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1000 results found for “aldolase”
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Name :
GST, 218 a.a.Description:
Glutathione S-Transferase, 218 a.a. Recombinant
Glutathione S-Transferase, GST, Glutathione S-transferase class-mu 28 kDa isozyme, GST 28, EC 2.5.1.18, Sj28GST, Sj28 antigen, Sj26 antigen.
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ENZ-1079Price :
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Description
GST Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 218 amino acids (1-218 a.a) and having a molecular mass of 25.4kDa
Source
Escherichia Coli.
Formulation
GST protein solution (1mg/ml) containing PBS and 10% glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
Biological Activity
The Specific activity is > 30 units/mg, and is defined as the amount of enzyme that conjugate 1.0 umole of 1-chloro-2,4-dinitrobenzene (CDNB) with reduced glutathione per minute at pH 6.5 at 25C.
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Introduction
Antioxidant enzyme Glutathione S- Transferase (GST) is thought to do the primary cellular defense mechanism against reactive oxygen species. GST reduces lipid hydroperoxides through its Se-independent glutathione peroxidase activity. The enzyme also detoxifies lipid peroxidation end products such as 4-hydroxynonenal (4-HNE).
The soluble GST is a 26 kDa protein which occurs as a dimer in all aerobic organisms. Each monomer has two domains, one that binds GSH and is an /-structure similar to thioredoxin and the other, all helical, that binds the hydrophobic substrate. The GST -fusion protein expression system is a widely used recombinant protein expression system that allows a peptide or a regulatory protein domain to be expressed as a fusion to the C-terminus of Schistosoma japonicum GST. Fusion proteins also possess GST -enzymatic activity and can undergo dimerization similar to in vivo. The fusion protein can be purified via GST -affinity column chromatography. In most cases, the desired peptides or domains are removed from GST by applying a specific protease that recognizes and cleaves the linker between the protein domain and GST. The technique has been widely used to generate different kinds of proteins for crystallization, molecular immunology studies, the production of vaccines and studies involving protein-protein and protein-DNA interactions. -
Synonyms
Glutathione S-Transferase, GST, Glutathione S-transferase class-mu 28 kDa isozyme, GST 28, EC 2.5.1.18, Sj28GST, Sj28 antigen, Sj26 antigen.
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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
MSPILGYWKI KGLVQPTRLL LEYLEEKYEE HLYERDEGDK WRNKKFELGL EFPNLPYYID GDVKLTQSMA IIRYIADKHN MLGGCPKERA EISMLEGAVL DIRYGVSRIA YSKDFETLKV DFLSKLPEML KMFEDRLCHK TYLNGDHVTH PDFMLYDALD VVLYMDPMCL DAFPKLVCFK KRIEAIPQID KYLKSSKYIA WPLQGWQATF GGGDHPPK.
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 :
GZMH HumanDescription:
Granzyme-H Human Recombinant
Granzyme H (Cathepsin G-Like 2, Protein H-CCPX), CTSGL2, Cytotoxic T-Lymphocyte Proteinase, CCP-X, CSP-C, Cytotoxic T-Lymphocyte-Associated Serine Esterase 1, Cytotoxin Serine Protease-C, Cytotoxic Serine Protease C, Cathepsin G-Like 2, EC 3.4.21.79, EC 3.4.21, Granzyme H, EC 3.4.21, CGL-2, CTLA1, CGL2, GZMH.
Product # :
ENZ-896Price :
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Description
GZMH Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 248 amino acids (20-246 a.a) and having a molecular mass of 27.5kDa.GZMH is fused to a 21 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
GZMH protein solution (0.25mg/ml) containing 20mM Tris-HCl (pH 8.0) and 10% glycerol.
Purity
Greater than 85.0% as determined by SDS-PAGE.
Citations
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Introduction
Granzyme H also known as GZMH belongs to the peptidase S1 family. GZMH is an essential part for HBV eradication. The HBx protein, which is required for the replication of HBV, is cleaved at Met(79) by GZMH. Furthermore, GZMH inhibitor can abolish GZNH- as well as lymphokine-activated killer cell-mediated HBx degradation and HBV clearance. A HBx-deficient HBV is resistant to GzmH- in addition to lymphokine-activated killer cell-mediated viral clearance.
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Synonyms
Granzyme H (Cathepsin G-Like 2, Protein H-CCPX), CTSGL2, Cytotoxic T-Lymphocyte Proteinase, CCP-X, CSP-C, Cytotoxic T-Lymphocyte-Associated Serine Esterase 1, Cytotoxin Serine Protease-C, Cytotoxic Serine Protease C, Cathepsin G-Like 2, EC 3.4.21.79, EC 3.4.21, Granzyme H, EC 3.4.21, CGL-2, CTLA1, CGL2, GZMH.
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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 MEIIGGHEAK PHSRPYMAFV QFLQEKSRKR CGGILVRKDF VLTAAHCQGS SINVTLGAHN IKEQERTQQF IPVKRPIPHP AYNPKNFSND IMLLQLERKA KWTTAVRPLR LPSSKAQVKP GQLCSVAGWG YVSMSTLATT LQEVLLTVQK DCQCERLFHG NYSRATEICV GDPKKTQTGF KGDSGGPLVC KDVAQGILSY GNKKGTPPGV YIKVSHFLPW IKRTMKRL
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 :
SRR HumanDescription:
Serine Racemase Human Recombinant
Serine racemase, D-serine ammonia-lyase, D-serine dehydratase, L-serine ammonia-lyase, L-serine dehydratase, SRR, ILV1, ISO1.
Product # :
ENZ-232Price :
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Description
SRR Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 364 amino acids (1-340) and having a molecular mass of 39.1kDa.SRR is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The SRR solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH8.0), 20% glycerol, 0.1M NaCl and 1mM DTT.
Purity
Greater than 85.0% as determined by SDS-PAGE.
Citations
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Introduction
Serine racemase (SRR) is an enzyme which generates D-serine from L-serine. D-serine functions as a neuronal signaling molecule by activating NMDA receptors in the brain. Mammalian SRR is a pyridoxal 5'-phosphate dependent enzyme which catalyzes both the racemization of L-serine to D-serine and also the elimination of water from L-serine, producing pyruvate and ammonia. The SRR enzyme is physiologically stimulated by divalent cations (e.g., magnesium) and is allosterically activated by the magnesium/ATP complex.
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Synonyms
Serine racemase, D-serine ammonia-lyase, D-serine dehydratase, L-serine ammonia-lyase, L-serine dehydratase, SRR, ILV1, ISO1.
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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 MGSHMCAQYC ISFADVEKAH INIRDSIHLT PVLTSSILNQ LTGRNLFFKC ELFQKTGSFK IRGALNAVRS LVPDALERKP KAVVTHSSGN HGQALTYAAK LEGIPAYIVV PQTAPDCKKL AIQAYGASIV YCEPSDESRE NVAKRVTEET EGIMVHPNQE PAVIAGQGTI ALEVLNQVPL VDALVVPVGG GGMLAGIAIT VKALKPSVKV YAAEPSNADD CYQSKLKGKL MPNLYPPETI ADGVKSSIGL NTWPIIRDLV DDIFTVTEDE IKCATQLVWE RMKLLIEPTA GVGVAAVLSQ HFQTVSPEVK NICIVLSGGN VDLTSSITWV KQAERPASYQ SVSV.
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 :
GCK Human, ActiveDescription:
Hexokinase-4 Human Recombinant, Active
Glucokinase, Glucokinase (Hexokinase 4), Hexokinase Type IV, HK IV, HK4, Maturity Onset Diabetes of The Young 2, ATP:D-Hexose 6-Phosphotransferase, Hexokinase D, Pancreatic Isozyme, Hexokinase-4, Hexokinase-D, Hexokinase 4.
