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1000 results found for “Aldolase”
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Name :
NANP HumanDescription:
N-Acetylneuraminic Acid Phosphatase Human Recombinant
N-acylneuraminate-9-phosphatase, Haloacid dehalogenase-like hydrolase domain-containing protein 4, Neu5Ac-9-Pase, NANP, HDHD4, MGC26833, C20orf147, dJ694B14.3.
Product # :
ENZ-009Price :
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Shipped with Ice Packs
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Description
NANP Human Recombinant fused with a 36 amino acid His tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 284 amino acids (1-248 a.a.) and having a molecular mass of 31.9kDa. The NANP is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The NANP solution (0.5 mg/ml) contains 20mM Tris-HCl buffer (pH8.0) containing 10% glycerol, 2mM DTT and 100mM NaCl.
Purity
Greater than 90.0% as determined by SDS-PAGE.
Citations
More Info
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Introduction
N-acylneuraminate-9-phosphatase (NANP) belongs to the haloacid dehalogenase (HAD) family and is responsible for dephosphorylating N-acylneuraminate 9-phosphate to form N-acylneuraminate (N-acylneuraminate 9-phosphate + H2O = N-acylneuraminate + phosphate). The catalytic activity of NANP is relies on the presence of magnesium and is inhibited by vanadate and calcium, which is typical of the HAD phosphatase family.
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Synonyms
N-acylneuraminate-9-phosphatase, Haloacid dehalogenase-like hydrolase domain-containing protein 4, Neu5Ac-9-Pase, NANP, HDHD4, MGC26833, C20orf147, dJ694B14.3.
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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
MRGSHHHHHH GMASMTGGQQ MGRDLYDDDD KDRWGSMGLS RVRAVFFDLD NTLIDTAGAS RRGMLEVIKL LQSKYHYKEE AEIICDKVQV KLSKECFHPY NTCITDLRTS HWEEAIQETK GGAANRKLAE ECYFLWKSTR LQHMTLAEDV KAMLTELRKE VRLLLLTNGD RQTQREKIEA CACQSYFDAV VVGGEQREEK PAPSIFYYCC NLLGVQPGDC VMVGDTLETD IQGGLNAGLK ATVWINKNGI VPLKSSPVPH YMVSSVLELP ALLQSIDCKV SMST.
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 :
DHPS HumanDescription:
Deoxyhypusine Synthase Human Recombinant
MIG13, EC 2.5.1.46, Deoxyhypusine synthase, DHS, DHPS, DS.
Product # :
ENZ-498Price :
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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.
Citations
More Info
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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.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA). Please avoid freeze-thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH 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.
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Name :
BPHL HumanDescription:
Biphenyl Hydrolase-Like Human Recombinant
Biphenyl Hydrolase-Like (serine hydrolase), Bph-rp, Breast Epithelial Mucin-Associated Antigen, MCNAA, VACVASE, MGC41865, MGC125930.
Product # :
ENZ-055Price :
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Description
BPHL produced in E.Coli is a single, non-glycosylated polypeptide chain containing 275 amino acids (38-291a.a.) and having a molecular mass of 31.1kDa.BPHL is fused to a 21 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The BPHL protein solution (0.5mg/1ml) is formulated in 20mM Tris-HCl buffer (pH8.0)
1mM DTT, 50mM NaCl and 10% glycerol.Purity
Greater than 95% as determined by SDS-PAGE.
Citations
More Info
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Introduction
BPHL is a Serine hydrolase that is a part of the AB hydrolase superfamily which catalyzes the hydrolytic activation of amino acid ester prodrugs of nucleoside analogs. BPHL is expressed large quantities in liver and kidney and in minor quantities in heart, intestine and skeletal muscle. BPHL takes part in detoxification processes and is a specific alpha-amino acid ester hydrolase which favors small, hydrophobic, and aromatic side chains and does not have a strict necessity for the leaving group except for favoring a primary alcohol.
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Synonyms
Biphenyl Hydrolase-Like (serine hydrolase), Bph-rp, Breast Epithelial Mucin-Associated Antigen, MCNAA, VACVASE, MGC41865, MGC125930.
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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.Please avoid freeze thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MSVTSAKVAV NGVQLHYQQT GEGDHAVLLL PGMLGSGETD FGPQLKNLNK KLFTVVAWDP RGYGHSRPPD RDFPADFFER DAKDAVDLMK ALKFKKVSLL GWSDGGITAL IAAAKYPSYI HKMVIWGANA YVTDEDSMIY EGIRDVSKWS ERTRKPLEAL YGYDYFARTC EKWVDGIRQF KHLPDGNICR HLLPRVQCPA LIVHGEKDPL VPRFHADFIH KHVKGSRLHL MPEGKHNLHL RFADEFNKLA EDFLQ
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 :
FBP1 HumanDescription:
Fructose-1,6-Bisphosphatase 1 Human Recombinant
FBP1, FBP, D-fructose-1,6-bisphosphate 1-phosphohydrolase 1, FBPase 1, Fructose-1,6-bisphosphatase 1.
Product # :
ENZ-454Price :
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Shipped with Ice Packs
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Description
The FBP1 Human recombinant protein is a single, non-glycosilated polypeptide chain produced in E. coli, having a molecular weight of 39kDa and containing 358 amino acids (1-338 a.a.). The FBP1 enzyme is fused to a 20 amino acid His-Tag at N-terminus and purified by proprietary chromatography techniques.
Source
Escherichia Coli.
Formulation
The FBP1 protein solution is formulated in 20mM Tris-HCl pH-8, 1mM DTT and 10% glycerol.
Purity
Greater than 90% as determined by SDS-PAGE.
Citations
More Info
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Introduction
FBP1 is a gluconeogenesis regulatory protein which catalyzes the hydrolysis of fructose 1,6-bisphosphate to fructose 6-phosphate and inorganic phosphate. FBP1 deficiency is associated with hypoglycemia and metabolic acidosis. FBP1 regulates mouse endogenous glucose production. FBP1 coupled with phosphofructokinase (PFK) takes part in the metabolism of pancreatic islet cells.
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Synonyms
FBP1, FBP, D-fructose-1,6-bisphosphate 1-phosphohydrolase 1, FBPase 1, Fructose-1,6-bisphosphatase 1.
