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Search results

1000 results found for “Enterokinase”

Name

Description

Product #

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Quantity

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  • View Data Sheet

    Name :

    FBP1 Human

    Description:

    Fructose-1,6-Bisphosphatase 1 Human Recombinant

    FBP1, FBP, D-fructose-1,6-bisphosphate 1-phosphohydrolase 1, FBPase 1, Fructose-1,6-bisphosphatase 1.

    Product # :

    ENZ-454

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    Quantity :

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    • source
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    • More Info

    Description

    The FBP1 Human recombinant protein is a single, non-glycosilated polypeptide chain produced in E. coli, having a molecular weight of 39kDa and containing 358 amino acids (1-338 a.a.). The FBP1 enzyme is fused to a 20 amino acid His-Tag at N-terminus and purified by proprietary chromatography techniques.

    Source

    Escherichia Coli.

    Formulation

    The FBP1 protein solution is formulated in 20mM Tris-HCl pH-8, 1mM DTT and 10% glycerol.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    More Info

    • Introduction

      FBP1 is a gluconeogenesis regulatory protein which catalyzes the hydrolysis of fructose 1,6-bisphosphate to fructose 6-phosphate and inorganic phosphate. FBP1 deficiency is associated with hypoglycemia and metabolic acidosis. FBP1 regulates mouse endogenous glucose production. FBP1 coupled with phosphofructokinase (PFK) takes part in the metabolism of pancreatic islet cells.

    • Synonyms

      FBP1, FBP, D-fructose-1,6-bisphosphate 1-phosphohydrolase 1, FBPase 1, Fructose-1,6-bisphosphatase 1.

    • Physical Appearance

      Sterile Filtered clear solution.

    • Stability

      Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MADQAPFDTD VNTLTRFVME EGRKARGTGE LTQLLNSLCT AVKAISSAVR KAGIAHLYGI AGSTNVTGDQ VKKLDVLSND LVMNMLKSSF ATCVLVSEED KHAIIVEPEK RGKYVVCFDP LDGSSNIDCL VSVGTIFGIY RKKSTDEPSE KDALQPGRNL VAAGYALYGS ATMLVLAMDC GVNCFMLDPA IGEFILVDKD VKIKKKGKIY SLNEGYARDF DPAVTEYIQR KKFPPDNSAP YGARYVGSMV ADVHRTLVYG GIFLYPANKK SPNGKLRLLY ECNPMAYVME KAGGMATTGK EAVLDVIPTD IHQRAPVILG SPDDVLEFLK VYEKHSAQ.

    ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

    Fbp1 Human
  • View Data Sheet

    Name :

    GLO1 Human

    Description:

    Glyoxalase-I Human Recombinant

    GLYI, GLOD1, GLO1, Glyoxalase-1, Lactoylglutathione lyase, Methylglyoxalase, Aldoketomutase, Ketone-aldehyde mutase, Glyoxalase I, S-D-lactoylglutathione methylglyoxal lyase, Glx I.

    Product # :

    ENZ-398

    Price :

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    Description

    Glyoxalase-I Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 184 amino acids and having a molecular mass of 20.7 kDa. Glyoxalase-1 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Glyoxalase-1 solution containing 20mM Tris-HCl pH-8, 1mM DTT and 10% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      GLO1 is involved in the catalysis and formation of S-lactoyl-glutathione from methylglyoxal condensation and reduced glutatione. GLO1 is linked to HLA and is localized to 6p21.3-p21.1, between HLA and the centromere. GLO1 enzyme is ubundantly expressed and present in numerous tumor cell lines, in which its concentration is often upregulated ubiquitisly. GLO1 is a major susceptible gene for autism in an ethnic Chinese population from Taiwan. GLO1 might be involved in the pathophysiology of mood disorders. GLO1 plays a role in the pathophysiology of mood disorders. Overexpression of GLO1 is associated with kidney tumor.

    • Synonyms

      GLYI, GLOD1, GLO1, Glyoxalase-1, Lactoylglutathione lyase, Methylglyoxalase, Aldoketomutase, Ketone-aldehyde mutase, Glyoxalase I, S-D-lactoylglutathione methylglyoxal lyase, Glx I.

    • Physical Appearance

      Sterile filtered colorless solution.

    • Stability

      Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.

    • Amino Acid Sequence

      MAEPQPPSGG LTDEAALSCC SDADPSTKDF LLQQTMLRVK DPKKSLDFYT RVLGMTLIQK CDFPIMKFSL YFLAYEDKND IPKEKDEKIAWALSRKATLE LTHNWGTEDD ETQSYHNGNS DPRGFGHIGI AVPDVYSACK RFEELGVKFV KKPDDGKMKG LAFIQDPDGY WIEILNPNKM ATLM.

    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.

    Glo1 Human
  • View Data Sheet

    Name :

    MMP9 Human, Sf9

    Description:

    Matrix Metalloproteinase-9 Human Recombinant, Sf9

    Matrix metalloproteinase-9, MMP-9, 92 kDa gelatinase, Gelatinase B, GELB, MMP9, CLG4B.

    Product # :

    ENZ-1091

    Price :

    Quantity :

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    • description
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    Description

    MMP9 produced in Sf9 Insect cells is a single, glycosylated polypeptide chain containing 694 amino acids (20-707a.a.) and having a molecular mass of 77.1 kDa (Molecular size on SDS-PAGE will appear at approximately 70-100kDa). MMP9 is expressed with a 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    MMP9 protein solution ( 0.5mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 10% glycerol.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    More Info

    • Introduction

      MMP9 is part of the matrix metalloproteinase family. MMP enzymes take part in the dismantle of extracellular matrix in different physiological pathways, for instance wound healing, bone development, reproduction etc. the enzyme is also involved in pathological pathways: metastasis, arthritis and intracerebral hemorrhage.

    • Synonyms

      Matrix metalloproteinase-9, MMP-9, 92 kDa gelatinase, Gelatinase B, GELB, MMP9, CLG4B.

    • Physical Appearance

      Sterile Filtered colorless solution.

    • Stability

      Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.

    • Amino Acid Sequence

      APRQRQSTLV LFPGDLRTNL TDRQLAEEYL YRYGYTRVAE MRGESKSLGP ALLLLQKQLS LPETGELDSA TLKAMRTPRC GVPDLGRFQTFEGDLKWHHH NITYWIQNYS EDLPRAVIDD AFARAFALWS AVTPLTFTRV YSRDADIVIQ FGVAEHGDGY PFDGKDGLLA HAFPPGPGIQ GDAHFDDDEL WSLGKGVVVP TRFGNADGAA CHFPFIFEGR SYSACTTDGR SDGLPWCSTT ANYDTDDRFG FCPSERLYTQ DGNADGKPCQ FPFIFQGQSY SACTTDGRSD GYRWCATTAN YDRDKLFGFC PTRADSTVMG GNSAGELCVF PFTFLGKEYS TCTSEGRGDG RLWCATTSNF DSDKKWGFCP DQGYSLFLVA AHEFGHALGL DHSSVPEALM YPMYRFTEGP PLHKDDVNGI RHLYGPRPEP EPRPPTTTTP QPTAPPTVCP TGPPTVHPSE RPTAGPTGPP SAGPTGPPTA GPSTATTVPL SPVDDACNVN IFDAIAEIGN QLYLFKDGKY WRFSEGRGSR PQGPFLIADK WPALPRKLDS VFEERLSKKL FFFSGRQVWV YTGASVLGPR RLDKLGLGAD VAQVTGALRS GRGKMLLFSG RRLWRFDVKA QMVDPRSASE VDRMFPGVPL DTHDVFQYRE KAYFCQDRFY WRVSSRSELN QVDQVGYVTY DILQCPEDHH 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.

