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1000 results found for “heparanase”
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Name :
SRR HumanDescription:
Serine Racemase Human Recombinant
Serine racemase, D-serine ammonia-lyase, D-serine dehydratase, L-serine ammonia-lyase, L-serine dehydratase, SRR, ILV1, ISO1.
Product # :
ENZ-232Price :
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Shipped with Ice Packs
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Description
SRR Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 364 amino acids (1-340) and having a molecular mass of 39.1kDa.SRR is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The SRR solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH8.0), 20% glycerol, 0.1M NaCl and 1mM DTT.
Purity
Greater than 85.0% as determined by SDS-PAGE.
More Info
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Introduction
Serine racemase (SRR) is an enzyme which generates D-serine from L-serine. D-serine functions as a neuronal signaling molecule by activating NMDA receptors in the brain. Mammalian SRR is a pyridoxal 5'-phosphate dependent enzyme which catalyzes both the racemization of L-serine to D-serine and also the elimination of water from L-serine, producing pyruvate and ammonia. The SRR enzyme is physiologically stimulated by divalent cations (e.g., magnesium) and is allosterically activated by the magnesium/ATP complex.
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Synonyms
Serine racemase, D-serine ammonia-lyase, D-serine dehydratase, L-serine ammonia-lyase, L-serine dehydratase, SRR, ILV1, ISO1.
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Physical Appearance
Sterile Filtered colorless solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSHMCAQYC ISFADVEKAH INIRDSIHLT PVLTSSILNQ LTGRNLFFKC ELFQKTGSFK IRGALNAVRS LVPDALERKP KAVVTHSSGN HGQALTYAAK LEGIPAYIVV PQTAPDCKKL AIQAYGASIV YCEPSDESRE NVAKRVTEET EGIMVHPNQE PAVIAGQGTI ALEVLNQVPL VDALVVPVGG GGMLAGIAIT VKALKPSVKV YAAEPSNADD CYQSKLKGKL MPNLYPPETI ADGVKSSIGL NTWPIIRDLV DDIFTVTEDE IKCATQLVWE RMKLLIEPTA GVGVAAVLSQ HFQTVSPEVK NICIVLSGGN VDLTSSITWV KQAERPASYQ SVSV.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
tPA Human, Sf9Description:
Tissue Plasminogen Activator Human Recombinant, Sf9
Tissue-type plasminogen activator, EC 3.4.21.68, tPA, t-PA, t-plasminogen activator, TPA, T-PA, DKFZp686I03148, PLAT and tPA.
Product # :
ENZ-1011Price :
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Description
tPA Human Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 545 amino acids (24-562 a.a) and having a molecular mass of 61.3kDa (Molecular size on SDS-PAGE will appear at approximately 50-70kDa).tPA is fused to a 6 amino acid His-tag at C-terminus & purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
tPA protein solution (0.25mg/ml) containing 50mM MES buffer(pH 5.5 ), 40% glycerol, 5mM CaCl2, 1mM DTT and 0.5M NaCl.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
Tissue plasminogen activator (abbreviated PLAT or tPA) is a secreted serine proteasewhich converts the proenzymeplasminogento plasmin, a fibrinolyticenzyme. Plasminogen is synthesized as a single chain which is cleaved by PLAT into the two chain disulfide linked plasmin.
This enzyme plays a role in cell migrationand tissue remodeling. Increased enzymatic activity causes hyperfibrinolysis, which manifests as excessive bleeding; decreased activity leads to hypofibrinolysiswhich can result in thrombosisor embolism. -
Synonyms
Tissue-type plasminogen activator, EC 3.4.21.68, tPA, t-PA, t-plasminogen activator, TPA, T-PA, DKFZp686I03148, PLAT and tPA.
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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
QEIHARFRRG ARSYQVICRD EKTQMIYQQH QSWLRPVLRS NRVEYCWCNS GRAQCHSVPV KSCSEPRCFN GGTCQQALYF SDFVCQCPEG FAGKCCEIDT RATCYEDQGI SYRGTWSTAE SGAECTNWNS SALAQKPYSG RRPDAIRLGL GNHNYCRNPD RDSKPWCYVF KAGKYSSEFC STPACSEGNS DCYFGNGSAY RGTHSLTESG ASCLPWNSMI LIGKVYTAQN PSAQALGLGK HNYCRNPDGD AKPWCHVLKN RRLTWEYCDV PSCSTCGLRQ YSQPQFRIKG GLFADIASHP WQAAIFAKHR RSPGERFLCG GILISSCWIL SAAHCFQERF PPHHLTVILG RTYRVVPGEE EQKFEVEKYI VHKEFDDDTY DNDIALLQLK SDSSRCAQES SVVRTVCLPP ADLQLPDWTE CELSGYGKHE ALSPFYSERL KEAHVRLYPS SRCTSQHLLN RTVTDNMLCA GDTRSGGPQA NLHDACQGDS GGPLVCLNDG RMTLVGIISW GLGCGQKDVP GVYTKVTNYL DWIRDNMRPHHHHHH.
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 :
BACE2 Mouse, HEKDescription:
Beta-Secretase 2 Mouse Recombinant, HEK
BAE2, CDA13, CEAP1, DRAP, ARP1, ASP1, ASP21, 1110059C24Rik, AEPLC, AI850424, ALP56, beta-site APPcleaving enzyme 2, beta-secretase 2, Aspartyl protease 1, Asp 1, Beta-site amyloid precursor protein cleaving enzyme 2, Memapsin-1, Membrane-associated aspartic protease 1, Theta-secretase.
Product # :
ENZ-1188Price :
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Description
BACE2 Mouse Recombinant produced in HEK293 Cells is a single, glycosylated, polypeptide chain (20-462 a.a) containing a total of 449 amino acids, having a molecular mass of 48.6 kDa. BACE2 Mouse is fused to a 6 amino acid His-tag at C-terminus and is purified by proprietary chromatographic techniques.
Source
HEK293 Cells.
Formulation
BACE2 (0.25mg/ml) is filtered in 10% (w/v) glycerol and Phosphate-Buffered Saline pH 7.4.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Biological Activity
Specific activity is > 20 pmol/min/ug in which one unit will convert 1.0pmole of Mca-SEVNLDAEFRK(Dnp)RR-NH2 to Mca- Pro-Leu-OH per minute at pH 3.5 at 25C.
More Info
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Synonyms
BAE2, CDA13, CEAP1, DRAP, ARP1, ASP1, ASP21, 1110059C24Rik, AEPLC, AI850424, ALP56, beta-site APPcleaving enzyme 2, beta-secretase 2, Aspartyl protease 1, Asp 1, Beta-site amyloid precursor protein cleaving enzyme 2, Memapsin-1, Membrane-associated aspartic protease 1, Theta-secretase.
