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Name :
HK3 HumanDescription:
Hexokinase-3 Human Recombinant
Hexokinase-3, EC 2.7.1.1, Hexokinase type III, HK III, HXK3, HK3.
Product # :
PKA-229Price :
Quantity :
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Shipped with Ice Packs
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Description
HK-3 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain fused to His tag at the N-terminal encoding the sequence of 943 amino acids and having a molecular mass of 101.1 kDa.HXK3 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The protein (1mg/ml) contains 20mM Tris pH 8.0 and 10% glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
Hexokinases phosphorylate glucose to produce glucose-6-phosphate, thus committing glucose to the glycolytic pathway. HK3 encodes hexokinase 3. Similar to hexokinases 1 and 2, this allosteric enzyme is inhibited by its product glucose-6-phosphate. Hexokinase3 lacks the hydrophobic N-terminal sequence critical for targeting to mitochondria. Hexpkinase3 may have anabolic functions, providing H6P for glycogen or lipid synthesis.
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Synonyms
Hexokinase-3, EC 2.7.1.1, Hexokinase type III, HK III, HXK3, HK3.
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Physical Appearance
Sterile filtered colorless solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks.Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA). Please avoid freeze-thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MDSIGSSGLR QGEETLSCSE EGLPGPSDSSE LVQECLQQFKVTRAQLQQI QASLLGSMEQ ALRGQASPAP AVRMLPTYVG STPHGTEQGD FVVLELGATG ASLRVLWVTL TGIEGHRVEP RSQEFVIPQE VMLGAGQQLF DFAAHCLSEF LDAQPVNKQGLQLGFSFSFP CHQTGLDRST LISWTKGFRC SGVEGQDVVQ LLRDAIRRQG AYNIDVVAVV NDTVGTMMGC EPGVRPCEVG LVVDTGTNAC YMEEARHVAV LDEDRGRVCV SVEWGSFSDD GALGPVLTTF DHTLDHESLN PGAQRFEKMI GGLYLGELVR LVLAHLARCG VLFGGCTSPA LLSQGSILLE HVAEMEDPST GAARVHAILQ DLGLSPGASD VELVQHVCAA VCTRAAQLCA AALAAVLSCL QHSREQQTLQ VAVATGGRVC ERHPRFCSVL QGTVMLLAPE CDVSLIPSVDGGGRGVAMVT AVAARLAAHR RLLEETLAPF RLNHDQLAAV QAQMRKAMAK GLRGEASSLR MLPTFVRATP DGSERGDFLA LDLGGTNFRV LLVRVTTGVQ ITSEIYSIPE TVAQGSGQQL FDHIVDCIVD FQQKQGLSGQ SLPLGFTFSF PCRQLGLDQG ILLNWTKGFK ASDCEGQDVV SLLREAITRR QAVELNVVAI VNDTVGTMMS CGYEDPRCEI GLIVGTGTNA CYMEELRNVAGVPGDSGRMC INMEWGAFGD DGSLAMLSTR FDASVDQASI NPGKQRFEKM ISGMYLGEIV RHILLHLTSL GVLFRGQQIQ RLQTRDIFKT KFLSEIESDS LALRQVRAIL EDLGLPLTSDDALMVLEVCQ AVSQRAAQLC GAGVAAVVEK IRENRGLEEL AVSVGVDGTL YKLHPRFSSL VAATVRELAP RCVVTFLQSE DGSGKGAALV TAVACRLAQL TRV.
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 :
APOC1 HumanDescription:
Apolipoprotein C-I Human Recombinant
Apolipoprotein C-I, Apo-CI, ApoC-I, Apolipoprotein C1, APOC1.
Product # :
CYT-812Price :
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Shipped with Ice Packs
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- sds-page
Description
APOC1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 80 amino acids (27-83 a.a.) and having a molecular mass of 9.0kDa. APOC1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
APOC1 protein solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl and 10% glycerol.
Purity
Greater than 85% as determined by SDS-PAGE.
sds-page
More Info
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Introduction
Apolipoprotein C-I (APOC1) which expressed mainly in the liver is a part of the apolipoprotein C family. APOC1 which is usually found in plasma and responsible for the activation of esterified lechitin cholesterol takes an important part in the exchange of esterified cholesterol among lipoproteins and in removal of cholesterol from tissues. APOC1 is activated when monocytes differentiate into macrophages. APOC1 protein’s main role is to inhibit CETP by altering the electric charge of HDL molecules. APOC1 is also binds free fatty acids and reduces their intracellular esterification.
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Synonyms
Apolipoprotein C-I, Apo-CI, ApoC-I, Apolipoprotein C1, APOC1.
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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 MGSTPDVSSA LDKLKEFGNT LEDKARELIS RIKQSELSAK MREWFSETFQ KVKEKLKIDS.
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Background
Apolipoprotein C-I Human Recombinant: Unraveling the Complexity of Lipid Regulation
Abstract:
Apolipoprotein C-I (ApoC-I) is a remarkable protein that plays a significant role in lipid metabolism and cardiovascular health. It is primarily synthesized in the liver and is associated with lipoproteins involved in lipid transport. This research paper aims to provide a comprehensive overview of ApoC-I human recombinant, shedding light on its physiological functions, production methods, and potential therapeutic applications. By delving into the intricacies of ApoC-I, we can gain valuable insights into its role as a key player in lipid regulation and its potential as a therapeutic target.
Introduction:
The prevalence of lipid disorders and cardiovascular diseases necessitates a deeper understanding of the mechanisms governing lipid metabolism. ApoC-I, a critical component of lipoproteins, offers unique insights into the regulation of lipid levels and its implications for cardiovascular health.
Structure and Function of Apolipoprotein C-I:
ApoC-I exhibits a complex molecular structure, comprising functional domains that enable its interaction with lipoproteins. It plays a crucial role in regulating lipoprotein metabolism by inhibiting the activity of lipoprotein lipase and modulating the clearance of triglyceride-rich lipoproteins.
Regulation of Apolipoprotein C-I Expression:
The synthesis and secretion of ApoC-I are tightly regulated processes influenced by various factors, including nutritional status and hormonal signals. Understanding the regulatory mechanisms underlying ApoC-I expression can provide insights into its role in maintaining lipid homeostasis.
Apolipoprotein C-I and Cardiovascular Diseases:
Dysregulation of ApoC-I has been associated with various lipid disorders and cardiovascular diseases. Altered levels of ApoC-I have been observed in conditions such as hypertriglyceridemia and atherosclerosis, highlighting its potential as a biomarker for cardiovascular risk assessment.
Production of Apolipoprotein C-I Human Recombinant:
Recombinant ApoC-I can be produced using advanced biotechnological approaches, including recombinant DNA technology and protein expression systems. These methods enable large-scale production, purification, and characterization of ApoC-I, facilitating its potential therapeutic applications.