Product # :
PKA-116Price :
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Description
GCK Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 485 amino acids (1-465 a.a) and having a molecular mass of 54.3kDa. GCK is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
GCK protein solution (1mg/ml) contains 20 mM Tris-HCl buffer (pH 8.0) and 10% glycerol.
Purity
Greater than 95% as determined by SDS-PAGE.
Biological Activity
Specific activity is > 2,000 pmol/min/ug. One unit will convert 1 pmoles of D-Glucose to D-Glucose-6-phosphate per minute at pH8.0 at 37C.
Citations
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Introduction
GCK is an enzyme that expedite the formation of glucose-6-phosphate for glucose by phosphorylation. Humans and other vertebrates have GCK in the cells of the pancreas and liver. In both organs, the enzyme has an important role in carbohydrate metabolism regulation by sensing sugar levels and acting according to the change in glucose levels, that can rise after a meal or fall during fasting. Mutations in the gene that codes for this enzyme can cause hypoglycemia or diabetes.
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Synonyms
Glucokinase, Glucokinase (Hexokinase 4), Hexokinase Type IV, HK IV, HK4, Maturity Onset Diabetes of The Young 2, ATP:D-Hexose 6-Phosphotransferase, Hexokinase D, Pancreatic Isozyme, Hexokinase-4, Hexokinase-D, Hexokinase 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 MLDDRARMEA AKKEKVEQIL AEFQLQEEDL KKVMRRMQKE MDRGLRLETH EEASVKMLPT YVRSTPEGSE VGDFLSLDLG GTNFRVMLVK VGEGEEGQWS VKTKHQMYSI PEDAMTGTAE MLFDYISECI SDFLDKHQMK HKKLPLGFTF SFPVRHEDID KGILLNWTKG FKASGAEGNN VVGLLRDAIK RRGDFEMDVV AMVNDTVATM ISCYYEDHQC EVGMIVGTGC NACYMEEMQN VELVEGDEGR MCVNTEWGAF GDSGELDEFL LEYDRLVDES SANPGQQLYE KLIGGKYMGE LVRLVLLRLV DENLLFHGEA SEQLRTRGAF ETRFVSQVES DTGDRKQIYN ILSTLGLRPS TTDCDIVRRA CESVSTRAAH MCSAGLAGVI NRMRESRSED VMRITVGVDG SVYKLHPSFK ERFHASVRRL TPSCEITFIE SEEGSGRGAA LVSAVACKKA CMLGQ.
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 :
CTSZ Human, Sf9Description:
Cathepsin-Z Human Recombinant, Sf9
Cathepsin Z, Cathepsin X, Cysteine-Type Carboxypeptidase, Lysosomal Carboxypeptidase B, Carboxypeptidase LB, Cathepsin B2, Cathepsin IV, Cathepsin Z1, Cathepsin P, Cathepsin Y, EC 3.4.18.1, Preprocathepsin P, CTSX.
Product # :
ENZ-1097Price :
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Description
CTSZ produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 288 amino acids (24-303.a.) and having a molecular mass of 32.5kDa. (Molecular size on SDS-PAGE will appear at approximately 28-40kDa).CTSZ is expressed with an 8 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
CTSZ protein solution (0.5mg/ml) contains 10% glycerol & Phosphate Buffered Saline (pH 7.4).
Purity
Greater than 95% as determined by SDS-PAGE.
Biological Activity
The specific activity is determent as the ability of 1 unit to convert 1.0 pmole of Mca-PLGL-Dpa-AR-NH2 to MCA- Pro-Leu-OH per minute at pH 3.5 at 25C and is > 1,400 pmol/min/ug.
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Introduction
Cathepsin-Z (CTSZ) is a lysosomal cysteine proteinase and a member of the peptidase C1 family. CTSZ, which is known also as cathepsin X and cathepsin P, exhibits carboxy-monopeptidase and carboxy-dipeptidase activities. CTSZ is expressed ubiquitously in cancer cell lines and primary tumors and as other members of this family, takes part in tumorigenesis.
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Synonyms
Cathepsin Z, Cathepsin X, Cysteine-Type Carboxypeptidase, Lysosomal Carboxypeptidase B, Carboxypeptidase LB, Cathepsin B2, Cathepsin IV, Cathepsin Z1, Cathepsin P, Cathepsin Y, EC 3.4.18.1, Preprocathepsin P, CTSX.
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Physical Appearance
Sterile Filtered clear solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please avoid freeze thaw cycles.
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Amino Acid Sequence
GLYFRRGQTC YRPLRGDGLA PLGRSTYPRP HEYLSPADLP KSWDWRNVDG VNYASITRNQ
HIPQYCGSCW AHASTSAMAD RINIKRKGAW PSTLLSVQNV IDCGNAGSCE GGNDLSVWDY
AHQHGIPDET CNNYQAKDQE CDKFNQCGTC NEFKECHAIR NYTLWRVGDY GSLSGREKMM
AEIYANGPIS CGIMATERLA NYTGGIYAEY QDTTYINHVV SVAGWGISDG TEYWIVRNSW
GEPWGERGWL RIVTSTYKDG KGARYNLAIE EHCTFGDPIV LEHHHHHH
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 :
ACPP MouseDescription:
Acid Phosphatase Prostate Mouse Recombinant
acid phosphatase, prostate, ACP3, ACP-3, ACPP, EC 3.1.3.2, PAP, Prostatic Acid Phosphatase, prostatic acid phosphatase, 5-nucleotidase, 5'-NT, Acid phosphatase 3, Ecto-5'-nucleotidase, Fluoride-resistant acid phosphatase, FRAP, Thiamine monophosphatase, TMPase, A030005E02Rik, Lap, PAP, Ppal.
Product # :
ENZ-1157Price :
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Description
ACPP Mouse produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 356 amino acids (32-381 aa) and having a molecular mass of 41.3kDa.ACPP is fused to a 6 amino acid His tag at C-terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
The ACPP 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 >80,000 unit/mg, and is defined as the amount of enzyme that hydrolyze 1.0nmole of pnitrophenyl phosphate (pNPP) per minute at pH 5.0 at 37C.
Citations
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Introduction
Prostatic Acid Phosphatase or ACPP is part of a family of proteins called histidine acid phosphatase. ACPP enhances the hydrolyzation of many phosphate monoesters and proteins that are phosphorylated. In order to function best, ACPP needs a range of range of 4-6 pH, furthermore, L(+)-tartrate inhibits ACPP’s catalyzation. This enzyme can act as a lipid phosphatase as well and can inhibit lysophosphatidic acid in seminal plasma.
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Synonyms
acid phosphatase, prostate, ACP3, ACP-3, ACPP, EC 3.1.3.2, PAP, Prostatic Acid Phosphatase, prostatic acid phosphatase, 5-nucleotidase, 5'-NT, Acid phosphatase 3, Ecto-5'-nucleotidase, Fluoride-resistant acid phosphatase, FRAP, Thiamine monophosphatase, TMPase, A030005E02Rik, Lap, PAP, Ppal.
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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
KELKFVTLVF RHGDRGPIET FPTDPITESS WPQGFGQLTQ WGMEQHYELG SYIRKRYGRF LNDTYKHDQI YIRSTDVDRT LMSAMTNLAA LFPPEGISIW NPRLLWQPIP VHTVSLSEDR LLYLPFRDCP RFEELKSETL ESEEFLKRLH PYKSFLDTLS SLSGFDDQDL FGIWSKVYDP LFCESVHNFT LPSWATEDAM IKLKELSELS LLSLYGIHKQ KEKSRLQGGV LVNEILKNMK LATQPQKYKK LVMYSAHDTT VSGLQMALDV YNGVLPPYAS CHMMELYHDK GGHFVEMYYR NETQNEPYPL TLPGCTHSCP LEKFAELLDP VISQDWATEC MATSSHQGRN 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 :
CAIII Human, HisDescription:
Carbonic Anhydrase III Human Recombinant, His Tag
Car3, CAIII, Carbonic anhydrase 3, EC 4.2.1.1, Carbonic anhydrase III, Carbonate dehydratase III, CA-III.