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Physical Appearance
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
AVPALAPAPF TLPLQVARAT NHRASAVPGL GTPELPRADG LALALEPVRA TANFLAMVDN LQGDSGRGYY LEMLIGTPPQ KVQILVDTGS SNFAVAGAPH SYIDTYFDSE SSSTYHSKGF DVTVKYTQGS WTGFVGEDLV TIPKGFNSSF LVNIATIFES ENFFLPGIKW NGILGLAYAA LAKPSSSLET FFDSLVAQAK IPDIFSMQMC GAGLPVAGSG TNGGSLVLGG IEPSLYKGDI
WYTPIKEEWY YQIEILKLEI GGQNLNLDCR EYNADKAIVD SGTTLLRLPQ KVFDAVVEAV ARTSLIPEFS DGFWTGAQLA CWTNSETPWA YFPKISIYLR DENASRSFRI TILPQLYIQP MMGAGFNYEC YRFGISSSTN ALVIGATVME GFYVVFDRAQ RRVGFAVSPC AEIEGTTVSE ISGPFSTEDI ASNCVPAQAL NEP HHHHHH.
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Background
BACE2 protein, a member of the beta-secretase family, has gained attention as a key player in the pathogenesis of neurological disorders, particularly Alzheimer's disease. This research aims to explore the function and potential therapeutic implications of BACE2 protein in neurodegenerative conditions. Understanding the role of BACE2 protein can provide valuable insights into its significance as a therapeutic target for the development of novel treatment strategies.
Function of BACE2 Protein:
BACE2 is a transmembrane aspartic protease predominantly expressed in the central nervous system. It exhibits distinct cleavage activity on various protein substrates, including neuregulins, APP-like proteins, and TGF-β. Unlike its close homolog BACE1, BACE2 has been proposed to have non-amyloidogenic processing capabilities and has shown potential neuroprotective effects.
Implications of BACE2 Protein in Alzheimer's Disease:
Alzheimer's disease is characterized by the accumulation of amyloid-beta (Aβ) peptides in the brain, which are generated through the sequential cleavage of amyloid precursor protein (APP). BACE1 is primarily responsible for the cleavage of APP, leading to the production of toxic Aβ peptides. In contrast, BACE2 has been suggested to compete with BACE1, thereby reducing the levels of Aβ generation. This has led to speculation about the neuroprotective role of BACE2 and its potential as a therapeutic target for Alzheimer's disease.
BACE2 Protein and Neuronal Survival:
Emerging evidence suggests that BACE2 may play a role in promoting neuronal survival and function. Studies have shown that BACE2 deficiency leads to impaired synaptic plasticity, reduced dendritic branching, and altered neurotransmitter release. BACE2 has also been implicated in the regulation of axonal growth and guidance during development. These findings highlight the potential importance of BACE2 in maintaining neuronal integrity.
Association of BACE2 Protein with Other Neurological Disorders:
Apart from Alzheimer's disease, BACE2 has been implicated in other neurological conditions as well. Genetic studies have identified BACE2 gene variants associated with an increased risk of Parkinson's disease, suggesting its involvement in the pathogenesis of this disorder. Furthermore, BACE2 has been linked to the regulation of insulin signaling and glucose homeostasis, making it a potential target for diabetes-associated cognitive decline.
Therapeutic Implications of BACE2 Protein:
Given its potential neuroprotective effects and modulatory role in amyloid processing, BACE2 protein has emerged as a promising therapeutic target for neurodegenerative disorders. Strategies aimed at enhancing BACE2 activity or selectively activating BACE2-mediated non-amyloidogenic processing pathways hold promise for reducing amyloid pathology and preserving neuronal function. However, further research is needed to better understand the complex mechanisms underlying BACE2 function and to develop safe and effective therapeutic interventions.
Conclusion:
The investigation of BACE2 protein has provided valuable insights into its role in neurodegenerative diseases, particularly Alzheimer's disease. The potential neuroprotective effects and modulation of amyloid processing pathways by BACE2 make it an intriguing therapeutic target. Future studies should focus on unraveling the precise mechanisms by which BACE2 influences disease pathogenesis and developing strategies to harness its therapeutic potential. The exploration of BACE2 protein opens new avenues for the development of innovative treatment approaches for neurodegenerative disorders.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
PAP HumanDescription:
Prostate Acid Phosphatase Human
Product # :
ENZ-1171Price :
Quantity :
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Shipped at Room temp
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Description
Human Prostate Acid Phosphatase produced in Pooled human seminal fluid having a molecular mass of approximately 100kD.
Source
Pooled human seminal fluid.
Formulation
PAP Human is lyophilized (0.2 µm filtered) from 0.02M NH4HCO3.
Purity
Greater than 96.0% as determined by SDS-PAGE.
More Info
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Introduction
Prostatic acid phosphatase, also known as PAP, is an enzyme produced by the prostate. PAP may be found in increased amounts in men with prostate cancer.
PAP’s physiological function may be associated with the liquefaction process of semen.
The highest levels of PAP are found in metastasized prostate cancer. Diseases of the bone, such as Paget's disease or hyperparathyroidism, diseases of blood cells (sickle-cell disease) or multiple myeloma or lysosomal storage diseases (Gaucher's disease), will show moderately higher levels.
Certain medications can cause temporary changes in PAP levels. Manipulation of the prostate gland through rectal exam, biopsy or massage may increase the level. -
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
PAP Human although stable at room temperature for 3 weeks, should be stored between 2-8°C.
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Solubility
It is recommended to reconstitute the lyophilized PAP Human in phosphate buffer containing 0.15M NaCl.
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Human Virus Test
Starting material tested and found negative for HIV I & II antibodies, Hepatitis B surface antigen, Hepatitis C antibodies and Syphilis.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
BDH2 HumanDescription:
3-Hydroxybutyrate Dehydrogenase, Type 2 Human Recombinant
3-hydroxybutyrate dehydrogenase type 2, FLJ13261, PRO20933, SDR15C1, UCPA-OR, UNQ6308, dehydrogenase/reductase (SDR family) member 6, Oxidoreductase UCPA, DHRS6, R-beta-hydroxybutyrate dehydrogenase, EFA6R, EC 1.1.1.30.
Product # :
ENZ-060Price :
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Description
BDH2 produced in E.Coli is a single, non-glycosylated polypeptide chain containing 265 amino acids (1-245a.a.) and having a molecular mass of 28.8kDa.BDH2 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The BDH2 protein solution (1mg/1ml) is formulated in 20mM Tris-HCl buffer (pH8.0) 0.1M NaCl and 10% glycerol.
Purity
Greater than 95% as determined by SDS-PAGE.
More Info
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Introduction
BDH2 is a member of the short-chain dehydrogenases/reductases (SDR) family. BDH2 protein has a significant part in the peripheral utilization of 3-hydroxybutyrate. BDH2 can convert high levels of circulating 3-hydroxybutyrate into acetoacetate due to cytoplasmic localization in high ratio of oxidized NAD+, the NAD+ dependence and the kinetic parameters.
