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Search results

1000 results found for “cytochrome”

Name

Description

Product #

Price

Quantity

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  • View Data Sheet

    Name :

    DYNLRB1 Human

    Description:

    Dynein Light Chain Roadblock-Type 1 Human Recombinant

    BITH, BLP, DNCL2A, DNLC2A, ROBLD1, HSPC162.

    Product # :

    PRO-489

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    Description

    DYNLRB1 Recombinant Human produced in E.Coli is a single, non-glycosylated polypeptide chain containing 104 amino acids (1-96 a.a.) and having a molecular mass of 11.9 kDa. The DYNLRB1 is fused to an 8 amino acid His-Tag at C-terminus and purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    DYNLRB1 protein solution (1mg/ml) containing 20mM Tris-HCl pH-8 & 10% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Dynein light chain roadblock-type (DYNLRB1) belongs to the roadblock dynein light chain family and encodes a cytoplasmic protein which is capable of binding intermediate chain proteins. Upregulation of the DYNLRB1 gene is linked with hepatocellular carcinomas, suggesting that DYNLRB1 may be involved in tumor progression.

    • Synonyms

      BITH, BLP, DNCL2A, DNLC2A, ROBLD1, HSPC162.

    • 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

      MAEVEETLKR LQSQKGVQGI IVVNTEGIPI KSTMDNPTTT QYASLMHSFI LKARSTVRDI DPQNDLTFLR IRSKKNEIMV APDKDYFLIV IQNPTELEHH 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.

    Dynlrb1 Human
  • View Data Sheet

    Name :

    PSMA6 Human

    Description:

    Proteasome Subunit Alpha Type 6 Human Recombinant

    Proteasome (prosome, macropain) subunit alpha type 6, PROS27, p27K, IOTA, Macropain iota chain, Multicatalytic endopeptidase complex iota chain, Proteasome iota chain, 27 kDa prosomal protein.

    Product # :

    ENZ-198

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    Description

    PSMA6 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 270 amino acids (1-246 a.a.) and having a molecular mass of 29.9kDa.PSMA6 is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    PSMA6 protein solution (0.25mg/ml) containing 20mM Tris-HCl buffer (pH8.0), 100mM NaCl, 1mM DTT and 40% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      PSMA6 belongs to the peptidase T1A family, which is a 20S core alpha subunit. The proteasome is a multicatalytic proteinase complex with an extremely organized ring-shaped 20S core structure. The core structure consists of 4 rings of 28 non-identical subunits; 2 rings consist of 7 alpha subunits and 2 rings consist of 7 beta subunits. PSMA6 is spread all over eukaryotic cells in large quantities and cleave peptides in an ATP/ubiquitin-dependent procedure in a non-lysosomal pathway.

    • Synonyms

      Proteasome (prosome, macropain) subunit alpha type 6, PROS27, p27K, IOTA, Macropain iota chain, Multicatalytic endopeptidase complex iota chain, Proteasome iota chain, 27 kDa prosomal protein.

    • 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 MGSHMSRGSS AGFDRHITIF SPEGRLYQVE YAFKAINQGG LTSVAVRGKD CAVIVTQKKV PDKLLDSSTVTHLFKITENI GCVMTGMTAD SRSQVQRARY EAANWKYKYG YEIPVDMLCK RIADISQVYT QNAEMRPLGC CMILIGIDEE QGPQVYKCDP AGYYCGFKAT AAGVKQTEST SFLEKKVKKK FDWTFEQTVE TAITCLSTVL SIDFKPSEIE VGVVTVENPK FRILTEAEID AHLVALAERD

    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.

    Psma6 Human
  • View Data Sheet

    Name :

    HCV Core 22kDa, Rhodamine

    Description:

    Hepatitis C Virus Core 22kDa, Rhodamine Recombinant

    Product # :

    HCV-262

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    Description

    The E.coli derived recombinant protein contains the HCV core nucleocapsid immunodominant regions, amino acids 2-192. The Rhodamine labeled protein is fused with b-galactosidase (114 kDa) at N-terminus.

    Formulation

    20mM Tris-Hcl pH 8, 8M urea and 10mM B-ME.

    Purity

    HCV-Core protein is >95% pure as determined by 10% PAGE (coomassie staining).

    More Info

    • Introduction

      HCV is a small 50nm, enveloped, single-stranded, positive sense RNA virus 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-Core although stable at 4°C for 1 week, should be stored below -18°C. Please prevent freeze thaw cycles.

    • Applications

      HCV Core antigen is suitable for ELISA and Western blots, excellent antigen for detection of HCV with minimal specificity problems.

    • Specificity

      Immunoreactive with sera of HCV-infected individuals.

    • Purification Method

      HCV-Core 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.

    Hcv Core 22Kda Rhodamine
  • View Data Sheet

    Name :

    SUOX Human

    Description:

    Sulfite Oxidase Human Recombinant

    Sulfite Oxidase, EC 1.8.3.1, Sulfite oxidase, mitochondrial.

