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1000 results found for “other enzymes”
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Name :
GARS Human, sf9Description:
Glycyl-TRNA Synthetase Human Recombinant, sf9
Glycine--tRNA ligase, EC 6.1.1.14, Diadenosine tetraphosphate synthetase, AP-4-A synthetase, Glycyl-tRNA synthetase, GlyRS, GARS, HMN5, CMT2D, DSMAV, SMAD1.
Product # :
ENZ-717Price :
Quantity :
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Shipped with Ice Packs
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Description
GARS Human Recombinant produced in SF9 is a glycosylated, polypeptide chain having a calculated molecular mass of 78,902 Dalton. GARS is expressed with a -10xHis tag at N-terminus and purified by proprietary chromatographic techniques.
Source
Sf9 Insect Cells.
Formulation
GARS is supplied in 20mM HEPES buffer pH-7.6, 250mM NaCl and 20% glycerol.
Purity
Greater than 80.0% as determined by SDS-PAGE.
More Info
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Introduction
GARS is an (alpha)2 dimer which is a member of the class II family of tRNA synthetases. GARS is a glycyl-tRNA synthetase, one of the aminoacyl-tRNA synthetases which charge tRNAs with their cognate amino acids. GARS catalyzes the attachment of glycine to tRNA(Gly). In addition, GARS is able to produce diadenosine tetraphosphate (Ap4A), which is a universal pleiotropic signaling molecule required for cell regulation pathways, by direct condensation of two ATPs. GARS has been demonstrated to be a target of autoantibodies in the human autoimmune diseases, polymyositis or dermatomyositis.
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Synonyms
Glycine--tRNA ligase, EC 6.1.1.14, Diadenosine tetraphosphate synthetase, AP-4-A synthetase, Glycyl-tRNA synthetase, GlyRS, GARS, HMN5, CMT2D, DSMAV, SMAD1.
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Physical Appearance
Sterile Filtered clear solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. Avoid multiple freeze-thaw cycles.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
MIOX HumanDescription:
Myo-Inositol Oxygenase Human Recombinant
Myo-Inositol Oxygenase, Kidney-Specific Protein 32, Aldehyde Reductase (Aldose Reductase) Like 6, Renal-Specific Oxidoreductase, Aldehyde Reductase-Like 6, MI Oxygenase, EC 1.13.99.1, ALDRL6, Inositol Oxygenase, KSP32, RSOR, MIOX.
Product # :
ENZ-812Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
MIOX Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain (Met1-Trp285) containing 295 amino acids including a 10 aa His tag at N-terminus. The total calculated molecular mass is 34.2kDa.
Source
Escherichia Coli.
Formulation
MIOX was filtered (0.4 µm) and lyophilized in 20mM Tris buffer, 50mM NaCl and 5% (w/v) trehalose, pH 7.5.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
Inositol oxygenase is a non-heme di-iron enzyme which oxidizes myo-inositol to glucuronic acid. In addition, inositol oxygenase oxidizes the less abundant chiro isomer of inositol. MIOX enzyme is a component of the only known pathway for the catabolism of inositol in humans. MIOX is expressed mostly in the kidneys. Reduction of Inositol Oxygenase and accumulation of polyols, such as inositol and xylitol, have been implicated as contributing factors in complications linked with diabetes.
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Synonyms
Myo-Inositol Oxygenase, Kidney-Specific Protein 32, Aldehyde Reductase (Aldose Reductase) Like 6, Renal-Specific Oxidoreductase, Aldehyde Reductase-Like 6, MI Oxygenase, EC 1.13.99.1, ALDRL6, Inositol Oxygenase, KSP32, RSOR, MIOX.
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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. MIOX 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
MKHHHHHHASMKVTVGPDPS LVYRPDVDPE VAKDKASFRN YTSGPLLDRV FTTYKLMHTH QTVDFVRSKH AQFGGFSYKK MTVMEAVDLL DGLVDESDPD VDFPNSFHAF QTAEGIRKAH PDKDWFHLVG LLHDLGKVLA LFGEPQWAVV GDTFPVGCRP QASVVFCDST FQDNPDLQDP RYSTELGMYQ PHCGLDRVLM SWGHDEYMYQ VMKFNKFSLP PEAFYMIRFH SFYPWHTGRD YQQLCSQQDL AMLPWVREFN KFDLYTKCPD LPDVDKLRPY YQGLIDKYCP GILSW.
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 :
SAE1 HumanDescription:
SUMO1 Activating Enzyme Subunit 1 Human Recombinant
AOS1, HSPC140, SUA1, UBLE1A, SAE1, SUMO1 Activating Enzyme Subunit 1, FLJ3091.
Product # :
ENZ-534Price :
Quantity :
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Shipped with Ice Packs
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Description
SAE1 Recombinant Human produced in E.Coli is a single, non-glycosylated polypeptide chain containing 378 amino acids (1-346 a.a.) and having a molecular mass of 42.2 kDa. The SAE1 is fused to 32 amino acid T7-Tag at N-terminus and purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
SAE1 Human solution containing 20mM Tris pH-8, 1mM DTT & 10% glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
SAE1 is part of the ubiquitin-activating E1 family of proteins and participates in the significant first step of the UBL1 conjugation pathway. Proteins conjugated to Ub are marked for progressive degradation by the 26S Proteasome. SAE1 acts as a UBLI E1 ligase mediating the ATP-dependent activation of UBL1. SAE1 binds with UBLE1A and UBLE1B to form a heterodimer which can bind UBL1. SAE1 is a dimeric enzyme that takes part as a E1 ligase for SUMO1, SUMO2, SUMO3, and probably SUMO4. SAE1 regulates ATP-dependent activation of SUMO proteins and formation of a thioester with a conserved cysteine residue on SAE2.
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Synonyms
AOS1, HSPC140, SUA1, UBLE1A, SAE1, SUMO1 Activating Enzyme Subunit 1, FLJ3091.
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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
MHHHHHHMAS MTGGQQMGRD LYDDDDKDRW GSMVEKEEAG GGISEEEAAQ YDRQIRLWGL EAQKRLRASR VLLVGLKGLG AEIAKNLILA GVKGLTMLDH EQVTPEDPGA QFLIRTGSVG RNRAEASLER AQNLNPMVDV KVDTEDIEKK PESFFTQFDA VCLTCCSRDV IVKVDQICHK NSIKFFTGDV FGYHGYTFAN LGEHEFVEEK TKVAKVSQGV EDGPDTKRAK LDSSETTMVK KKVVFCPVKE ALEVDWSSEK AKAALKRTTS DYFLLQVLLK FRTDKGRDPS SDTYEEDSEL LLQIRNDVLD SLGISPDLLP EDFVRYCFSE MAPVCAVVGG ILAQEIVKAL SQRDPPHNNF FFFDGMKGNG IVECLGPK.
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 :
lldD E. coliDescription:
L-Lactate Dehydrogenase E.Coli Recombinant
L-lactate dehydrogenase [cytochrome], lldD, lctD, b3605, JW3580.
Product # :
ENZ-618Price :
Quantity :
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Shipped with Ice Packs
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Description
lldD E.Coli Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 420 amino acids (1-396) and having a molecular mass of 45.3kDa.lldD is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
The lldD solution (1mg/ml) contains 20mM Tris-HCl buffer (pH8.0), 10% glycerol and 1mM DTT.