Therapeutic Potential of Apolipoprotein C-I Human Recombinant:
Targeting ApoC-I opens up exciting avenues for therapeutic interventions in lipid disorders and cardiovascular diseases. Modulating ApoC-I expression or function holds promise for restoring lipid balance and reducing the risk of cardiovascular complications.
Conclusion:
Apolipoprotein C-I human recombinant represents a fascinating area of research in the field of lipid metabolism and cardiovascular health. By unraveling the intricate interplay between ApoC-I, lipoproteins, and cardiovascular diseases, we can pave the way for novel therapeutic strategies and improved risk assessment. Further studies are required to fully understand the therapeutic potential of ApoC-I human recombinant and translate these findings into clinical applications.
What is the molecular weight/Mw of APOC1 Protein?
APOC1 Protein has a total Mw of 9kDa.
What is the source or expression system of APOC1 Protein?
Escherichia Coli.
What is the Purity of APOC1 Protein?
APOC1 Protein is >85% pure as determined by SDS-PAGE.
What is the Biological Activity of APOC1 Protein?
The biological functionality of APOC1 Protein will be determined in the future.
What is the amino acid sequence of APOC1 Protein?
MGSSHHHHHH SSGLVPRGSH MGSTPDVSSA LDKLKEFGNT LEDKARELIS RIKQSELSAK MREWFSETFQ KVKEKLKIDS.
What applications can APOC1 Protein be used in?
APOC1 Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for APOC1 Protein?
The endotoxin level is minimal, APOC1 Protein was purified using conventional chromatography techniques.
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 :
EXOSC10 HumanDescription:
Exosome Component 10 Human Recombinant
Exosome component 10, Polymyositis/scleroderma autoantigen 2, Autoantigen PM/Scl 2, Polymyositis/scleroderma autoantigen 100 kDa, PM/Scl-100, P100 polymyositis-scleroderma overlap syndrome-associated autoantigen, EXOSC10, PMSCL, PMSCL2, p2, p3, p4, RRP6, Rrp6p, PM-Scl.
Product # :
PRO-444Price :
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Shipped with Ice Packs
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Description
EXOSC10 Human Recombinant produced in SF9 is a glycosylated, polypeptide chain having a molecular mass of 102 kDa. EXOSC10 is expressed with a -6xHis tag and purified by proprietary chromatographic techniques.
Source
Sf9 insect cells.
Formulation
EXOSC10 is supplied in 20mM HEPES, pH-7.5, 100mM NaCl, 0.01mM EDTA, 0.02% SDS.
Purity
Greater than 93% as determined by SDS-PAGE.
More Info
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Introduction
EXOSC10 is a nucleolar protein and represents one crucial component of the so-called "PM/Scl complex" or "nuclear exosome", which is an RNA-processing complex consisting of a number of exoribonucleases (not to be confused with certain multivesicular bodies which are shed by cultured cells into the culture fluid and are also called exosomes).
Autoantibodies against EXOSC10 occur in patients suffering from polymyositis, scleroderma or polymyositis/scleroderma overlap syndromes. While antibodies to other components of the exosome complex (PM/Scl 75, several Rrp proteins) can be found in some sera, practically all patients with autoantibodies against the PM/Scl complex are positive for EXOSC10 antibodies, making this specificity an important marker. The presence of EXOSC10 autoantibodies is a comparatively "good" prognostic sign in polymyositis/scleroderma overlap syndrome unlike the poor prognosis seen when other myositis and systemic sclerosis specific autoantibodies are present. -
Synonyms
Exosome component 10, Polymyositis/scleroderma autoantigen 2, Autoantigen PM/Scl 2, Polymyositis/scleroderma autoantigen 100 kDa, PM/Scl-100, P100 polymyositis-scleroderma overlap syndrome-associated autoantigen, EXOSC10, PMSCL, PMSCL2, p2, p3, p4, RRP6, Rrp6p, PM-Scl.
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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.
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Immunological Functions
1. Binds IgG-type human auto-antibodies.2. Standard ELISA test (checker-board analysis of positive/negative sera panels).
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coating concentration
0.4-0.8 µg/ml (depending on the type of ELISA plate and coating buffer).Suitable for biotinylation and iodination.
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Applications
Western-Blot with monoclonal anti-hexa-His-tag antibody & polymyositis patient sera.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
POR HumanDescription:
P450 Oxidoreductase Human Recombinant
P450 (Cytochrome) Oxidoreductase, EC 1.6.2.4, CYPOR, P450R, CPR, NADPH-Dependent Cytochrome P450 Reductase, NADPH--Cytochrome P450 Reductase, NADPH--cytochrome P450 reductase.
Product # :
ENZ-890Price :
Quantity :
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Description
POR produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 686 amino acids (1-680a.a.) and having a molecular mass of 77.9kDa. POR is expressed with a 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
POR protein solution (0.25mg/ml) contains Phosphate buffer saline (pH 7.4) and 10% glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
P450 Oxidoreductase, also known as POR is a flavoprotein which contributes electrons to all microsomal P450 enzymes. POR is localized to the endoplasmic reticulum, where it is also capable of transfering electrons to heme oxygenase as well as cytochrome b5. POR is structurally related to two separate flavoprotein families; first one is ferredoxin nucleotide reductase and the second flavodoxin.
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Synonyms
P450 (Cytochrome) Oxidoreductase, EC 1.6.2.4, CYPOR, P450R, CPR, NADPH-Dependent Cytochrome P450 Reductase, NADPH--Cytochrome P450 Reductase, NADPH--cytochrome P450 reductase.
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Physical Appearance
Sterile filtered colorless solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MINMGDSHVD TSSTVSEAVA EEVSLFSMTD MILFSLIVGL LTYWFLFRKK KEEVPEFTKI QTLTSSVRES SFVEKMKKTG RNIIVFYGSQ TGTAEEFANR LSKDAHRYGM RGMSADPEEY DLADLSSLPE IDNALVVFCM ATYGEGDPTD NAQDFYDWLQ ETDVDLSGVK FAVFGLGNKT YEHFNAMGKY VDKRLEQLGA QRIFELGLGD DDGNLEEDFI TWREQFWLAV CEHFGVEATG EESSIRQYEL VVHTDIDAAK VYMGEMGRLK SYENQKPPFD AKNPFLAAVT TNRKLNQGTE RHLMHLELDI SDSKIRYESG DHVAVYPAND SALVNQLGKI LGADLDVVMS LNNLDEESNK KHPFPCPTSY RTALTYYLDI TNPPRTNVLY ELAQYASEPS EQELLRKMAS SSGEGKELYL SWVVEARRHI LAILQDCPSL RPPIDHLCEL LPRLQARYYS IASSSKVHPN SVHICAVVVE YETKAGRINK GVATNWLRAK EPVGENGGRA LVPMFVRKSQ FRLPFKATTP VIMVGPGTGV APFIGFIQER AWLRQQGKEV GETLLYYGCR RSDEDYLYRE ELAQFHRDGA LTQLNVAFSR EQSHKVYVQH LLKQDREHLW KLIEGGAHIY VCGDARNMAR DVQNTFYDIV AELGAMEHAQ AVDYIKKLMT KGRYSLDVWS HHHHHH.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
TXN1, HisDescription:
Thioredoxin Recombinant, His Tag
Thioredoxin-1, Trx-1, trxA, fipA, tsnC, b3781, JW5856.