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Synonyms
3-hydroxybutyrate dehydrogenase type 2, FLJ13261, PRO20933, SDR15C1, UCPA-OR, UNQ6308, dehydrogenase/reductase (SDR family) member 6, Oxidoreductase UCPA, DHRS6, R-beta-hydroxybutyrate dehydrogenase, EFA6R, EC 1.1.1.30.
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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 MGRLDGKVII LTAAAQGIGQ AAALAFAREG AKVIATDINE SKLQELEKYP GIQTRVLDVT KKKQIDQFAN EVERLDVLFN VAGFVHHGTV LDCEEKDWDF SMNLNVRSMY LMIKAFLPKM LAQKSGNIIN MSSVASSVKG VVNRCVYSTT KAAVIGLTKS VAADFIQQGI RCNCVCPGTV DTPSLQERIQ ARGNPEEARN DFLKRQKTGR FATAEEIAML CVYLASDESA YVTGNPVIID GGWSL
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 :
ADPRH HumanDescription:
ADP-Ribosylarginine Hydrolase Human Recombinant
[Protein ADP-ribosylarginine] hydrolase, ADP-ribosylarginine hydrolase, ADP-ribose-L-arginine cleaving enzyme, ADPRH, ARH1.
Product # :
ENZ-631Price :
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Description
ADPRH Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 381 amino acids (1-357) and having a molecular mass of 42.1kDa.ADPRH is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
The ADPRH solution (0.5mg/ml) contains 20mM Tris-HCl buffer, pH8.0, 10% glycerol, 1mM DTT and 100mM NaCl.
Purity
Greater than 90% as determined by SDS-PAGE.
More Info
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Introduction
ADP-ribosylarginine hydrolase (ADPRH) is a member of the ADP-ribosylglycohydrolase family. ADPRH catalyzes the removal of mono-ADP-ribose from arginine residues of proteins in the ADP-ribosylation cycle. The human ADPRH enzyme is DTT-independent as opposed to the rat and mouse enzymes, which require DTT for maximal activity.
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Synonyms
[Protein ADP-ribosylarginine] hydrolase, ADP-ribosylarginine hydrolase, ADP-ribose-L-arginine cleaving enzyme, ADPRH, ARH1.
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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 MGSHMEKYVA AMVLSAAGDA LGYYNGKWEF LQDGEKIHRQ LAQLGGLDAL DVGRWRVSDD TVMHLATAEA LVEAGKAPKL TQLYYLLAKH YQDCMEDMDG RAPGGASVHN AMQLKPGKPN GWRIPFNSHE GGCGAAMRAM CIGLRFPHHS QLDTLIQVSI ESGRMTHHHP TGYLGALASA LFTAYAVNSR PPLQWGKGLM ELLPEAKKYI VQSGYFVEEN LQHWSYFQTK WENYLKLRGI LDGESAPTFP ESFGVKERDQ FYTSLSYSGW GGSSGHDAPM IAYDAVLAAG DSWKELAHRA FFHGGDSDST AAIAGCWWGV MYGFKGVSPS NYEKLEYRNR
LEETARALYS LGSKEDTVIS 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 :
NDUFB4 HumanDescription:
NADH Dehydrogenase 1 Beta Subcomplex 4 Human Recombinant
B15, CI-B15, Complex I-B15, NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 4, NADH-ubiquinone oxidoreductase B15 subunit.
Product # :
ENZ-699Price :
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Description
NDUFB4 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 110 amino acids (1-87) and having a molecular mass of 12.6kDa.NDUFB4 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.Coli
Formulation
The NDUFB4 solution (1mg/ml) contains 20mM Tris-HCl buffer, (pH 8.0), 0.4M Urea And 10% glycerol.
Purity
Greater than 90% as determined by SDS-PAGE.
More Info
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Introduction
NADH Dehydrogenase 1 Beta Subcomplex 4 (NDUFB4) is a member of the complex I NDUFB4 subunit family. NDUFB4 is a non-catalytic subunit of the multisubunit NADH:ubiquinone oxidoreductase, which is the first enzyme complex in the mitochondrial electron transport chain (complex I). Mammalian complex I is comprised of 45 different subunits and transfers electrons from NADH to ubiquinone.
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Synonyms
B15, CI-B15, Complex I-B15, NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 4, NADH-ubiquinone oxidoreductase B15 subunit.
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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 MGSMSFPKYK PSSLRTLPET LDPAEYNISP ETRRAQAERL AIRAQLKREY LLQYNDPNRR GLIENPALLR WAYARTINVY PNFRPTPKNS.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
CAIII Human, HisDescription:
Carbonic Anhydrase III Human Recombinant, His Tag
Car3, CAIII, Carbonic anhydrase 3, EC 4.2.1.1, Carbonic anhydrase III, Carbonate dehydratase III, CA-III.
Product # :
ENZ-270Price :
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Description
Carbonic anhydrase III Human Recombinant produced in E.Coli, and having a molecular mass of 33.9 kDa. CAIII is expressed with an amino-terminal hexahistidine tag.The CA-III is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Supplied in 10mM Tris-HCl (pH 8), 250mM NaCl, 0.5mM DTT, 1.5mM Cysteine, and 50% Glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
Carbonic anhydrase (carbonate dehydratase) is a family of metalloenzymes (enzymes that contain one or more metal atoms as a functional component of the enzyme) that catalyze the rapid (and reversible) conversion of carbon dioxide to bicarbonate and protons, a reaction that occurs rather slowly in the absence of a catalyst. Carbonic anhydrase greatly increases the rate of the reaction, with typical catalytic rates of the different forms of this enzyme ranging between 104 and 106 reactions per second. The active site of most carbonic anhydrases contains a zincion. CAIII is a cytoplasmic isoenzyme, but is released into the circulation following injury.
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Synonyms
Car3, CAIII, Carbonic anhydrase 3, EC 4.2.1.1, Carbonic anhydrase III, Carbonate dehydratase III, CA-III.
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Physical Appearance
Sterile Filtered blue solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
LHPP HumanDescription:
Phospholysine Phosphohistidine Inorganic Pyrophosphate Phosphatase Human Recombinant
Phospholysine phosphohistidine inorganic pyrophosphate phosphatase, hLHPP, LHPP, HDHD2B.
Product # :
ENZ-575Price :
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Description
LHPP Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 307 amino acids (1-270) and having a molecular mass of 33.5kDa.LHPP is fused to a 37 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The LHPP solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 1mM DTT, 10% glycerol and 0.1M NaCl.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
Phospholysine phosphohistidine inorganic pyrophosphate phosphatase (LHPP) belongs to the HAD-like hydrolase superfamily. LHPP is an exceptional enzyme which hydrolyzes not only oxygen-phosphorus bonds in inorganic pyrophosphate but also nitrogen-phosphorus bonds in phospholysine, phosphohistidine and imidodiphosphate in vitro. LHPP is expressed in the liver, kidney and moderately in the brain.
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Synonyms
Phospholysine phosphohistidine inorganic pyrophosphate phosphatase, hLHPP, LHPP, HDHD2B.