Purity
Greater than 90% as determined by SDS-PAGE.
More Info
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Introduction
L-lactate dehydrogenase (lldD) is present in a various organisms, including plants and animals. lldD is an oxidoreductase which catalyses the interconversion of pyruvate and lactate with concurrent interconversion of NADH and NAD+. Seeing that lldD can catalyze the oxidation of hydroxybutyrate, it is occasionally called Hydroxybutyrate Dehydrogenase (HBD).
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Synonyms
L-lactate dehydrogenase [cytochrome], lldD, lctD, b3605, JW3580.
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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 MGSHMIISAA SDYRAAAQRI LPPFLFHYMD GGAYSEYTLR RNVEDLSEVA LRQRILKNMS DLSLETTLFN EKLSMPVALA PVGLCGMYAR RGEVQAAKAA DAHGIPFTLS TVSVCPIEEV APAIKRPMWF QLYVLRDRGF MRNALERAKA AGCSTLVFTV DMPTPGARYR DAHSGMSGPN AAMRRYLQAV THPQWAWDVG LNGRPHDLGN ISAYLGKPTG LEDYIGWLGN NFDPSISWKD LEWIRDFWDG PMVIKGILDP EDARDAVRFG ADGIVVSNHG GRQLDGVLSS ARALPAIADA VKGDIAILAD SGIRNGLDVV RMIALGADTV LLGRAFLYAL ATAGQAGVAN LLNLIEKEMK VAMTLTGAKS ISEITQDSLV QGLGKELPAA LAPMAKGNAA.
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 :
KLK5 HumanDescription:
Kallikrein-5 Human Recombinant
Kallikrein-5, Kallikrein-like protein 2, KLK-L2, Stratum corneum tryptic enzyme, KLK5, SCTE, UNQ570/PRO1132, KLKL2.
Product # :
ENZ-630Price :
Quantity :
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Description
KLK5 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 252 amino acids (67-293) and having a molecular mass of 27.8kDa.KLK5 is fused to a 25 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The KLK5 solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 2M Urea and 20% glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
Kallikrein-5 (KLK5) is a member of the serine protease family of proteolytic enzymes. KLK5 is expressed in various tissues including the salivary gland, stomach, uterus, lung, thymus, prostate, colon, brain, thyroid, and trachea. KLK5 expression is up-regulated by estrogens and progestins. KLK5 is secreted and may be involved in desquamation in the epidermis. Kallikreins which are a subgroup of serine proteases, have distinct physiological functions. Many kallikreins are associated with carcinogenesis and some have potential as novel cancer and other disease biomarkers. The KLK5 gene is one of the 15 kallikrein subfamily members located in a cluster on chromosome 19.
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Synonyms
Kallikrein-5, Kallikrein-like protein 2, KLK-L2, Stratum corneum tryptic enzyme, KLK5, SCTE, UNQ570/PRO1132, KLKL2.
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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 MGSHMIINGS DCDMHTQPWQ AALLLRPNQL YCGAVLVHPQ WLLTAAHCRK KVFRVRLGHY SLSPVYESGQ QMFQGVKSIP HPGYSHPGHS NDLMLIKLNR RIRPTKDVRP INVSSHCPSA GTKCLVSGWG TTKSPQVHFP KVLQCLNISV LSQKRCEDAY PRQIDDTMFC AGDKAGRDSC QGDSGGPVVC NGSLQGLVSW GDYPCARPNR PGVYTNLCKF TKWIQETIQA NS.
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 :
PHOSPHO1 HumanDescription:
Phosphatase Orphan-1 Human Recombinant
Phosphoethanolamine/phosphocholine phosphatase, Phosphatase, Orphan 1, EC 3.1.3.75, Phospho1.
Product # :
ENZ-363Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Human Phospho1 Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 295 amino acids and having a molecular mass of 31.3 kDa. The Human Phospho1 is fused to a 14 aa His tag at N-Terminus. Human Phosphocholine Phosphatase is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Filtered (0.4µm) and lyophilized from 0.5mg/ml in 30mM acetate buffer pH-4.
Purity
Greater than 95% as determined by SDS-PAGE.
More Info
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Introduction
PHOSPHO1 is involved in mineralization process & plays a role in bone and cartilage matrix mineralization.
PHOSPHO1 is expressed at sites of mineralization in bone and cartilage. Highly expressed in osteoblast cell line SaOS-2 which produces a mineralized matrix.
Orphan-1 is collagen type -2 is specific for cartilaginous tissues. Orphan1 is essential for the normal embryonic development of the skeleton, for linear growth and for the ability of cartilage to resist compressive forces.
Phosphoethanolamine (2-O3POCH2CH2NH3) is a key intermediate in the formation of cephalins, it is formed in liver and brain by phosphorylation of ethanolamine.
PHOSPHO2 and PHOSPHO1 suggest subtle differences in the charge distributions around the putative substrate entry site and in the location of potential H-bond donors.
PHOSPHO1 exhibits high specific phosphoethanolamine and phosphocholine phosphatase activities PHOSPHO1 is a phosphatase enzyme for which expression is upregulated in mineralizing cells. PHOSPHO1 has been implicated in the generation of Pi for matrix mineralization, a process central to skeletal development. PHOSPHO1 is a member of the haloacid dehalogenase (HAD) superfamily of Mg2+-dependent hydrolases. PHOSPHO1 exhibits high specific activities toward phosphoethanolamine (PEA) and phosphocholine (PCho). -
Synonyms
Phosphoethanolamine/phosphocholine phosphatase, Phosphatase, Orphan 1, EC 3.1.3.75, Phospho1.
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Physical Appearance
Filtered 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.
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Solubility
It is recommended to add 0.1M Acetate buffer pH4 to prepare a working stock solution of approximately 0.5mg/ml and let the lyophilized pellet dissolve completely. For conversion into higher pH value, we recommend intensive dilution by relevant buffer to a concentration of 10µg/ml. In higher concentrations the solubility of this protein is limited. Product 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
MRGSHHHHHH GMASMSGCFP VSGLRCLSRD GRMAAQGAPR FLLTFDFDET IVDENSDDSI VRAAPGQRLP ESLRATYREG FYNEYMQRVF KYLGEQGVRP RDLSAIYEAI PLSPGMSDLL QFVAKQGACF EVILISDANT FGVESSLRAA GHHSLFRRIL SNPSGPDARG LLALRPFHTH SCARCPANMC KHKVLSDYLR ERAHDGVHFE RLFYVGDGAN DFCPMGLLAG GDVAFPRRGY PMHRLIQEAQ KAEPSSFRAS VVPWETAADV RLHLQQVLKSC.
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 :
STK17A HumanDescription:
Serine/Threonine Kinase 17A Human Recombinant
DRAK1, Serine/threonine-protein kinase 17A, DAP kinase-related apoptosis-inducing protein kinase 1, STK17A.
Product # :
PKA-314Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
STK17A Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 281 amino acids (64-321 a.a) and having a molecular mass of 31.9kDa.STK17A is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
STK17A protein solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 10% glycerol and 0.4M Urea.
Purity
Greater than 80.0% as determined by SDS-PAGE.