Product # :
PRO-784Price :
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Description
Recombinant Thioredoxin produced in E.Coli is a single, non-glycosylated polypeptide chain containing 117 amino acids (2-109 a.a.) and having a molecular mass of 12.8kDa. TRX contains 9 amino acid His Tag N-terminus and is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The TRX His Tag protein solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 10% glycerol and 1mM DTT.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Biological Activity
Specific activity is >70 A650/cm/min/mg, detected by measuring the increase of insulin precipitation in absorbance at 650 nm resulting from the reduction of insulin.
More Info
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Introduction
Thioredoxins are small disulphide-containing redox proteins (within the conserved Cys-Gly-Pro-Cys active site) that have been found in all the kingdoms of living organisms. Thioredoxin contains a single disulfide active site and serves as a general protein disulphide oxidoreductase. Thioredoxins are involved in the first unique step in DNA synthesis. It interacts with a broad range of proteins by a redox mechanism based on reversible oxidation of two cysteine thiol groups to a disulphide, accompanied by the transfer of two electrons and two protons. The net result is the covalent interconversion of a disulphide and a dithiol. Trx also provides control over a number of transcription factors affecting cell proliferation and death through a mechanism referred to as redox regulation. It has been suggested that thioredoxin may catalyze the formation of correct disulfides during protein folding because of its ability to act as an efficient oxidoreductant. This could be especially useful in
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Synonyms
Thioredoxin-1, Trx-1, trxA, fipA, tsnC, b3781, JW5856.
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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
MHHHHHHMGS DKIIHLTDDS FDTDVLKADG AILVDFWAEW CGPCKMIAPI LDEIADEYQG KLTVAKLNID QNPGTAPKYG IRGIPTLLLF KNGEVAATKV GALSKGQLKE FLDANLAGS.
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 :
UPP1 HumanDescription:
Uridine Phosphorylase 1 Human Recombinant
UP, UPASE, UPP, UrdPase 1.
Product # :
ENZ-560Price :
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Description
UPP1 Human Recombinant protein produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 330 amino acids (1-310) and having a molecular mass of 29.3 kDa. UPP1 is fused to a 20 amino acid His Tag at N-terminus and is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
UPP1 protein solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 1mM DTT, 0.2M NaCl and 40% glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
UPP1 catalyzes the reversible phosphorylytic cleavage of uridine and deoxyuridine to uracil and ribose- or deoxyribose-1-phosphate which are used as carbon and energy sources or in the release of pyrimidine bases for nucleotide synthesis. UPP1 is part of the family of glycosyltransferases, specifically the pentosyltransferases. Pyrimidine nucleoside phosphorylases add ribose or deoxyribose to pyrimidine bases to form nucleosides that can be incorporated into RNA or DNA.
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Synonyms
UP, UPASE, UPP, UrdPase 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 MAATGANAEK AESHNDCPVR LLNPNIAKMK EDILYHFNLT TSRHNFPALF GDVKFVCVGG SPSRMKAFIR CVGAELGLDC PGRDYPNICA GTDRYAMYKV GPVLSVSHGM GIPSISIMLH ELIKLLYYAR
CSNVTIIRIG TSGGIGLEPG TVVITEQAVD TCFKAEFEQI VLGKRVIRKT DLNKKLVQEL LLCSAELSEF TTVVGNTMCT LDFYEGQGRL DGALCSYTEK DKQAYLEAAY AAGVRNIEME SSVFAAMCSA CGLQAAVVCV TLLNRLEGDQ
ISSPRNVLSE YQQRPQRLVS YFIKKKLSKA.
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 :
HARS Human, HisDescription:
Histidyl-tRNA Synthetase Human Recombinant, His Tag
Histidyl-tRNA synthetase cytoplasmic, Histidine--tRNA ligase, HisRS, HARS, HRS, FLJ20491.
Product # :
ENZ-001Price :
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Shipped with Ice Packs
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Description
HARS Human Recombinant fused with a 23 amino acid His tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 532 amino acids (1-509 a.a.) and having a molecular mass of 59.4kDa. The HARS is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The HARS solution (1mg/ml) contains 20mM Tris-HCl buffer(pH 8.0), 10% glycerol,
1mM DTT and 0.1M NaCl.Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
Histidyl-tRNA synthetase (HARS) functions to catalyze the aminoacylation of tRNAs by their corresponding amino acids. HARS is a member of the class II family of aminoacyl-tRNA synthetases. HARS is responsible for the synthesis of histidyl-transfer RNA, which is vital for the incorporation of histidine into proteins. HARS is a frequent target of autoantibodies in the human autoimmune disease polymyositis/dermatomyositis.
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Synonyms
Histidyl-tRNA synthetase cytoplasmic, Histidine--tRNA ligase, HisRS, HARS, HRS, FLJ20491.
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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 MGSMAERAAL EELVKLQGER VRGLKQQKAS AELIEEEVAK LLKLKAQLGP DESKQKFVLK TPKGTRDYSP RQMAVREKVF DVIIRCFKRH GAEVIDTPVF ELKETLMGKY GEDSKLIYDL KDQGGELLSL RYDLTVPFAR YLAMNKLTNI KRYHIAKVYR RDNPAMTRGR YREFYQCDFD IAGNFDPMIP DAECLKIMCE ILSSLQIGDF LVKVNDRRIL DGMFAICGVS DSKFRTICSS VDKLDKVSWE EVKNEMVGEK GLAPEVADRI GDYVQQHGGV SLVEQLLQDP KLSQNKQALE GLGDLKLLFE YLTLFGIDDK ISFDLSLARG LDYYTGVIYE AVLLQTPAQA GEEPLGVGSV AAGGRYDGLV GMFDPKGRKV PCVGLSIGVE RIFSIVEQRL EALEEKIRTT ETQVLVASAQ KKLLEERLKL VSELWDAGIK AELLYKKNPK LLNQLQYCEE AGIPLVAIIG EQELKDGVIK LRSVTSREEV DVRREDLVEE IKRRTGQPLC IC.
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 :
HBG1 HumanDescription:
Hemoglobin Gamma A Human Recombinant
HBGA, HBGR, HSGGL1, PRO2979, Hemoglobin subunit gamma-1, Gamma-1-globin, Hb F Agamma, Hemoglobin gamma-1 chain, Hemoglobin gamma-A chain, HBG1.