    Mmp9 Enzyme
  • View Data Sheet

    Name :

    CES2E Mouse

    Description:

    Carboxylesterase 2E Mouse Recombinant

    9030624L02Rik, Ces5, Ces2e.

    Product # :

    ENZ-1141

    Price :

    Quantity :

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    • description
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    • biological activity
    • More Info

    Description

    CES2E Mouse produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 541 amino acids ( 27-559 aa) and having a molecular mass of 60.5kDa.CES2E is fused to a 8 amino acid His tag at C-terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    The CES2E solution (0.25 mg/ml) contains 10% Glycerol and Phosphate-Buffered Saline (pH 7.4).

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Biological Activity

    Specific activity is > 30unit/mg, and is defined as the amount of enzyme that hydrolyze 1.0 umole of pnitrophenyl acetate to p-nitrophenol per minute at pH 7.5 at 25C˚.

    More Info

    • Introduction

      Carboxylesterase 2E or CES2E is an enzyme that hydrolyzes various carboxylic acid esters. This enzyme can be found mainly in mammalian liver cells. CES2E is taking part in chemical reactions, especially in carboxylic ester and water catalyzation to alcohol & carboxylate.

    • Synonyms

      9030624L02Rik, Ces5, Ces2e.

    • Physical Appearance

      Sterile Filtered colorless solution.

    • Stability

      Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.

    • Amino Acid Sequence

      QDSASPIRNT HTGQVRGSLV HVKDTDIAVH TFLGIPFAKP PVGPLRFAPP EAPEPWSGVR DGTSHPNMCL QNDNLMGSED LKMMNLILPP ISMSEDCLYL NIYVPAHAHE GSNLPVMVWI HGGALTVGMA SMYDGSMLAA TEDVVVVAIQ YRLGVLGFFS TGDQHAKGNW GYLDQVAALR WVQQNIVHFG GNPDRVTIFG ESAGGTSVSS HVVSPMSQGL FHGAIMESGV AVLPDLISSS
      SEMVHRIVAN LSGCAAVNSE TLMCCLRGKN EAEMLAINKV FKIIPGVVDG EFLPKHPQEL MASKDFHPVP SIIGINNDEY GWILPTIMDP AQKIEEITRK TLPAVLKSTA LKMMLPPECG DLLMEEYMGD TEDPETLQAQ FREMKGDFMF VIPALQVAHF QRSHAPVYFY EFQHRPSFFK DFRPPYVKAD HGDEIFLVFG YQFGNIKLPY TEEEEQLSRR IMKYWANFAR HGNPNSEGLP YWPVMDHDEQ YLQLDIQPSV GRALKARRLQ FWTKTLPQKI QELKGSQERH KELLEHHHHH H

    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.

    Ces2E Mouse
  • View Data Sheet

    Name :

    PTGES3 Human

    Description:

    Prostaglandin E Synthase 3 Human Recombinant

    TEBP, CPGES, SID3177, 5730442A20Rik, p23, HSP90 co-chaperone, Prostaglandin E synthase 3, Cytosolic prostaglandin E2 synthase, Telomerase-binding protein p23, Progesterone receptor complex p23, PTGES3.

    Product # :

    ENZ-458

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    Description

    Recombinant Human PTGES3 produced in E.Coli is a single,non-glycosylated polypeptide chain containing 160 amino acids (1-160 a.a.) and having a molecular mass of 18.6 kDa.PTGES3 is purified by convential chromatogrpahy techniques.

    Source

    Escherichia Coli.

    Formulation

    The PTGES3 protein solution contains 20mM Tris-HCl, pH-8, 1mM DTT & 10% Glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      PTGES3 takes part as a cochaperone and is involved in signal transduction.
      PTGES3 is a molecular chaperone that localizes to genomic response elements in a hormone-dependent manner and disrupts receptor-mediated transcriptional activation, by promoting disassembly of transcriptional regulatory complexess. PTGES3 is necessary for appropriate functioning of the glucocorticoid and other steroid receptors.
      PTGES3 localizes to genomic response elements in a hormone-dependent method and disrupts receptor-mediated transcriptional activation, by promoting disassembly of transcriptional regulatory complexes.

    • Synonyms

      TEBP, CPGES, SID3177, 5730442A20Rik, p23, HSP90 co-chaperone, Prostaglandin E synthase 3, Cytosolic prostaglandin E2 synthase, Telomerase-binding protein p23, Progesterone receptor complex p23, PTGES3.

    • Physical Appearance

      Sterile filtered colorless solution.

    • Stability

      Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA). Avoid multiple freeze-thaw cycles.

    • Amino Acid Sequence

      MQPASAKWYD RRDYVFIEFC VEDSKDVNVN FEKSKLTFSC LGGSDNFKHL NEIDLFHCID PNDSKHKRTD RSILCCLRKG ESGQSWPRLT KERAKLNWLS VDFNNWKDWE DDSDEDMSNF DRFSEMMNNM GGDEDVDLPE VDGADDDSQD SDDEKMPDLE.

    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.

    Ptges3 Human
  • View Data Sheet

    Name :

    WWOX Human

    Description:

    WW Domain Containing Oxidoreductase Human Recombinant

    FOR, WOX1, FRA16D, HHCMA56, PRO0128, SDR41C1, D16S432E, WWOX, WW domain-containing oxidoreductase, Fragile site FRA16D oxidoreductase.

    Product # :

    ENZ-422

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    Description

    WWOX Human Recombinant fused with 20 amino acid His tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 254 amino acids (1-234 a.a.) and having a molecular mass of 28.3 kDa.The WWOX is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The WWOX solution (1mg/ml) contains 20mM Tris pH-8, & 10% glycerol.

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      WWOX is a proapoptotic protein and a tumor suppressor protein. WWOX is found in all eukaryotes and involved in the regulation of a broad range of cellular functions such as protein degradation, transcription, and RNA splicing. WWOX functions synergistically with TP53/p53 to control genotoxic stress-induced cell death. WWOX takes part in tumor necrosis factor (TNF)-mediated cell death. Loss of WWOX expression is associated with pancreatobiliary cancers. Reduced expression levels of WWOX protein is associated with the pathogenesis of basal-like differentiation in breast cancer. Loss of WWOX expression is associated with extrahepatic cholangiocarcinoma. WWOX gene alteration is an early genetic alteration contributes to oral carcinogenesis. WWOX induces apoptosis and inhibits human hepatocellular carcinoma cell growth through a mechanism enhanced by JNK inhibition.