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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
MRGSHHHHHP WYASMTGGQQ MGRDLYDDDD KDRWGSHMAP WGKRLAGVRG VLLDISGVLY DSGAGGGTAI AGSVEAVARL KRSRLKVRFC TNESQKSRAE LVGQLQRLGF DISEQEVTAP APAACQILKE QGLRPYLLIH DGVRSEFDQI DTSNPNCVVI ADAGESFSYQ NMNNAFQVLM ELEKPVLISL GKGRYYKETS GLMLDVGPYM KALEYACGIK AEVVGKPSPE FFKSALQAIG VEAHQAVMIG DDIVGDVGGA QRCGMRALQV RTGKFRPSDE HHPEVKADGY VDNLAEAVDL LLQHADK.
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 :
IDI1 HumanDescription:
Isopentenyl-Diphosphate Delta Isomerase 1 Human Recombinant
Isopentenyl-diphosphate Delta-isomerase 1, Isopentenyl pyrophosphate isomerase 1, IPP isomerase 1, IPPI1, IDI1, IPP1.
Product # :
ENZ-189Price :
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Description
IDI1 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 248 amino acids (1-228) and having a molecular mass of 28.6kDa.IDI1 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
The IDI1 solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 1mM DTT, 10% glycerol and 0.1M NaCl.
Purity
Greater than 90% as determined by SDS-PAGE.
More Info
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Introduction
Isopentenyl-diphosphate isomerase 1 (IDI1) belongs to the IPP isomerase type I family and is involved in cholesterol biosynthesis. IDI1 is a peroxisomally-localized enzyme which catalyzes the interconversion of isopentenyl diphosphate (IPP) to its highly electrophilic isomer, dimethylallyl diphosphate (DMAPP), which is the substrate for the sequential reaction that results in the synthesis of farnesyl diphosphate and, eventually, cholesterol. Peroxisomal deficiency diseases such as Zellweger syndrome and neonatal adrenoleukodystrophy show a reduction in IPP isomerase activity.
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Synonyms
Isopentenyl-diphosphate Delta-isomerase 1, Isopentenyl pyrophosphate isomerase 1, IPP isomerase 1, IPPI1, IDI1, IPP1.
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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 MMPEINTNHL DKQQVQLLAE MCILIDENDN KIGAETKKNC HLNENIEKGL LHRAFSVFLF NTENKLLLQQ RSDAKITFPG CFTNTCCSHP LSNPAELEES DALGVRRAAQ RRLKAELGIP LEEVPPEEIN YLTRIHYKAQ SDGIWGEHEI DYILLVRKNV
TLNPDPNEIK SYCYVSKEEL KELLKKAASG EIKITPWFKI IAATFLFKWW DNLNHLNQFV DHEKIYRM.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
GPT MouseDescription:
Glutamic-Pyruvate Transaminase Mouse Recombinant
Alanine aminotransferase 1, ALT1, Glutamate pyruvate transaminase 1, GPT 1, Glutamic--alanine transaminase 1, Glutamic--pyruvic transaminase 1.
Product # :
ENZ-1030Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
GPT Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 519 amino acids (1-496 a.a) and having a molecular mass of 57.5kDa.GPT is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
GPT protein solution (0.5mg/ml) containing Phosphate Buffered Saline (pH7.4), 1mM DTT and 10% glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
Biological Activity
Specific activity is > 40units/mg, and is defined as the amount of enzyme that convert 1umole of L-Alanine to L-Glutamate per minute at pH 7.5 at 37C.
More Info
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Introduction
GPT catalyzes the reversible transamination between alanine and 2-oxoglutarate to create pyruvate and glutamate. GPT has a crucial part in the intermediary metabolism of glucose and amino acids. GPT is broadly used as an indicator of liver reliability or hepatocellular destruction in clinical tests.
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Synonyms
Alanine aminotransferase 1, ALT1, Glutamate pyruvate transaminase 1, GPT 1, Glutamic--alanine transaminase 1, Glutamic--pyruvic transaminase 1.
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Physical Appearance
Sterile filtered colorless solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSMASQRND RIQASRNGLK GKVLTLDTMN PCVRRVEYAV RGPIVQRALE LEQELRQGVK KPFTEVIRAN IGDAQAMGQR PITFFRQVLA LCVYPNLLSS PDFPEDAKRR AERILQACGG HSLGAYSISS GIQPIREDVA QYIERRDGGI PADPNNIFLS TGASDAIVTM LKLLVAGEGR ARTGVLIPIP QYPLYSAALA ELDAVQVDYY LDEERAWALD IAELRRALCQ ARDRCCPRVL CVINPGNPTG QVQTRECIEA VIRFAFEEGL FLMADEVYQD NVYAEGSQFH SFKKVLTEMG PPYATQQELA SFHSVSKGYM GECGFRGGYV EVVNMDAEVQ KQMAKLMSVR LCPPVPGQAL MGMVVSPPTP SEPSFKQFQA ERQEVLAELA AKAKLTEQVF NEAPGIRCNP VQGAMYSFPQ IQLPLKAVQR AQDLGLAPDM FFCLCLLEET GICVVPGSGF GQQEGTYHFR MTILPPMEKL RVLLEKLRHF HAKFTHEYS.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
HDAC8 MouseDescription:
Histone Deacetylase 8 Mouse Recombinant
Histone deacetylase 8, HD8, Hdac8.
Product # :
ENZ-1026Price :
Quantity :
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Description
HDAC8 Mouse Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 383 amino acids (1-377 a.a.) and having a molecular mass of 42.5kDa (Migrates at 40-57kDa on SDS-PAGE under reducing conditions).HDAC8 is expressed with a 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
HDAC8 protein solution (0.25mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 10% glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
Histone deacetylase 8 (HDAC8) is a member of the class 1 of the histone deacetylase/acuc/apha family. HDAC8 is biologically involved in skull morphogenesis and metabolic control of the ERR-alpha/PGC1-alpha transcriptional complex. Histones play a key role in transcriptional regulation, cell cycle progression, and developmental events. Histone acetylation/deacetylation modifies chromosome structure and affects transcription factor access to DNA.
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Synonyms
Histone deacetylase 8, HD8, Hdac8.
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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
MEMPEEPANS GHSLPPVYIY SPEYVSICDS LVKVPKRASM VHSLIEAYAL HKQMRIVKPK VASMEEMATF HTDAYLQHLQ KVSQEGDEDH PDSIEYGLGY DCPATEGIFD YAAAIGGGTI TAAQCLIDGK CKVAINWSGG WHHAKKDEAS GFCYLNDAVL GILRLRRKFD RILYVDLDLH HGDGVEDAFS FTSKVMTVSL HKFSPGFFPG TGDMSDVGLG KGRYYSVNVP IQDGIQDEKY YHICESVLKE VYQAFNPKAV VLQLGADTIA GDPMCSFNMT PVGIGKCLKY VLQWQLATLI LGGGGYNLAN TARCWTYLTG VILGKTLSSE IPDHEFFTAY GPDYVLEITP SCRPDRNEPH RIQQILNYIK GNLKHVVHHH 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.