Product # :
PRO-1502Price :
Quantity :
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Description
HBG1 Human Recombinant produced in E. coli is a single polypeptide chain containing 170 amino acids (1-147) and having a molecular mass of 18kDa. HBG1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The HBG1 solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl and 10% glycerol.
Purity
Greater than 85% as determined by SDS-PAGE.
More Info
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Introduction
The gamma globin genes which are HBG1 and HBG2, usually expressed in the fetal liver, spleen and bone marrow. 2 gamma chains together along with 2 alpha chains comprise fetal hemoglobin (HbF) which is normally replaced by mature hemoglobin (HbA) at birth. Gamma chain production continues into adulthood in several beta-thalassemias and linked situations. The two types of gamma chains differ at residue 136 where glycine is found in the G-gamma product (HBG2) and alanine is found in the A-gamma product (HBG1). The former is predominant at birth.
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Synonyms
HBGA, HBGR, HSGGL1, PRO2979, Hemoglobin subunit gamma-1, Gamma-1-globin, Hb F Agamma, Hemoglobin gamma-1 chain, Hemoglobin gamma-A chain, HBG1.
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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 MGSMGHFTEE DKATITSLWG KVNVEDAGGE TLGRLLVVYP WTQRFFDSFG NLSSASAIMG NPKVKAHGKK VLTSLGDATK HLDDLKGTFA QLSELHCDKL HVDPENFKLL GNVLVTVLAI HFGKEFTPEV QASWQKMVTA VASALSSRYH.
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 :
AFP AntibodyDescription:
Mouse Anti Human Alpha Fetoprotein
Alpha-fetoprotein, Alpha-fetoglobulin, Alpha-1-fetoprotein, AFP, FETA, HPAFP.
Product # :
ANT-718Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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- More Info
Formulation
1mg/ml containing PBS, pH-7.4, 10% Glycerol and 0.02% Sodium Azide.
More Info
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Introduction
AFP is normally synthesized in the liver, intestinal tract, and yolk sac of the fetus. Antibody to AFP has been shown to be useful in detecting hepatocellular carcinomas (HCC) and germ cell neoplasms, especially yolk sac tumors.
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Synonyms
Alpha-fetoprotein, Alpha-fetoglobulin, Alpha-1-fetoprotein, AFP, FETA, HPAFP.
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Physical Appearance
Sterile filtered colorless solution.
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Immunogen
Anti-human AFP mAb, is derived from hybridization of mouse F0 myeloma cells with spleen cells from BALB/c mice immunized with a recombinant human AFP protein 19-609 amino acids purified from insect cell.
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Ig Subclass
Mouse IgG1 heavy chain and k light chain.
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Clone
PAT73E10AT.
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Applications
AFP antibody has been tested by ELISA and Western blot analysis to assure specificity and reactivity. Since application varies, however, each investigation should be titrated by the reagent to obtain optimal results.
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Type
Mouse Anti Human Monoclonal.
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Storage Procedures
For periods up to 1 month store at 4°C, for longer periods of time, store at -20°C. Prevent freeze thaw cycles.
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Purification Method
AFP antibody was purified from mouse ascitic fluids by protein-A affinity chromatography.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
PNPO AntibodyDescription:
Pyridoxamine 5'-Phosphate Oxidase, Mouse Anti Human
Pyridoxine-5'-phosphate oxidase, Pyridoxamine-phosphate oxidase, PNPO, PDXPO, FLJ10535.
Product # :
ANT-063Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- formulation
- More Info
Formulation
1mg/ml containing PBS, pH-7.4, & 0.1% Sodium Azide.
More Info
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Introduction
Pyridoxine-5'-phosphate oxidase (PNPO) is the rate-limiting enzyme in vitamin B6 synthesis. Vitamin B6 (Pyridoxal 5-prime-phosphate or PLP) is vital for normal cellular function, and some cancer cells have notable differences in vitamin B6 metabolism compared to their normal counterparts.Vitamin B6 is an essential co-factor for enzymes involved in both homocysteine metabolism and synthesis of neurotransmitters such as catecholamine. Mutations in the PNPO gene result in PNPO deficiency, a form of neonatal epileptic encephalopathy.
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Synonyms
Pyridoxine-5'-phosphate oxidase, Pyridoxamine-phosphate oxidase, PNPO, PDXPO, FLJ10535.
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Immunogen
Anti-human PNPO mAb, is derived from hybridization of mouse FO myeloma cells with spleen cells from BALB/c mice immunized with recombinant human PNPO amino acids 57-261 purified from E. coli.
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Ig Subclass
Mouse IgG1 heavy chain and k light chain.
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Clone
PAT2C7AT.
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Applications
PNPO antibody has been tested by ELISA and Western blot analysis to assure specificity and reactivity. Since application varies, however, each investigation should be titrated by the reagent to obtain optimal results. Recommended dilution range for Western blot analysis is 1:500 ~ 1:5000.
Recommended starting dilution is 1:1000. -
Type
Mouse Anti Human Monoclonal.
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Storage Procedures
For periods up to 1 month store at 4°C, for longer periods of time, store at -20°C. Prevent freeze thaw cycles.
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Purification Method
PNPO antibody was purified from mouse ascitic fluids by protein-G affinity chromatography.
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 :
CoV-2 S1, Sf9Description:
Coronavirus 2019 Spike Glycoprotein-S1 Sf9, Recombinant
Product # :
SARS-019Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
The Sf9 derived recombinant protein contains the Coronavirus 2019 CoV-2 Spike Glycoprotein S1, Wuhan-Hu-1 strain, amino acids 1-674 fused to His tag at C-terminal.
Source
Sf9, Baculovirus Cells.
Formulation
CoV-2 S1 protein solution is supplied in DPBS.
Purity
Protein is >85% pure as determined SDS-PAGE.
More Info
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Introduction
A human infecting coronavirus (viral pneumonia) called 2019 novel coronavirus, 2019-nCoV was found in the fish market at the city of Wuhan, Hubei province of China on December 2019.
The 2019-nCoV shares an 87% identity to the 2 bat-derived severe acute respiratory syndrome 2018 SARS-CoV-2 located in Zhoushan of eastern China. 2019-nCoV has an analogous receptor-BD-structure to that of 2018 SARS-CoV, even though there is a.a. diversity so thus the 2019-nCoV might bind to ACE2 receptor protein (angiotensin-converting enzyme 2) in humans.
While bats are possibly the host of 2019-nCoV, researchers suspect that animal from the ocean sold at the seafood market was an intermediate host. RSCU analysis proposes that the 2019-nCoV is a recombinant within the viral spike glycoprotein between the bat coronavirus and an unknown coronavirus.
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Physical Appearance
Sterile Filtered clear solution.
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Stability
CoV-2 S1 Glycoprotein is shipped on ice packs. Upon arrival, Store at -20°C.
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Purification Method
Purified by Metal-Afinity chromatographic technique.