    • Synonyms

      FOR, WOX1, FRA16D, HHCMA56, PRO0128, SDR41C1, D16S432E, WWOX, WW domain-containing oxidoreductase, Fragile site FRA16D oxidoreductase.

    • Physical Appearance

      Sterile Filtered colorless solution.

    • Stability

      Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MAALRYAGLD DTDSEDELPP GWEERTTKDG WVYYANHTEE KTQWEHPKTG KRKRVAGDLP YGWEQETDEN GQVFFVDHIN KRTTYLDPRL AFTVDDNPTK PTTRQRYDGS TTAMEILQGR DFTGKVVVVT GANSGIGFET AKSFALHGAH VILACRNMAR ASEAVSRILE EWQQGAATTV YCAAVPELEG LGGMYFNNCC RCMPSPEAQS EETARTLWAL SERLIQERLG SQSG.

    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.

    Wwox Human
  • View Data Sheet

    Name :

    ACE2 (18-740) Human, Biotin

    Description:

    Angiotensin Converting Enzyme 2 (18-740 a.a.), Biotinylated Human Recombinant

    Product # :

    ENZ-1127

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    Description

    The HEK293 derived ACE2 Human recombinant biotinylated protein contains the amino acids Gln 18-Ser 740 fused to His-AVI tag at C-terminal having a predicted Mw of 87.2 kDa ( migrates 95-125 kDa under reducing conditions on sds-page due to glycosilation). ACE2 Protein binds to SARS Coronavirus-2 [ CoV-2019 ] Spike receptor binding domain.

    Source

    HEK293 Cells

    Formulation

    ACE2 Human protein solution is supplied in 50mM Tris, pH7.5, 150mM NaCl and 20% glycerol.

    Purity

    ACE-2 Protein is >90% pure as determined SDS-PAGE.

    Biological Activity

    ACE2 activity was measured by its binding ability in a functional ELISA.

    The immobilized Recombinant Human ACE2 protein binds to SARS CoV2 Spike protein Receptor Binding Domain at 2ug per ml.

    More Info

    • Introduction

      ACE-2 (Angiotensin converting enzyme 2) an enzyme bound to cell membranes in various organs such as intestines arteries , lungs, heart & kidney. ACE2 an entry receptor of SARS coronaviruses as well as SARS-CoV-2,.The coronavirus spike (S) glycoprotein is a class I viral fusion antigen located on the external envelope of the virion that takes part in a critical part in viral infection by identifying host cell receptors and facilitating fusion of the viral and cellular membranes. 2 main domains in coronavirus S1 have been recognized, the N-terminal domain and C-terminal domain. One or the other and/or both S1 domains function as a receptor-binding domain. SARS-CoV + MERS-CoV equally use C-domain to attach their receptors.ACE2 is a type I transmembrane antigen with an extracellular N-terminal domain having the catalytic site and an intracellular C-terminal tail. ACE2 obtains a signal peptide, a transmembrane domain, and a single metalloproteinase active site containing an HEXXH zinc-binding domain. ACE-2 plays a role as a mono-carboxypeptidase which degrades Ang I to produce the nonapeptide Ang 1–9 and Ang II to create the heptapeptide Ang 1–7.

    • Physical Appearance

      Sterile Filtered clear solution.

    • Stability

      ACE-2 Human Recombinant Protein is shipped on ice packs. Upon arrival, Store at -20°C. The addition of 0.1% albmin is highly recommended for long term storage use.

    • Purification Method

      Purified by Protein-G 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.

    Ace 2 Protein
  • View Data Sheet

    Name :

    AKR1C3 Human, His

    Description:

    Aldo-Keto Reductase Family 1 Member C3 Human Recombinant, His Tag

    DD3, DDX, HAKRB, HAKRe, HA1753, HSD17B5, hluPGFS, KIAA0119, AKR1C3, Aldo-keto reductase family 1 member C3, 3-alpha-HSD type 2, 17-beta-HSD 5, PGFS, DD-3.

    Product # :

    ENZ-406

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    Description

    AKR1C3 Human Recombinant fused to 20 amino acid His Tag at N-terminal produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 343 amino acids (1-323 a.a.) and having a molecular mass of 39 kDa. The AKR1C3 is fused to a 20 amino acid His tag purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The AKR1C3 solution contains 20mM Tris-HCl pH-8 and 10% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Biological Activity

    Specific activity: approximately < 0.1 units/mg.
    Enzymatic activity was confirmed by measuring the amount of enzyme catalyzing the oxidation of 1 micromole NADPH per minute at 25C. Specific activity was expressed as units/mg protein.

    More Info

    • Introduction

      AKR1C3 is part of the aldo/keto reductase superfamily, which has at least 40 identified proteins. AKR1C3 catalyzes the conversion of aldehydes and ketones to their corresponding alcohols by utilizing NADH and/or NADPH as cofactors. AKR1C3 displays overlapping but distinct substrate specificity. AKR1C3 catalyzes the reduction of prostaglandin (PG) D2, PGH2 and phenanthrenequinone (PQ), and the oxidation of 9alpha,11beta-PGF2 to PGD2. AKR1C3 is involved in the pathogenesis of allergic diseases such as asthma. AKR1C3 controls cell growth and/or differentiation. AKR1C3 takes part in adrenal testosterone production. AKR1C3 expression is affected by metabolic disease, and its levels are considerably reduced in response to diet-induced weight loss and correlate with leptin levels.

    • Synonyms

      DD3, DDX, HAKRB, HAKRe, HA1753, HSD17B5, hluPGFS, KIAA0119, AKR1C3, Aldo-keto reductase family 1 member C3, 3-alpha-HSD type 2, 17-beta-HSD 5, PGFS, DD-3.

    • Physical Appearance

      Sterile Filtered clear colorless solution.

    • Stability

      Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MDSKHQCVKL NDGHFMPVLG FGTYAPPEVP RSKALEVTKL AIEAGFRHID SAHLYNNEEQ VGLAIRSKIA DGSVKREDIF YTSKLWSTFH RPELVRPALE NSLKKAQLDY VDLYLIHSPM SLKPGEELSP TDENGKVIFD IVDLCTTWEA MEKCKDAGLA KSIGVSNFNR RQLEMILNKPGLKYKPVCNQ VECHPYFNRS KLLDFCKSKD IVLVAYSALG SQRDKRWVDP NSPVLLEDPV LCALAKKHKR TPALIALRYQ LQRGVVVLAK SYNEQRIRQN VQVFEFQLTA EDMKAIDGLD RNLHYFNSDS FASHPNYPYS DEY.

    ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

    Akr1C3 Human
  • View Data Sheet

    Name :

    UBE2D3 Human

    Description:

    Ubiquitin Conjugating Enzyme E2D3 Human Recombinant

    Ubiquitin-conjugating enzyme E2 D3, EC 6.3.2.19, Ubiquitin-protein ligase D3, Ubiquitin carrier protein D3, Ubiquitin-conjugating enzyme E2-17 kDa 3, E2(17)KB 3, UBC4/5, UBCH5C, MGC5416, MGC43926, UBE2D3.