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Physical Appearance
Sterile Filtered clear solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MADQAPFDTD VNTLTRFVME EGRKARGTGE LTQLLNSLCT AVKAISSAVR KAGIAHLYGI AGSTNVTGDQ VKKLDVLSND LVMNMLKSSF ATCVLVSEED KHAIIVEPEK RGKYVVCFDP LDGSSNIDCL VSVGTIFGIY RKKSTDEPSE KDALQPGRNL VAAGYALYGS ATMLVLAMDC GVNCFMLDPA IGEFILVDKD VKIKKKGKIY SLNEGYARDF DPAVTEYIQR KKFPPDNSAP YGARYVGSMV ADVHRTLVYG GIFLYPANKK SPNGKLRLLY ECNPMAYVME KAGGMATTGK EAVLDVIPTD IHQRAPVILG SPDDVLEFLK VYEKHSAQ.
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 :
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 :
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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.
Citations
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.
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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 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.
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Name :
GALE HumanDescription:
UDP-Galactose-4-Epimerase Human Recombinant
UDP-glucose 4-epimerase, EC=5.1.3.2, Galactowaldenase, UDP-galactose 4 epimerase, GALE, SDR1E1, FLJ95174, FLJ97302.
Product # :
ENZ-537Price :
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Shipped with Ice Packs
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Description
GALE Recombinant Human produced in E.Coli is a single, non-glycosylated polypeptide chain containing 368 amino acids (1-348 a.a.) and having a molecular mass of 40.4 kDa. The GALE is fused to a 20 amino acids His-Tag at N-terminus and purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
GALE Human solution containing 20mM Tris pH-8, 5mM DTT, 0.1M NaCl, 1mM EDTA & 10% glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Citations
More Info
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Introduction
GALE is an enzyme that participates as the third enzyme in the Leloir pathway of galactose metabolism. GALE is a homodimeric epimerase localized in bacterial, plant, and mammalian cells. GALE inhances the reverse chemical reaction, the conversion of UDP-glucose to UDP-galactose. UDP-galactose builds galactose-containing proteins and fats, which have a crucial part in chemical signaling, building cellular structures, transporting molecules, and producing energy.
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Synonyms
UDP-glucose 4-epimerase, EC=5.1.3.2, Galactowaldenase, UDP-galactose 4 epimerase, GALE, SDR1E1, FLJ95174, FLJ97302.
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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 MAEKVLVTGG AGYIGSHTVL ELLEAGYLPV VIDNFHNAFR GGGSLPESLR RVQELTGRSV EFEEMDILDQ GALQRLFKKY SFMAVIHFAG LKAVGESVQK PLDYYRVNLT GTIQLLEIMK AHGVKNLVFS SSATVYGNPQ YLPLDEAHPT GGCTNPYGKS KFFIEEMIRD LCQADKTWNA VLLRYFNPTG AHASGCIGED PQGIPNNLMP YVSQVAIGRR EALNVFGNDY DTEDGTGVRD YIHVVDLAKG HIAALRKLKE QCGCRIYNLG TGTGYSVLQM VQAMEKASGK KIPYKVVARR EGDVAACYAN PSLAQEELGW TAALGLDRMC EDLWRWQKQN PSGFGTQA.
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 :
GCLM HumanDescription:
Glutamate-Cysteine Ligase, Modifier Subunit Human Recombinant
Glutamate--cysteine ligase regulatory subunit, GCS light chain, Gamma-ECS regulatory subunit, Gamma-glutamylcysteine synthetase regulatory subunit, Glutamate--cysteine ligase modifier subunit, GCLM, GLCLR.
Product # :
ENZ-636Price :
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Description
GCLM Human Recombinant produced in E. coli is a single polypeptide chain containing 298 amino acids (1-274) and having a molecular mass of 33.3kDa.GCLM is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The GCLM solution (1mg/ml) contains 20mM Tris-HCl buffer (pH8.0), 10% glycerol and 0.15M NaCl.
Purity
Greater than 90.0% as determined by SDS-PAGE.
Citations
More Info
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Introduction
Glutamate-cysteine ligase (GCLM) is the first rate limiting enzyme of glutathione synthesis. The GCLM enzyme is comprised of 2 subunits, a heavy catalytic subunit and a light regulatory subunit. GCLM deficiency is associated with some forms of hemolytic anemia.
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Synonyms
Glutamate--cysteine ligase regulatory subunit, GCS light chain, Gamma-ECS regulatory subunit, Gamma-glutamylcysteine synthetase regulatory subunit, Glutamate--cysteine ligase modifier subunit, GCLM, GLCLR.
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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 MGSHMGTDSR AAKALLARAR TLHLQTGNLL NWGRLRKKCP STHSEELHDC IQKTLNEWSS QINPDLVREF PDVLECTVSH AVEKINPDER EEMKVSAKLF IVESNSSSST RSAVDMACSV LGVAQLDSVI IASPPIEDGV NLSLEHLQPY WEELENLVQS KKIVAIGTSD LDKTQLEQLY QWAQVKPNSN QVNLASCCVM PPDLTAFAKQ FDIQLLTHND PKELLSEASF QEALQESIPD IQAHEWVPLW LLRYSVIVKS RGIIKSKGYI LQAKRRGS.
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 :
GGPS1 HumanDescription:
Geranylgeranyl Diphosphate Synthase 1 Human Recombinant
GGPPS, GGPPS1, GGPP synthetase.
Product # :
ENZ-555Price :
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Shipped with Ice Packs
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Description
GGPS1 Recombinant Human produced in E.Coli is a single, non-glycosylated polypeptide chain containing 320 amino acids (1-300 a.a.) and having a molecular mass of 37 kDa. The GGPS1 is fused to a 20 amino acids His-Tag at N-terminus and purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
GGPS1 Human recombinant (1mg/ml) protein solution contains 20mM Tris-HCl pH-8, 1mM DTT & 10% glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
Citations
More Info
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Introduction
GGPS1 is PART of the prenyltransferase family. GGPS1 is widely expressed in testis, heart and skeletal muscle, GGPS1 is localized in the cytoplasm and catalyzes the formation of geranylgeranyl pyrophosphate, a precursor of geranylgeranylated proteins and carotenoids. GGPS1 is a significant enzyme that is responsible for the C20-prenylation of proteins and for the regulation of a nuclear hormone receptor.