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Name :
Carbonic Anhydrase 2 HumanDescription:
Carbonic Anhydrase 2 Human Recombinant
Carbonic anhydrase 2, Carbonate dehydratase 2, Carbonic Anhydrase II, CA-II, Carbonic anhydrase C, CAC, CA2, CAII, Car2.
Product # :
ENZ-420Price :
Quantity :
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Description
Carbonic anhydrase 2 Human Recombinant protein produced in E.Coli containing 260 amino acids (1-260) and having a molecular mass of 29.2 kDa. The Carbonic anhydrase 2 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Carbonic Anhydrase 2 protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 1mM DTT, 50mM NaCl and 10% glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Biological Activity
Specific activity is 50-70 nmoles/min/µg and was obtained by measuring the increase in the amount of p-nitrophenol by its esterase activity. Specific activity is defined as the amount ofp-nitrophenol that 1ug of enzyme can reduce at 25C for 1 minute.More Info
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Introduction
The enzyme Carbonic anhydrase II having an accession number of NP_414668 is also called carbonate dehydratase which is part of the enzyme family that catalyses rapid inter-conversion of carbon dioxide & water to bicarbonate, carbonic acid and protons (CO2 + H2O ? HCO3? + H+), a reaction that occurs rather slowly in the absence of a catalyst. The majority of carbonic anhydrases enclose a zinc ion in their active site and therefore is classified as metalloenzymes.
The most important function of Carbonic anhydrase is known to preserve acid-base balance in blood and other tissues, and to help transport carbon dioxide of tissues. Carbonic anhydrases have been found in all kingdoms of life. Carbonic anhydrase has 3 different classes: alpha, beta and gamma which share very little sequence or structural similarity, thus far they all perform the same function and require a zinc ion at the active site. Mammalian carbonic anhydrase is monomeric and belongs to the alpha class. Plant carbonic anhydrase is dimeric and belongs to the beta class.
Methane-producing bacteria carbonic anhydrase is trimeric and grows in hot springs which forms the gamma class. -
Synonyms
Carbonic anhydrase 2, Carbonate dehydratase 2, Carbonic Anhydrase II, CA-II, Carbonic anhydrase C, CAC, CA2, CAII, Car2.
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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
MSHHWGYGKH NGPEHWHKDF PIAKGERQSP VDIDTHTAKY DPSLKPLSVS YDQATSLRIL NNGHAFNVEF DDSQDKAVLK GGPLDGTYRL IQFHFHWGSL DGQGSEHTVD KKKYAAELHL VHWNTKYGDF GKAVQQPDGL AVLGIFLKVG SAKPGLQKVV DVLDSIKTKG KSADFTNFDP RGLLPESLDY WTYPGSLTTP PLLECVTWIV LKEPISVSSE QVLKFRKLNF NGEGEPEELM VDNWRPAQPL KNRQIKASFK
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 :
HCV NS4, HRPDescription:
Hepatitis C Virus NS4 Horseradish Peroxidase Recombinant
Product # :
HCV-220Price :
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Shipped with Ice Packs
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Description
The E.coli derived recombinant Horseradish Peroxidase Labeled protein contains the HCV NS4 immunodominant regions.
Source
Escherichia Coli.
Formulation
25mM Tris-HCl pH 8, 1mM EDTA, 1.5M urea & 50%glycerol.
Purity
HCV NS4 Protein is >95% pure as determined by 10% PAGE (coomassie staining).
More Info
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Introduction
HCV is a small 50nm, enveloped, single-stranded, positive sense RNAvirus in the family Flaviviridae.
HCV has a high rate of replication with approximately one trillion particles produced each day in an infected individual. Due to lack of proofreading by the HCV RNA polymerase, the HCV has an exceptionally high mutation rate, a factor that may help it elude the host's immune response. Hepatitis C virus is classified into six genotypes(1-6) with several subtypes within each genotype. The preponderance and distribution of HCV genotypes varies globally. Genotype is clinically important in determining potential response to interferon-based therapy and the required duration of such therapy. Genotypes 1 and 4 are less responsive to interferon-based treatment than are the other genotypes (2, 3, 5 and 6). -
Stability
HCV NS4 a+b HRP although stable at 4°C for 1 week, should be stored below -18°C. Please prevent freeze thaw cycles.
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Applications
HCV NS4 Antigen is suitable for ELISA and Western blots, excellent antigen for detection of HCV with minimal specificity problems.
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Specificity
Immunoreactive with sera of HCV-infected individuals.
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Purification Method
HCV NS4 protein was purified by proprietary 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 :
GMPR2 HumanDescription:
Guanosine Monophosphate Reductase 2 Human Recombinant
GMP reductase 2, Guanosine 5''-monophosphate oxidoreductase 2.
Product # :
ENZ-557Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
GMPR2 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 368 amino acids (1-348 a.a.) and having a molecular mass of 40 kDa. GMPR2 is fused to a 20 amino acid His-tag at N-terminus and purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
GMPR2 1mg/ml solution contains 20mM Tris pH-8, 1mM DTT and 10% glycerol.
Purity
Greater than 90% as determined by SDS-PAGE.
More Info
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Introduction
GMPR2 is the single known metabolic step by which guanine nucleotides can be transformed to the pivotal precursor of both adenine and guanine nucleotides. GMPR2 catalyzes the permanent NADPH-dependent reductive deamination of GMP to IMP, and is involved in re-utilization of free intracellular bases and purine nucleosides.
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Synonyms
GMP reductase 2, Guanosine 5''-monophosphate oxidoreductase 2.
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Physical Appearance
Sterile filtered colorless solution.
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Stability
GMPR2 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 MPHIDNDVKL DFKDVLLRPK RSTLKSRSEV DLTRSFSFRN SKQTYSGVPI IAANMDTVGT FEMAKVLCKF
SLFTAVHKHY SLVQWQEFAG QNPDCLEHLA ASSGTGSSDF EQLEQILEAI PQVKYICLDV ANGYSEHFVE FVKDVRKRFP QHTIMAGNVV
TGEMVEELIL SGADIIKVGI GPGSVCTTRK KTGVGYPQLS AVMECADAAH GLKGHIISDG GCSCPGDVAK AFGAGADFVM LGGMLAGHSE
SGGELIERDG KKYKLFYGMS SEMAMKKYAG GVAEYRASEG KTVEVPFKGD VEHTIRDILG GIRSTCTYVG AAKLKELSRR TTFIRVTQQV
NPIFSEAC.
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 :
GLB1 E.ColiDescription:
Galactosidase-Beta 1 E.coli Recombinant
lacZ, beta-gal, β-gal.
Product # :
ENZ-041Price :
Quantity :
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Description
The E.Coli derived recombinant protein Beta-galactosidase (114 kDa) is enzymatically inactive and Non-reactive with human serum.
Source
Escherichia Coli.