    Product # :

    ENZ-343

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    Description

    UBE2D3 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 169 amino acids (1-149a.a.) and having a molecular mass of 19.1kDa. UBE2D3 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The UBE2D3 solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH8.0), 40% glycerol, 0.15M NaCl and 1mM DTT.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      UBE2D3 enzymes are human homologs of the yeast UBC4/5 family and play many important regulatory roles in inflammation and cancer. UbcH5a mediates the degradation of a myriad of short-lived regulatory proteins (such as p53 in the presence of E6/E6-AP or MDM2, c-Fos, I?B?, p105) and abnormal proteins. UBE2D3 has 88% and 89% sequence identity with UbcH5a and UbcH5b respectively.

    • Synonyms

      Ubiquitin-conjugating enzyme E2 D3, EC 6.3.2.19, Ubiquitin-protein ligase D3, Ubiquitin carrier protein D3, Ubiquitin-conjugating enzyme E2-17 kDa 3, E2(17)KB 3, UBC4/5, UBCH5C, MGC5416, MGC43926, UBE2D3.

    • Physical Appearance

      Sterile filtered colorless solution.

    • Stability

      Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MLSNRKCLSK ELSDLARDPP AQCSAGPVGD DMFHWQATIM GPNDSPYQGG VFFLTIHFPT DYPFKPPKVA FTTRIYHPNI NSNGSICLDI LRSQWSPALT ISKVLLSICS LLCDPNPDDP LVPEIARIYK TDRDKYNRIS REWTQKYAM.

    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.

    Ube2D3 Human
  • View Data Sheet

    Name :

    NT5C3B Human

    Description:

    5'-Nucleotidase, Cytosolic IIIB Human Recombinant

    NT5C3L, 7-methylguanosine phosphate-specific 5'-nucleotidase, Cytosolic 5'-nucleotidase 3B, Cytosolic 5'-nucleotidase III-like protein, cN-III-like protein, N(7)-methylguanylate 5'-phosphatase.

    Product # :

    ENZ-836

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    Description

    NT5C3B Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 323 amino acids (1-300 a.a) and having a molecular mass of 36.8kDa.NT5C3B is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    NT5C3B protein solution (1mg/ml) containing Phosphate Buffered Saline (pH7.4), 20% glycerol and 1mM DTT.

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      7-methylguanosine phosphate-specific 5'-nucleotidase (NT5C3B) includes transferase activity and nucleotide binding. Among NT5C3B’s related super-pathways are adenosine nucleotides degradation II and Pyrimidine metabolism. NT5C3B hydrolyzes 7-methylguanosine monophosphate (m(7)GMP) to 7-methylguanosine and inorganic phosphate. The specific activity for m(7)GMP guards cells against undesired retrieval of m(7)GMP and its incorporation into nucleic acids. In addition, NT5C3B has weak activity for CMP.

    • Synonyms

      NT5C3L, 7-methylguanosine phosphate-specific 5'-nucleotidase, Cytosolic 5'-nucleotidase 3B, Cytosolic 5'-nucleotidase III-like protein, cN-III-like protein, N(7)-methylguanylate 5'-phosphatase.

    • Physical Appearance

      Sterile Filtered colorless solution.

    • Stability

      Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MGSMAEEVST LMKATVLMRQ PGRVQEIVGA LRKGGGDRLQ VISDFDMTLS RFAYNGKRCP SSYNILDNSK IISEECRKEL TALLHHYYPI EIDPHRTVKE KLPHMVEWWT KAHNLLCQQK IQKFQIAQVV RESNAMLREG YKTFFNTLYH NNIPLFIFSA GIGDILEEII RQMKVFHPNI HIVSNYMDFN EDGFLQGFKG QLIHTYNKNS SACENSGYFQ QLEGKTNVIL LGDSIGDLTM ADGVPGVQNI LKIGFLNDKV EERRERYMDS YDIVLEKDET LDVVNGLLQH ILCQGVQLEM QGP.

    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.

    Nt5C3B Human
  • View Data Sheet

    Name :

    G6PD E.Coli

    Description:

    Glucose-6-Phosphate Dehydrogenase E.coli Recombinant

    G6PD, G6PD1, Glucose-6-phosphate 1-dehydrogenase.

    Product # :

    ENZ-399

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    Description

    G6PD E.Coli Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 491 amino acids and having a molecular mass of 55.7kDa. The G6PD is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The G6PD protein contains 50mM MES 6.0, 0.1mM PMSF, 2mM EDTA, 0.5mM DTT and 10% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    Biological Activity

    Specific activity > 70 units/mg obtained by measuring  the increase of beta-NADPH in absorbance at 340 nm resulting from the reduction beta- NADP. One unit oxidizes 1.0 umole D-glucose-6-phosphate to 6-phospho-D-gluconate per min in the presence of beta-NADP at pH 7.4 at 25C.

    More Info

    • Introduction

      G6PD is the rate-limiting enzyme of the pentose phosphate pathway, a metabolic pathway that supplies reducing energy to cells by maintaining the level of NADPH. G6PD converts glucose-6-phosphate into 6-phosphoglucono-?-lactone and at the same time produces NADPH. The NADPH maintains the level of glutathione in these cells that helps protect the red blood cells against oxidative damage. G6PD deficiency causes acute hemolytic anemia, neonatal jaundice or acute hemolysis. G6PD is a cytosolic enzyme encoded by an X-linked gene whose main function is to produce NADPH, a crucial electron donor in the defense against oxidizing agents and in reductive biosynthetic reactions. G6PD produces pentose sugars for nucleic acid synthesis and is a main producer of NADPH reducing power.

    • Synonyms

      G6PD, G6PD1, Glucose-6-phosphate 1-dehydrogenase.

    • Physical Appearance

      Sterile filtered colorless solution.

    • Stability

      Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.

    • Amino Acid Sequence

      MAVTQTAQAC DLVIFGAKGD LARRKLLPSL YQLEKAGQLN PDTRIIGVGR ADWDKAAYTK VVREALETFM KETIDEGLWD TLSARLDFCN LDVNDTAAFS RLGAMLDQKN RITINYFAMP PSTFGAICKG LGEAKLNAKP ARVVMEKPLG TSLATSQEIN DQVGEYFEEC QVYRIDHYLG KETVLNLLAL RFANSLFVNN WDNRTIDHVE ITVAEEVGIE GRWGYFDKAG QMRDMIQNHL LQILCMIAMS PPSDLSADSI RDEKVKVLKS LRRIDRSNVR EKTVRGQYTA GFAQGKKVPG YLEEEGANKS SNTETFVAIR VDIDNWRWAG VPFYLRTGKR LPTKCSEVVV YFKTPELNLF KESWQDLPQN KLTIRLQPDE GVDIQVLNKV PGLDHKHNLQ ITKLDLSYSE TFNQTHLADA YERLLLETMR GIQALFVRRD EVEEAWKWVDSITEAWAMDN DAPKPYQAGT WGPVASVAMI TRDGRSWNEF E.

    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.