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Synonyms
GGPPS, GGPPS1, GGPP synthetase.
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Physical Appearance
Sterile filtered colorless solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MEKTQETVQR ILLEPYKYLL QLPGKQVRTK LSQAFNHWLK VPEDKLQIII EVTEMLHNAS LLIDDIEDNS KLRRGFPVAH SIYGIPSVIN SANYVYFLGL EKVLTLDHPD AVKLFTRQLL ELHQGQGLDI YWRDNYTCPT EEEYKAMVLQ KTGGLFGLAV
GLMQLFSDYK EDLKPLLNTL GLFFQIRDDY ANLHSKEYSE NKSFCEDLTE GKFSFPTIHA IWSRPESTQV QNILRQRTEN IDIKKYCVHY LEDVGSFEYT RNTLKELEAK AYKQIDARGG NPELVALVKH LSKMFKEENE.
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 :
GRHPR HumanDescription:
Glyoxylate Reductase/Hydroxypyruvate Reductase Human Recombinant
EC 1.1.1.79, GLXR, GLYD, GRHPR, PH2.
Product # :
ENZ-521Price :
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Shipped with Ice Packs
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Description
GRHPR Recombinant Human produced in E.Coli is a single, non-glycosylated polypeptide chain containing 348 amino acids (1-328 a.a.) and having a molecular mass of 37.8 kDa. The GRHPR is fused to a 20 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The GRHPR solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH8.0), 20% glycerol, 5mM DTT and 0.2M NaCl.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Citations
More Info
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Introduction
GRHPR located in the cytosol, belongs to the D-isomer specific 2-hydroxyacid dehydrogenase family of proteins. GRHPR is widely expressed in liver. GRHPR has widespread tissue expression and is involved in metabolism. GRHPR is an enzyme with hydroxypyruvate reductase, glyoxylate reductase, and D-glycerate dehydrogenase enzymatic activities.
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Synonyms
EC 1.1.1.79, GLXR, GLYD, GRHPR, PH2.
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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 MRPVRLMKVF VTRRIPAEGR VALARAADCE VEQWDSDEPI PAKELERGVA GAHGLLCLLS DHVDKRILDA AGANLKVIST MSVGIDHLAL DEIKKRGIRV GYTPDVLTDT TAELAVSLLL TTCRRLPEAI EEVKNGGWTS WKPLWLCGYG LTQSTVGIIG LGRIGQAIAR RLKPFGVQRF LYTGRQPRPE EAAEFQAEFV STPELAAQSD FIVVACSLTP ATEGLCNKDF FQKMKETAVF INISRGDVVN QDDLYQALAS GKIAAAGLDV TSPEPLPTNH PLLTLKNCVI LPHIGSATHR TRNTMSLLAA NNLLAGLRGE PMPSELKL.
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 :
UROD HumanDescription:
Uroporphyrinogen Decarboxylase Human Recombinant
UPD, PCT, EC 4.1.1.37, URO-D, UROD, Uroporphyrinogen Decarboxylase.
Product # :
ENZ-536Price :
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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.
Citations
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.
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Name :
PAP HumanDescription:
Prostate Acid Phosphatase Human
Product # :
ENZ-1171Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Human Prostate Acid Phosphatase produced in Pooled human seminal fluid having a molecular mass of approximately 100kD.
Source
Pooled human seminal fluid.
Formulation
PAP Human is lyophilized (0.2 µm filtered) from 0.02M NH4HCO3.
Purity
Greater than 96.0% as determined by SDS-PAGE.
Citations
More Info
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Introduction
Prostatic acid phosphatase, also known as PAP, is an enzyme produced by the prostate. PAP may be found in increased amounts in men with prostate cancer.
PAP’s physiological function may be associated with the liquefaction process of semen.
The highest levels of PAP are found in metastasized prostate cancer. Diseases of the bone, such as Paget's disease or hyperparathyroidism, diseases of blood cells (sickle-cell disease) or multiple myeloma or lysosomal storage diseases (Gaucher's disease), will show moderately higher levels.
Certain medications can cause temporary changes in PAP levels. Manipulation of the prostate gland through rectal exam, biopsy or massage may increase the level. -
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
-
Stability
PAP Human although stable at room temperature for 3 weeks, should be stored between 2-8°C.
-
Solubility
It is recommended to reconstitute the lyophilized PAP Human in phosphate buffer containing 0.15M NaCl.
-
Human Virus Test
Starting material tested and found negative for HIV I & II antibodies, Hepatitis B surface antigen, Hepatitis C antibodies and Syphilis.
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 :
ALCAM (CD166) HumanDescription:
Activated Leukocyte Cell Adhesion Molecule (CD166) Human Recombinant
Activated Leukocyte Cell Adhesion Molecule, CD166 Antigen, MEMD, Activated Leucocyte Cell Adhesion Molecule, CD166, ALCAM.
Product # :
PRO-2388Price :
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Description
ALCAM Human Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 742 amino acids (28-527a.a.) and having a molecular mass of 83.1kDa (Molecular size on SDS-PAGE will appear at approximately 70-100 kDa).CD166 is expressed with a 239 amino acid hIgGHis tag at C-Terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
CD166 protein solution (0.25mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 10% glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
Citations
More Info
-
Introduction
CD166 antigen isoform 2 (ALCAM) is a type 1 membrane glycoprotein and belongs to the immunoglobulin superfamily. ALCAM is expressed on thymic epithelium, microvascular endothelium, activated lymphocytes and monocytes, and monocyte-derived dendritic cells. CD166 and CD6 interaction plays a role in T cell development and T cell regulation, as well as in the binding of T cells and B cells to activated leukocytes.
-
Synonyms
Activated Leukocyte Cell Adhesion Molecule, CD166 Antigen, MEMD, Activated Leucocyte Cell Adhesion Molecule, CD166, ALCAM.