More Info
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Introduction
STK17A belongs to the DAP kinase-associated apoptosis-inducing protein kinase family and encodes an autophosphorylated nuclear protein with a protein kinase domain. STK17A acts as a positive regulator of apoptosis. STK17A is greatly expressed in the placenta with lower levels in the heart, lung, skeletal muscle, kidney and pancreas.
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Synonyms
DRAK1, Serine/threonine-protein kinase 17A, DAP kinase-related apoptosis-inducing protein kinase 1, STK17A.
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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 MGSGRELGRG KFAVVRKCIK KDSGKEFAAK FMRKRRKGQD CRMEIIHEIA VLELAQDNPW VINLHEVYET ASEMILVLEY AAGGEIFDQC VADREEAFKE KDVQRLMRQI LEGVHFLHTR DVVHLDLKPQ NILLTSESPL GDIKIVDFGL SRILKNSEEL REIMGTPEYV APEILSYDPI SMATDMWSIG VLTYVMLTGI SPFLGNDKQE TFLNISQMNL SYSEEEFDVL SESAVDFIRT LLVKKPEDRA TAEECLKHPW L.
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 :
REV1 HumanDescription:
REV1 Polymerase Human Recombinant
REV1 Polymerase (DNA Directed), REV1L, Alpha Integrin-Binding Protein 80, Rev1-Like Terminal Deoxycytidyl Transferase, AIBP80, REV1 (Yeast Homolog)- Like, REV1 Homolog (S. Cerevisiae) , REV1-Like (Yeast) , DNA Repair Protein REV1, REV1 Homolog, REV1- Like, EC 2.7.7.-.
Product # :
ENZ-796Price :
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Shipping Method :
Shipped with Ice Packs
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Description
REV1 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 227 amino acids (51-256) and having a molecular mass of 25.2kDa.REV1 is fused to a 21 amino acid His-tag at N-terminus.
Source
Escherichia Coli.
Formulation
The REV1 solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.4M Urea and 10% glycerol.
Purity
Greater than 85.0% as determined by SDS-PAGE.
More Info
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Introduction
REV1 Polymerase (REV1) contains a BRCT domain, which is imperative in protein-protein interactions. REV1 is a deoxycytidyl transferase involved in DNA repair. REV1 assists in the 1st step in the bypass of abasic lesions by the incorporation of a nucleotide opposite the lesion. REV1 is essential for normal generation of mutations by physical and chemical agents. REV1 transfers a dCMP residue from dCTP to the 3'-end of a DNA primer in a template-dependent reaction. A role for the human Rev1-like protein has been suggested as a scaffold which recruits DNA polymerases involved in translesion synthesis (TLS) of damaged DNA.
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Synonyms
REV1 Polymerase (DNA Directed), REV1L, Alpha Integrin-Binding Protein 80, Rev1-Like Terminal Deoxycytidyl Transferase, AIBP80, REV1 (Yeast Homolog)- Like, REV1 Homolog (S. Cerevisiae) , REV1-Like (Yeast) , DNA Repair Protein REV1, REV1 Homolog, REV1- Like, EC 2.7.7.-.
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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 MGVAIYVNGY TDPSAEELRK LMMLHGGQYH VYYSRSKTTH IIATNLPNAK IKELKGEKVI RPEWIVESIK AGRLLSYIPY QLYTKQSSVQ KGLSFNPVCR PEDPLPGPSN IAKQLNNRVN HIVKKIETEN EVKVNGMNSW NEEDENNDFS FVDLEQTSPG RKQNGIPHPR GSTAIFNGHT PSSNGALKTQ DCLVPMVNSV ASRLSPA.
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 :
PGP HumanDescription:
Phosphoglycolate Phosphatase Human Recombinant
Phosphoglycolate phosphatase, PGP, PGPase.
Product # :
ENZ-692Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
PGP produced in E.Coli is a single, non-glycosylated polypeptide chain containing 345 amino acids (1-321 a.a.) and having a molecular mass of 36.5kDa. PGP is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The PGP protein solution (0.5mg/1ml) is formulated in 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 10% glycerol and 1mM DTT.
Purity
Greater than 95% as determined by SDS-PAGE.
More Info
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Introduction
Phosphoglycolate phosphatase (PGP) is discovered in all tissues including red cells, lymphocytes and cultured fibroblasts (at protein level). PGP is most active in skeletal muscle and cardiac muscle. The catalytic activity of PGP is 2-phosphoglycolate + H2O = glycolate + phosphate. Diseases associated with PGP include tardive dyskinesia and polycystic kidney disease.
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Synonyms
Phosphoglycolate phosphatase, PGP, PGPase.
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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 MGSHMAAAEA GGDDARCVRL SAERAQALLA DVDTLLFDCD GVLWRGETAV PGAPEALRAL RARGKRLGFI TNNSSKTRAA YAEKLRRLGF GGPAGPGASL EVFGTAYCTA LYLRQRLAGA PAPKAYVLGS PALAAELEAV GVASVGVGPE PLQGEGPGDW LHAPLEPDVR AVVVGFDPHF SYMKLTKALR YLQQPGCLLV GTNMDNRLPL ENGRFIAGTG CLVRAVEMAA QRQADIIGKP SRFIFDCVSQ EYGINPERTV MVGDRLDTDI LLGATCGLKT ILTLTGVSTL GDVKNNQESD CVSKKKMVPD FYVDSIADLL PALQG.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
CASP3 HumanDescription:
Caspase 3 Apoptosis-Related Cysteine Peptidase Human Recombinant
Caspase 3 Apoptosis-Related Cysteine Peptidase, CPP32 Caspase 3 Apoptosis-Related Cysteine Protease, Cysteine Protease CPP32, Protein Yama, CASP-3, CPP-32, SCA-1, SREBP Cleavage Activity 1, EC 3.4.22.56, CPP32B, caspase-3, PARP Cleavage Protease, procaspase3, Apopain, EC 3.4.22, CASP3.
Product # :
ENZ-791Price :
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Shipping Method :
Shipped with Ice Packs
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Description
CASP3 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 103 amino acids (176-277) and having a molecular mass of 12kDa.CASP3 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The CASP3 solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.4M Urea and 10% glycerol.
Purity
Greater than 80.0% as determined by SDS-PAGE.
More Info
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Introduction
Caspase 3 Apoptosis-Related Cysteine Peptidase (CASP3) belongs to the cysteine-aspartic acid protease (caspase) family. Sequential activation of caspases plays a key role in the execution-phase of cell apoptosis. Caspases exist as inactive proenzymes which undergo proteolytic processing at conserved aspartic residues to generate 2 subunits, large and small, that dimerize to create the active enzyme. CASP3 protein cleaves and activates caspases 6, 7 and 9, and the protein itself is processed by caspases 8, 9 and 10. CASP3 is the leading caspase involved in the cleavage of amyloid-beta 4A precursor protein, which is linked with neuronal death in Alzheimer's disease. In addition, CASP3 is involved in the cleavage of huntingtin. CASP3 also cleaves and activates sterol regulatory element binding proteins (SREBPs) between the basic helix-loop-helix leucine zipper domain and the membrane attachment domain. CASP3 initiates cell adhesion in sympathetic neurons through RET cleavage.