    G6Pd
  • View Data Sheet

    Name :

    CES1D Mouse

    Description:

    Carboxylesterase 1D Mouse Recombinant

    Carboxylesterase 1D, Carboxylesterase 3 (EC:3.1.1.1, EC:3.1.1.67), Fatty acid ethyl ester synthase, FAEE synthase, Triacylglycerol hydrolase, TGH, CES1D.

    Product # :

    ENZ-1007

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    Description

    CES1D Mouse Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 555 amino acids (19-565 a.a) and having a molecular mass of 60.9kDa (Molecular size on SDS-PAGE will appear at approximately 50-70kDa).CES1D is fused to an 8 amino acid His-tag at C-terminus & purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    CES1D 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 > 80,000 pmol/min/ug and is defined as the amount of enzyme that hydrolyze 1pmole of p-nitrophenyl acetate to pnitrophenol per minute at pH 7.5 at 37C.

    More Info

    • Introduction

      Carboxylesterase 1D, also known as CES1D is part of a big family of carboxylesterases which are responsible for the hydrolysis of ester in addition to amide bonds. CES1D is the principle lipase of white adipose tissue fat cake extracts. Partially purified white adipose tissue Ces1d had lipase activity in addition to lesser but detectable neutral cholesteryl ester hydrolase activity. CES1D demonstrates low catalytic efficiency for hydrolysis of CPT-11, a prodrugs for camptothecin used in cancer therapeutics.

    • Synonyms

      Carboxylesterase 1D, Carboxylesterase 3 (EC:3.1.1.1, EC:3.1.1.67), Fatty acid ethyl ester synthase, FAEE synthase, Triacylglycerol hydrolase, TGH, CES1D.

    • Physical Appearance

      Sterile Filtered colorless solution.

    • Stability

      Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA). Avoid multiple freeze-thaw cycles.

    • Amino Acid Sequence

      YPSSPPVVNT VKGKVLGKYV NLEGFTQPVA VFLGVPFAKP PLGSLRFAPP QPAEPWSFVK NTTSYPPMCS QDAVGGQVLS ELFTNRKENI PLQFSEDCLY LNIYTPADLT KNSRLPVMVW IHGGGLVVGG ASTYDGLALS AHENVVVVTI QYRLGIWGFF STGDEHSRGN WGHLDQVAALRWVQDNIANF GGNPGSVTIF GESAGGFSVS VLVLSPLAKN LFHRAISESG VSLTAALITT DVKPIAGLVA TLSGCKTTTS AVMVHCLRQK TEDELLETSL KLNLFKLDLL GNPKESYPFL PTVIDGVVLP KAPEEILAEK SFSTVPYIVG INKQEFGWII PTLMGYPLAE GKLDQKTANSLLWKSYPTLK ISENMIPVVA EKYLGGTDDL TKKKDLFQDL MADVVFGVPS VIVSRSHRDA GASTYMYEFE YRPSFVSAMR PKAVIGDHGD EIFSVFGSPF LKDGASEEET NLSKMVMKFW ANFARNGNPN GGGLPHWPEY DQKEGYLKIG ASTQAAQRLK DKEVSFWAEL RAKESAQRPSHREHVELLEH HHHHH.

    ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

    Ces1D Mouse
  • View Data Sheet

    Name :

    Placental Lactogen Bovine

    Description:

    Placental Lactogen Bovine Recombinant

    Chorionic Somatomammotropin Hormone 1, CSH1, CSB, CS-1, hCS-B, BPL, BPLP-I.

    Product # :

    CYT-511

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    Description

    Placental Lactogen Bovine Recombinant, is a single polypeptide chain containing 199 amino acids and an additional Ala at the N-terminus having a molecular mass of 23 kDa. Placental Lactogen Recombinant is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The protein was lyophilized from a concentrated (1mg/ml) solution with 0.02-0.03% NaHCO3.

    Purity

    Greater than 99.0% as determined by:
    (a) Analysis by SEC-HPLC.
    (b) Analysis by SDS-PAGE.

    Biological Activity

    Placental Lactogen Bovine is biologically active as evidenced by inducing proliferation of Nb2 cells.

    More Info

    • Introduction

      Placental Lactogen is a polypeptide hormone that is produced by the Syncytiotrophoblasts of the Placenta, also known as chorionic somatomammotropin. It has both Growth Hormone and Prolactin activities on growth, lactation, and luteal steroid production. In women, placental lactogen secretion begins soon after implantation and increases to 1 g or more a day in late pregnancy. Placental lactogen is also an insulin antagonist.
      Placental Lactogen Bovine is also capable of activating human and other heterologous GH receptors but not ruminat GH receptors.

    • Synonyms

      Chorionic Somatomammotropin Hormone 1, CSH1, CSB, CS-1, hCS-B, BPL, BPLP-I.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized Placental Lactogen Bovine Recombinant although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Placental Lactogen should be stored at 4°C between 2-7 days and for future use below -18°C. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.

    • Solubility

      It is recommended to reconstitute the lyophilized Placental Lactogen in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      The sequence of the first six N-terminal amino acids was determined and was found to be Ala-Glu-Asp-Tyr-Ala-Pro.

    • Protein content

      UV spectroscopy at 280 nm using the absorbency value of 0.86 as the extinction coefficient for a 0.1% (1mg/ml) solution at pH 8. This value is calculated by the DNAman computer analysis program of protein sequences.

    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.

    Placental Lactogen Bovine
  • View Data Sheet

    Name :

    UBE2L3 Human

    Description:

    Ubiquitin-Conjugating Enzyme E2L 3 Human Recombinant

    Ubiquitin-conjugating enzyme E2 L3, EC 6.3.2.19, Ubiquitin-protein ligase L3,Ubiquitin carrier protein L3, UbcH7, E2-F1, L-UBC, UbcM4.

    Product # :

    ENZ-342

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    Description

    Ubiquitin-Conjugating Enzyme E2L 3 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 154 amino acids & having a molecular mass of 17.9 kDa.

    Source

    Escherichia Coli.

    Formulation

    The protein contains 50mM HEPES (pH-7.5) 150mM NaCl, 1mM DTT, and 10% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Human Ubquitin-conjugating enzyme 7 (UbcH7) is a ubiquitin-conjugating enzyme (E2) mediating c-fos degradation, transcription factor NF-B maturation, and human papilloma virus-mediated p53 and Myc protein degradation, in vitro. The ubiquitin-conjugating enzymes (E2s) are essential components of the post-translational protein ubiquitination pathway, mediating the transfer of activated ubiquitin to substrate proteins. The human UBE2L1-UBE2L4 gene could potentially encode different isoforms of the UbcH7. UBE2L3 gene, located at chromosome 22q11.2, is the only identical family member with introns and encodes a polypeptide sequence identical to that of UbcH7.

    • Synonyms

      Ubiquitin-conjugating enzyme E2 L3, EC 6.3.2.19, Ubiquitin-protein ligase L3,Ubiquitin carrier protein L3, UbcH7, E2-F1, L-UBC, UbcM4.

    • Physical Appearance

      Sterile filtered colorless solution.

    • Stability

      Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.