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 :
ADAL HumanDescription:
Adenosine Deaminase-Like Human Recombinant
Adenosine Deaminase-Like, Adenosine Deaminase-Like Protein, EC 3.5.4.-, EC 3.5.4, ADAL.
Product # :
ENZ-788Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
ADAL Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 292 amino acids (1-267) and having a molecular mass of 32.7kDa.ADAL is fused to a 25 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The ADAL solution (1mg/ml) contains 20mM Tris-HCl buffer (pH8.0), 10% glycerol and 0.4M Urea.
Purity
Greater than 80% as determined by Analysis by SDS-PAGE.
More Info
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Introduction
Adenosine deaminase-like protein (ADAL) is a putative nucleoside deaminase. ADAL catalyzes the hydrolytic deamination of adenosine or some similar substrate and has a role in purine metabolism.
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Synonyms
Adenosine Deaminase-Like, Adenosine Deaminase-Like Protein, EC 3.5.4.-, EC 3.5.4, ADAL.
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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 MGSEFMIEAE EQQPCKTDFY SELPKVELHA HLNGSISSHT MKKLIAQKPD LKIHDQMTVI DKGKKRTLEE CFQMFQTIHQ LTSSPEDILM VTKDVIKEFA DDGVKYLELR STPRRENATG MTKKTYVESI LEGIKQSKQE NLDIDVRYLI AVDRRGGPLV AKETVKLAEE FFLSTEGTVL GLDLSGDPTV GQAKDFLEPL LEAKKAGLKL ALHLSEIPNQ KKETQILLDL LPDRIGHGTF LNSGEGGSLD LVDFVRQHRI PLGKAWSFRS SR.
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 :
DDT HumanDescription:
D-Dopachrome Tautomerase Human Recombinant
EC 4.1.1.84, DDCT, D-dopachtome decarboxylase, D-Dopachrome Tautomerase.
Product # :
ENZ-527Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
DDT Recombinant E.coli produced in E.Coli is a single, non-glycosylated polypeptide chain containing 138 amino acids (1-118 a.a.) and having a molecular mass of 14.8 kDa. The DDT is fused to a 20 amino acids His-Tag at N-terminus and purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
DDT Human solution containing 20mM Tris-HCl pH-8, & 10% glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
DDT is an enzyme that catayzes the tautomerization of D-dopachrome to give 5,6-dihydroxyindole (DHI). DDT is part of the family of lyases, specifically the carboxy-lyases, which cleave carbon-carbon bonds. DDT shares a homologous amino acid sequence (33% identical) with MIF and has similar tautomerase activity. DDT functions a proinflammatory cytokine.
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Synonyms
EC 4.1.1.84, DDCT, D-dopachtome decarboxylase, D-Dopachrome Tautomerase.
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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 MPFLELDTNL PANRVPAGLE KRLCAAAASI LGKPADRVNV TVRPGLAMAL SGSTEPCAQL SISSIGVVGT AEDNRSHSAH FFEFLTKELA LGQDRILIRF FPLESWQIGK IGTVMTFL.
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 :
ARL2 HumanDescription:
ADP-Ribosylation Factor-Like 2 Human Recombinant
ADP-ribosylation factor-like protein 2, ARL2, ARFL2.
Product # :
PRO-074Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
ARL2 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 204 amino acids (1-184 a.a.) and having a molecular mass of 23kDa. The ARL2 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The ARL2 solution (0.25 mg/ml) contains 20mM Tris-HCl buffer (pH8.0), 0.1mM PMSF, 1mM DTT and 40% Glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
-
Introduction
ARL2 is a member of the ADP-ribosylation factor (ARF) family. ARL2 functions as a component of a secretory pathway which is involved in the Ca2-dependent release of acetylcholine. ARL2 has a role in the folding of tubule proteins, thus playing a significant role in microtubule dynamics and cell cycle progression. Unlike other members of the ARF family, ARL2 doesn’t act as an activator of the catalytic subunit of cholera toxin.
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Synonyms
ADP-ribosylation factor-like protein 2, ARL2, ARFL2.
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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 MGLLTILKKM KQKERELRLL MLGLDNAGKT TILKKFNGED IDTISPTLGF NIKTLEHRGF KLNIWDVGGQ KSLRSYWRNY FESTDGLIWV VDSADRQRMQ DCQRELQSLL VEERLAGATL LIFANKQDLP GALSSNAIRE ALELDSIRSH HWCIQGCSAV TGENLLPGID WLLDDISSRI FTAD.
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 :
ASL HumanDescription:
Argininosuccinate Lyase Human Recombinant
Argininosuccinate lyase, ASAL, Arginosuccinase, ASL.
Product # :
ENZ-185Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
ASL Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 484 amino acids (1-464) and having a molecular mass of 53.8kDa.ASL is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The ASL solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 2mM DTT, 10% glycerol and 100mM NaCl.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
Argininosuccinate lyase (ASL) is a member of the lyase 1 family. ASL is an enzyme which catalyzes the reversible breakdown of Argininosuccinate (ASA) yielding the amino acids arginine and fumarate. ASL which is located in the liver cytosol is the 4th enzyme of the urea cycle and involved in the biosynthesis of arginine in all species and the production of urea in ureotelic species. While Argininosuccinate synthetase (ASS) catalyzes the formation of argininosuccinate from citrulline and aspartate, ASL breaks down the newly formed argininosuccinate into L-arginine and fumarate. L-arginine continues within the urea cycle to form urea and orinthine, whereas fumarate can enter the citric acid cycle. ASL gene Mutations result in the autosomal recessive disorder argininosuccinic aciduria, or argininosuccinic acid lyase deficiency.
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Synonyms
Argininosuccinate lyase, ASAL, Arginosuccinase, ASL.
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Physical Appearance
Sterile Filtered colorless solution.
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Stability
NPL Human Recombinant although stable at 4°C for 1 week, should be stored below -18°C. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MASESGKLWG GRFVGAVDPI MEKFNASIAY DRHLWEVDVQ GSKAYSRGLE KAGLLTKAEM DQILHGLDKV AEEWAQGTFK LNSNDEDIHT ANERRLKELI GATAGKLHTG RSRNDQVVTD LRLWMRQTCS TLSGLLWELI RTMVDRAEAE RDVLFPGYTH LQRAQPIRWS HWILSHAVAL TRDSERLLEV RKRINVLPLG SGAIAGNPLG VDRELLRAEL NFGAITLNSM DATSERDFVA EFLFWASLCM THLSRMAEDL ILYCTKEFSF VQLSDAYSTG SSLMPQKKNP DSLELIRSKA GRVFGRCAGL LMTLKGLPST YNKDLQEDKE AVFEVSDTMS AVLQVATGVI STLQIHQENM GQALSPDMLA TDLAYYLVRK GMPFRQAHEA SGKAVFMAET KGVALNQLSL QELQTISPLF SGDVICVWDY GHSVEQYGAL GGTARSSVDW QIRQVRALLQ AQQA.
