist almost in every bacteria and eukaryotes and catalyze the hydrolytic deamidation of l-glutamine to l-glutamate and free NH4+.
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Synonyms
Glutaminase 1, ybaS.
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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 MLDANKLQQA VDQAYTQFHS LNGGQNADYI PFLANVPGQL AAVAIVTCDG NVYSAGDSDY RFALESISKV CTLALALEDV GPQAVQDKIG ADPTGLPFNS VIALELHGGK PLSPLVNAGA IATTSLINAE NVEQRWQRIL HIQQQLAGEQ VALSDEVNQS EQTTNFHNRA IAWLLYSAGY LYCDAMEACD VYTRQCSTLL NTIELATLGA TLAAGGVNPL THKRVLQADN VPYILAEMMM EGLYGRSGDW AYRVGLPGKS GVGGGILAVV PGVMGIAAFS PPLDEDGNSV RGQKMVASVA KQLGYNVFKG
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 :
ABHD10 HumanDescription:
Abhydrolase Domain Containing 10 Human Recombinant
Abhydrolase domain containing 10 mitochondrial2, FLJ11342, EC 3.4.-.-.
Product # :
ENZ-612Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
ABHD10 Human Recombinant produced in E. coli is a single polypeptide chain containing 279 amino acids (53-306) and having a molecular mass of 30.9kDa.ABHD10 is fused to a 25 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
The ABHD10 solution (1mg/1ml) contains 20mM Tris-HCl buffer (pH 8.0), 1mM DTT, 100mM NaCl and 20% glycerol.
Purity
Greater than 85% as determined by SDS-PAGE.
More Info
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Introduction
Abhydrolase domain-containing protein 10 (ABHD10) is a member of the AB hydrolase superfamily.
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Synonyms
Abhydrolase domain containing 10 mitochondrial2, FLJ11342, EC 3.4.-.-.
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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 MGSHMTSLSF LNRPDLPNLA YKKLKGKSPG IIFIPGYLSY MNGTKALAIE EFCKSLGHAC IRFDYSGVGS SDGNSEESTL GKWRKDVLSI IDDLADGPQI LVGSSLGGWL MLHAAIARPE KVVALIGVAT AADTLVTKFN QLPVELKKEV EMKGVWSMPS KYSEEGVYNV QYSFIKEAEH HCLLHSPIPV NCPIRLLHGM KDDIVPWHTS MQVADRVLST DVDVILRKHS DHRMREKADI QLLVYTIDDL IDKLSTIVN
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.
- View Data Sheet
Name :
ECI1 HumanDescription:
Enoyl-CoA Delta Isomerase 1 Human Recombinant
Enoyl-CoA delta isomerase 1, mitochondrial, 3,2-trans-enoyl-CoA isomerase, Enoyl-CoA Delta Isomerase 1, Delta(3),Delta(2)-enoyl-CoA isomerase, D3,D2-enoyl-CoA isomerase, Dodecenoyl-CoA isomerase, ECI1, DCI.
Product # :
ENZ-758Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
ECI1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 284 amino acids (42-302 a.a.) and having a molecular mass of 31.1kDa. ECI1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
ECI1 protein solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 10% glycerol and 1mM DTT.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
Enoyl-CoA Delta Isomerase 1 (ECI1) is a main mitochondrial enzyme which takes part in beta-oxidation of unsaturated fatty acids. ECI1 is a member of the hydratase/isomerase superfamily. ECI1 catalyzes the transformation of 3-cis and 3-trans-enoyl-CoA esters to the 2-trans-enoylCoA intermediates.
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Synonyms
Enoyl-CoA delta isomerase 1, mitochondrial, 3,2-trans-enoyl-CoA isomerase, Enoyl-CoA Delta Isomerase 1, Delta(3),Delta(2)-enoyl-CoA isomerase, D3,D2-enoyl-CoA isomerase, Dodecenoyl-CoA isomerase, ECI1, DCI.
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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 MGSFGSQRVL VEPDAGAGVA VMKFKNPPVN SLSLEFLTEL VISLEKLEND KSFRGVILTS DRPGVFSAGL DLTEMCGRSP AHYAGYWKAV QELWLRLYQS NLVLVSAING ACPAGGCLVA LTCDYRILAD NPRYCIGLNE TQLGIIAPFW LKDTLENTIG HRAAERALQL GLLFPPAEAL QVGIVDQVVP EEQVQSTALS AIAQWMAIPD HARQLTKAMM RKATASRLVT QRDADVQNFV SFISKDSIQK SLQMYLERLK EEKG.
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 :
IDE Human, ActiveDescription:
Insulin-Degrading Enzyme Human Recombinant
Insulin-Degrading Enzyme, Abeta-Degrading Protease, Insulysin, EC 3.4.24.56, Insulinase, Insulin Protease, INSULYSIN, EC 3.4.24, IDE, insulin-degrading enzyme isoform 1.