    • Amino Acid Sequence

      MAASRRLMKE LEEIRKCGMK NFRNIQVDEA NLLTWQGLIV PDNPPYDKGA FRIEINFPAE YPFKPPKITF KTKIYHPNID EKGQVCLPVI SAENWKPATK TDQVIQSLIA LVNDPQPEHP LRADLAEEYS KDRKKFCKNA EEFTKKYGEK RPVD.

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    Ube2L3 Human
  • View Data Sheet

    Name :

    SARS Human

    Description:

    Seryl-tRNA Synthetase Human Recombinant

    Serine--tRNA ligase cytoplasmic, Seryl-tRNA synthetase, SerRS, Seryl-tRNA(Ser/Sec) synthetase, SARS, SERS.

    Product # :

    ENZ-229

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    Description

    SARS Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 537 amino acids (1-514) and having a molecular mass of 61.2kDa.SARS is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The SARS solution (0.5mg/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

    • Introduction

      Seryl-tRNA synthetase, cytoplasmic (SARS) is a member of the class-II aminoacyl-tRNA synthetase family. Aminoacyl-tRNA synthetases’ role is to catalyze the aminoacylation of tRNAs by their corresponding amino acids, as a result linking amino acids with tRNA-contained nucleotide triplets. The SARS enzyme catalyzes the attachment of serine to tRNA (Ser). SARS enzyme is probably able to aminoacylate tRNA (Sec) with serine, to form the misacylated tRNA L-seryl-tRNA (Sec), which will be then converted into selenocysteinyl-tRNA (Sec).

    • Synonyms

      Serine--tRNA ligase cytoplasmic, Seryl-tRNA synthetase, SerRS, Seryl-tRNA(Ser/Sec) synthetase, SARS, SERS.

    • Physical Appearance

      Sterile Filtered colorless solution.

    • Stability

      Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MGSMVLDLDL FRVDKGGDPA LIRETQEKRF KDPGLVDQLV KADSEWRRCR FRADNLNKLK NLCSKTIGEK MKKKEPVGDD ESVPENVLSF DDLTADALAN LKVSQIKKVR LLIDEAILKC DAERIKLEAE RFENLREIGN LLHPSVPISN DEDVDNKVER IWGDCTVRKK YSHVDLVVMV DGFEGEKGAV VAGSRGYFLK GVLVFLEQAL IQYALRTLGS RGYIPIYTPF FMRKEVMQEV AQLSQFDEEL YKVIGKGSEK SDDNSYDEKY LIATSEQPIA ALHRDEWLRP EDLPIKYAGL STCFRQEVGS HGRDTRGIFR VHQFEKIEQF VYSSPHDNKS WEMFEEMITT AEEFYQSLGI PYHIVNIVSG SLNHAASKKL DLEAWFPGSG AFRELVSCSN CTDYQARRLR IRYGQTKKMM DKVEFVHMLN ATMCATTRTI CAILENYQTE KGITVPEKLK EFMPPGLQEL IPFVKPAPIE QEPSKKQKKQ HEGSKKKAAA RDVTLENRLQ NMEVTDA.

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    Sars Human
  • View Data Sheet

    Name :

    CA1 Human, Active

    Description:

    Carbonic Anhydrase-1 Human Recombinant, BioActive

    CA1, CA-I, CAB.

    Product # :

    ENZ-1137

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    Description

    CA1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 281 amino acids (1-261) and having a molecular mass of 31.0 kDa. CA1 Humanis fused to a 20 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    CA1 Human protein (1mg/ml) is formulated in 20mM Tris-HCl buffer (pH 8.0) containing 1mM DTT, 10% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Biological Activity

    Specific activity is > 300pmol/min/ug, and is defined as the amount of enzyme that hydrolyze 1.0pmole of 4-nitrophenyl acetate to 4-nitrophenol per minute at pH 8.0 at 37C.

    More Info

    • Introduction

      CA, also known as carbonic anhydrase is an enzyme. Its main function revolves around the CO2 + H2O HCO3- + H+ (conversion of carbon dioxide to bicarbonate & protons). CA has a zinc ion in its active site. The main function of CA is to keep acid-base balance in the blood stream and various tissues. This enzyme also assists Carbonic Anhydrase I to move CO2 to and from tissues.

    • Synonyms

      CA1, CA-I, CAB.

    • Physical Appearance

      Sterile Filtered clear solution.

    • Stability

      Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MASPDWGYDD KNGPEQWSKL YPIANGNNQS PVDIKTSETK HDTSLKPISV SYNPATAKEI INVGHSFHVN FEDNDNRSVL KGGPFSDSYR LFQFHFHWGS TNEHGSEHTV DGVKYSAELH VAHWNSAKYS SLAEAASKAD GLAVIGVLMK VGEANPKLQK VLDALQAIKT KGKRAPFTNF DPSTLLPSSL DFWTYPGSLT HPPLYESVTW IICKESISVS SEQLAQFRSL LSNVEGDNAV PMQHNNRPTQ PLKGRTVRAS F.

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    Ca1 Enzyme
  • View Data Sheet

    Name :

    NARS Human

    Description:

    Asparaginyl-TRNA Synthetase Human Recombinant

    NARS, Asparaginyl-TRNA Synthetase, AsnRS, EC 6.1.1.22, Asparaginyl-TRNA Synthetase, Cytoplasmic, Asparagine TRNA Ligase 1, Cytoplasmic, Asparagine--TRNA Ligase, Cytoplasmic, Asparagine TRNA Ligase 1, Cytoplasmic, NARS1.

    Product # :

    ENZ-915

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    Description

    NARS Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 571 amino acids (1-548 a.a) and having a molecular mass of 65.3kDa. NARS is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    NARS protein solution (0.25mg/ml) containing Phosphate Buffered Saline (pH7.4) and 10% glycerol.

    Purity

    Greater than 80.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Aminoacyl-tRNA synthetases are a class of enzymes which charge tRNAs with their cognate amino acids. Asparaginyl-tRNA synthetase (NARS) is localized to the cytoplasm and is a member of the class II family of tRNA synthetases. The N-terminal domain characterizes the signature sequence for the eukaryotic asparaginyl-tRNA synthetases.

    • Synonyms

      NARS, Asparaginyl-TRNA Synthetase, AsnRS, EC 6.1.1.22, Asparaginyl-TRNA Synthetase, Cytoplasmic, Asparagine TRNA Ligase 1, Cytoplasmic, Asparagine--TRNA Ligase, Cytoplasmic, Asparagine TRNA Ligase 1, Cytoplasmic, NARS1.

    • Physical Appearance

      Sterile Filtered colorless solution.

    • Stability

      Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.