-
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
ADPWYTVNSA YGDTIIIPCR LDVPQNLMFG KWKYEKPDGS PVFIAFRSST KKSVQYDDVP EYKDRLNLSE NYTLSISNAR ISDEKRFVCM LVTEDNVFEA PTIVKVFKQP SKPEIVSKAL FLETEQLKKL GDCISEDSYP DGNITWYRNG KVLHPLEGAV VIIFKKEMDP VTQLYTMTST
LEYKTTKADI QMPFTCSVTY YGPSGQKTIH SEQAVFDIYY PTEQVTIQVL PPKNAIKEGD NITLKCLGNG NPPPEEFLFY LPGQPEGIRS SNTYTLTDVR RNATGDYKCS LIDKKSMIAS TAITVHYLDL SLNPSGEVTR QIGDALPVSC TISASRNATV VWMKDNIRLR SSPSFSSLHY
QDAGNYVCET ALQEVEGLKK RESLTLIVEG KPQIKMTKKT DPSGLSKTII CHVEGFPKPA IQWTITGSGS VINQTEESPY INGRYYSKII ISPEENVTLT CTAENQLERT VNSLNVSANE NREKVNDQAK LIVGIVVGLL LAALEPKSCD KTHTCPPCPA PELLGGPSVF LFPPKPKDTL
MISRTPEVTC VVVDVSHEDP EVKFNWYVDG VEVHNAKTKP REEQYNSTYR VVSVLTVLHQ DWLNGKEYKC KVSNKALPAP IEKTISKAKG QPREPQVYTL PPSRDELTKN QVSLTCLVKG FYPSDIAVEW ESNGQPENNY KTTPPVLDSD GSFFLYSKLT VDKSRWQQGN VFSCSVMHEA
LHNHYTQKSL SLSPGKHHHH HH.
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 :
Insulin Human, HisDescription:
Insulin Human Recombinant, His Tag
Insulin, Insulin-Dependent Diabetes Mellitus 2, Preproinsulin, Proinsulin, MODY10, IDDM1, IDDM2, IDDM, ILPR, IRDN.
Product # :
CYT-1076Price :
Quantity :
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Description
Insulin Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 109 amino acids (25-110 a.a) and having a molecular mass of 11.8kDa. Insulin is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Insulin protein solution (0.5mg/ml) containing Phosphate-Buffered Saline (pH 7.4) and 10% Glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Biological Activity
Measured in a cell proliferation assay using MCF7 human breast cancer cell. The ED50 for this effect is less or equal to 4 ug/ml.
Citations
More Info
-
Introduction
Insulin decreases blood glucose concentration. it increases cell permeability to monosaccharides, amino acids and fatty acids. it accelerates glycolysis, the pentose phosphate cycle, and glycogen synthesis in liver.
-
Synonyms
Insulin, Insulin-Dependent Diabetes Mellitus 2, Preproinsulin, Proinsulin, MODY10, IDDM1, IDDM2, IDDM, ILPR, IRDN.
-
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 MGSFVNQHLC GSHLVEALYL VCGERGFFYT PKTRREAEDL QVGQVELGGG PGAGSLQPLA LEGSLQKRGI VEQCCTSICS LYQLENYCN
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 :
CBR3 HumanDescription:
Carbonyl Reductase-3 Human Recombinant
Carbonyl reductase [NADPH] 3, NADPH-dependent carbonyl reductase 3, CBR3, carbonyl reductase 3, hCBR3, SDR21C2.
Product # :
ENZ-428Price :
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Description
Recombinant Human CBR3 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 33kDa. CBR3 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The CBR3 protein solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0) and 10% glycerol.
Purity
Greater than 95.0% as determined by analysis by SDS-PAGE.
Citations
More Info
-
Introduction
CBR3 catalyzes the reduction of a large number of biologically and pharmacologically active carbonyl compounds to their corresponding alcohols. CBR3 is one of several monomeric NADPH-dependent oxidoreductases. Furthermore, CBR3 contains 3 exons spanning 11.2 kilobases and is strongly linked to another carbonyl reductase gene, the CBR1. It was suggested that CBR3 mediates 9-cis-retinoic acid-induced cytostatis and is a potential prognostic marker for oral malignancy.
CBR3 is identified in the ovary, pancreas, intestine, colon, kidney, brain, thymus, lung, heart, liver, spleen, leukocyte, prostate and the testis.
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Synonyms
Carbonyl reductase [NADPH] 3, NADPH-dependent carbonyl reductase 3, CBR3, carbonyl reductase 3, hCBR3, SDR21C2.
-
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 MSSCSRVALV TGANRGIGLA IARELCRQFS GDVVLTARDV ARGQAAVQQL QAEGLSPRFH QLDIDDLQSI RALRDFLRKE YGGLNVLVNN AAVAFKSDDP MPFDIKAEMT LKTNFFATRN MCNELLPIMK PHGRVVNISS LQCLRAFENC SEDLQERFHS ETLTEGDLVD LMKKFVEDTK NEVHEREGWP NSPYGVSKLG VTVLSRILAR RLDEKRKADR ILVNACCPGP VKTDMDGKDS IRTVEEGAET PVYLALLPPD ATEPQGQLVH DKVVQNW.
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 :
MBP E.Coli, HisDescription:
Maltose Binding Protein E.coli Recombinant, His Tag
Maltose-binding periplasmic protein, MBP, MMBP, Maltodextrin-binding protein, malE, b4034, JW3994.
Product # :
PRO-2322Price :
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Description
Recombinant E.Coli MBP produced in E.Coli is a single, non-glycosylated polypeptide chain containing 410 amino acids (27-392 a.a) and having a molecular mass of 44.9kDa. MBP is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
MBP protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.1M NaCl and 10% glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Citations
More Info
-
Introduction
Maltose Binding Protein is a member of the maltose/maltodextrin system of E.Coli, which is accountable for the uptake and efficient catabolism of maltodextrins. The maltose/maltodextrin is a complex regulatory and transport system involving many proteins and protein complexes.
MBP elevates the yield of its fusion partner in many cases and is often able to promote the solubility of polypeptides to which it is fused. -
Synonyms
Maltose-binding periplasmic protein, MBP, MMBP, Maltodextrin-binding protein, malE, b4034, JW3994.