Product # :
ENZ-1192Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
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Description
IDE Human, Active Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain (42-1019 a.a) containing a total of 984 amino acids, having a molecular mass of 114 kDa. IDE is fused to a 6 amino acid His-tag at C-terminus and is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The IDE solution (0.5mg/ml) contains 10% Glycerol, 100mM NaCl, 0.05% Brij35 and 20mM Tris-HCl buffer (pH 7.5).
Purity
Greater than 90.0% as determined by SDS-PAGE.
Biological Activity
Specific activity is greater than 3,000 pmol/min/ug in which 1 unit will convert 1.0 pmole of Mca-RPPGFSAFK(Dnp)-OH to MCA-Pro-Leu-OH per minute at pH 7.5 at 25°C.
More Info
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Synonyms
Insulin-Degrading Enzyme, Abeta-Degrading Protease, Insulysin, EC 3.4.24.56, Insulinase, Insulin Protease, INSULYSIN, EC 3.4.24, IDE, insulin-degrading enzyme isoform 1.
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Physical Appearance
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
MNNPAIKRIG NHITKSPEDK REYRGLELAN GIKVLLISDP TTDKSSAALD VHIGSLSDPP NIAGLSHFCE HMLFLGTKKY PKENEYSQFL SEHAGSSNAF TSGEHTNYYF DVSHEHLEGA LDRFAQFFLC PLFDESCKDR EVNAVDSEHE KNVMNDAWRL FQLEKATGNP KHPFSKFGTG NKYTLETRPN QEGIDVRQEL LKFHSAYYSS NLMAVCVLGR ESLDDLTNLV VKLFSEVENK NVPLPEFPEH PFQEEHLKQL YKIVPIKDIR NLYVTFPIPD LQKYYKSNPG HYLGHLIGHE GPGSLLSELK SKGWVNTLVG GQKEGARGFM FFIINVDLTE EGLLHVEDII LHMFQYIQKL RAEGPQEWVF QECKDLNAVA FRFKDKERPR GYTSKIAGIL HYYPLEEVLT AEYLLEEFRP DLIEMVLDKL RPENVRVAIV SKSFEGKTDR TEEWYGTQYK QEAIPDEVIK KWQNADLNGK FKLPTKNEFI PTNFEILPLE KEATPYPALI KDTAMSKLWF KQDDKFFLPK ACLNFEFFSP FAYVDPLHCN MAYLYLELLK DSLNEYAYAA ELAGLSYDLQ NTIYGMYLSV KGYNDKQPIL LKKIIEKMAT FEIDEKRFEI IKEAYMRSLN NFRAEQPHQH AMYYLRLLMT EVAWTKDELK EALDDVTLPR LKAFIPQLLS RLHIEALLHG NITKQAALGI MQMVEDTLIE HAHTKPLLPS
QLVRYREVQL PDRGWFVYQQ RNEVHNNCGI EIYYQTDMQS TSENMFLELF CQIISEPCFN TLRTKEQLGY IVFSGPRRAN GIQGLRFIIQ SEKPPHYLES RVEAFLITME KSIEDMTEEA FQKHIQALAI RRLDKPKKLS AECAKYWGEI ISQQYNFDRD NTEVAYLKTL TKEDIIKFYK EMLAVDAPRR HKVSVHVLAR EMDSCPVVGE FPCQNDINLS QAPALPQPEV IQNMTEFKRG LPLFPLVKPH INFMAAKLHH HHHH. -
Background
Insulin-degrading enzyme (IDE) is a crucial protease that plays a significant role in maintaining glucose homeostasis by degrading insulin and other bioactive peptides. Dysregulation of IDE has been implicated in various metabolic disorders, particularly type 2 diabetes mellitus. IDE is also associated with the clearance of amyloid-beta peptides in the brain, making it relevant to Alzheimer's disease pathology. Studying the recombinant form of IDE is fundamental to understanding its functional mechanisms and exploring potential avenues for therapeutic interventions.
The primary goal of this research is to express and purify recombinant IDE using diverse expression systems. Recombinant DNA techniques will be employed to construct expression vectors containing the IDE gene, followed by expression in bacterial, yeast, or mammalian cell-based systems. The recombinant IDE will be purified using affinity chromatography or other appropriate methods, facilitating subsequent biochemical and biophysical characterization.
The second objective is to investigate the substrate specificity and catalytic activity of the purified IDE. In vitro enzymatic assays will be conducted to analyse the ability of the recombinant IDE to degrade insulin and other potential substrates. The effects of various factors, such as pH, temperature, and potential modulators, on IDE activity will be evaluated. Additionally, the interactions between IDE and its substrates will be explored using binding assays.
The third objective is to elucidate the three-dimensional structure of the IDE recombinant using techniques like X-ray crystallography or nuclear magnetic resonance (NMR) spectroscopy. Structural insights into the active site and binding pockets of IDE will provide valuable information for understanding its substrate recognition and catalytic mechanisms. This knowledge could be instrumental in designing targeted therapeutic compounds.
By characterizing the IDE recombinant, this research aims to contribute to our understanding of its role in insulin metabolism, glucose regulation, and potential therapeutic applications. The findings from this study may have implications for the development of novel treatments for diabetes and other related disorders.
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.