    • Amino Acid Sequence

      GSSHHHHHH SSGLVPRGSH MGSMVLAELY VSDREGSDAT GDGTKEKPFK TGLKALMTVG KEPFPTIYVD SQKENERWNV ISKSQLKNIK KMWHREQMKS ESREKKEAED SLRREKNLEE AKKITIKNDP SLPEPKCVKI GALEGYRGQR VKVFGWVHRL RRQGKNLMFL VLRDGTGYLQ CVLADELCQC YNGVLLSTES SVAVYGMLNL TPKGKQAPGG HELSCDFWEL IGLAPAGGAD NLINEESDVD VQLNNRHMMI RGENMSKILK ARSMVTRCFR DHFFDRGYYE VTPPTLVQTQ VEGGATLFKL DYFGEEAFLT QSSQLYLETC LPALGDVFCI AQSYRAEQSR TRRHLAEYTH VEAECPFLTF DDLLNRLEDL VCDVVDRILK SPAGSIVHEL NPNFQPPKRP FKRMNYSDAI VWLKEHDVKK EDGTFYEFGE DIPEAPERLM TDTINEPILL CRFPVEIKSF YMQRCPEDSR LTESVDVLMP NVGEIVGGSM RIFDSEEILA GYKREGIDPT PYYWYTDQRK YGTCPHGGYG LGLERFLTWI LNRYHIRDVC LYPRFVQRCT P.

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    Human Nars
  • View Data Sheet

    Name :

    GLO1 Mouse

    Description:

    Glyoxalase-I Mouse Recombinant

    Lactoylglutathione lyase, Aldoketomutase, Glyoxalase I, Glx I, Ketone-aldehyde mutase, Methylglyoxalase, S-D-lactoylglutathione methylglyoxal lyase.

    Product # :

    ENZ-953

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    Description

    GLO1 Mouse Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 192 amino acids (1-184a.a.) and having a molecular mass of 21.8kDa (Molecular size on SDS-PAGE will appear at approximately 28-40kDa). GLO1 is expressed with an 8 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    GLO1 protein solution (0.5mg/ml) containing Phosphate Buffered Saline (pH 7.4) and 10% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Biological Activity

    Specific activity is > 210 units/mg, and is defined as the amount of enzyme that will form 1.0 µmol of S-lactoylglutathione from methylglyoxal and reduced glutathione per minute at pH 6.5 at 25C.

    More Info

    • Introduction

      GLO1 is involved in the catalysis and formation of S-lactoyl-glutathione from methylglyoxal condensation and reduced glutatione. GLO1 is linked to HLA and is localized to 6p21.3-p21.1, between HLA and the centromere. GLO1 enzyme is ubundantly expressed and present in numerous tumor cell lines, in which its concentration is often upregulated ubiquitisly. GLO1 is a major susceptible gene for autism in an ethnic Chinese population from Taiwan. GLO1 might be involved in the pathophysiology of mood disorders. GLO1 plays a role in the pathophysiology of mood disorders. Overexpression of GLO1 is associated with kidney tumor.

    • Synonyms

      Lactoylglutathione lyase, Aldoketomutase, Glyoxalase I, Glx I, Ketone-aldehyde mutase, Methylglyoxalase, S-D-lactoylglutathione methylglyoxal lyase.

    • Physical Appearance

      Sterile Filtered colorless solution.

    • Stability

      Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.

    • Amino Acid Sequence

      MAEPQPASSG LTDETAFSCC SDPDPSTKDF LLQQTMLRIK DPKKSLDFYT RVLGLTLLQK LDFPAMKFSL YFLAYEDKND IPKDKSEKTA WTFSRKATLE LTHNWGTEDD ETQSYHNGNS DPRGFGHIGI AVPDVYSACK RFEELGVKFV KKPDDGKMKG LAFIQDPDGY WIEILNPNKI ATIILEHHHH HH.

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    Glo1 Mouse
  • View Data Sheet

    Name :

    REXO2 Human

    Description:

    RNA Exonuclease 2 Human Recombinant

    REX2, RNA exonuclease 2 homolog (S. cerevisiae), CGI-114, RFN, SFN, Oligoribonuclease, mitochondrial, RNA exonuclease 2 homolog, Small fragment nuclease,REXO2, SMFN.

    Product # :

    ENZ-715

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    Description

    REXO2 Human Recombinant produced in E. coli is a single polypeptide chain containing 235 amino acids (26-237) and having a molecular mass of 26.8kDa. REXO2 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The REXO2 solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl and 20% glycerol.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    More Info

    • Introduction

      EXO2 is a 3'-to-5' exonuclease specific for small (primarily 5 nucleotides or less in length) single-stranded RNA and DNA oligomers. RNA Exonuclease 2 (REXO2) takes part in DNA repair, replication, and recombination, and in RNA processing and degradation. EXO2 is involved in resistance of human cells to UV-C-induced cell death via its part in the DNA repair process.

    • Synonyms

      REX2, RNA exonuclease 2 homolog (S. cerevisiae), CGI-114, RFN, SFN, Oligoribonuclease, mitochondrial, RNA exonuclease 2 homolog, Small fragment nuclease,REXO2, SMFN.

    • Physical Appearance

      Sterile Filtered colorless solution.

    • Stability

      Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MGSVREGGAA MAAGESMAQR MVWVDLEMTG LDIEKDQIIE MACLITDSDL NILAEGPNLI IKQPDELLDS MSDWCKEHHG KSGLTKAVKE STITLQQAEY EFLSFVRQQT PPGLCPLAGN SVHEDKKFLD KYMPQFMKHL HYRIIDVSTV KELCRRWYPE EYEFAPKKAA SHRALDDISE SIKELQFYRN NIFKKKIDEK KRKIIENGEN EKTVS.

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    Rexo2 Human
  • View Data Sheet

    Name :

    MPI Human

    Description:

    Mannose Phosphate Isomerase Human Recombinant

    Mannose-6-phosphate isomerase, PMI1, CDG1B, Phosphohexomutase, Phosphomannose isomerase, EC 5.3.1.8, FLJ39201.

    Product # :

    ENZ-169

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    Description

    MPI Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 382 amino acids (1-362) and having a molecular mass of 41.9 kDa.The MPI is fused to a 20 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    The MPI solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.4M Urea and 5% glycerol.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    More Info

    • Introduction

      MPI is a member of the mannose-6-phosphate isomerase type 1 family. Although MPI is expressed in all tissues, it can be found more abundantly in heart, brain and skeletal muscle. Localized to the cytoplasm, MPI exploits zinc as a cofactor and catalyzes the interconversion of fructose-6-phosphate and mannose-6-phosphate. Mutations in the MPI gene are the cause of carbohydrate-deficient glycoprotein syndrome, type Ib.

    • Synonyms

      Mannose-6-phosphate isomerase, PMI1, CDG1B, Phosphohexomutase, Phosphomannose isomerase, EC 5.3.1.8, FLJ39201.

    • Physical Appearance

      Sterile Filtered colorless solution.

    • Stability

      Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MAAPRVFPLS CAVQQYAWGK MGSNSEVARL LASSDPLAQI AEDKPYAELW MGTHPRGDAK ILDNRISQKT LSQWIAENQD SLGSKVKDTF NGNLPFLFKV LSVETPLSIQ AHPNKELAEK LHLQAPQHYP DANHKPEMAI ALTPFQGLCG FRPVEEIVTF LKTAAGNNME DIFGELLLQL HQQYPGDIGC FAIYFLNLLT LKPGEAMFLE ANVPHAYLKG DCVECMACSD NTVRAGLTPK FIDVPTLCEM LSYTPSSSKD RLFLPTRSQE DPYLSIYDPP VPDFTIMKTE VPGSVTEYKV LALDSASILL MVQGTVIAST PTTQTPIPLQ RGGVLFIGAN ESVSLKLTEP KDLLIFRACC LL

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    Mpi Human
  • View Data Sheet

    Name :

    BHMT Human

    Description:

    Betaine Homocysteine S-Methyltransferase Human Recombinant

    BHMT, Betaine Homocysteine S-Methyltransferase 1, BHMT1.