Product # :
ENZ-270Price :
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Description
Carbonic anhydrase III Human Recombinant produced in E.Coli, and having a molecular mass of 33.9 kDa. CAIII is expressed with an amino-terminal hexahistidine tag.The CA-III is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Supplied in 10mM Tris-HCl (pH 8), 250mM NaCl, 0.5mM DTT, 1.5mM Cysteine, and 50% Glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Citations
More Info
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Introduction
Carbonic anhydrase (carbonate dehydratase) is a family of metalloenzymes (enzymes that contain one or more metal atoms as a functional component of the enzyme) that catalyze the rapid (and reversible) conversion of carbon dioxide to bicarbonate and protons, a reaction that occurs rather slowly in the absence of a catalyst. Carbonic anhydrase greatly increases the rate of the reaction, with typical catalytic rates of the different forms of this enzyme ranging between 104 and 106 reactions per second. The active site of most carbonic anhydrases contains a zincion. CAIII is a cytoplasmic isoenzyme, but is released into the circulation following injury.
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Synonyms
Car3, CAIII, Carbonic anhydrase 3, EC 4.2.1.1, Carbonic anhydrase III, Carbonate dehydratase III, CA-III.
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Physical Appearance
Sterile Filtered blue 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.
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 :
JMJD6 HumanDescription:
Jumonji Domain Containing 6 Human Recombinant
Jumonji Domain Containing 6, Phosphatidylserine Receptor, Jumonji Domain-Containing Protein 6, Histone Arginine Demethylase JMJD6, Peptide-Lysine 5-Dioxygenase JMJD6, JmjC Domain-Containing Protein 6, Lysyl-Hydroxylase JMJD6, PTDSR, PSR, Bifunctional Arginine Demethylase And Lysyl-Hydroxylase JMJD6, Protein PTDSR, EC 1.14.11.-, EC 1.14.11, KIAA0585, PTDSR1, Bifunctional arginine demethylase and lysyl-hydroxylase JMJD6 (EC:1.14.11.-).
Product # :
PRO-2183Price :
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Description
JMJD6 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 437 amino acids (1-414 a.a) and having a molecular mass of 50.0kDa. JMJD6 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
JMJD6 protein solution (0.5mg/ml) containing Phosphate buffered saline (pH7.4), 30% glycerol and 1mM DTT.
Purity
Greater than 90% as determined by SDS-PAGE.
Citations
More Info
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Introduction
Jumonji Domain Containing 6, also known as JMJD6 performs as a lysyl-hydroxylase which catalyzes 5-hydroxylation on specific lysine residues of target proteins for instance U2AF2/U2AF65 and LUC7L2, as a regulator of RNA splicing by mediating 5-hydroxylation of U2AF2/U2AF65, affecting the pre-mRNA splicing activity of U2AF2/U2AF65. Additionally to peptidyl-lysine 5-dioxygenase activity, JMJD6 performs as an RNA hydroxylase, as proposed by its ability to bind single strand RNA. Furthermore, it acts as an arginine demethylase which demethylates histone H3 at 'Arg-2' (H3R2me) as well as histone H4 at 'Arg-3' (H4R3me), thus taking a part in histone code.
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Synonyms
Jumonji Domain Containing 6, Phosphatidylserine Receptor, Jumonji Domain-Containing Protein 6, Histone Arginine Demethylase JMJD6, Peptide-Lysine 5-Dioxygenase JMJD6, JmjC Domain-Containing Protein 6, Lysyl-Hydroxylase JMJD6, PTDSR, PSR, Bifunctional Arginine Demethylase And Lysyl-Hydroxylase JMJD6, Protein PTDSR, EC 1.14.11.-, EC 1.14.11, KIAA0585, PTDSR1, Bifunctional arginine demethylase and lysyl-hydroxylase JMJD6 (EC:1.14.11.-).
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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 MGSMNHKSKK RIREAKRSAR PELKDSLDWT RHNYYESFSL SPAAVADNVE RADALQLSVE EFVERYERPY KPVVLLNAQE GWSAQEKWTL ERLKRKYRNQ KFKCGEDNDG YSVKMKMKYY IEYMESTRDD SPLYIFDSSY GEHPKRRKLL EDYKVPKFFT DDLFQYAGEK RRPPYRWFVM GPPRSGTGIH IDPLGTSAWN ALVQGHKRWC LFPTSTPREL IKVTRDEGGN QQDEAITWFN VIYPRTQLPT WPPEFKPLEI LQKPGETVFV PGGWWHVVLN LDTTIAITQN FASSTNFPVV WHKTVRGRPK LSRKWYRILK QEHPELAVLA DSVDLQESTG IASDSSSDSS SSSSSSSSDS DSECESGSEG DGTVHRRKKR RTCSMVGNGD TTSQDDCVSK ERSSSRIRDT CGGRAHP.
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 :
KEL MouseDescription:
Kell Metallo-Endopeptidase Mouse Recombinant
kell blood group antigen, kell blood group glycoprotein, Kell blood group, Kell blood group glycoprotein homolog, KEL, Kell, CD238 antigen, CD238, ECE3, Kell blood group-metalloendopeptidase, Kell blood group-metalloendopeptidase.
Product # :
ENZ-1158Price :
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Description
KEL Mouse produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 674 amino acids (49-713 aa) and having a molecular mass of 76.3kDa.KEL is fused to a 9 amino acid His tag at C-terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
The KEL solution (0.25mg/ml) contains 10% Glycerol and Phosphate-Buffered Saline (pH 7.4).
Purity
Greater than 90.0% as determined by SDS-PAGE.
Citations
More Info
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Introduction
Kell blood group glycoprotein homolog or KEL, is an enzyme, part of the zinc endopeptidase of the neprilysin (NEP) group of proteins. KEL has a crucial part in the production of the potent bioactive ET-3, which also includes enzymes that are endothelin convertingenzymes (PEX, XCE, DINE &various NEP-like proteins). KEL uses a single disulfide bond to XK, a gated membranal transporter. The Kell antigen system that includes two proteins, is very crucial among blood group systems.
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Synonyms
kell blood group antigen, kell blood group glycoprotein, Kell blood group, Kell blood group glycoprotein homolog, KEL, Kell, CD238 antigen, CD238, ECE3, Kell blood group-metalloendopeptidase, Kell blood group-metalloendopeptidase.