Formulation
Beta-Galactosidase (1mg/1ml) is formulated in 8M urea, 20mM Tris-HCl pH 8.0, and 10mM beta-mercaptoethanol
Purity
Protein is >95% pure as determined by SDS-PAGE, by measuring optical density at 280 nm and by method of Bradford et al.
More Info
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Introduction
Beta-galactosidase is a hydrolase enzyme that catalyzes the hydrolysis of Beta-galactosides into monosaccharides. Substrates of different Beta-galactosidases include ganglioside GM1, lactosylceramides, lactose, and various glycoproteins. Beta-galactosidase is produced In E. coli by activation of the lac operon as the lacZ gene.
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Synonyms
lacZ, beta-gal, β-gal.
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Physical Appearance
Sterile filtered colorless solution.
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Stability
Protein should be stored for Short Term at 4°C and for long term at -20°C.
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Purification Method
Purified by proprietary 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 :
PLA2G12 HumanDescription:
Secreted Phospholipase A2-XII Human Recombinant
Group XIIA secretory phospholipase A2, EC 3.1.1.4, Phosphatidylcholine 2-acylhydrolase GXII, GXII sPLA2, PLA2G12, sPLA2-XII, PLA2G12A.
Product # :
ENZ-330Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Secreted Phospholipase A2-XII Human Recombiannt was produced with N-terminal His-Tag. PLA2G12 His-Tagged Fusion Protein is 20.6 kDa containing 167 amino acid residues of the human secreted phospholipase A2-XII and 16 additional amino acid residues – His-Tag (underlined).
Source
Escherichia Coli.
Formulation
Filtered (0.4µm) and lyophilized from 0.5 mg/ml in 0.01M Tris buffer pH 8.6.
Purity
Greater than 95% as determined by SDS PAGE.
More Info
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Introduction
Phospholipase A2 (PLA2) catalyzes the hydrolysis of the sn-2 position of membrane glycerophospholipids to liberate arachidonic acid (AA), a precursor of eicosanoids including prostaglandins and leukotrienes. The same reaction also produces lysophosholipids, which represent another class of lipid mediators.
The secretory PLA2 (sPLA2) family, in which 10 isozymes have been identified, consists of low molecular weight, Ca2+-requiring secretory enzymes that have been implicated in a number of biological processes, such as modification of eicosanoid generation, inflammation, and host defense.
This enzyme has been proposed to hydrolyze phosphatidylcholine (PC) in lipoproteins to liberate lyso- PC and free fatty acids in the arterial wall, thereby facilitating the accumulation of bioactive lipids and modified lipoproteins in atherosclerotic foci.
In mice, sPLA2 expression significantly influences HDL particle size and composition and demonstrate that an induction of sPLA2 is required for the decrease in plasma HDL cholesterol in response to inflammatory stimuli. Instillation of bacteria into the bronchi was associated with surfactant degradation and a decrease in large:small ratio of surfactant aggregates in rats. -
Synonyms
Group XIIA secretory phospholipase A2, EC 3.1.1.4, Phosphatidylcholine 2-acylhydrolase GXII, GXII sPLA2, PLA2G12, sPLA2-XII, PLA2G12A.
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Physical Appearance
Filtered White lyophilized (freeze-dried) powder.
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Stability
Store lyophilized protein at -20°C. Aliquot the product after reconstitution to avoid repeated freezing/thawing cycles. Reconstituted protein can be stored at 4°C for a limited period of time; it does not show any change after two weeks at 4°C.
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Solubility
It is recommended to add deionized water to prepare a working stock solution of approximately 0.5mg/ml and let the lyophilized pellet dissolve completely. Product is not sterile! Please filter the product by an appropriate sterile filter before using it on cell culture.
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Amino Acid Sequence
MRGSHHHHHH GMASHMQEQA QTTDWRATLK TIRNGVHKID TYLNAALDLL GGEDGLCQYK CSDGSKPFPR YGYKPSPPNG CGSPLFGVHL NIGIPSLTKC CNQHDRCYET CGKSKNDCDE EFQYCLSKIC RDVQKTLGLTQ HVQACETTVE LLFDSVIHLG CKPYLDSQRA ACRCHYEEKT DL
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Applications
Western blotting.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
POFUT1 HumanDescription:
Protein O-Fucosyltransferase 1 Human Recombinant
FUT12, O-Fuc-T, O-FucT-1, O-FUT, GDP-fucose protein O-fucosyltransferase 1, Peptide-O-fucosyltraferase 1,KIAA0180.
Product # :
ENZ-679Price :
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Description
POFUT1 Human Recombinant produced in E. coli is a single polypeptide chain containing 385 amino acids (27-388) and having a molecular mass of 43.7 kDa. POFUT1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The POFUT1 solution (1mg/1ml) contains 20mM Tris-HCl buffer (pH 8.0), 2M Urea and 10% glycerol.
Purity
Greater than 85.0% as determined by SDS-PAGE.
More Info
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Introduction
GDP-fucose protein O-fucosyltransferase 1 (POUFUT1), belongs to the glycosyltransferase O-Fuc family. POUFUT1 encodes a member of the glycosyltransferase O-Fuc family and Expressed mainly in pancreas, kidney, lung, heart, brain, liver, placenta and skeletal muscle.POUFUT1 adds O-fucose through an O-glycosidic linkage to Preserve serine or threonine residues in the epidermal growth factor-like repeats of a number of cell surface and emitted proteins. POUFUT1 is involved in ligand-induced receptor signaling. Alternative splicing of this gene results in 2 transcript variants encoding different isoforms.POFUT1 participates in Notch signaling, as Notch ligands can use as POFUT1 substrates.
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Synonyms
FUT12, O-Fuc-T, O-FucT-1, O-FUT, GDP-fucose protein O-fucosyltransferase 1, Peptide-O-fucosyltraferase 1,KIAA0180.
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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 MGSGSWDPAG YLLYCPCMGR FGNQADHFLG SLAFAKLLNR TLAVPPWIEY QHHKPPFTNL HVSYQKYFKL EPLQAYHRVI SLEDFMEKLA PTHWPPEKRV AYCFEVAAQR SPDKKTCPMK EGNPFGPFWD QFHVSFNKSE LFTGISFSAS YREQWSQRFS PKEHPVLALP GAPAQFPVLE EHRPLQKYMV WSDEMVKTGE AQIHAHLVRP YVGIHLRIGS DWKNACAMLK DGTAGSHFMA SPQCVGYSRS TAAPLTMTMC LPDLKEIQRA VKLWVRSLDA QSVYVATDSE SYVPELQQLF KGKVKVVSLK PEVAQVDLYI LGQADHFIGN CVSSFTAFVK RERDLQGRPS SFFGMDRPPK LRDEF.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
GPT HumanDescription:
Glutamic-Pyruvate Transaminase Human Recombinant
Glutamic-pyruvate transaminase (alanine aminotransferase), GPT1, ALT1, AAT1, Glutamic-alanine transaminase 1, EC 2.6.1.2.