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Synonyms
Caspase 3 Apoptosis-Related Cysteine Peptidase, CPP32 Caspase 3 Apoptosis-Related Cysteine Protease, Cysteine Protease CPP32, Protein Yama, CASP-3, CPP-32, SCA-1, SREBP Cleavage Activity 1, EC 3.4.22.56, CPP32B, caspase-3, PARP Cleavage Protease, procaspase3, Apopain, EC 3.4.22, CASP3.
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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
MSGVDDDMAC HKIPVEADFL YAYSTAPGYY SWRNSKDGSW FIQSLCAMLK QYADKLEFMH ILTRVNRKVA TEFESFSFDA TFHAKKQIPC IVSMLTKELY FYH.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
LDHA, E.Coli ActiveDescription:
Lactate Dehydrogenase A, BioActive E.Coli Recombinant
LDH-A, GSD11, LDH1, LDHM, PIG19, EC 1.1.1.27, lactate dehydrogenase M, LDH-M, LDH-1, L-lactate dehydrogenase A chain, LDH muscle subunit, Renal carcinoma antigen NY-REN-59, Cell proliferation-inducing gene 19 protein, LDHA.
Product # :
ENZ-1144Price :
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Shipped with Ice Packs
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Description
LDHA E.Coli Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 353 amino acids (1-329) and having a molecular mass of 39.1 kDa.LDHA E.Coli is fused to a 24 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
LDHA E.Coli protein (1mg/ml) is formulated in 20mM Tris-HCl buffer (pH 8.0), containing 100mM NaCland 10% glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Biological Activity
Specific activity is > 200unit/mg. 1 unit converts 1.0 umole of pyruvate to L-lactate and beta-NAD per minute at pH 7.5 at 37˚C
More Info
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Introduction
D-lactate dehydrogenase or ldhA is an enzyme, part of the D-lactate dehydrogenase protein family. IDHA is a cytochrome that enhances the catalyzation of D-lactate dehydrogenase ldhA reaction. This enzyme has 2 substrates ((D) -lactate & ferricytochrome c), thus, it has 2 end products (pyruvate & ferrocytochrome c).
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Synonyms
LDH-A, GSD11, LDH1, LDHM, PIG19, EC 1.1.1.27, lactate dehydrogenase M, LDH-M, LDH-1, L-lactate dehydrogenase A chain, LDH muscle subunit, Renal carcinoma antigen NY-REN-59, Cell proliferation-inducing gene 19 protein, LDHA.
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Physical Appearance
Sterile Filtered colorless solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSHMKLAVY STKQYDKKYL QQVNESFGFE LEFFDFLLTE KTAKTANGCE AVCIFVNDDG SRPVLEELKK HGVKYIALRC AGFNNVDLDA AKELGLKVVR VPAYDPEAVA EHAIGMMMTL NRRIHRAYQR TRDANFSLEG LTGFTMYGKT AGVIGTGKIG VAMLRILKGF GMRLLAFDPY PSAAALELGV EYVDLPTLFS ESDVISLHCP LTPENYHLLN EAAFEQMKNG VMIVNTSRGA LIDSQAAIEA LKNQKIGSLG MDVYENERDL FFEDKSNDVI QDDVFRRLSA CHNVLFTGHQ AFLTAEALTS ISQTTLQNLS NLEKGETCPN ELV
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 :
ADK Human, ActiveDescription:
Adenosine Kinase Human Recombinant, Active
Adenosine 5'-phosphotransferase, EC 2.7.1.20, AK, ADK, Adenosine Kinase, Adenosine 5-Phosphotransferase, Testicular Tissue Protein Li 14, EC 2.7.1.
Product # :
PKA-108Price :
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Shipped with Ice Packs
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Description
ADK produced in E.Coli is a single, non-glycosylated polypeptide chain containing 362 amino acids (22-362a.a.) and having a molecular mass of 40.5kDa.ADK is fused to a 21 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The ADK protein solution (0.5mg/ml) contains 20% glycerol, 20mM Tris-HCl buffer (pH8.0), 1mM DTT, 1mM EDTA & 50mM NaCl.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Biological Activity
Specific activity is > 30 pmol/min/ug and is defined as the amount of enzyme that convert 1.0 pmole of adenosine to AMP per minute at pH 7.5 at 37C in a couple system with PK and LDH.
More Info
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Introduction
Adenosine Kinase is an abundant enzyme in mammalian tissues which catalyzes the transfer of the gamma-phosphate from ATP to adenosine, thus is as a regulator of concentrations of both extracellular adenosine and intracellular adenine nucleotides. Adenosine has extensive effects on the cardiovascular, nervous, respiratory, and immune systems and inhibitors of the enzyme take a crucial pharmacological part in growing intravascular adenosine concentrations and acting as anti-inflammatory agents.
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Synonyms
Adenosine 5'-phosphotransferase, EC 2.7.1.20, AK, ADK, Adenosine Kinase, Adenosine 5-Phosphotransferase, Testicular Tissue Protein Li 14, EC 2.7.1.
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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 MRENILFGMG NPLLDISAVV DKDFLDKYSL KPNDQILAED KHKELFDELV KKFKVEYHAG GSTQNSIKVA QWMIQQPHKA ATFFGCIGID KFGEILKRKA AEAHVDAHYY EQNEQPTGTC AACITGDNRS LIANLAAANC YKKEKHLDLE KNWMLVEKAR
VCYIAGFFLT VSPESVLKVA HHASENNRIF TLNLSAPFIS QFYKESLMKV MPYVDILFGN ETEAATFARE QGFETKDIKE IAKKTQALPK MNSKRQRIVI FTQGRDDTIM ATESEVTAFA VLDQDQKEII DTNGAGDAFV GGFLSQLVSD KPLTECIRAG HYAASIIIRR TGCTFPEKPD
FH.
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 :
UBE2M HumanDescription:
Ubiquitin Conjugating Enzyme E2M Human Recombinant
NEDD8-conjugating enzyme Ubc12, Ubiquitin-conjugating enzyme E2 M, NEDD8 protein ligase, NEDD8 carrier protein, UBC12, hUbc12, UBC-RS2.
Product # :
ENZ-345Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
UBE2M Human Recombinant produced E. coli is a single polypeptide chain containing 207 amino acids (1-183) and having a molecular mass of 23.5kDa.UBE2M is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The UBE2M solution (1mg/1ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.2M NaCl, 1mM DTT and 20% glycerol.
Purity
Greater than 95% as determined by SDS-PAGE.
More Info
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Introduction
UbcH12 is functional in in vitro NEDDylation reactions. It has been shown to form a thioester linkage with NEDD8 in the presence of the NEDD8 activating enzyme complex Uba3/APP-BP1. APP-BP1 binds to the amyloid precursor protein (APP) carboxy terminal domain and is important in conjunction with Uba3 and UbcH12 in driving cells through the S to M checkpoint. It was demonstrated to be the E2 responsible for the NEDDylation of the Cul-1 component of the SCF (?-TRCP) complex which is important as the E3-ligase in the ubiquitinylation of I?B?. NEDDylation of Cul-1 is essential for conjugation and processing of NF-?B p105 by SCF (?-TRCP) following phosphorylation of the complex. A dominant negative form of UbcH12, previously demonstrated to sequester NEDD8 and inhibit its conjugation, inhibits both conjugation and processing of p105, which is alleviated by wild-type UbcH12.