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 :
SNCG HumanDescription:
Gamma-Synuclein Human Recombinant
Gamma-synuclein, Persyn, Breast cancer-specific gene 1 protein, Synoretin, SR, SNCG, BCSG1, PERSYN, PRSN, g-Synuclein.
Product # :
PRO-395Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
g-Synuclein Human Recombinant produced in E.Coli is a single,non-glycosylated polypeptide chain containing 127 amino acids and having a molecular mass of 13,300 Dalton. The protein coding region of g-synuclein was amplified by RT-PCR and cloned into an E.coli expression vector. g-synuclein was overexpressed in E. coli and purified to apparent homogeneity by taking advantage of the thermosolubility of the protein and by using conventional column chromatography techniques.
Source
Escherichia Coli.
Formulation
The protein (1mg/ml) contains 20mM Tris-HCl buffer (pH 7.5) and 0.1M NaCl.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
g-synuclein(Originally known as a breast cancer specific gene product, BCSG1) is an acidic neuronal protein of 127 amino acids. Gamma-Synuclein is a member of the Synuclein protein family, which is believed to be involved in the pathogenesis of neurodegenerative diseases. High levels of Gamma-Synuclein have been found in advanced breast carcinomas suggesting a correlation between overexpression of SNCG and breast tumor development. Synuclein-Gamma is found mostly in the peripheral nervous system (in primary sensory neurons, sympathetic neurons, and motor neurons) and retina. SNCG is also identified in the brain, ovarian tumors, and in the olfactory epithelium. SNCG expression in breast tumors is a marker for tumor progression. A modification in the expression of gamma-synuclein has been detected in the retina of Alzheimer's patients.
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Synonyms
Gamma-synuclein, Persyn, Breast cancer-specific gene 1 protein, Synoretin, SR, SNCG, BCSG1, PERSYN, PRSN, g-Synuclein.
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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
MDVFKKGFSI AKEGVVGAVE KTKQGVTEAA EKTKEGVMYV GAKTKENVVQSVTSVAEKTK EQANAVSEAV VSSVNTVATK TVEEAENIAV TSGVVRKEDL RPSAPQQEGV ASKEKEEVAE EAQSGGD.
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 :
NUDT14 HumanDescription:
Nudix Type Motif 14 Human Recombinant
UGPP, UGPPase, Uridine diphosphate glucose pyrophosphatase, UDPG pyrophosphatase, Nucleoside diphosphate-linked moiety X motif 14, Nudix motif 14, NUDT14.
Product # :
ENZ-691Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
NUDT14 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 245 amino acids (1-222) and having a molecular mass of 26.5kDa. NUDT14 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The NUDT14 solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.1M NaCl, 10% glycerol and 1mM DTT.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
-
Introduction
Uridine diphosphate glucose pyrophosphatase (NUDT14), is a part of the nudix hydrolase family. NUDT14 is a cytoplasmic protein which contains one nudix hydrolase domain and acts as the sugar donor in numerous glycosylation reactions, including those involved in the production of glycogen. NUDT14 hydrolyzes ADP-ribose into ribose 5-phosphate and AMP, and UDP-glucose to glucose 1-phosphate and UMP. NUDT14 is a homodimer which binds magnesium as a cofactor and is encoded by a gene located on human chromosome 14.
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Synonyms
UGPP, UGPPase, Uridine diphosphate glucose pyrophosphatase, UDPG pyrophosphatase, Nucleoside diphosphate-linked moiety X motif 14, Nudix motif 14, NUDT14.
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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 MGSMERIEGA SVGRCAASPY LRPLTLHYRQ NGAQKSWDFM KTHDSVTVLL FNSSRRSLVL VKQFRPAVYA GEVERRFPGS LAAVDQDGPR ELQPALPGSA GVTVELCAGL VDQPGLSLEE VACKEAWEEC GYHLAPSDLR RVATYWSGVG LTGSRQTMFY TEVTDAQRSG PGGGLVEEGE LIEVVHLPLE GAQAFADDPD IPKTLGVIFG VSWFLSQVAP NLDLQ.
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 :
NUDT9 HumanDescription:
Nudix Type Motif 9 Human Recombinant
ADP-ribose pyrophosphatase mitochondrial, ADP-ribose diphosphatase, ADP-ribose phosphohydrolase, Adenosine diphosphoribose pyrophosphatase, ADPR-PPase, Nucleoside diphosphate-linked moiety X motif 9, Nudix motif 9, NUDT9, NUDT10, PSEC0099, UNQ3012/PRO9771.
Product # :
ENZ-137Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
NUDT9 produced in E.Coli is a single, non-glycosylated polypeptide chain containing 325 amino acids (47-350 a.a.) and having a molecular mass of 36.5kDa (molecular weight on SDS-PAGE will appear higher).NUDT9 is fused to a 21 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
NUDT9 protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 10% glycerol, 1mM DTT and 0.1M NaCl.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
NUDT9 is a member of a superfamily of Nudix hydrolases. NUDT9 functions as a highly specific adenosine diphosphate ribose pyrophosphatase which hydrolyzes ADP ribose to AMP and ribose 5'-phosphate. In addition, NUDT9 may be involved in the regulation of the menstrual cycle and may be related to the proliferation of glandular cells in the human endometrium.
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Synonyms
ADP-ribose pyrophosphatase mitochondrial, ADP-ribose diphosphatase, ADP-ribose phosphohydrolase, Adenosine diphosphoribose pyrophosphatase, ADPR-PPase, Nucleoside diphosphate-linked moiety X motif 9, Nudix motif 9, NUDT9, NUDT10, PSEC0099, UNQ3012/PRO9771.
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Physical Appearance
Sterile Filtered colorless solution.
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Stability
NUDT9 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 MNTNVMSGSN GSKENSHNKA RTSPYPGSKV ERSQVPNEKV GWLVEWQDYK PVEYTAVSVL AGPRWADPQI SESNFSPKFN EKDGHVERKS KNGLYEIENG RPRNPAGRTG LVGRGLLGRW GPNHAADPII TRWKRDSSGN KIMHPVSGKH ILQFVAIKRK DCGEWAIPGG MVDPGEKISA TLKREFGEEA LNSLQKTSAE KREIEEKLHK LFSQDHLVIY KGYVDDPRNT DNAWMETEAV NYHDETGEIM DNLMLEAGDD AGKVKWVDIN DKLKLYASHS QFIKLVAEKR DAHWSEDSEA DCHAL.
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 :
ENOPH1 HumanDescription:
Enolase-Phosphatase-1 Human Recombinant
Enolase-phosphatase E1, 2,3-diketo-5-methylthio-1-phosphopentane phosphatase, MASA homolog, ENOPH1, MASA, E1, MST145, FLJ12594, DKFZp586M0524.