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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 MGSMKIEEGK LVIWINGDKG YNGLAEVGKK FEKDTGIKVT VEHPDKLEEK FPQVAATGDG PDIIFWAHDR FGGYAQSGLL AEITPDKAFQ DKLYPFTWDA VRYNGKLIAY PIAVEALSLI YNKDLLPNPP KTWEEIPALD KELKAKGKSA LMFNLQEPYF TWPLIAADGG YAFKYENGKY DIKDVGVDNA GAKAGLTFLV DLIKNKHMNA DTDYSIAEAA FNKGETAMTI NGPWAWSNID TSKVNYGVTV LPTFKGQPSK PFVGVLSAGI NAASPNKELA KEFLENYLLT DEGLEAVNKD KPLGAVALKS YEEELAKDPR IAATMENAQK GEIMPNIPQM SAFWYAVRTA VINAASGRQT VDEALKDAQT NSSSNNNNNN NNNNLGIEGR.
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 :
ACHE HumanDescription:
Acetylcholinesterase Human Recombinant
AChE, ACEE, ACES_HUMAN, Acetylcholinesterase, ACHE, ARACHE, N-ACHE, VT, Acetylcholinesterase isoform E4-E6
Product # :
ENZ-1174Price :
Quantity :
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Description
ACHE Human Recombinant produced in HEK cells is a single, glycosylated, polypeptide chain (32-614 a.a) containing a total of 592 amino acids, having a molecular mass of 65.6 kDa. ACHE is fused to a 6 amino acid His-tag at C-terminus,and is purified by proprietary chromatographic techniques.
Source
HEK293 Cells.
Formulation
The ACHE solution (0.25mg/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 > 6,000 nmol/min/ug. Defined by the amount of enzyme that cleaves 1 nmole of acetylthiocholine per minute at pH 7.5 at 25˚C.
Citations
More Info
-
Introduction
Acetylcholinesterase (ACHE) belongs to the type-B carboxylesterase/lipase family. ACHE catalyzes the breakdown of acetylcholine and other choline esters that play a role as neurotransmitters. During neurotransmission, ACH is released from the presynaptic neuron into the synaptic cleft and binds ACH receptors on the post-synaptic membrane, transmitting the signal from the nerve. ACHE is located on the post-synaptic membrane, terminates the signal transmission by hydrolyzing ACH.
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Synonyms
AChE, ACEE, ACES_HUMAN, Acetylcholinesterase, ACHE, ARACHE, N-ACHE, VT, Acetylcholinesterase isoform E4-E6
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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
DGSEGREDAE LLVTVRGGRL RGIRLKTPGG PVSAFLGIPF AEPPMGPRRF LPPEPKQPWS GVVDATTFQS VCYQYVDTLY PGFEGTEMWN PNRELSEDCL YLNVWTPYPR PTSPTPVLVW IYGGGFYSGA SSLDVYDGRF LVQAERTVLV SMNYRVGAFG FLALPGSREA PGNVGLLDQR LALQWVQENV AAFGGDPTSV TLFGESAGAA SVGMHLLSPP SRGLFHRAVL QSGAPNGPWA TVGMGEARRR ATQLAHLVGC PPGGTGGNDT ELVACLRTRP AQVLVNHEWH VLPQESVFRF SFVPVVDGDF LSDTPEALIN AGDFHGLQVL VGVVKDEGSY FLVYGAPGFS KDNESLISRA EFLAGVRVGV PQVSDLAAEA VVLHYTDWLH PEDPARLREA LSDVVGDHNV VCPVAQLAGR LAAQGARVYA YVFEHRASTL SWPLWMGVPH GYEIEFIFGI PLDPSRNYTA EEKIFAQRLM RYWANFARTG DPNEPRDPKA PQWPPYTAGA QQYVSLDLRP LEVRRGLRAQ ACAFWNRFLP KLLSATDTLD EAERQWKAEF HRWSSYMVHW KNQFDHYSKQ DRCSDLHHHH HH
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 :
AK1 MouseDescription:
Adenylate Kinase 1 Mouse Recombinant
Adenylate kinase Isoenzyme 1 isoform 1, Ak-1, B430205N08Rik, ATP-AMP transphosphorylase 1, ATP:AMP phosphotransferase, Adenylate monophosphate kinase, Myokinase.
Product # :
PKA-106Price :
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Description
AK1 Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 233 amino acids (1-210 a.a) and having a molecular mass of 25.5kDa.AK1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
AK1 protein solution (0.5mg/ml) containing 20mM Tris-Hcl buffer (pH8.0), 10% glycerol and 1mM DTT.
Purity
Greater than 90.0% as determined by SDS-PAGE.
Biological Activity
Specific activity is > 150 units/mg. One unit will convert 2.0 umoles of ADP to ATP + AMP per minute at pH 7.5 at 37C.
Citations
More Info
-
Introduction
AK1 is a small ubiquitous enzyme which is essential for maintenance and cell growth. It is involved in the regulation of adenine nucleotide composition within a cell by catalyzing the reversible transfer of the terminal phosphate group between ATP and AMP. The AK1 protein is found in the cytosol of skeletal muscle, brain and erythrocytes. Defects in the AK1 gene are the cause of a form of hemolytic anemia.
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Synonyms
Adenylate kinase Isoenzyme 1 isoform 1, Ak-1, B430205N08Rik, ATP-AMP transphosphorylase 1, ATP:AMP phosphotransferase, Adenylate monophosphate kinase, Myokinase.
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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 MGSMGCCVSS EPQEEGGRKT GEKLKKAKII FVVGGPGSGK GTQCEKIVQK YGYTHLSTGD LLRAEVSSGS ERGKKLSAIM EKGELVPLDT VLDMLRDAML AKVDSSNGFL IDGYPREVKQ GEEFEQKIGQ PTLLLYVDAG AETMTQRLLK RGETSGRVDD
NEETIKKRLE TYYNATEPVI SFYDKRGIVR KVNAEGTVDT VFSEVCTYLD SLK.
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 :
NAGA HumanDescription:
N-Acetylgalactosaminidase Alpha Human Recombinant
Alpha-N-acetylgalactosaminidase, N-Acetylgalactosaminidase Alpha, NAGA, Alpha-galactosidase B, NAGA, D22S674, GALB.