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Synonyms
NEDD8-conjugating enzyme Ubc12, Ubiquitin-conjugating enzyme E2 M, NEDD8 protein ligase, NEDD8 carrier protein, UBC12, hUbc12, UBC-RS2.
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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 MGSHMIKLFS LKQQKKEEES AGGTKGSSKK ASAAQLRIQK DINELNLPKT CDISFSDPDD LLNFKLVICP DEGFYKSGKF VFSFKVGQGY PHDPPKVKCE TMVYHPNIDL EGNVCLNILR EDWKPVLTIN SIIYGLQYLF LEPNPEDPLN KEAAEVLQNN RRLFEQNVQR SMRGGYIGST YFERCLK
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 :
Cyclophilin G HumanDescription:
Cyclophilin-G Human Recombinant
Peptidyl-prolyl cis-trans isomerase G, PPIase G, Rotamase G, PPIG, peptidylprolyl isomerase G, Cyclophilin G, Peptidyl-prolyl isomerase G, Rotamase G, Clk-associating RS-cyclophilin, CARS-cyclophilin, CARS-Cyp, SR-cyclophilin, SR-cyp, SRcyp, CASP10, CYP, MGC133241.
Product # :
ENZ-463Price :
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Shipped with Ice Packs
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Description
Cyclophilin-G Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 195 amino acids (1-175 a.a.) and having a molecular mass of 21.6 kDa. Cyclophilin-G is fused to a 20 amino acid His Tag at N-terminus and is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Cyclophilin-G solution containing 20mM Tris-HCl pH-8, 1mM DTT and 10% glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Biological Activity
Specific activity is > 200 nmoles/min/mg, and is defined as the amount of enzyme that cleaves 1umole of suc-AAFP-pNA per minute at 25C in Tris-Hcl pH8.0 using chymotrypsin.More Info
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Introduction
Cyclophilin-G is a member of the peptidyl-prolyl cis-trans isomerase (PPIase) family. PPIases catalyze the cis-trans isomerization of proline imidic peptide bonds in oligopeptides and speeds up the protein folding. PPIG catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides and is involved in the folding, transport, and assembly of proteins. PPIG is localized to the nuclear speckles, a nuclear compartment rich in splicing factors, and cooperates with the splicing factors SC35 and pinin. Cyclophilin-G also takes part in the regulation of pre-mRNA splicing.
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Synonyms
Peptidyl-prolyl cis-trans isomerase G, PPIase G, Rotamase G, PPIG, peptidylprolyl isomerase G, Cyclophilin G, Peptidyl-prolyl isomerase G, Rotamase G, Clk-associating RS-cyclophilin, CARS-cyclophilin, CARS-Cyp, SR-cyclophilin, SR-cyp, SRcyp, CASP10, CYP, MGC133241.
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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 MGIKVQRPRC FFDIAINNQP AGRVVFELFS DVCPKTCENF RCLCTGEKGT GKSTQKPLHY KSCLFHRVVK DFMVQGGDFS EGNGRGGESI YGGFFEDESF AVKHNKEFLL SMANRGKDTN GSQFFITTKP TPHLDGHHVV FGQVISGQEV VREIENQKTD AASKPFAEVR ILSCG.
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 :
GLK E.coliDescription:
Glucokinase E.coli Recombinant
Glucokinase, Glucose kinase, glk, b2388, JW2385.
Product # :
PKA-059Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
GLK E.coli Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 344 amino acids (1-321 a.a) and having a molecular mass of 37.1kDa. GLK is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
GLK protein solution (1.0 mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl and 10% glycerol.
Purity
Greater than 95% as determined by SDS-PAGE.
More Info
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Introduction
Glucokinase also known as GLK is a member of the bacterial glucokinase family. GLK is not highly significant in E.coli since glucoseis already transported into the cell through the PTS system as glucose 6-phosphate.
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Synonyms
Glucokinase, Glucose kinase, glk, b2388, JW2385.
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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 MGSMTKYALV GDVGGTNARL ALCDIASGEI SQAKTYSGLD YPSLEAVIRV YLEEHKVEVK DGCIAIACPI TGDWVAMTNH TWAFSIAEMK KNLGFSHLEI INDFTAVSMA IPMLKKEHLI QFGGAEPVEG KPIAVYGAGT GLGVAHLVHV DKRWVSLPGE GGHVDFAPNS EEEAIILEIL RAEIGHVSAE RVLSGPGLVN LYRAIVKADN RLPENLKPKD ITERALADSC TDCRRALSLF CVIMGRFGGN LALNLGTFGG VFIAGGIVPR FLEFFKASGF RAAFEDKGRF KEYVHDIPVY LIVHDNPGLL GSGAHLRQTL GHIL.
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 :
AKR1C3 Human, HisDescription:
Aldo-Keto Reductase Family 1 Member C3 Human Recombinant, His Tag
DD3, DDX, HAKRB, HAKRe, HA1753, HSD17B5, hluPGFS, KIAA0119, AKR1C3, Aldo-keto reductase family 1 member C3, 3-alpha-HSD type 2, 17-beta-HSD 5, PGFS, DD-3.
Product # :
ENZ-406Price :
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Description
AKR1C3 Human Recombinant fused to 20 amino acid His Tag at N-terminal produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 343 amino acids (1-323 a.a.) and having a molecular mass of 39 kDa. The AKR1C3 is fused to a 20 amino acid His tag purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The AKR1C3 solution contains 20mM Tris-HCl pH-8 and 10% glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Biological Activity
Specific activity: approximately < 0.1 units/mg.
Enzymatic activity was confirmed by measuring the amount of enzyme catalyzing the oxidation of 1 micromole NADPH per minute at 25C. Specific activity was expressed as units/mg protein.More Info
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Introduction
AKR1C3 is part of the aldo/keto reductase superfamily, which has at least 40 identified proteins. AKR1C3 catalyzes the conversion of aldehydes and ketones to their corresponding alcohols by utilizing NADH and/or NADPH as cofactors. AKR1C3 displays overlapping but distinct substrate specificity. AKR1C3 catalyzes the reduction of prostaglandin (PG) D2, PGH2 and phenanthrenequinone (PQ), and the oxidation of 9alpha,11beta-PGF2 to PGD2. AKR1C3 is involved in the pathogenesis of allergic diseases such as asthma. AKR1C3 controls cell growth and/or differentiation. AKR1C3 takes part in adrenal testosterone production. AKR1C3 expression is affected by metabolic disease, and its levels are considerably reduced in response to diet-induced weight loss and correlate with leptin levels.
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Synonyms
DD3, DDX, HAKRB, HAKRe, HA1753, HSD17B5, hluPGFS, KIAA0119, AKR1C3, Aldo-keto reductase family 1 member C3, 3-alpha-HSD type 2, 17-beta-HSD 5, PGFS, DD-3.
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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).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MDSKHQCVKL NDGHFMPVLG FGTYAPPEVP RSKALEVTKL AIEAGFRHID SAHLYNNEEQ VGLAIRSKIA DGSVKREDIF YTSKLWSTFH RPELVRPALE NSLKKAQLDY VDLYLIHSPM SLKPGEELSP TDENGKVIFD IVDLCTTWEA MEKCKDAGLA KSIGVSNFNR RQLEMILNKPGLKYKPVCNQ VECHPYFNRS KLLDFCKSKD IVLVAYSALG SQRDKRWVDP NSPVLLEDPV LCALAKKHKR TPALIALRYQ LQRGVVVLAK SYNEQRIRQN VQVFEFQLTA EDMKAIDGLD RNLHYFNSDS FASHPNYPYS DEY.