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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
ADPIFRNCGP CPCETPVCME LLDHYLASGN RSVAPCTDFF SFACEKANGT SDSFQALTEE NKSRLWRLLE APGSWHLGSG EEKAFQFYNS CMDTDAIEAS GSGPLIQIIE ELGGWNITGN WTSLDFNQNL RLLMSQYGHF PFFRAYLRPH PAPPHTPIIQ IDQPEFDILL QQEQEQKVYA QILREYVTYL NRLGTLLGSN PQEAQQHASW SIVFTSRLFQ FLRPQQQQQA QDKLFHVVTI DELQEMAPAI DWLSCLQAIF TPMSLNSSQT LVVHDLDYLR NMSQLVEEGL LNHRESIQSY MILGLVDTLS PALDTKFQEA RRELIQELRK LKERPPLPAY PRWMKCVEQT GAFFEPTLAA LFVREAFGPS IQSAAMELFA EIKDAVIIRL KKLSWISEET QKEALNKLAQ LQVEMGAPKR AVKPDIATQE YNDIQLGPSF LQSFLSCVRS LRARNVQSFL QPFPYHRWQK SPWEVNAYYS ISDHMVVFPA GLLQPPFFHP GYPRAVNFGA AGSIMAHELL HIFYQLLLPG GCPACDTHVL QEALLCLERH YAAFPLPSIS SFNGSHTLLE NAADIGGVAI AFQAYSKRIV EHTGELTLPN LDLSPYQLFF RSYAQVMCRG LSSQDPQDPH SPPSLRVHGP LSNTPDFAKH FHCPRGTLLN PSARCKLWHH HHHH.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
HPGDS HumanDescription:
Hematopoietic Prostaglandin D Synthase Human Recombinant
Hematopoietic prostaglandin D synthase, H-PGDS, GST class-sigma, Glutathione S-transferase, Glutathione-dependent PGD synthase, Glutathione-requiring prostaglandin D synthase, Prostaglandin-H2 D-isomerase, HPGDS, GSTS, PGDS, PTGDS2GSTS, PGD2, GSTS1-1.
Product # :
ENZ-616Price :
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Description
HPGDS Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 223 amino acids (1-199 a.a.) and having a molecular mass of 25.9kDa.HPGDS is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
HPGDS protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH8.0), 10% glycerol, 0.15M NaCl and 1mM DTT.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Citations
More Info
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Introduction
Hematopoietic Prostaglandin D Synthase (HPGDS) belongs to the sigma class glutathione-S-transferase family. The HPGDS enzyme catalyzes the conversion of PGH2 to PGD2 and has a role in the production of prostanoids in the immune system and mast cells. The presence of the HPGDS enzyme can be utilized to identify the differentiation stage of human megakaryocytes. Furthermore, HPGDS is a prostaglandin involved in smooth muscle contraction/relaxation and an effective inhibitor of platelet aggregation, and the conjugation of glutathione with a extensive range of aryl halides and organic isothiocyanates. In addition, HPGDS displays low glutathione-peroxidase activity towards cumene hydroperoxide. HPGDS is expressed in a number of megakaryocytic cell lines but not in platelets. HPGDS is highly expressed in the adipose tissue, macrophages and placenta; however it is expressed at lower levels in the lung, heart, lymph nodes, appendix, bone marrow and fetal liver.
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Synonyms
Hematopoietic prostaglandin D synthase, H-PGDS, GST class-sigma, Glutathione S-transferase, Glutathione-dependent PGD synthase, Glutathione-requiring prostaglandin D synthase, Prostaglandin-H2 D-isomerase, HPGDS, GSTS, PGDS, PTGDS2GSTS, PGD2, GSTS1-1.
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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
MGSSHHHHHH SSGLVPRGSH MGSHMPNYKL TYFNMRGRAE IIRYIFAYLD IQYEDHRIEQ ADWPEIKSTL PFGKIPILEV DGLTLHQSLA IARYLTKNTD LAGNTEMEQC HVDAIVDTLD DFMSCFPWAE KKQDVKEQMF NELLTYNAPH LMQDLDTYLG GREWLIGNSV TWADFYWEIC
STTLLVFKPD LLDNHPRLVT LRKKVQAIPA VANWIKRRPQ TKL.
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 :
DHFR MouseDescription:
Dihydrofolate Reductase Mouse Recombinant
Dihydrofolate reductase, DHFR, DHFRP1, AA607882, AI662710, AW555094, 8430436I03Rik.
Product # :
ENZ-069Price :
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Description
DHFR Mouse Recombinant fused with a 20 amino acid His tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 207 amino acids (1-187 a.a.) and having a molecular mass of 23.8kDa. The DHFR is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The DHFR solution (1 mg/ml) contains 20mM Tris-HCl buffer(pH 8.0), 10% glycerol, 2mM DTT and 0.1M NaCl.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Biological Activity
Specific activity is > 0.2 units/mg, in which one unit will convert 1.0 umole of 7,8 –dihydrofloate and beta-NADPH to 5,6,7,8-tetrahydrofloate and beta-NADP per min at pH 6.5 at 25C.Citations
More Info
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Introduction
Dihydrofolate reductase (DHFR) is an enzyme that reduces dihydrofolic acid to tetrahydrofolic acid, with NADPH as electron donor that can be converted to the kinds of tetrahydrofolate cofactors applied in 1-carbon transfer chemistry. DHFR converts dihydrofolate into tetrahydrofolate, which is a methyl group shuttle required for the de novo synthesis of purines, thymidylic acid, and specific amino acids. Even though the functional DHFR gene is mapped to chromosome 5, numerous intronless processed pseudogenes or dihydrofolate reductase-like genes are identified on separate chromosomes. DHFR deficiency is associated with megaloblastic anemia. DHFR knockdown plays a role in the anticancer activity of 2-hydroxyoleic acid. DHFR gene insertion/deletion polymorphism is linked to variation in serum and red blood cell folate concentrations in women.
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Synonyms
Dihydrofolate reductase, DHFR, DHFRP1, AA607882, AI662710, AW555094, 8430436I03Rik.
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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 MVRPLNCIVA VSQNMGIGKN GDLPWPPLRN EFKYFQRMTT TSSVEGKQNL VIMGRKTWFS IPEKNRPLKD RINIVLSREL KEPPRGAHFL AKSLDDALRL IEQPELASKV DMVWIVGGSS VYQEAMNQPG HLRLFVTRIM QEFESDTFFP EIDLGKYKLL PEYPGVLSEV QEEKGIKYKF EVYEKKD.
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 :
NUDT16L1 HumanDescription:
Nudix Type Motif 16 Like-1 Human Recombinant
Protein syndesmos, NUDT16-like protein 1, NUDT16L1, SDOS, MGC11275.
Product # :
ENZ-079Price :
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Description
NUDT16L1 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 231 amino acids (1-211 a.a.) and having a molecular mass of 25.5kDa. The NUDT16L1 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The NUDT16L1 solution (0.5 mg/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.
Citations
More Info
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Introduction
Syndesmos (NUDT16L1) is a cytoplasmic protein which interacts specifically with the cytoplasmic domain of syndecan-4, and co-localizes with syndecan-4 in focal contacts. NUDT16L1 interacts with the focal adhesion adaptor protein paxillin. The binding of NUDT16L1 to paxillin is direct, and these interactions are triggered by the activation of protein kinase C.
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Synonyms
Protein syndesmos, NUDT16-like protein 1, NUDT16L1, SDOS, MGC11275.
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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 MSTAAVPELK QISRVEAMRL GPGWSHSCHA MLYAANPGQL FGRIPMRFSV LMQMRFDGLL GFPGGFVDRR FWSLEDGLNR VLGLGLGCLR LTEADYLSSH LTEGPHRVVA HLYARQLTLE QLHAVEISAV HSRDHGLEVL GLVRVPLYTQ KDRVGGFPNF LSNAFVSTAK CQLLFALKVL NMMPEEKLVE ALAAATEKQK KALEKLLPAS S.
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 :
PLA2G12 HumanDescription:
Secreted Phospholipase A2-XII Human Recombinant
Group XIIA secretory phospholipase A2, EC 3.1.1.4, Phosphatidylcholine 2-acylhydrolase GXII, GXII sPLA2, PLA2G12, sPLA2-XII, PLA2G12A.
Product # :
ENZ-330Price :
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Shipping Method :
Shipped at Room temp
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Description
Secreted Phospholipase A2-XII Human Recombiannt was produced with N-terminal His-Tag. PLA2G12 His-Tagged Fusion Protein is 20.6 kDa containing 167 amino acid residues of the human secreted phospholipase A2-XII and 16 additional amino acid residues – His-Tag (underlined).
Source
Escherichia Coli.