Product # :
ENZ-192Price :
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Shipped with Ice Packs
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Description
GPT Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 516 amino acids (1-496) and having a molecular mass of 56.8 kDa.GPT is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
The GPT solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 2mM DTT and 20% glycerol.
Purity
Greater than 90% as determined by SDS-PAGE.
More Info
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Introduction
GPT catalyzes the reversible transamination between alanine and 2-oxoglutarate to create pyruvate and glutamate. GPT has a crucial part in the intermediary metabolism of glucose and amino acids. GPT is broadly used as an indicator of liver reliability or hepatocellular destruction in clinical tests.
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Synonyms
Glutamic-pyruvate transaminase (alanine aminotransferase), GPT1, ALT1, AAT1, Glutamic-alanine transaminase 1, EC 2.6.1.2.
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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 MASSTGDRSQ AVRHGLRAKV LTLDGMNPRV RRVEYAVRGP IVQRALELEQ ELRQGVKKPF TEVIRANIGD AQAMGQRPIT FLRQVLALCV NPDLLSSPNF PDDAKKRAER ILQACGGHSL GAYSVSSGIQ LIREDVARYI ERRDGGIPAD PNNVFLSTGA SDAIVTVLKL LVAGEGHTRT GVLIPIPQYP LYSATLAELG AVQVDYYLDE ERAWALDVAE LHRALGQARD HCRPRALCVI NPGNPTGQVQ TRECIEAVIR FAFEERLFLL ADEVYQDNVY AAGSQFHSFK KVLMEMGPPY AGQQELASFH STSKGYMGEC GFRGGYVEVV NMDAAVQQQM LKLMSVRLCP PVPGQALLDL VVSPPAPTDP SFAQFQAEKQ AVLAELAAKA KLTEQVFNEA PGISCNPVQG AMYSFPRVQL PPRAVERAQE LGLAPDMFFC LRLLEETGIC VVPGSGFGQR EGTYHFRMTI LPPLEKLRLL LEKLSRFHAK FTLEYS
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 :
HTRA2 HumanDescription:
HTRA2 Human Recombinant
Serine protease HTRA2 mitochondrial, EC 3.4.21.108, High temperature requirement protein A2, HtrA2, Omi stress-regulated endoprotease, Serine proteinase OMI, Serine protease 25, OMI, PARK13, PRSS25.
Product # :
ENZ-332Price :
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Description
HtrA2 Human Recombinant amino acids 134-458 His-Tag fusion protein produced in E.Coli is a single, non-glycosylated polypeptide chain having a molecular mass of 36kDa.The HtrA2 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The protein (0.5 mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 50mM NaCl, 1mM DTT, and 20% Glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
HtrA2 also called Omi is a mammalian serine protease at high temperatures and has a chaperone activity at low temperature. The full-length HtrA2 is synthesized as a precursor protein and then targeted to the mitochondria where it is matured by the removal of N-terminal 133 residues. Mature HtrA2 consists of a putative transmembrane domain; an inhibitor of apoptosis protein (IAP)-binding motif; a single C-terminal PDZ domain that mediates protein-protein interactions. Recently, HtrA2 has known to contribute both to caspase-dependent and caspase-independent cell death.
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Synonyms
Serine protease HTRA2 mitochondrial, EC 3.4.21.108, High temperature requirement protein A2, HtrA2, Omi stress-regulated endoprotease, Serine proteinase OMI, Serine protease 25, OMI, PARK13, PRSS25.
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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
MAVPSPPPAS PPSQYNFIAD VVEKTAPAVV YIEILDRHPF LGREVPISNG SGFVVAADGL IVTNAHVVAD RRRVRVRLLS GDTYEAVVTA VDPVADIATL RIQTKEPLPT LPLGRSADVR QGEFVVAMGS PFALQNTITS GIVSSAQRPA RDLGLPQTNV EYIQTDAAID FGNAGGPLVN LDGEVIGVNT MKVTAGISFA IPSDRLREFL HRGEKKNSSS GISGSQRRYI GVMMLTLSPS ILAELQLREP SFPDVQHGVL IHKVILGSPA HRAGLRPGDV ILAIGEQMVQ NAEDVYEAVR TQSQLAVQIR RGRETLTLYV TPEVTEGSHH HHHH.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
CCBL1 HumanDescription:
Cysteine Conjugate-Beta Lyase Cytoplasmic Human Recombinant
Cysteine Conjugate-Beta Lyase, Cytoplasmic, Glutamine Transaminase K, Cysteine Conjugate-Beta Lyase; Cytoplasmic (Glutamine Transaminase K, Kyneurenine Aminotransferase), Kynurenine--Oxoglutarate Transaminase I, Glutamine--Phenylpyruvate Transaminase, Cysteine-S-Conjugate Beta-Lyase, Kynurenine Aminotransferase I, Kyneurenine Aminotransferase, KATI, GTK, Glutamine-Phenylpyruvate Aminotransferase, Kynurenine--Oxoglutarate Transaminase 1, Beta-Lysase, Kidney, EC 4.4.1.13, EC 2.6.1.64, EC 2.6.1.7, KAT1, Kynurenine--oxoglutarate transaminase 1.
Product # :
ENZ-878Price :
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Description
CCBL1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 445 amino acids (1-422 a.a) and having a molecular mass of 50.3kDa. CCBL1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
CCBL1 protein solution (1mg/ml) containing Phosphate buffered saline (pH7.4), 10% glycerol and 1mM DTT.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
Cysteine Conjugate-Beta Lyase Cytoplasmic also known as CCBL1 is a member of the class-I pyridoxal-phosphate-dependent aminotransferase family. CCBL1 catalyzes the irreversible transamination of the L-tryptophan metabolite L-kynurenine to form kynurenic acid (KA) it also metabolizes the cysteine conjugates of certain halogenated alkenes and alkanes to form reactive metabolites. Furthermore, CCBL1 catalyzes the beta-elimination of S-conjugates and Se-conjugates of L-(seleno) cysteine, resulting in the cleavage of the C-S or C-Se bond.
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Synonyms
Cysteine Conjugate-Beta Lyase, Cytoplasmic, Glutamine Transaminase K, Cysteine Conjugate-Beta Lyase; Cytoplasmic (Glutamine Transaminase K, Kyneurenine Aminotransferase), Kynurenine--Oxoglutarate Transaminase I, Glutamine--Phenylpyruvate Transaminase, Cysteine-S-Conjugate Beta-Lyase, Kynurenine Aminotransferase I, Kyneurenine Aminotransferase, KATI, GTK, Glutamine-Phenylpyruvate Aminotransferase, Kynurenine--Oxoglutarate Transaminase 1, Beta-Lysase, Kidney, EC 4.4.1.13, EC 2.6.1.64, EC 2.6.1.7, KAT1, Kynurenine--oxoglutarate transaminase 1.