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 :
GSTM1 Mouse, HisDescription:
Glutathione S-Transferase M1 Mouse Recombinant, His Tag
GST1, GTH4, GTM1, GSTM1-1, MGC26563, GSTM1a-1a, GSTM1b-1b, GSTM1, Glutathione S-transferase Mu 1, GST class-mu 1, Glutathione S-transferase GT8.7, pmGT10, GST 1-1.
Product # :
ENZ-456Price :
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Shipped with Ice Packs
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Description
GSTM1 Mouse Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 238 amino acids (1-218 a.a.) and having a molecular mass of 28.1kDa. The GTM1 is fused to a 20 amino acid His-Tag at N-Terminus and purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The GSTM1 solution contains 20 mM Tris-HCl buffer ( pH8.0), 1mM DTT and 10% glycerol
Purity
Greater than 95.0% as determined by SDS-PAGE.
Biological Activity
Specific activity is < 11 units/mg, and is defined as the amount of enzyme that conjugate 1.0 u mole of 1-chloro-2,4-dinitrobenzene (CDNB) with reduced glutathione per minute at pH 6.5 at 25C.More Info
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Introduction
Cytosolic and membrane-bound types of GST are encoded by 2 different supergene families. There are 8 classes of the soluble cytoplasmic mammalian GST: alpha, kappa, mu, omega, pi, sigma, theta and zeta. The mu class of enzymes functions in the detoxification of electrophilic compounds, including carcinogens, therapeutic drugs, environmental toxins and products of oxidative stress, by conjugation with glutathione. The genes encoding the mu class of enzymes are arranged in a gene cluster on chromosome 1p13.3 and aare highly polymorphic. These genetic differences can change an individual's resistance to carcinogens and toxins as well as affect the toxicity and efficacy of certain drugs. Null mutations of this class mu gene have been linked with the rise in a number of cancers.
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Synonyms
GST1, GTH4, GTM1, GSTM1-1, MGC26563, GSTM1a-1a, GSTM1b-1b, GSTM1, Glutathione S-transferase Mu 1, GST class-mu 1, Glutathione S-transferase GT8.7, pmGT10, GST 1-1.
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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 MPMILGYWNV RGLTHPIRML LEYTDSSYDE KRYTMGDAPD FDRSQWLNEK FKLGLDFPNL PYLIDGSHKI TQSNAILRYL ARKHHLDGET EEERIRADIV ENQVMDTRMQ LIMLCYNPDF EKQKPEFLKT IPEKMKLYSE FLGKRPWFAG DKVTYVDFLA YDILDQYRMF EPKCLDAFPN LRDFLARFEG LKKISAYMKS SRYIATPIFS KMAHWSNK.
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 :
TXNRD1 HumanDescription:
Thioredoxin Reductase 1 Human Recombinant
Thioredoxin reductase 1 cytoplasmic, TR, GRIM-12, Gene associated with retinoic and IFN-induced mortality 12 protein, KM-102-derived reductase-like factor, Thioredoxin reductase TR1, TXNRD1, GRIM12, KDRF, TR1, TXNR, TRXR1, MGC9145.
Product # :
ENZ-518Price :
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Shipped with Ice Packs
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Description
TXNRD1 Human Recombinant produced in E.Coli is a single, non-glycosylated,polypeptide chain containing 508 amino acids (161-647 a.a.) and having a molecular mass of 55.7 kDa. TXNRD1 protein is fused to a 21 amino acid His tag at N-terminus and is purified by standard chromatography.
Source
Escherichia Coli.
Formulation
TXNRD1 Human solution (0.5mg/ml) containing 1x PBS pH-7.4 & 20% glycerol.
Purity
Greater than 90% as determined by SDS-PAGE.
Biological Activity
Specific activity is > 15 units/mg, and was measured in a coupled assay with 5,5'-Dithiobis(2-nitrobenzoic acid)(DTNB)and NADPH. The amount of TNB generated by NADPH was measured in absorbance at 412 nm.More Info
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Introduction
TXNRD1 belongs to the selenium-containing pyridine nucleotide-disulphide oxidoreductase family, which has a conserved catalytic site of Cys-Val-Asn-Val-Gly-Cys. TXNRD1 decreases thioredoxins as well as other substrates, and participates in selenium metabolism and protection against oxidative stress. Inhibition of TXNRD1 activity serves as a potential treatment for cancer, AIDS and other autoimmune diseases as well as bacterial infections and parasitic diseases.
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Synonyms
Thioredoxin reductase 1 cytoplasmic, TR, GRIM-12, Gene associated with retinoic and IFN-induced mortality 12 protein, KM-102-derived reductase-like factor, Thioredoxin reductase TR1, TXNRD1, GRIM12, KDRF, TR1, TXNR, TRXR1, MGC9145.
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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 MYDYDLIIIG GGSGGLAAAK EAAQYGKKVM VLDFVTPTPL GTRWGLGGTC VNVGCIPKKL MHQAALLGQALQDSRNYGWK VEETVKHDWD RMIEAVQNHI GSLNWGYRVA LREKKVVYEN AYGQFIGPHR IKATNNKGKE KIYSAERFLI ATGERPRYLGIPGDKEYCIS SDDLFSLPYC PGKTLVVGAS YVALECAGFL AGIGLDVTVM VRSILLRGFD QDMANKIGEH MEEHGIKFIR QFVPIKVEQIEAGTPGRLRV VAQSTNSEEI IEGEYNTVML AIGRDACTRK IGLETVGVKI NEKTGKIPVT DEEQTNVPYI YAIGDILEDK VELTPVAIQAGRLLAQRLYA GSTVKCDYEN VPTTVFTPLE YGACGLSEEK AVEKFGEENI EVYHSYFWPL EWTIPSRDNN KCYAKIICNT KDNERVVGFH VLGPNAGEVT QGFAAALKCG LTKKQLDSTI GIHPVCAEVF TTLSVTKRSG ASILQAGC.
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 :
BCKDHA HumanDescription:
Branched Chain keto Acid Dehydrogenase E1 Alpha Human Recombinant
2-oxoisovalerate dehydrogenase subunit alpha mitochondrial, Branched-chain alpha-keto acid dehydrogenase E1 component alpha chain, BCKDE1A, BCKDH E1-alpha, BCKDHA, MSU, MSUD1, OVD1A, FLJ45695.
Product # :
ENZ-090Price :
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Shipped with Ice Packs
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Description
BCKDHA Human Recombinant fused with a 21 amino acid His tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 421 amino acids (46-445 a.a.) and having a molecular mass of 47.8kDa. The BCKDHA is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The BCKDHA solution (0.25 mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 5mM DTT, 30% glycerol and 0.2M NaCl.
Purity
Greater than 80.0% as determined by SDS-PAGE.