Formulation
Filtered (0.4µm) and lyophilized from 0.5 mg/ml in 0.01M Tris buffer pH 8.6.
Purity
Greater than 95% as determined by SDS PAGE.
Citations
More Info
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Introduction
Phospholipase A2 (PLA2) catalyzes the hydrolysis of the sn-2 position of membrane glycerophospholipids to liberate arachidonic acid (AA), a precursor of eicosanoids including prostaglandins and leukotrienes. The same reaction also produces lysophosholipids, which represent another class of lipid mediators.
The secretory PLA2 (sPLA2) family, in which 10 isozymes have been identified, consists of low molecular weight, Ca2+-requiring secretory enzymes that have been implicated in a number of biological processes, such as modification of eicosanoid generation, inflammation, and host defense.
This enzyme has been proposed to hydrolyze phosphatidylcholine (PC) in lipoproteins to liberate lyso- PC and free fatty acids in the arterial wall, thereby facilitating the accumulation of bioactive lipids and modified lipoproteins in atherosclerotic foci.
In mice, sPLA2 expression significantly influences HDL particle size and composition and demonstrate that an induction of sPLA2 is required for the decrease in plasma HDL cholesterol in response to inflammatory stimuli. Instillation of bacteria into the bronchi was associated with surfactant degradation and a decrease in large:small ratio of surfactant aggregates in rats. -
Synonyms
Group XIIA secretory phospholipase A2, EC 3.1.1.4, Phosphatidylcholine 2-acylhydrolase GXII, GXII sPLA2, PLA2G12, sPLA2-XII, PLA2G12A.
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Physical Appearance
Filtered White lyophilized (freeze-dried) powder.
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Stability
Store lyophilized protein at -20°C. Aliquot the product after reconstitution to avoid repeated freezing/thawing cycles. Reconstituted protein can be stored at 4°C for a limited period of time; it does not show any change after two weeks at 4°C.
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Solubility
It is recommended to add deionized water to prepare a working stock solution of approximately 0.5mg/ml and let the lyophilized pellet dissolve completely. Product is not sterile! Please filter the product by an appropriate sterile filter before using it on cell culture.
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Amino Acid Sequence
MRGSHHHHHH GMASHMQEQA QTTDWRATLK TIRNGVHKID TYLNAALDLL GGEDGLCQYK CSDGSKPFPR YGYKPSPPNG CGSPLFGVHL NIGIPSLTKC CNQHDRCYET CGKSKNDCDE EFQYCLSKIC RDVQKTLGLTQ HVQACETTVE LLFDSVIHLG CKPYLDSQRA ACRCHYEEKT DL
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Applications
Western blotting.
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 :
PSMA3 HumanDescription:
Proteasome Subunit Alpha Type 3 Human Recombinant
proteasome (prosome, macropain) subunit alpha type-3, HC8, Macropain subunit C8, Multicatalytic endopeptidase complex subunit C8, Proteasome component C8, PSC3, PSC8, EC 3.4.25.1.
Product # :
ENZ-196Price :
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Description
PSMA3 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 275 amino acids (1-255) and having a molecular mass of 30.6 kDa.PSMA3 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
The PSMA3 solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 1mM DTT and 10% glycerol.
Purity
Greater than 95% as determined by SDS-PAGE.
Citations
More Info
-
Introduction
The proteasome is a multicatalytic proteinase complex which holds an extremely organized 20S core structure shaped like a ring. The central structure is assembled from 4 rings of 28 non-identical subunits; 2 rings are composed of 7 alpha subunits and 2 rings are composed of 7 beta subunits. There is a high concentration of proteasomes all over the eukaryotic cells and their job is to cleave peptides in an ATP/ubiquitin-dependent procedure in a non-lysosomal pathway. PSMA3 encodes several of the peptidase T1A family which is a 20S core alpha subunit. Two alternative transcripts encoding diverse isoforms were recognized.
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Synonyms
proteasome (prosome, macropain) subunit alpha type-3, HC8, Macropain subunit C8, Multicatalytic endopeptidase complex subunit C8, Proteasome component C8, PSC3, PSC8, EC 3.4.25.1.
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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 MSSIGTGYDL SASTFSPDGR VFQVEYAMKA VENSSTAIGI RCKDGVVFGV EKLVLSKLYE EGSNKRLFNV DRHVGMAVAG LLADARSLAD IAREEASNFR SNFGYNIPLK HLADRVAMYV HAYTLYSAVR PFGCSFMLGS YSVNDGAQLY MIDPSGVSYG YWGCAIGKAR QAAKTEIEKL QMKEMTCRDI VKEVAKIIYI VHDEVKDKAF ELELSWVGEL TNGRHEIVPK DIREEAEKYA KESLKEEDES DDDNM
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 :
BDNF HumanDescription:
Brain-Derived Neurotrophic Factor Human Recombinant
Brain-Derived Neurotrophic Factor, BDNF, MGC34632.
Product # :
CYT-207Price :
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Description
BDNF Human Recombinant produced in E.Coli is a homodimer, non-glycosylated, polypeptide chain containing 2 x 119 amino acids (and an N-terminal Met) and having a total molecular mass of 28kDa. BDNF Human Recombinant is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The protein was lyophilized with 20mM PB and 400mM NaCl, pH 7.2.
Purity
BDNF is greater than 950% as determined SDS-PAGE.
Biological Activity
The activity was determined using Immobilized Human TrkB-His tag protein 2ug/ml (100 μl/well) for its binding to NHS-Biotin BDNF. The ED50 of was found to be ≤20ng/mLActivity
Citations
More Info
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Introduction
BDNF promotes the survival of neuronal populations that are all located either in the central nervous system or directly connected to it. BDNF is a major regulator of synaptic transmission and plasticity at adult synapses in many regions of the cns. The versatility of BDNF is emphasized by its contribution to a range of adaptive neuronal responses including long-term potentiation (ltp), long-term depression (ltd), certain forms of short-term synaptic plasticity, as well as homeostatic regulation of intrinsic neuronal excitability.
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Synonyms
Brain-Derived Neurotrophic Factor, BDNF, MGC34632.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized BDNF although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution BDNF should be stored at 4°C between 2-7 days and for future use below -18°C.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.
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Solubility
It is recommended to reconstitute the lyophilized BDNF in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
HSDPARRGE LSVCDSISEW VTAADKKTAV DMSGGTVTVL EKVPVSKGQL KQYFYETKCN PMGYTKEGCR GIDKRHWNSQ CRTTQSYVRA LTMDSKKRIG WRFIRIDTSC VCTLTIKRGR.
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Background
Final Thoughts
Although more research is needed on the safety and effectiveness of BDNF human recombinant, trials suggest that this laboratory-produced protein may be effective in managing and treating several neurological and psychiatric disorders. It's important for experts to stay up to date on the latest developments and research to learn more about potential risks and benefits.
What is the molecular weight/Mw of BDNF Protein?
BDNF Protein has a total Mw of 27kDa.
What is the source or expression system of BDNF Protein?
Escherichia Coli.
What is the Purity of BDNF Protein?
BDNF Protein is >97% pure as determined by SDS-PAGE.
What is the Biological Activity of BDNF Protein?
The ED50, as determined by the dose-dependent induction of C6 cells proliferation, is 1.3-2µg/ml.
What is the amino acid sequence of BDNF Protein?
MHSDPARRGE LSVCDSISEW VTAADKKTAV DMSGGTVTVL EKVPVSKGQL KQYFYETKCN PMGYTKEGCR GIDKRHWNSQ CRTTQSYVRA LTMDSKKRIG WRFIRIDTSC VCTLTIKRGR.
What applications can BDNF Protein be used in?
BDNF Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for BDNF Protein?
The endotoxin level is minimal, BDNF Protein was purified using conventional chromatography techniques.