Product # :
ENZ-077Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
ENOPH1 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 281 amino acids (1-261 a.a.) and having a molecular mass of 31kDa. The ENOPH1 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The ENOPH1 solution (1 mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 1mM DTT, 10% glycerol and 100mM NaCl.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
Enolase-phosphatase E1 (ENOPH1) belongs to the MasA family of the HAD (halo-acid dehalogenase)-like hydrolase superfamily. ENOPH1 is a bifunctional enzyme which demonstrates both phosphatase and atypical enolase activities. ENOPH1 has a significant role in the ubiquitous methionine salvage pathway which is a biochemical pathway found in all organisms that regulate methionine levels in the cell.
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Synonyms
Enolase-phosphatase E1, 2,3-diketo-5-methylthio-1-phosphopentane phosphatase, MASA homolog, ENOPH1, MASA, E1, MST145, FLJ12594, DKFZp586M0524.
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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 MVVLSVPAEV TVILLDIEGT TTPIAFVKDI LFPYIEENVK EYLQTHWEEE ECQQDVSLLR KQAEEDAHLD GAVPIPAASG NGVDDLQQMI QAVVDNVCWQ MSLDRKTTAL KQLQGHMWRA AFTAGRMKAE FFADVVPAVR KWREAGMKVY IYSSGSVEAQ KLLFGHSTEG DILELVDGHF DTKIGHKVES ESYRKIADSI GCSTNNILFL TDVTREASAA EEADVHVAVV VRPGNAGLTD DEKTYYSLIT SFSELYLPSS T.
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 :
PDK1 HumanDescription:
Pyruvate Dehydrogenase Kinase Isozyme 1 Human Recombinant
Pyruvate dehydrogenase kinase isoform 1, PDK1, Pyruvate dehydrogenase (lipoamide) kinase isozyme 1 mitochondrial.
Product # :
PKA-263Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
PDK1 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 429 amino acids (29-436) and having a molecular mass of 48.6 kDa. PDK1 is fused to 20 a.a. His-Tag at N-terminus and purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
PDK1 solution containing 20mM Tris pH-7, 0.5mM DTT, 0.1M NaCl, 0.1mM EDTA 0.1mM PMSF, 1mM MgCl2 and 40% glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
PDK1 takes part in the regulation of enzymatic activity of mammalian pyruvate dehydrogenase which is part of a mitochondrial multienzyme complex to catalyze the oxidative decarboxylation of pyruvate and is one of the major enzymes responsible for the regulation of homeostasis of carbohydrate fuels in mammals. PDK1 inhibits glioblastoma growth. PDK1 inhibits the mitochondrial pyruvate dehydrogenase complex by phosphorylation of the e1 alpha subunit, therefore contributing to the regulation of glucose metabolism. PDK1 kinase activity is negatively regulated by binding to 14-3-3.
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Synonyms
Pyruvate dehydrogenase kinase isoform 1, PDK1, Pyruvate dehydrogenase (lipoamide) kinase isozyme 1 mitochondrial.
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Physical Appearance
Sterile filtered colorless solution.
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Stability
PDK1 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 MSSDSGSSPA SERGVPGQVD FYARFSPSPL SMKQFLDFGS VNACEKTSFM FLRQELPVRL ANIMKEISLLPDNLLRTPSV QLVQSWYIQS LQELLDFKDK SAEDAKAIYD FTDTVIRIRN RHNDVIPTMA QGVIEYKESF GVDPVTSQNV QYFLDRFYMS RISIRMLLNQ HSLLFGGKGK GSPSHRKHIG SINPNCNVLE VIKDGYENAR RLCDLYYINS PELELEELNA KSPGQPIQVV YVPSHLYHMVFELFKNAMRA TMEHHANRGV YPPIQVHVTL GNEDLTVKMS DRGGGVPLRK IDRLFNYMYS TAPRPRVETS RAVPLAGFGY GLPISRLYAQ YFQGDLKLYS LEGYGTDAVI YIKALSTDSI ERLPVYNKAA WKHYNTNHEA DDWCVPSREP KDMTTFRSA.
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 :
PEDF Human, HisDescription:
Pigment Epithelium-Derived Factor Human Recombinant, His Tag
Pigment epithelium-derived factor, PEDF, Serpin-F1, SerpinF1, EPC-1, EPC1, PIG35.
Product # :
CYT-552Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
PEDF Human Recombinant produced in E.Coli containing a natural variant M72T is a single, non-glycosylated, polypeptide chain containing 420 amino acids (20-418 a.a.) and having a total molecular mass of 46.7 kDa. PEDF is fused to a 20 amino acid His Tag at N-terminus and purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The PEDF solution contains 20mM Tris-HCl buffer(pH 8.0), 0.1M NaCl , and 20% glycerol.
Purity
Greater than 90% as determined by SDS-PAGE.
More Info
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Introduction
PEDF is a neurotrophic protein that induces extensive neuronal differentiation in retinoblastoma cells. SerpinF1 is a potent inhibitor of angiogenesis. EPC1 doesn’t undergo the stressed to relaxed conformation transition characteristic as of the active serpins since it exhibits no serine protease inhibitory activity.
Aqueous humour level of asymmetric dimethylarginine is correlated with PEDF in humans. ADMA and PEDF levels are increased in response to inflammation in uveitis.
Lack of PEDF expression is a potent factor for the enhancement of tumor growth and angiogenesis in breast cancer.
PEDF & VEGF genes contribute to the development of diabetic retinopathy.
PEDF and VEGF structural changes in blood vessel wall play an important role in the pathophysiology of PD patients.
PEDF-overexpressing tumors exhibited reduced intratumoral angiogenesis.
SerpinF1 is a new promising approach for the treatment of osteosarcoma.
Levels of the natural ocular anti-angiogenic factor SentrinF1 (PEDF) is associated with proliferative retinopathy.
VEGF secreted by retinal pigment epithelial cells upregulates PEDF expression via VEGFR-1 in an autocrine manner.
Sentrin-F1 concentration in the aqueous humor of diabetic patients predicts who will develop progression of retinopathy.
PEDF blocks angiogenic effects of leptin through its anti-oxidative properties. -
Synonyms
Pigment epithelium-derived factor, PEDF, Serpin-F1, SerpinF1, EPC-1, EPC1, PIG35.
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Physical Appearance
Sterile Filtered colorless solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA). Please prevent freeze-thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MQNPASPPEE GSPDPDSTGA LVEEEDPFFK VPVNKLAAAV SNFGYDLYRV RSSMSPTTNV LLSPLSVATA LSALSLGAEQ RTESIIHRAL YYDLISSPDI HGTYKELLDT VTAPQKNLKS ASRIVFEKKL RIKSSFVAPL EKSYGTRPRV LTGNPRLDLQ EINNWVQAQM KGKLARSTKE IPDEISILLL GVAHFKGQWV TKFDSRKTSL EDFYLDEERT VRVPMMSDPK AVLRYGLDSD LSCKIAQLPL TGSMSIIFFL PLKVTQNLTL IEESLTSEFI HDIDRELKTV QAVLTVPKLK LSYEGEVTKS LQEMKLQSLF DSPDFSKITG KPIKLTQVEH RAGFEWNEDG AGTTPSPGLQ PAHLTFPLDY HLNQPFIFVL RDTDTGALLF IGKILDPRGP.