More Info
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Introduction
Branched-chain ?-keto acid dehydrogenase E1 component ? chain (BCKDHA) is a member of the BCKDHA family. The BCKD (branched-chain alpha-keto acid dehydrogenase) complex is an inner mitochondrial enzyme complex which catalyzes the second major step in the catabolism of the branched-chain amino acids leucine, isoleucine, and valine. This complex consists of 3 catalytic components: a heterotetrameric (alpha2-beta2) branched-chain alpha-keto acid decarboxylase (E1), a dihydrolipoyl transacylase (E2), and a dihydrolipoamide dehydrogenase (E3). Mutations in the BCKDHA gene result in maple syrup urine disease, type IA.
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Synonyms
2-oxoisovalerate dehydrogenase subunit alpha mitochondrial, Branched-chain alpha-keto acid dehydrogenase E1 component alpha chain, BCKDE1A, BCKDH E1-alpha, BCKDHA, MSU, MSUD1, OVD1A, FLJ45695.
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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 MSSLDDKPQF PGASAEFIDK LEFIQPNVIS GIPIYRVMDR QGQIINPSED PHLPKEKVLK LYKSMTLLNT MDRILYESQR QGRISFYMTN YGEEGTHVGS AAALDNTDLV FGQYREAGVL MYRDYPLELF MAQCYGNISD LGKGRQMPVH YGCKERHFVT ISSPLATQIP QAVGAAYAAK RANANRVVIC YFGEGAASEG DAHAGFNFAA TLECPIIFFC RNNGYAISTP TSEQYRGDGI AARGPGYGIM SIRVDGNDVF AVYNATKEAR RRAVAENQPF LIEAMTYRIG HHSTSDDSSA YRSVDEVNYW DKQDHPISRL RHYLLSQGWW DEEQEKAWRK QSRRKVMEAF EQAERKPKPN PNLLFSDVYQ EMPAQLRKQQ ESLARHLQTY GEHYPLDHFD K.
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 :
RNPA E.ColiDescription:
Ribonuclease P protein component E.Coli Recombinant
ECK3696, Rnase P protein, RnaseP protein, b3704, JW3681, Ribonuclease P protein component, EC 3.1.26.5, Protein C5.
Product # :
ENZ-1169Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
RNPA E.Coli Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 119 amino acids (1-119a.a) and having a molecular mass of 13.7kDa.RNPA is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
RNPA protein solution (0.25mg/ml) in Phosphate-Buffered Saline (pH 7.4) and 10% Glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
Rnase P protein, AKA rnpA, is an important enzyme consisting of the C5 protein (which encoded by rnpA) and the catalytic M1 RNA (encoded by rnpB) subunits. rnpA is ribonucleoprotein that catalyzes the removal of the 50- leader elements of precursor tRNAs and generates the mature 50-end of tRNAs. This step is critical for theformation of functional tRNA molecules in bacteria, archaea and eukarya. More importantly, it has lately been established that RNase P is essential for the endonucleolytic separation of certain polycistronic tRNA transcripts such as valV valW, leuQ leuP leuV and secG leuU. Therefore, it was hypothesized that the essential function of RNase P might be related to the complete absence of a particular tRNAthat was dependent on the enzyme for initial separation from polycistronic transcripts.
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Synonyms
ECK3696, Rnase P protein, RnaseP protein, b3704, JW3681, Ribonuclease P protein component, EC 3.1.26.5, Protein C5.
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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
MVKLAFPREL RLLTPSQFTF VFQQPQRAGT PQITILGRLN SLGHPRIGLT VAKKNVRRAH ERNRIKRLTR ESFRLRQHEL PAMDFVVVAK KGVADLDNRA LSEALEKLWR RHCRLARGS
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 :
PRSS3 Human, sf9Description:
Recombinant Human Protease Serine 3, sf9
Protease, Serine, 3, Protease, Serine, 4 (Trypsin 4, Brain), Brain Trypsinogen, Mesotrypsinogen, Mesotrypsin, Trypsin III, EC 3.4.21.4 4, Trypsin IV, PRSS4, TRY3, TRY4 Protease, Serine, 3 (Mesotrypsin), Pancreatic Trypsinogen III, Serine Protease 3, Serine Protease 4, Trypsinogen IV, Trypsinogen 4, Trypsinogen 5, EC 3.4.21, MTG, T9.
Product # :
ENZ-925Price :
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Shipped with Ice Packs
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Description
PRSS3 produced in Sf9 Insect cells is a single, glycosylated polypeptide chain containing 233 amino acids (81-304a.a.) and having a molecular mass of 25.3kDa (Molecular size on SDS-PAGE will appear at approximately 28-40kDa).PRSS3 is expressed with a 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Insect cells.
Formulation
PRSS3 protein solution (0.5mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 10% glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
PRSS3 is a trypsinogen, and a member of the trypsin family of serine proteases. PRSS3 is expressed in the pancreas and brain and is unaffected by common trypsin inhibitors. It is active on peptide linkages involving the carboxyl group of lysine or arginine. PRSS3 is restricted to the locus of T cell receptor beta variable orphans on chromosome 9. 4 different isoforms encoded by 4 transcript variants were identified for this gene.
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Synonyms
Protease, Serine, 3, Protease, Serine, 4 (Trypsin 4, Brain), Brain Trypsinogen, Mesotrypsinogen, Mesotrypsin, Trypsin III, EC 3.4.21.4 4, Trypsin IV, PRSS4, TRY3, TRY4 Protease, Serine, 3 (Mesotrypsin), Pancreatic Trypsinogen III, Serine Protease 3, Serine Protease 4, Trypsinogen IV, Trypsinogen 4, Trypsinogen 5, EC 3.4.21, MTG, T9.
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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
ADPIVGGYTC EENSLPYQVS LNSGSHFCGG SLISEQWVVS AAHCYKTRIQ VRLGEHNIKV LEGNEQFINA AKIIRHPKYN RDTLDNDIML IKLSSPAVIN ARVSTISLPT APPAAGTECL ISGWGNTLSF GADYPDELKC LDAPVLTQAE CKASYPGKIT NSMFCVGFLE GGKDSCQRDS GGPVVCNGQL QGVVSWGHGC AWKNRPGVYT KVYNYVDWIK DTIAANSHHH HHH.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
NAA30 HumanDescription:
N Alpha-Acetyltransferase 30, NatC Catalytic Subunit Human Recombinant
N(Alpha)-Acetyltransferase 30, NatC Catalytic Subunit, C14orf35, NAT12, N-Acetyltransferase 12 (GCN5-Related, Putative), N-Acetyltransferase 12, NatC Catalytic Subunit, MAK3, N-Acetyltransferase MAK3 Homolog, Chromosome 14 Open Reading Frame 35, Mak3p, NAT12P, N-Alpha-Acetyltransferase 30, N-Alpha-Acetyltransferase 30, NatC Catalytic Subunit, Putative N-Acetyltransferase, EC 2.3.1.88.
Product # :
ENZ-720Price :
Quantity :
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Shipped with Ice Packs
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Description
NAA30 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 385 amino acids (1-362 a.a) and having a molecular mass of 41.7kDa.NAA30 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
NAA30 protein solution (0.25mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 10% glycerol and 1mM DTT.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
N-alpha-acetyltransferase 30 (NAA30) is catalytic subunit of the N-terminal acetyltransferase C (NatC) complex. NAA30 catalyzes acetylation of the N-terminal methionine residues of peptides beginning with Met-Leu-Ala and Met-Leu-Gly. In addition, NAA30 is essential for the lysosomal localization and function of ARL8B. The disease Eastern equine encephalitis has been associated with NAA30.