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Protein content
BDNF quantitation was carried out by two independent methods:1. UV spectroscopy at 280 nm using the absorbency value of 1.6 as the extinction coefficient for a 0.1% (1mg/ml) solution. This value is calculated by the PC GENE computer analysis program of protein sequences (IntelliGenetics). 2. Analysis by RP-HPLC, using a standard solution of Brain-derived Neurotrophic Factor as a Reference Standard.
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 :
PMSGDescription:
Pregnant Mare Serum Gonadotropin
Product # :
HOR-272Price :
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Description
PMSG is a complex glycoprotein obtained from the serum of pregnant mares. This 43-63 kda protein is capable of supplementing and being substituted for the follicle stimulating and interstitial cell-stimulating hormone of the anterior pituitary gland in both the male and female. Thus PMSG-Intervet stimulates development of the ovarian follicle in the female.
Source
Serum of pregnant mares.
Formulation
The PMSG was lyophilized with no additives.
Citations
More Info
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Introduction
PMSG Hormone is a well know used hormone together with progestogen to increase ovulation just before to artificial insemination. PMSG hormone is a placental glycoprotein produced from the serum of pregnant mares. PMSG comprises of an alfa subunit and a beta subunit. PMSG hormone is secreted from endometrial cups within the pregnant mare uterus aging from 40 to 130 days into their maturation, and once extracted, it can been used to promote artificially estrus in female animals. These assemblies produce PMSG hormone to induce mare's ovarian and repsouctive structures. PMSG can induce the growth of follicles by ovaries and results in ovulatation. PMSG hormone has an about a 4 day half-life of bioactivity in species other than horses. The extended biological activity can cause ovarian stimulation and ovulation. However, PMSG use alone often causes cystic ovarian disease because of the unrestrained ovarian stimulation and due to the sugar molecules which decrease clearance of the hormone. PMSG is more likely to be used than other pituitary hormones due to the extended circulatory half-life. PMSG solely exhibits luteinizing hormone like activity, however in other animal classes it has FSH & LH like activity.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized PMSG although stable at room temperature for 3 weeks, should be stored between 2-8°C.
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Solubility
It is recommended to reconstitute the lyophilized PMSG in sterile 18M-cm H2O at a concentration of 1000 IU/ml, which can then be further diluted to other aqueous solutions.
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 :
ENTPD3 HumanDescription:
Ectonucleoside Triphosphate Diphosphohydrolase 3 Human Recombinant
Ectonucleoside Triphosphate Diphosphohydrolase 3, CD39L3, Ecto-ATP Diphosphohydrolase 3, CD39 Antigen-Like 3, Ecto-ATPDase 3, Ecto-Apyrase 3, Ecto-ATPase 3, EC 3.6.1.5, NTPDase 3, HB6, NTPDase-3.
Product # :
ENZ-844Price :
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Description
ENTPD3 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 465 amino acids (44-485 a.a) and having a molecular mass of 52kDa. ENTPD3 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
ENTPD3 protein solution (0.25mg/ml) containing 20mM Tris-HCl buffer (pH 8.0) and 10% glycerol.
Purity
Greater than 85.0% as determined by SDS-PAGE.
Citations
More Info
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Introduction
Ectonucleoside Triphosphate Diphosphohydrolase 3, also known as ENTPD3, which owns a threefold preference for the hydrolysis of ATP over ADP is similar to E-type nucleotidases (NTPases). ENTPD3 is a protein coding gene which contains four apyrase-conserved areas which is characteristic of NTPases.
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Synonyms
Ectonucleoside Triphosphate Diphosphohydrolase 3, CD39L3, Ecto-ATP Diphosphohydrolase 3, CD39 Antigen-Like 3, Ecto-ATPDase 3, Ecto-Apyrase 3, Ecto-ATPase 3, EC 3.6.1.5, NTPDase 3, HB6, NTPDase-3.
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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 MGSQIHKQEV LPPGLKYGIV LDAGSSRTTV YVYQWPAEKE NNTGVVSQTF KCSVKGSGIS SYGNNPQDVP RAFEECMQKV KGQVPSHLHG STPIHLGATA GMRLLRLQNE TAANEVLESI QSYFKSQPFD FRGAQIISGQ EEGVYGWITA NYLMGNFLEK NLWHMWVHPH GVETTGALDL GGASTQISFV AGEKMDLNTS DIMQVSLYGY VYTLYTHSFQ CYGRNEAEKK FLAMLLQNSP TKNHLTNPCY PRDYSISFTM GHVFDSLCTV DQRPESYNPN DVITFEGTGD PSLCKEKVAS IFDFKACHDQ ETCSFDGVYQ PKIKGPFVAF AGFYYTASAL NLSGSFSLDT FNSSTWNFCS QNWSQLPLLL PKFDEVYARS YCFSANYIYH LFVNGYKFTE ETWPQIHFEK EVGNSSIAWS LGYMLSLTNQ IPAESPLIRL PIEPP.
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 :
ENTPD3 Human, sf9Description:
Ectonucleoside Triphosphate Diphosphohydrolase 3 Human Recombinant, sf9
Ectonucleoside Triphosphate Diphosphohydrolase 3, CD39L3, Ecto-ATP Diphosphohydrolase 3, CD39 Antigen-Like 3, Ecto-ATPDase 3, Ecto-Apyrase 3, Ecto-ATPase 3, EC 3.6.1.5, NTPDase 3, HB6, NTPDase-3.
Product # :
ENZ-958Price :
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Description
ENTPD3 Human Recombinant produced in in Sf9 Baculovirus cells is a single, non-glycosylated polypeptide chain containing 451 amino acids (44-485a.a) and having a molecular mass of 50.7kDa (Migrates at 50-70kDa on SDS-PAGE under reducing conditions). ENTPD3 is fused to a 6 amino acids His-tag at C-Terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
ENTPD3 protein solution (0.5mg/ml) containing Phosphate Buffered Saline (pH 7.4) and 10% glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
Citations
More Info
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Introduction
Ectonucleoside Triphosphate Diphosphohydrolase 3, also known as ENTPD3, which owns a threefold preference for the hydrolysis of ATP over ADP is similar to E-type nucleotidases (NTPases). ENTPD3 is a protein coding gene which contains four apyrase-conserved areas which is characteristic of NTPases.
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Synonyms
Ectonucleoside Triphosphate Diphosphohydrolase 3, CD39L3, Ecto-ATP Diphosphohydrolase 3, CD39 Antigen-Like 3, Ecto-ATPDase 3, Ecto-Apyrase 3, Ecto-ATPase 3, EC 3.6.1.5, NTPDase 3, HB6, NTPDase-3.
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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
ADLQIHKQEV LPPGLKYGIV LDAGSSRTTV YVYQWPAEKE NNTGVVSQTF KCSVKGSGIS SYGNNPQDVP RAFEECMQKV KGQVPSHLHG STPIHLGATA GMRLLRLQNE TAANEVLESI QSYFKSQPFD FRGAQIISGQ EEGVYGWITA NYLMGNFLEK NLWHMWVHPH GVETTGALDL GGASTQISFV AGEKMDLNTS DIMQVSLYGY VYTLYTHSFQ CYGRNEAEKK FLAMLLQNSP TKNHLTNPCY PRDYSISFTM GHVFDSLCTV DQRPESYNPN DVITFEGTGD PSLCKEKVAS IFDFKACHDQ ETCSFDGVYQ PKIKGPFVAF AGFYYTASAL NLSGSFSLDT FNSSTWNFCS QNWSQLPLLL PKFDEVYARS YCFSANYIYH LFVNGYKFTE ETWPQIHFEK EVGNSSIAWS LGYMLSLTNQ IPAESPLIRL PIEPPHHHHHH.