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Physical Appearance
Sterile Filtered colorless solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSMAKQLQA RRLDGIDYNP WVEFVKLASE HDVVNLGQGF PDFPPPDFAV EAFQHAVSGD FMLNQYTKTF GYPPLTKILA SFFGELLGQE IDPLRNVLVT VGGYGALFTA FQALVDEGDE VIIIEPFFDC YEPMTMMAGG RPVFVSLKPG PIQNGELGSS SNWQLDPMEL AGKFTSRTKA LVLNTPNNPL GKVFSREELE LVASLCQQHD VVCITDEVYQ WMVYDGHQHI SIASLPGMWE RTLTIGSAGK TFSATGWKVG WVLGPDHIMK HLRTVHQNSV FHCPTQSQAA VAESFEREQL LFRQPSSYFV QFPQAMQRCR DHMIRSLQSV GLKPIIPQGS YFLITDISDF KRKMPDLPGA VDEPYDRRFV KWMIKNKGLV AIPVSIFYSV PHQKHFDHYI RFCFVKDEAT LQAMDEKLRK WKVEL.
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 :
BPNT1 HumanDescription:
3(2) 5-Bisphosphate Nucleotidase 1 Human Recombinant
3'(2'), 5'-bisphosphate nucleotidase 1, Bisphosphate 3'-nucleotidase 1, PAP-inositol-1,4-phosphatase, PIP, EC 3.1.3.7, BPntase.
Product # :
ENZ-061Price :
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Description
BPNT1 produced in E.Coli is a single, non-glycosylated polypeptide chain containing 344 amino acids (1-308a.a.) and having a molecular mass of 37.5kDa.BPNT1 is fused to a 36 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The BPNT1 protein solution (0.5mg/1ml) is formulated in 20mM Tris-HCl buffer (pH8.0) 5mM DTT, 0.1M NaCl and 10% glycerol.
Purity
Greater than 90% as determined by SDS-PAGE.
More Info
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Introduction
BPNT1 belongs to the magnesium-dependent, lithium-sensitive phosphomono-esterase superfamily. BPNT1 catalyzes the conversion of PAPS (adenosine 3'-phosphate 5' phosphosulfate) to APS (adenosine 5'-phosphosulfate) and the conversion of PAP (3'(2')-phosphoadenosine 5' phosphate) to AMP (adenosine 5'-phosphate) using magnesium as a cofactor. BPNT1 is expressed everywhere but at maximum levels in brain and kidney. BPNT1 is potently inhibited by lithium, a drug used for the treatment of manic depression and bipolar affective disorder, which suggests that BPNT1 has a possible role in the etiology of mood disorders.
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Synonyms
3'(2'), 5'-bisphosphate nucleotidase 1, Bisphosphate 3'-nucleotidase 1, PAP-inositol-1,4-phosphatase, PIP, EC 3.1.3.7, BPntase.
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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
MRGSHHHHHH GMASMTGGQQ MGRDLYDDDD KDRWGSMASS NTVLMRLVAS AYSIAQKAGM IVRRVIAEGD LGIVEKTCAT DLQTKADRLA QMSICSSLAR KFPKLTIIGE EDLPSEEVDQ ELIEDSQWEE ILKQPCPSQY SAIKEEDLVV WVDPLDGTKE YTEGLLDNVT VLIGIAYEGK AIAGVINQPY YNYEAGPDAV LGRTIWGVLG LGAFGFQLKE VPAGKHIITT TRSHSNKLVT DCVAAMNPDA VLRVGGAGNK IIQLIEGKAS AYVFASPGCK KWDTCAPEVI LHAVGGKLTD IHGNVLQYHK DVKHMNSAGV LATLRNYDYY ASRVPESIKN ALVP
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
ENTPD3 Human, sf9 BioactiveDescription:
Ectonucleoside Triphosphate Diphosphohydrolase 3 Human Recombinant, sf9 Bioactive
Ectonucleoside Triphosphate Diphosphohydrolase 3, Ecto-ATP Diphosphohydrolase 3, CD39 Antigen-Like 3, Ecto-ATPDase 3, Ecto-Apyrase 3, Ecto-ATPase 3, EC 3.6.1.5, NTPDase 3, CD39L3, HB6, NTPDase-3, EC 3.6.1, Ectonucleoside triphosphate diphosphohydrolase 3, NTPDase 3, CD39 antigen-like 3, Ecto-ATP diphosphohydrolase 3, Ecto-ATPDase 3, Ecto-ATPase 3, Ecto-apyrase 3, HB6.
Product # :
ENZ-1020Price :
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Description
ENTPD3 Human Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 451 amino acids (44-485a.a.) and having a molecular mass of 50.7kDa (Molecular size on SDS-PAGE will appear at approximately 50-70kDa).ENTPD3 is expressed with a 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
ENTPD3 protein solution (0.5mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 10% glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
Biological Activity
Specific activity is > 250,000 pmol/min/ug, and is defined as the amount of enzyme that hydrolyze ATP per minute at pH 7.5 at 37C.More Info
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Introduction
Ectonucleoside Triphosphate Diphosphohydrolase 3, also known as ENTPD3, which owns a threefold preference for the hydrolysis of ATP over ADP is similar to E-type nucleotidases (NTPases). ENTPD3 is a protein coding gene which contains four apyrase-conserved areas which is characteristic of NTPases.
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Synonyms
Ectonucleoside Triphosphate Diphosphohydrolase 3, Ecto-ATP Diphosphohydrolase 3, CD39 Antigen-Like 3, Ecto-ATPDase 3, Ecto-Apyrase 3, Ecto-ATPase 3, EC 3.6.1.5, NTPDase 3, CD39L3, HB6, NTPDase-3, EC 3.6.1, Ectonucleoside triphosphate diphosphohydrolase 3, NTPDase 3, CD39 antigen-like 3, Ecto-ATP diphosphohydrolase 3, Ecto-ATPDase 3, Ecto-ATPase 3, Ecto-apyrase 3, HB6.
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Physical Appearance
Sterile Filtered colorless solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks.Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
ADLQIHKQEV LPPGLKYGIV LDAGSSRTTV YVYQWPAEKE NNTGVVSQTF KCSVKGSGIS SYGNNPQDVP RAFEECMQKV KGQVPSHLHG STPIHLGATA GMRLLRLQNE TAANEVLESI QSYFKSQPFD FRGAQIISGQ EEGVYGWITA NYLMGNFLEK NLWHMWVHPH GVETTGALDL GGASTQISFV AGEKMDLNTS DIMQVSLYGY VYTLYTHSFQ CYGRNEAEKK FLAMLLQNSP TKNHLTNPCY PRDYSISFTM GHVFDSLCTV DQRPESYNPN DVITFEGTGD PSLCKEKVAS IFDFKACHDQ ETCSFDGVYQ PKIKGPFVAF AGFYYTASAL NLSGSFSLDT FNSSTWNFCS QNWSQLPLLL PKFDEVYARS YCFSANYIYH LFVNGYKFTE ETWPQIHFEK EVGNSSIAWS LGYMLSLTNQ IPAESPLIRL PIEPPHHHHHH.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
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 :
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Shipped with Ice Packs
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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.