Product # :
ENZ-963Price :
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Description
NAGA Human Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 400 amino acids (18-411) and having a molecular mass of 45.5kDa (Molecular size on SDS-PAGE will appear at approximately 40-57kDa).NAGA is fused to 6 amino acid His-Tag at C-terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
NAGA protein solution (0.5mg/ml) containing Phosphate buffered saline (pH7.4), 10% glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
Citations
More Info
-
Introduction
N-Acetylgalactosaminidase Alpha (NAGA) is a lysosomal exoglycosidase which removes terminal alpha-N-acetylgalactosamine residues from glycopeptides and glycolipids. NAGA is necessary for the breakdown of glycolipids.
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Synonyms
Alpha-N-acetylgalactosaminidase, N-Acetylgalactosaminidase Alpha, NAGA, Alpha-galactosidase B, NAGA, D22S674, GALB.
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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.
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Amino Acid Sequence
LDNGLLQTPP MGWLAWERFR CNINCDEDPK NCISEQLFME MADRMAQDGW RDMGYTYLNI DDCWIGGRDA SGRLMPDPKR FPHGIPFLAD YVHSLGLKLG IYADMGNFTC MGYPGTTLDK VVQDAQTFAE WKVDMLKLDG CFSTPEERAQ GYPKMAAALN ATGRPIAFSC SWPAYEGGLP PRVNYSLLAD ICNLWRNYDD IQDSWWSVLS ILNWFVEHQD ILQPVAGPGH WNDPDMLLIG NFGLSLEQSR AQMALWTVLA APLLMSTDLR TISAQNMDIL QNPLMIKINQ DPLGIQGRRI HKEKSLIEVY MRPLSNKASA LVFFSCRTDM PYRYHSSLGQ LNFTGSVIYE AQDVYSGDII SGLRDETNFT VIINPSGVVM WYLYPIKNLE MSQQHHHHHH.
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 :
TDO2 HumanDescription:
Tryptophan 2,3-Dioxygenase Human Recombinant
Tryptophan 2,3-dioxygenase, TDO, Tryptamin 2,3-dioxygenase, Tryptophan oxygenase, TO, TRPO, Tryptophan pyrrolase, Tryptophanase, TDO2, TPH2.
Product # :
ENZ-081Price :
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Description
TDO2 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 426 amino acids (1-406 a.a.) and having a molecular mass of 50kDa. The TDO2 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The TDO2 solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH8.0), 0.2M NaCl, 5mM DTT, 1mM EDTA and 30% glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
Citations
More Info
-
Introduction
TDO2 is a ferrous heme enzyme that catalyzes the first and rate-limiting step in the kynurenine pathway which is the major pathway of tryptophan metabolism. TDO2 integrates oxygen into the indole moiety of tryptophan. TDO2 has broad specificity towards tryptamine and derivatives including D- and L-tryptophan, 5-hydroxytryptophan and serotonin.
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Synonyms
Tryptophan 2,3-dioxygenase, TDO, Tryptamin 2,3-dioxygenase, Tryptophan oxygenase, TO, TRPO, Tryptophan pyrrolase, Tryptophanase, TDO2, TPH2.
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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 MSGCPFLGNN FGYTFKKLPV EGSEEDKSQT GVNRASKGGL IYGNYLHLEK VLNAQELQSE TKGNKIHDEH LFIITHQAYE LWFKQILWEL DSVREIFQNG HVRDERNMLK VVSRMHRVSV ILKLLVQQFS ILETMTALDF NDFREYLSPA SGFQSLQFRL LENKIGVLQN MRVPYNRRHY RDNFKGEENE LLLKSEQEKT LLELVEAWLE RTPGLEPHGF NFWGKLEKNI TRGLEEEFIR IQAKEESEEK EEQVAEFQKQ KEVLLSLFDE KRHEHLLSKG ERRLSYRALQ GALMIYFYRE EPRFQVPFQL LTSLMDIDSL MTKWRYNHVC MVHRMLGSKA GTGGSSGYHY LRSTVSDRYK VFVDLFNLST YLIPRHWIPK MNPTIHKFLY TAEYCDSSYF SSDESD.
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 :
FOLH1 MouseDescription:
Folate Hydrolase 1 Mouse Recombinant
Folh1, GCP2, mopsm, Glutamate carboxypeptidase 2, Folate hydrolase 1, Folylpoly-gamma-glutamate carboxypeptidase, FGCP, Glutamate carboxypeptidase II, GCPII, Naalad1.
Product # :
ENZ-957Price :
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Description
FOLH1 Mouse Recombinant produced in in Sf9 Baculovirus cells is a single, non-glycosylated polypeptide chain containing 717 amino acids (45-752a.a) and having a molecular mass of 80.5kDa (Migrates at 70-100kDa on SDS-PAGE under reducing conditions). FOLH1 is fused to a 6 amino acid His-tag at C-Terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
The FOLH1 solution (0.5mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 10% glycerol.
Purity
Greater than 85% as determined by SDS-PAGE.
Citations
More Info
-
Introduction
Folate Hydrolase 1 (Folh1) is a single pass type 2 membrane protein which is expressed mainly in prostate epithelium. Folh1 which is a part of the peptidase M28 family and M28B subfamily has both folate hydrolase and N-acetylated-alpha-linked-acidic dipeptidase activity. Folh1 can be found in urinary bladder, kidney, testis, ovary, stomach, small intestine colon, and the capillary endothelium of various tumors. Therefore, Folh1 plays a role in directed imaging and therapy of recurrent of metastatic disease.
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Synonyms
Folh1, GCP2, mopsm, Glutamate carboxypeptidase 2, Folate hydrolase 1, Folylpoly-gamma-glutamate carboxypeptidase, FGCP, Glutamate carboxypeptidase II, GCPII, Naalad1.