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 :
PEPD HumanDescription:
Peptidase D Human Recombinant
Xaa-Pro dipeptidase, X-Pro dipeptidase, Imidodipeptidase, Peptidase D, Proline dipeptidase, Prolidase, PRD, PEPD, Xaa-Pro dipeptidase isoform 1, PROLIDASE.
Product # :
ENZ-856Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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- description
- source
- formulation
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Description
PEPD Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 516 amino acids (1-493a.a.) and having a molecular mass of 56.9kDa.PEPD is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
PEPD protein solution (0.5mg/ml) containing Phosphate buffered saline (pH7.4), 10% glycerol and 1mM DTT.
Purity
Greater than 90% as determined by SDS-PAGE.
More Info
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Introduction
Peptidase D, also known as PEPD, Is a part of the peptidase family. PEPD is involved in collagen metabolism due to the high level of iminoacids in collagen. PEPD recycles proline, and sets the pace for the production of collagen. PEPD is also parts dipeptides with a prolyl or hydroxyprolyl residue in the C-terminal position.
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Synonyms
Xaa-Pro dipeptidase, X-Pro dipeptidase, Imidodipeptidase, Peptidase D, Proline dipeptidase, Prolidase, PRD, PEPD, Xaa-Pro dipeptidase isoform 1, PROLIDASE.
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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 MGSMAAATGP SFWLGNETLK VPLALFALNR QRLCERLRKN PAVQAGSIVV LQGGEETQRY CTDTGVLFRQ ESFFHWAFGV TEPGCYGVID VDTGKSTLFV PRLPASHATW MGKIHSKEHF KEKYAVDDVQ YVDEIASVLT SQKPSVLLTL RGVNTDSGSVCREASFDGIS KFEVNNTILH PEIVECRVFK TDMELEVLRY TNKISSEAHR EVMKAVKVGM KEYELESLFE HYCYSRGGMR HSSYTCICGS GENSAVLHYG HAGAPNDRTI QNGDMCLFDM GGEYYCFASD ITCSFPANGK FTADQKAVYE AVLRSSRAVM GAMKPGVWWP DMHRLADRIH LEELAHMGIL SGSVDAMVQA HLGAVFMPHG LGHFLGIDVH DVGGYPEGVE RIDEPGLRSL RTARHLQPGM VLTVEPGIYF IDHLLDEALA DPARASFLNR EVLQRFRGFG GVRIEEDVVV TDSGIELLTC VPRTVEEIEA CMAGCDKAFT PFSGPK.
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 :
ITPA HumanDescription:
Inosine Triphosphatase Human Recombinant
EC 3.6.1.19, C20orf37, dJ794I6.3, HLC14-06-P, ITPase, My049, OK/SW-cl.9, Inosine Triphosphatase, ITPA.
Product # :
ENZ-549Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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- description
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- formulation
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Description
ITPA Recombinant Human produced in E.Coli is a single, non-glycosylated polypeptide chain containing 215 amino acids (1-194 a.a.) and having a molecular mass of 23.7 kDa. The ITPA is fused to a 21 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The ITPA solution (1mg/ml) contains 20mM Tris-HCl pH-8 & 10% glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
ITPA enzyme catalyzes the pyrophosphohydrolysis of both ITP (inosine triphosphate) and dITP (deoxyinosine triphosphate) to IMP (inosine monophosphate) and diphosphate. IMP is exercised as a substrate for purine nucleotide pathways. IMP is phosphorylated to ITP, and ITPA mediates the concentration of ITP in the cell by changing ITP back to IMP. Defects in ITPA result in ITPA deficiency which is thought to be inherited and is characterized by an over-accumulation of ITP in erythocytes, leukocytes and fibroblasts.
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Synonyms
EC 3.6.1.19, C20orf37, dJ794I6.3, HLC14-06-P, ITPase, My049, OK/SW-cl.9, Inosine Triphosphatase, ITPA.
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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 MMAASLVGKK IVFVTGNAKK LEEVVQILGD KFPCTLVAQK IDLPEYQGEP DEISIQKCQE AVRQVQGPVL VEDTCLCFNA LGGLPGPYIK WFLEKLKPEG LHQLLAGFED KSAYALCTFA LSTGDPSQPV RLFRGRTSGR IVAPRGCQDF GWDPCFQPDG YEQTYAEMPK AEKNAVSHRF RALLELQEYF GSLAA.
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 :
IVD HumanDescription:
Isovaleryl Coenzyme A Dehydrogenase Human Recombinant
FLJ12715, isovaleryl-CoA dehydrogenase mitochondrial, FLJ34849, EC 1.3.99.10, IVD, ACAD2.
Product # :
ENZ-490Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
Description
IVD Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 415 amino acids (33-426 a.a.) and having a molecular mass of 45.3 kDa. The IVD is fused to a 20 amino acid his tag at N-terminus and purified by conventional chromatography.
Source
Escherichia Coli.
Formulation
The IVD protein solution (1mg/ml) contains 20mM Tris-HCl pH-8, 1mM DTT and 10% glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
IVD is a mitochondrial matrix enzyme that is part of the cyl-CoA dehydrogenase family which catalyzes the third step in leucine catabolism. The genetic deficiency of IVD leads to a buildup of isovaleric acid, which is toxic to the central nervous system and results in isovaleric acidemia. IVD is a homotetrameric flavoenzyme which catalyzes the conversion of isovaleryl-CoA to 3-methylcrotonyl-CoA.
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Synonyms
FLJ12715, isovaleryl-CoA dehydrogenase mitochondrial, FLJ34849, EC 1.3.99.10, IVD, ACAD2.
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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 MHSLLPVDDA INGLSEEQRQ LRQTMAKFLQ EHLAPKAQEI DRSNEFKNLR EFWKQLGNLG VLGITAPVQY GGSGLGYLEH VLVMEEISRA SGAVGLSYGA HSNLCINQLV RNGNEAQKEK YLPKLISGEY IGALAMSEPN AGSDVVSMKL KAEKKGNHYI LNGNKFWITN GPDADVLIVY AKTDLAAVPA SRGITAFIVE KGMPGFSTSK KLDKLGMRGS NTCELIFEDC KIPAANILGH ENKGVYVLMS GLDLERLVLA GGPLGLMQAV LDHTIPYLHV REAFGQKIGH FQLMQGKMAD MYTRLMACRQ YVYNVAKACD EGHCTAKDCA GVILYSAECA TQVALDGIQC FGGNGYINDF PMGRFLRDAK LYEIGAGTSE VRRLVIGRAF NADFH.
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.