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 :
MMP 3 Human, HEKDescription:
Matrix Metalloproteinase-3 Human Recombinant, HEK
Stromelysin-1, EC 3.4.24.17, Matrix metalloproteinase-3, MMP-3, Transin-1, SL-1, STMY, STR1, STMY1, MGC126102, MGC126103, MGC126104.
Product # :
ENZ-284Price :
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Description
MMP-3 Human Recombinant produced in HEK293 cells is a proform of the Human MMP3 [Tyr18-Cys477 (Lys45Glu)] and fused with a ployhistide tag at the C-terminus, having an Mw of 52kDa. MMP-3 is purified by proprietary chromatographic techniques.
Source
HEK293 cells.
Formulation
The MMP-3 is supplied as a 0.2µm filtered solution in 20mM Tris-HCl, 150mM NaCl and 0.05% Brij35, pH 7.5.
Purity
Greater than 95% as determined by SDS-PAGE.
Biological Activity
The activity was measured by its ability to cleave the fluorogenic peptide substrate, Mca-RPKPVE-Nval-WRK(Dnp)-NH2. The specific activity is > 150 pmoles/min/µg.
Recombinant Human MMP-3 protein pro form needs to be activated with Chymotrypsin.
Activation Protocol:
1. Dilute MMP3 to 20µg/ml in the Assay Buffer: 50mM Tris, 10mM CaCl2, 150mM NaCl, 0.05% (w/v) and Brij 35, pH 7.5.
2. Activate MMP3 by adding Chymotrypsin(Sigma, Catalog#C3142,1mg/ml stock in 1mM HCl) to a final concentration of 5ug/ml.
3. Incubate at 37°C for 30 minutes.
4. Stop activation with 2mM PMSF. Pre-warm the PMSF to 37°C prior to adding to sample.sds-page
Citations
More Info
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Introduction
MMP-3 enzyme is also known as Stromelysin-1or as Transin-1 which hydrolyzes natural collagen at physiological pH and temperature. It dissolves the intervertebral nucleus pulposus and annulus fibrosus of Herniated Lumbar Intervertebral Disk . MMP-3 hydrolyzes components of the extracellular matrix like proteoglycan, laminin, fibronectin, gelatin and collagen types III, IV and IX. It also activates pro-MMP-9 and pro-MMP-8 and superactivates plasmin activated MMP-1. MMP-3 is secreted as a latent proenzyme and is activated by a variety of proteinases, e.g. plasmin, trypsin, chymotrypsin, cathepsin G or human neutrophil elastase. MMP-3 was found to be capable of activating the precursor of IL1-beta.
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Synonyms
Stromelysin-1, EC 3.4.24.17, Matrix metalloproteinase-3, MMP-3, Transin-1, SL-1, STMY, STR1, STMY1, MGC126102, MGC126103, MGC126104.
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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.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 :
DHRS9 HumanDescription:
Dehydrogenase/Reductase Member 9 Human Recombinant
Dehydrogenase/reductase SDR family member 9, 3-alpha hydroxysteroid dehydrogenase, 3-alpha-HSD, NADP-dependent retinol dehydrogenase/reductase, RDH-E2, RDHL, Short-chain dehydrogenase/reductase retSDR8, DHRS9, RDH15, RDHTBE, SDR9C4, RETSDR8, 3ALPHA-HSD.
Product # :
ENZ-216Price :
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Description
DHRS9 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 327 amino acids (18-319) and having a molecular mass of 35.9kDa.DHRS9 is fused to a 21 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The DHRS9 solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH8.0), 20% glycerol, 0.1M NaCl, 1mM DTT and 0.1mM PMSF.
Purity
Greater than 90.0% as determined by SDS-PAGE.
Citations
More Info
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Introduction
Dehydrogenase/reductase SDR family member 9 (DHRS9) functions as a homotetramer, which converts both 3-alpha-tetrahydroprogesterone (allopregnanolone) and 3-alpha-androstanediol to dihydroxyprogesterone and is believed to have a part in retinoic acid biosynthesis.
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Synonyms
Dehydrogenase/reductase SDR family member 9, 3-alpha hydroxysteroid dehydrogenase, 3-alpha-HSD, NADP-dependent retinol dehydrogenase/reductase, RDH-E2, RDHL, Short-chain dehydrogenase/reductase retSDR8, DHRS9, RDH15, RDHTBE, SDR9C4, RETSDR8, 3ALPHA-HSD.
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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 MGSHMRKGKL KIEDITDKYI FITGCDSGFG NLAARTFDKK GFHVIAACLT ESGSTALKAE TSERLRTVLL DVTDPENVKR TAQWVKNQVG EKGLWGLINN AGVPGVLAPT DWLTLEDYRE PIEVNLFGLI SVTLNMLPLV KKAQGRVINV SSVGGRLAIV GGGYTPSKYA VEGFNDSLRR DMKAFGVHVS CIEPGLFKTN LADPVKVIEK KLAIWEQLSP DIKQQYGEGY IEKSLDKLKG NKSYVNMDLS PVVECMDHAL TSLFPKTHYA AGKDAKIFWI PLSHMPAALQ DFLLLKQKAE LANPKAV.
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 :
LIPG Human, HEKDescription:
Lipase Endothelial Human Recombinant, HEK
LIPG, Lipase Endothelial, EDL, EL, Endothelial Cell-Derived Lipase, EC 3.1.1.3, PRO719, Endothelial Lipase, Lipoprotein Lipase H, EC 3.1.1.
Product # :
ENZ-810Price :
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Shipping Method :
Shipped at Room temp
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Description
LIPG Human Recombinant produced in HEK cells is a single, glycosylated, polypeptide chain (Ser21-Pro500) containing a total of 490 amino acids, having a calculated molecular mass of 55.8kDa. LIPG is fused to a 2 aa N-terminal linker, a 2 aa C-terminal linker and a 6 aa His tag at C-Terminus.
Source
HEK 293.
Formulation
LIPG was filtered (0.4 µm) and lyophilized from a solution in phosphate buffered saline pH 7.5 (PBS), 1% (w/v) Sucrose and 4% (w/v) Mannitol.
Purity
Greater than 85.0% as determined by SDS-PAGE.
Citations
More Info
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Introduction
Lipase Endothelial (LIPG) has extensive phospholipase activity and may be involved in lipoprotein metabolism and vascular biology. The LIPG protein is considered a member of the TG lipase family through its sequence and characteristic lid region which provides substrate specificity for enzymes of the TG lipase family. In addition, the LIPG has triglyceride lipase activities. LIPG hydrolyzes HDLs more efficiently than other lipoproteins. LIPG also binds heparin.
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Synonyms
LIPG, Lipase Endothelial, EDL, EL, Endothelial Cell-Derived Lipase, EC 3.1.1.3, PRO719, Endothelial Lipase, Lipoprotein Lipase H, EC 3.1.1.
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Physical Appearance
Filtered White lyophilized (freeze-dried) powder.
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Stability
Store lyophilized protein at -20°C. Aliquot the product after reconstitution to avoid repeated freezing/thawing cycles. Reconstituted protein can be stored at 4°C for a limited period of time; it does not show any change after two weeks at 4°C.
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Solubility
It is recommended to add deionized water to prepare a working stock solution of approximately 0.5 mg/ml and let the lyophilized pellet dissolve completely. LIPG is not sterile! Please filter the product by an appropriate sterile filter before using it in the cell culture.