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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
ADPKPSNEAT GNVSHSGMKK EFLHELKAEN IKKFLYNFTR TPHLAGTQNN FELAKQIHDQ WKEFGLDLVE LSHYDVLLSY PNKTHPNYIS IINEDGNEIF KTSLSEQPPP GYENISDVVP PYSAFSPQGT PEGDLVYVNY ARTEDFFKLE REMKISCSGK IVIARYGKVF RGNMVKNAQL AGAKGMILYS DPADYFVPAV KSYPDGWNLP GGGVQRGNVL NLNGAGDPLT PGYPANEHAY RHELTNAVGL PSIPVHPIGY DDAQKLLEHM GGPAPPDSSW KGGLKVPYNV GPGFAGNFST QKVKMHIHSY TKVTRIYNVI GTLKGALEPD RYVILGGHRD AWVFGGIDPQ SGAAVVHEIV RSFGTLKKKG RRPRRTILFA SWDAEEFGLL GSTEWAEEHS RLLQERGVAY INADSSIEGN YTLRVDCTPL MYSLVYNLTK ELQSPDEGFE GKSLYDSWKE KSPSPEFIGM PRISKLGSGN DFEVFFQRLG IASGRARYTK NWKTNKVSSY PLYHSVYETY ELVVKFYDPT FKYHLTVAQV RGAMVFELAN SIVLPFDCQS YAVALKKYAD TIYNISMKHP QEMKAYMISF DSLFSAVNNF TDVASKFNQR LQELDKSNPI LLRIMNDQLM YLERAFIDPL GLPGRPFYRH IIYAPSSHNK YAGESFPGIY DALFDISSKV NASKAWNEVK RQISIATFTV QAAAETLREV AHHHHHH.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
ABO HumanDescription:
ABO Blood Group Human Recombinant
Histo-blood group ABO system transferase, Fucosylglycoprotein 3-alpha-galactosyltransferase, Fucosylglycoprotein alpha-N-acetylgalactosaminyltransferase, Glycoprotein-fucosylgalactoside alpha-N-acetylgalactosaminyltransferase, Glycoprotein-fucosylgalactoside alpha-galactosyltransferase, Histo-blood group A transferase, A transferase, Histo-blood group B transferase, B transferase, NAGAT, ABO, GTB, A3GALNT, A3GALT1.
Product # :
ENZ-167Price :
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Description
ABO Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 322 amino acids (54-354 a.a) and having a molecular mass of 37.4kDa.ABO is fused to a 21 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
ABO protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 2mM DTT, 20% glycerol and 200mM NaCl.
Purity
Greater than 85.0% as determined by SDS-PAGE.
Citations
More Info
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Introduction
NAGAT (ABO) is a member of the glycosyltransferase 6 family. The ABO protein is the basis of the ABO blood group system and related to the first discovered blood group system, ABO. The allele that is present in an individual determines the blood group. The histo-blood group ABO is comprised of 3 carbohydrate antigens: A, B, and H. A, B, and AB individuals express a glycosyltransferase activity which converts the H antigen to the A antigen (by addition of UDP-GalNAc) or to the B antigen (by addition of UDP-Gal), whereas O individuals are deficient of such activity.
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Synonyms
Histo-blood group ABO system transferase, Fucosylglycoprotein 3-alpha-galactosyltransferase, Fucosylglycoprotein alpha-N-acetylgalactosaminyltransferase, Glycoprotein-fucosylgalactoside alpha-N-acetylgalactosaminyltransferase, Glycoprotein-fucosylgalactoside alpha-galactosyltransferase, Histo-blood group A transferase, A transferase, Histo-blood group B transferase, B transferase, NAGAT, ABO, GTB, A3GALNT, A3GALT1.
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Physical Appearance
Sterile Filtered colorless solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MAVREPDHLQ RVSLPRMVYP QPKVLTPCRK DVLVVTPWLA PIVWEGTFNI DILNEQFRLQ NTTIGLTVFA IKKYVAFLKL FLETAEKHFM VGHRVHYYVF TDQPAAVPRV TLGTGRQLSV LEVRAYKRWQ DVSMRRMEMI SDFCERRFLS EVDYLVCVDV DMEFRDHVGV EILTPLFGTL HPGFYGSSRE AFTYERRPQS QAYIPKDEGD FYYLGGFFGG SVQEVQRLTR ACHQAMMVDQ ANGIEAVWHD ESHLNKYLLR HKPTKVLSPE YLWDQQLLGW PAVLRKLRFT AVPKNHQAVR NP.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
AK2 HumanDescription:
Adenylate Kinase 2 Human Recombinant
ADK2, AK-2, Adenylate kinase isoenzyme 2 mitochondrial, ATP-AMP transphosphorylase 2, adenylate kinase 2.
Product # :
PKA-260Price :
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Description
AK2 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 259 amino acids and having a molecular mass of 28.6 kDa. AK2 is fused to 20 a.a. His-Tag at N-terminus and purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
AK2 solution containing 20mM Tris pH-7.5, 5mM DTT and 20% glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Biological Activity
Specific activity: > 1.5 units/ml. One unit will convert 2.0 umoles of ADP to ATP + AMP per minute at pH 7.5 at 25C.Citations
More Info
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Introduction
Adenylate kinases play a role in regulating the adenine nucleotide composition within a cell by catalyzing the reversible transfer of phosphate groups among adenine nucleotides. There are 3 types of adenylate kinase isozymes, AK1, AK2, and AK3 in vertebrates. Expression of these isozymes are tissue-specific and developmentally regulated. AK2 is localized in the mitochondrial intermembrane space and is involved in apoptosis. AK2 is mutated in individuals with reticular dysgenesis.
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Synonyms
ADK2, AK-2, Adenylate kinase isoenzyme 2 mitochondrial, ATP-AMP transphosphorylase 2, adenylate kinase 2.
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Physical Appearance
Sterile filtered colorless solution.
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Stability
AK2 Human Recombinant although stable at 4°C for 1 week, should be stored below -18°C. Please prevent freeze thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MAPSVPAAEP EYPKGIRAVL LGPPGAGKGTQAPRLAENFC VCHLATGDML RAMVASGSEL GKKLKATMDA GKLVSDEMVV ELIEKNLETP LCKNGFLLDG FPRTVRQAEM LDDLMEKRKE KLDSVIEFSIPDSLLIRRIT GRLIHPKSGR SYHEEFNPPK EPMKDDITGE PLIRRSDDNE KALKIRLQAY HTQTTPLIEY YRKRGIHSAI DASQTPDVVF ASILAAFSKA TCKDLVMFI.