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Synonyms
N(Alpha)-Acetyltransferase 30, NatC Catalytic Subunit, C14orf35, NAT12, N-Acetyltransferase 12 (GCN5-Related, Putative), N-Acetyltransferase 12, NatC Catalytic Subunit, MAK3, N-Acetyltransferase MAK3 Homolog, Chromosome 14 Open Reading Frame 35, Mak3p, NAT12P, N-Alpha-Acetyltransferase 30, N-Alpha-Acetyltransferase 30, NatC Catalytic Subunit, Putative N-Acetyltransferase, EC 2.3.1.88.
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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 MGSMAEVPPG PSSLLPPPAP PAPAAVEPRC PFPAGAALAC CSEDEEDDEE HEGGGSRSPA GGESATVAAK GHPCLRCPQP PQEQQQLNGL ISPELRHLRA AASLKSKVLS VAEVAATTAT PDGGPRATAT KGAGVHSGER PPHSLSSNAR TAVPSPVEAA AASDPAAARN GLAEGTEQEE EEEDEQVRLL SSSLTADCSL RSPSGREVEP GEDRTIRYVR YESELQMPDI MRLITKDLSE PYSIYTYRYF IHNWPQLCFL AMVGEECVGA IVCKLDMHKK MFRRGYIAML AVDSKYRRNG IGTNLVKKAI YAMVEGDCDE VVLETEITNK SALKLYENLG FVRDKRLFRY YLNGVDALRL KLWLR
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 :
NUDT2 HumanDescription:
Nudix Type Motif 2 Human Recombinant
nudix (nucleoside diphosphate linked moiety X)-type motif 2, APAH1, Diadenosine 5',5'''-P1,P4-tetraphosphate asymmetrical hydrolase, Diadenosine tetraphosphatase, Nucleoside diphosphate-linked moiety X motif 2, Ap4Aase, EC 3.6.1.17, MGC10404, Ap4A hydrolase 1, bis(5'-nucleosyl)-tetraphosphatase (asymmetrical), diadenosine 5',5''-P1,P4-tetraphosphate pyrophosphohydrolase.
Product # :
ENZ-063Price :
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Shipping Method :
Shipped with Ice Packs
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Description
NUDT2 produced in E.Coli is a single, non-glycosylated polypeptide chain containing 167 amino acids (1-147a.a.) and having a molecular mass of 19.0kDa.NUDT2 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The NUDT2 protein solution (1mg/1ml) is formulated in 20mM Tris-HCl buffer (pH8.0) 1mM DTT, 0.1M NaCl and 10% glycerol.
Purity
Greater than 90% as determined by SDS-PAGE.
More Info
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Introduction
NUDT2 belongs to the MutT family of nucleotide pyrophosphatases, a subset of the larger NUDIX hydrolase family. NUDT2 conserves homeostasis by using water to cleave the metabolite NUDT symmetrically back into its original ATP and AMP molecules. In addition, NUDT2 is active towards other adenosine and diadenosine polyphosphates with four or more phosphate groups, however, not towards diadenosine triphosphate. NUDT2 has a role in heat shock and metabolic stress by regulating intracellular dinucleoside polyphosphate concentrations.
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Synonyms
nudix (nucleoside diphosphate linked moiety X)-type motif 2, APAH1, Diadenosine 5',5'''-P1,P4-tetraphosphate asymmetrical hydrolase, Diadenosine tetraphosphatase, Nucleoside diphosphate-linked moiety X motif 2, Ap4Aase, EC 3.6.1.17, MGC10404, Ap4A hydrolase 1, bis(5'-nucleosyl)-tetraphosphatase (asymmetrical), diadenosine 5',5''-P1,P4-tetraphosphate pyrophosphohydrolase.
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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 MALRACGLII FRRCLIPKVD NNAIEFLLLQ ASDGIHHWTP PKGHVEPGED DLETALRETQ EEAGIEAGQL TIIEGFKREL NYVARNKPKT VIYWLAEVKD YDVEIRLSHE HQAYRWLGLE EACQLAQFKE MKAALQEGHQ FLCSIEA
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 :
ACSF2 HumanDescription:
Acyl-CoA Synthetase Family Member 2 Human Recombinant
Acyl-CoA Synthetase Family Member 2, PPARG Binding, Long Chain Fatty Acid Acyl Co-A Ligase Like, Acyl-CoA Synthetase Family Member 2, Mitochondrial, EC 6.2.1.26, EC 6.2.1.-, FLJ20920, EC 6.2.1, AVYV493, ACSMW, Acyl-CoA synthetase family member 2, mitochondrial.
Product # :
ENZ-919Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
ACSF2 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 597 amino acids (42-615 a.a) and having a molecular mass of 66.1kDa. ACSF2 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
ACSF2 protein solution (0.5mg/ml) containing Phosphate Buffered Saline pH 7.4 and 10% glycerol.
Purity
Greater than 95% as determined by SDS-PAGE.
More Info
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Introduction
Acyl-CoA synthetase family member 2, also known as ACSF2 is a member of the ATP-dependent AMP-binding enzyme family. Acyl-CoA synthetases are a family of enzymes which catalyze the thioesterification of fatty acids with coenzymeA to form activated intermediates, which play a basic part in lipid metabolism as well as homeostasis of lipid-related processes. ACSF2 is required for the complex of lipid synthesis, energy production via beta-oxidation, protein acylation and fatty-acid dependent transcriptional regulation. Moreover, ACSF2 is required for fatty acid import into cells by the process of vectorial acylation.
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Synonyms
Acyl-CoA Synthetase Family Member 2, PPARG Binding, Long Chain Fatty Acid Acyl Co-A Ligase Like, Acyl-CoA Synthetase Family Member 2, Mitochondrial, EC 6.2.1.26, EC 6.2.1.-, FLJ20920, EC 6.2.1, AVYV493, ACSMW, Acyl-CoA synthetase family member 2, mitochondrial.
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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 MGSLSSREVD RMVSTPIGGL SYVQGCTKKH LNSKTVGQCL ETTAQRVPER EALVVLHEDV RLTFAQLKEE VDKAASGLLS IGLCKGDRLG MWGPNSYAWV LMQLATAQAG IILVSVNPAY QAMELEYVLK KVGCKALVFP KQFKTQQYYN VLKQICPEVE NAQPGALKSQ RLPDLTTVIS VDAPLPGTLL LDEVVAAGST RQHLDQLQYN QQFLSCHDPI NIQFTSGTTG SPKGATLSHY NIVNNSNILG ERLKLHEKTP EQLRMILPNP LYHCLGSVAG TMMCLMYGAT LILASPIFNG KKALEAISRE RGTFLYGTPT MFVDILNQPD FSSYDISTMC GGVIAGSPAP PELIRAIINK INMKDLVVAY GTTENSPVTF AHFPEDTVEQ KAESVGRIMP HTEARIMNME AGTLAKLNTP GELCIRGYCV MLGYWGEPQK TEEAVDQDKW YWTGDVATMN EQGFCKIVGR SKDMIIRGGE NIYPAELEDF FHTHPKVQEV QVVGVKDDRM GEEICACIRL KDGEETTVEE IKAFCKGKIS HFKIPKYIVF VTNYPLTISG KIQKFKLREQ MERHLNL.
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.