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Amino Acid Sequence
ASSPVPFGPE GRLEDKLHKP KATQTEVKPS VRFNLRTSKD PEHEGCYLSV GHSQPLEDCS FNMTAKTFFI IHGWTMSGIF ENWLHKLVSA LHTREKDANV VVVDWLPLAH QLYTDAVNNT RVVGHSIARM LDWLQEKDDF SLGNVHLIGY SLGAHVAGYA GNFVKGTVGR ITGLDPAGPM FEGADIHKRL SPDDADFVDV LHTYTRSFGL SIGIQMPVGH IDIYPNGGDF QPGCGLNDVL GSIAYGTITE VVKCEHERAV HLFVDSLVNQ DKPSFAFQCT DSNRFKKGIC LSCRKNRCNS IGYNAKKMRN KRNSKMYLKT RAGMPFRVYH YQMKIHVFSY KNMGEIEPTF YVTLYGTNAD SQTLPLEIVE RIEQNATNTF LVYTEEDLGD LLKIQLTWEG ASQSWYNLWK EFRSYLSQPR NPGRELNIRR IRVKSGETQR KLTFCTEDPE NTSISPGREL WFRKCRDGWR MKNETSPTVE LP KLHHHHHH.
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 :
PRTN3 HumanDescription:
Proteinase-3 Human
AGP7, P29, PR-3, ACPA, C-ANCA, MBT, MBN, Leukocyte proteinase 3, Neutrophil proteinase 4, Wegener granulomatosis autoantigen, Azurophil granule protein 7, myeloblastin, Serine proteinase neutrophil.
Product # :
ENZ-075Price :
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Description
PRTN3 is a natural antigen having a molecular mass of 25kDa. PRTN3 is isolated from human peripheral blood leukocytes.
Source
Native.
Formulation
PRTN3 is supplied in 20mM Sodium Phosphate pH-6.2, 300mM NaCl, and 0.02% Lubrol.
Purity
Greater than 95% in the sum of different glycosylation isoforms according to following section as determined by SDS-PAGE and capillary electrophoresis.
Citations
More Info
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Introduction
PRTN3 is a polymorphonuclear leukocyte serine protease which degrades elastin, fibronectin, laminin, vitronectin, and collagen types I, III, and IV (in vitro) and causes emphysema once managed by tracheal insufflation to hamsters.
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Synonyms
AGP7, P29, PR-3, ACPA, C-ANCA, MBT, MBN, Leukocyte proteinase 3, Neutrophil proteinase 4, Wegener granulomatosis autoantigen, Azurophil granule protein 7, myeloblastin, Serine proteinase neutrophil.
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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.
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Immunological Functions
1. Binds IgG-type human auto-antibodies. Auto-antibodies to PR3 recognize conformation-dependent epitopes. 2. Standard ELISA test (checker-board analysis of positive/negative samples), immunodot analysis with positive/negative samples.
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coating concentration
0.5-1.0 µg/ml (depending on the type of ELISA plate and coating buffer). Suitable for labeling of functional groups.
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Applications
Western blot with rabbit anti-PR3 antisera and mouse anti-PR3 monoclonal antibodies.
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 :
GPT MouseDescription:
Glutamic-Pyruvate Transaminase Mouse Recombinant
Alanine aminotransferase 1, ALT1, Glutamate pyruvate transaminase 1, GPT 1, Glutamic--alanine transaminase 1, Glutamic--pyruvic transaminase 1.
Product # :
ENZ-1030Price :
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Description
GPT Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 519 amino acids (1-496 a.a) and having a molecular mass of 57.5kDa.GPT is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
GPT protein solution (0.5mg/ml) containing Phosphate Buffered Saline (pH7.4), 1mM DTT and 10% glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
Biological Activity
Specific activity is > 40units/mg, and is defined as the amount of enzyme that convert 1umole of L-Alanine to L-Glutamate per minute at pH 7.5 at 37C.
Citations
More Info
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Introduction
GPT catalyzes the reversible transamination between alanine and 2-oxoglutarate to create pyruvate and glutamate. GPT has a crucial part in the intermediary metabolism of glucose and amino acids. GPT is broadly used as an indicator of liver reliability or hepatocellular destruction in clinical tests.
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Synonyms
Alanine aminotransferase 1, ALT1, Glutamate pyruvate transaminase 1, GPT 1, Glutamic--alanine transaminase 1, Glutamic--pyruvic transaminase 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
MGSSHHHHHH SSGLVPRGSH MGSMASQRND RIQASRNGLK GKVLTLDTMN PCVRRVEYAV RGPIVQRALE LEQELRQGVK KPFTEVIRAN IGDAQAMGQR PITFFRQVLA LCVYPNLLSS PDFPEDAKRR AERILQACGG HSLGAYSISS GIQPIREDVA QYIERRDGGI PADPNNIFLS TGASDAIVTM LKLLVAGEGR ARTGVLIPIP QYPLYSAALA ELDAVQVDYY LDEERAWALD IAELRRALCQ ARDRCCPRVL CVINPGNPTG QVQTRECIEA VIRFAFEEGL FLMADEVYQD NVYAEGSQFH SFKKVLTEMG PPYATQQELA SFHSVSKGYM GECGFRGGYV EVVNMDAEVQ KQMAKLMSVR LCPPVPGQAL MGMVVSPPTP SEPSFKQFQA ERQEVLAELA AKAKLTEQVF NEAPGIRCNP VQGAMYSFPQ IQLPLKAVQR AQDLGLAPDM FFCLCLLEET GICVVPGSGF GQQEGTYHFR MTILPPMEKL RVLLEKLRHF HAKFTHEYS.
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 :
GSR HumanDescription:
Glutathione Reductase Human Recombinant
Glutathione reductase mitochondrial, GR, GRase, GSR, GLUR, GRD1.
Product # :
ENZ-202Price :
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Description
GSR Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 504 amino acids (43-522) and having a molecular mass of 54.3kDa.GSR is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The GSR solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 1mM DTT, 10% glycerol and 0.1M NaCl.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Biological Activity
Specific activity: > 29 unit/ml.
One unit will reduce 1.0 umol of oxidized glutathione per minute at pH 7.5 at 25°C.Citations
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Introduction
Glutathione reductase (GSR) belongs to the class-I pyridine nucleotide-disulfide oxidoreductase family. The GSR enzyme is a homodimeric flavoprotein and has a role in maintaining glutathione (GSH) in its reduced form by catalyzing the reduction of glutathione disulfide (GSSG): GSSG + NADPH + H+ ->2GSH + NADP+. In the majority of eukaryotic cells, GSR upholds the ratio of [GSH] / [GSSG], and partakes in quite a few critical functions such as the detoxification of reactive oxygen species as well as protein and DNA biosynthesis.
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Synonyms
Glutathione reductase mitochondrial, GR, GRase, GSR, GLUR, GRD1.
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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 MGSMAMACRQ EPQPQGPPPA AGAVASYDYL VIGGGSGGLA SARRAAELGA RAAVVESHKL GGTCVNVGCV PKKVMWNTAV HSEFMHDHAD YGFPSCEGKF NWRVIKEKRD AYVSRLNAIY QNNLTKSHIE IIRGHAAFTS DPKPTIEVSG KKYTAPHILI
ATGGMPSTPH ESQIPGASLG ITSDGFFQLE ELPGRSVIVG AGYIAVEMAG ILSALGSKTS LMIRHDKVLR SFDSMISTNC TEELENAGVE VLKFSQVKEV KKTLSGLEVS MVTAVPGRLP VMTMIPDVDC LLWAIGRVPN TKDLSLNKLG IQTDDKGHII VDEFQNTNVK GIYAVGDVCG
KALLTPVAIA AGRKLAHRLF EYKEDSKLDY NNIPTVVFSH PPIGTVGLTE DEAIHKYGIE NVKTYSTSFT PMYHAVTKRK TKCVMKMVCA NKEEKVVGIH MQGLGCDEML QGFAVAVKMG ATKADFDNTV AIHPTSSEEL VTLR.
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.