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 :
HMGCL Human, Sf9Description:
3-Hydroxymethyl-3-Methylglutaryl-CoA Lyase Human Recombinant, Sf9
3-Hydroxymethyl-3-Methylglutaryl-CoA Lyase, 3-Hydroxymethyl-3-Methylglutaryl-Coenzyme A Lyase, 3-Hydroxy-3-Methylglutarate-CoA Lyase, Hydroxymethylglutaricaciduria, HMG-CoA Lyase, EC 4.1.3.4, HL, Mitochondrial 3-Hydroxy-3-Methylglutaryl-CoA Lyase, Hydroxymethylglutaryl-CoA Lyase, Mitochondrial, 3-Hydroxy-3-Methylglutaryl-CoA Lyase, Hydroxymethylglutaryl-CoA lyase, mitochondrial, HMG-CoA lyase, 3-hydroxy-3-methylglutarate-CoA lyase.
Product # :
ENZ-1056Price :
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Description
HMGCL Human Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 305 amino acids (28-325 a.a.) and having a molecular mass of 32.5kDa (Molecular size on SDS-PAGE will appear at approximately 28-40kDa). HMGCL is expressed with a 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
HMGCL protein solution (1mg/ml) contains Phosphate Buffered Saline (pH 7.4), 20% glycerol and 1mM DTT.
Purity
Greater than 90.0% as determined by SDS-PAGE.
Citations
More Info
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Introduction
Hydroxymethylglutaryl-CoA lyase (HMGCL) is a mitochondrial matrix protein which is a member of the HMG-CoA lyase family. HMGCL is a homodimer and participates in leucine catabolism and ketogenesis, the hepatic synthesis of ketone bodies which, during fasting, provides a major source of energy for the heart, brain and kidney. More precisely, HMGCL catalyzes the final step of these processes, the cleavage of 3-hydroxy-3-methylglutaryl-CoA to acetoacetic acid and acetyl-CoA.
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Synonyms
3-Hydroxymethyl-3-Methylglutaryl-CoA Lyase, 3-Hydroxymethyl-3-Methylglutaryl-Coenzyme A Lyase, 3-Hydroxy-3-Methylglutarate-CoA Lyase, Hydroxymethylglutaricaciduria, HMG-CoA Lyase, EC 4.1.3.4, HL, Mitochondrial 3-Hydroxy-3-Methylglutaryl-CoA Lyase, Hydroxymethylglutaryl-CoA Lyase, Mitochondrial, 3-Hydroxy-3-Methylglutaryl-CoA Lyase, Hydroxymethylglutaryl-CoA lyase, mitochondrial, HMG-CoA lyase, 3-hydroxy-3-methylglutarate-CoA lyase.
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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
MTLPKRVKIV EVGPRDGLQN EKNIVSTPVK IKLIDMLSEA GLSVIETTSF VSPKWVPQMG DHTEVLKGIQ KFPGINYPVL TPNLKGFEAA VAAGAKEVVI FGAASELFTK KNINCSIEES FQRFDAILKA AQSANISVRG YVSCALGCPY EGKISPAKVA EVTKKFYSMG CYEISLGDTI GVGTPGIMKD MLSAVMQEVP LAALAVHCHD TYGQALANTL MALQMGVSVV DSSVAGLGGC PYAQGASGNL ATEDLVYMLE GLGIHTGVNL QKLLEAGNFI CQALNRKTSS KVAQATCKLH HHHHH.
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 :
NAE1 HumanDescription:
NEDD8 Activating Enzyme E1 Subunit 1 Human Recombinant
NEDD8-activating enzyme E1 regulatory subunit, Amyloid beta precursor protein-binding protein 1 59 kDa, APP-BP1, Amyloid protein-binding protein 1, Proto-oncogene protein 1, NAE1, APPBP1, HPP1, ula-1, A-116A10.1.
Product # :
ENZ-227Price :
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Shipped with Ice Packs
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Description
NAE1 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 557 amino acids (1-534) and having a molecular mass of 62.7kDa.NAE1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The NAE1 solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 2mM DTT, 10% glycerol and 200mM NaCl.
Purity
Greater than 90% as determined by SDS-PAGE.
Citations
More Info
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Introduction
NEDD8-activating enzyme E1 regulatory subunit (NAE1) is a member of the ubiquitin-activating E1 family. NAE1 binds to the beta-amyloid precursor protein. Beta-amyloid precursor protein is a cell surface protein with signal-transducing properties, and it is believed to have a role in the pathogenesis of Alzheimer's disease. NAE1 participates in a unique ubiquitinylation-related pathway involving the ubiquitin-like molecule NEDD8. Furthermore, the NAE1 protein is essential for cell cycle progression through the S/M checkpoint.
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Synonyms
NEDD8-activating enzyme E1 regulatory subunit, Amyloid beta precursor protein-binding protein 1 59 kDa, APP-BP1, Amyloid protein-binding protein 1, Proto-oncogene protein 1, NAE1, APPBP1, HPP1, ula-1, A-116A10.1.
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Physical Appearance
Sterile Filtered clear solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSMAQLGKL LKEQKYDRQL RLWGDHGQEA LESAHVCLIN ATATGTEILK NLVLPGIGSF TIIDGNQVSG EDAGNNFFLQ RSSIGKNRAE AAMEFLQELN SDVSGSFVEE SPENLLDNDP SFFCRFTVVV ATQLPESTSL RLADVLWNSQ IPLLICRTYG LVGYMRIIIK EHPVIESHPD NALEDLRLDK PFPELREHFQ SYDLDHMEKK DHSHTPWIVI IAKYLAQWYS ETNGRIPKTY KEKEDFRDLI RQGILKNENG APEDEENFEE AIKNVNTALN TTQIPSSIED IFNDDRCINI TKQTPSFWIL ARALKEFVAK EGQGNLPVRG TIPDMIADSG KYIKLQNVYR EKAKKDAAAV GNHVAKLLQS IGQAPESISE KELKLLCSNS AFLRVVRCRS LAEEYGLDTI NKDEIISSMD NPDNEIVLYL MLRAVDRFHK QQGRYPGVSN YQVEEDIGKL KSCLTGFLQE YGLSVMVKDD YVHEFCRYGA AEPHTIAAFL GGAAAQEVIK IITKQFVIFN NTYIYSGMSQ TSATFQL.
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.