    Product # :

    ENZ-292

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    Description

    Betaine Homocysteine S-Methyltransferase Human Recombinant fused to His Tag at N-terminal produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 443 amino acids (21-236) and having a molecular mass of 49.2 kDa. The BHMT is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The BHMT solution contains 20mM Tris-HCl pH-7.5 and 20% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Betaine-homocysteine methyltransferase (BHMT) is a cytosolic enzyme that catalyzes the conversion of betaine and homocysteine to dimethylglycine and methionine, respectively. BHMT displays differential expression in a model of liver cirrhosis.

    • Synonyms

      BHMT, Betaine Homocysteine S-Methyltransferase 1, BHMT1.

    • Physical Appearance

      Sterile Filtered clear colorless solution 1 mg/ml.

    • 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.

    • Amino Acid Sequence

      MRGSHHHHHH GMASMTGGQQ MGRDLYDDDD KDRWGSHMPP VGGKKAKKGI LERLNAGEIV IGDGGFVFAL EKRGYVKAGP WTPEAAVEHP EAVRQLHREF LRAGSNVMQT FTFYASEDKL ENRGNYVLEK ISGQEVNEAA CDIARQVADE GDALVAGGVS QTPSYLSCKS ETEVKKVFLQ QLEVFMKKNV DFLIAEYFEH VEEAVWAVET LIASGKPVAA TMCIGPEGDL HGVPPGECAV RLVKAGASII GVNCHFDPTI SLKTVKLMKE GLEAARLKAH LMSQPLAYHT PDCNKQGFIDLPEFPFGLEP RVATRWDIQK YAREAYNLGV RYIGGCCGFE PYHIRAIAEE LAPERGFLPPASEKHGSWGS GLDMHTKPWV RARARKEYWE NLRIASGRPY NPSMSKPDGW GVTKGTAELM QQKEATTEQQ LKELFEKQKF KSQ.

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    Bhmt Human
  • View Data Sheet

    Name :

    PEPD Human

    Description:

    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-856

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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

    • 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.

    • Synonyms

      Xaa-Pro dipeptidase, X-Pro dipeptidase, Imidodipeptidase, Peptidase D, Proline dipeptidase, Prolidase, PRD, PEPD, Xaa-Pro dipeptidase isoform 1, PROLIDASE.

    • Physical Appearance

      Sterile Filtered colorless solution.

    • Stability

      Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH 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.

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    Pepd Human
  • View Data Sheet

    Name :

    GCLM Human

    Description:

    Glutamate-Cysteine Ligase, Modifier Subunit Human Recombinant

    Glutamate--cysteine ligase regulatory subunit, GCS light chain, Gamma-ECS regulatory subunit, Gamma-glutamylcysteine synthetase regulatory subunit, Glutamate--cysteine ligase modifier subunit, GCLM, GLCLR.

    Product # :

    ENZ-636

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    • description
    • source
    • formulation
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    Description

    GCLM Human Recombinant produced in E. coli is a single polypeptide chain containing 298 amino acids (1-274) and having a molecular mass of 33.3kDa.GCLM is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The GCLM solution (1mg/ml) contains 20mM Tris-HCl buffer (pH8.0), 10% glycerol and 0.15M NaCl.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Glutamate-cysteine ligase (GCLM) is the first rate limiting enzyme of glutathione synthesis. The GCLM enzyme is comprised of 2 subunits, a heavy catalytic subunit and a light regulatory subunit. GCLM deficiency is associated with some forms of hemolytic anemia.

    • Synonyms

      Glutamate--cysteine ligase regulatory subunit, GCS light chain, Gamma-ECS regulatory subunit, Gamma-glutamylcysteine synthetase regulatory subunit, Glutamate--cysteine ligase modifier subunit, GCLM, GLCLR.

    • Physical Appearance

      Sterile Filtered colorless solution.

    • Stability

      Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MGSHMGTDSR AAKALLARAR TLHLQTGNLL NWGRLRKKCP STHSEELHDC IQKTLNEWSS QINPDLVREF PDVLECTVSH AVEKINPDER EEMKVSAKLF IVESNSSSST RSAVDMACSV LGVAQLDSVI IASPPIEDGV NLSLEHLQPY WEELENLVQS KKIVAIGTSD LDKTQLEQLY QWAQVKPNSN QVNLASCCVM PPDLTAFAKQ FDIQLLTHND PKELLSEASF QEALQESIPD IQAHEWVPLW LLRYSVIVKS RGIIKSKGYI LQAKRRGS.

    ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

    Gclm Human
  • View Data Sheet

    Name :

    QDPR Human

    Description:

    Quinoid Dihydropteridine Reductase Human Recombinant

    Dihydropteridine reductase, HDHPR, Quinoid dihydropteridine reductase, QDPR, DHPR, PKU2, SDR33C1.

    Product # :

    ENZ-163

    Price :

    Quantity :

    Shipping Method :

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    More Info

    • description
    • source
    • formulation
    • purity
    • More Info

    Description

    QDPR Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 267 amino acids (1-244 a.a.) and having a molecular mass of 28.2kDa.QDPR is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    QDPR protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 10% glycerol and 2mM DTT.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      QDPR belongs to the short-chain dehydrogenases/reductase (SDR) family of enzymes. Operating as a homodimer, QDPR has an imperative role in the recycling of tetrahydrobiopterin (BH4), a vital cofactor for the hydroxylation of the aromatic amino acids (tryptophan, tyrosine and phenylalanine). More precisely, QDPR catalyzes the regeneration of BH4 from quinonoid dihydrobiopterin (qBH2), the product generated from the hydroxylation reactions. Mutations in the QDPR gene may lead to phenylketonuria II.

    • Synonyms

      Dihydropteridine reductase, HDHPR, Quinoid dihydropteridine reductase, QDPR, DHPR, PKU2, SDR33C1.

    • Physical Appearance

      Sterile Filtered colorless solution.

    • Stability

      Store at 4°C if entire vial will be used within 2-4 weeks.Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MGSMAAAAAA GEARRVLVYG GRGALGSRCV QAFRARNWWV ASVDVVENEE ASASIIVKMT DSFTEQADQV TAEVGKLLGE EKVDAILCVA GGWAGGNAKS KSLFKNCDLM WKQSIWTSTI SSHLATKHLK EGGLLTLAGA KAALDGTPGM IGYGMAKGAV HQLCQSLAGK NSGMPPGAAA IAVLPVTLDT PMNRKSMPEA DFSSWTPLEF LVETFHDWIT GKNRPSSGSL IQVVTTEGRT ELTPAYF.

    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.

    Qdpr Human
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