    Product # :

    ENZ-887

    Price :

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    Description

    SUOX Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 489 amino acids (80-545 a.a) and having a molecular mass of 53.9kDa. SUOX is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    SUOX protein solution (1mg/ml) containing Phosphate buffered saline (pH7.4), 30% glycerol and 1mM DTT.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    More Info

    • Introduction

      Sulfite oxidase, also known as SUOX is a homodimeric protein localized to the intermembrane space of mitochondria. Each subunit includes a heme domain as well as a molybdopterin-binding domain. The SUOX enzyme catalyzes the oxidation of sulfite to sulfate, the last reaction in the oxidative degradation of the sulfur amino acids cysteine and methionine. In addition, the deficiency of SUOX results in neurological abnormalities which are often fatal at an early age.

    • Synonyms

      Sulfite Oxidase, EC 1.8.3.1, Sulfite oxidase, mitochondrial.

    • 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 MGSESTHIYT KEEVSSHTSP ETGIWVTLGS EVFDVTEFVD LHPGGPSKLM LAAGGPLEPF WALYAVHNQS HVRELLAQYK IGELNPEDKV APTVETSDPY ADDPVRHPAL KVNSQRPFNA EPPPELLTEN YITPNPIFFT RNHLPVPNLD PDTYRLHVVG APGGQSLSLS LDDLHNFPRY EITVTLQCAG NRRSEMTQVK EVKGLEWRTG AISTARWAGA RLCDVLAQAG HQLCETEAHV CFEGLDSDPT GTAYGASIPL ARAMDPEAEV LLAYEMNGQP LPRDHGFPVR VVVPGVVGAR HVKWLGRVSV QPEESYSHWQ RRDYKGFSPS VDWETVDFDS APSIQELPVQ SAITEPRDGE TVESGEVTIK GYAWSGGGRA VIRVDVSLDG GLTWQVAKLD GEEQRPRKAW AWRLWQLKAP VPAGQKELNI VCKAVDDGYN VQPDTVAPIW NLRGVLSNAW HRVHVYVSP.

    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.

    Suox Human
  • View Data Sheet

    Name :

    CBR3 Human

    Description:

    Carbonyl Reductase-3 Human Recombinant

    Carbonyl reductase [NADPH] 3, NADPH-dependent carbonyl reductase 3, CBR3, carbonyl reductase 3, hCBR3, SDR21C2.

    Product # :

    ENZ-428

    Price :

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    Description

    Recombinant Human CBR3 fused with a 20 amino acid His tag at N-terminus produced in E.Coli is a single, non-glycosylated polypeptide chain containing 297 amino acids (1-277 a.a) and having a molecular mass of 33kDa. CBR3 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The CBR3 protein solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0) and 10% glycerol.

    Purity

    Greater than 95.0% as determined by analysis by SDS-PAGE.

    More Info

    • Introduction

      CBR3 catalyzes the reduction of a large number of biologically and pharmacologically active carbonyl compounds to their corresponding alcohols. CBR3 is one of several monomeric NADPH-dependent oxidoreductases. Furthermore, CBR3 contains 3 exons spanning 11.2 kilobases and is strongly linked to another carbonyl reductase gene, the CBR1. It was suggested that CBR3 mediates 9-cis-retinoic acid-induced cytostatis and is a potential prognostic marker for oral malignancy.
      CBR3 is identified in the ovary, pancreas, intestine, colon, kidney, brain, thymus, lung, heart, liver, spleen, leukocyte, prostate and the testis.

    • Synonyms

      Carbonyl reductase [NADPH] 3, NADPH-dependent carbonyl reductase 3, CBR3, carbonyl reductase 3, hCBR3, SDR21C2.

    • Physical Appearance

      Sterile filtered colorless solution.

    • Stability

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

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MSSCSRVALV TGANRGIGLA IARELCRQFS GDVVLTARDV ARGQAAVQQL QAEGLSPRFH QLDIDDLQSI RALRDFLRKE YGGLNVLVNN AAVAFKSDDP MPFDIKAEMT LKTNFFATRN MCNELLPIMK PHGRVVNISS LQCLRAFENC SEDLQERFHS ETLTEGDLVD LMKKFVEDTK NEVHEREGWP NSPYGVSKLG VTVLSRILAR RLDEKRKADR ILVNACCPGP VKTDMDGKDS IRTVEEGAET PVYLALLPPD ATEPQGQLVH DKVVQNW.

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

    Cbr3 Human
  • View Data Sheet

    Name :

    Cyclophilin E Human

    Description:

    Cyclophilin-E Human Recombinant

    Peptidyl-prolyl cis-trans isomerase E, PPIase E, Rotamase E, Cyclophilin-33, PPIE, peptidylprolyl isomerase E, CYP33, Cyclophilin E, CYP-33, MGC3736, MGC111222.

    Product # :

    ENZ-383

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    Description

    Cyclophilin-E Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 337 amino acids (1-301 a.a.) and having a molecular mass of 37.5 kDa. Cyclophilin-E is fused to a 36 amino acids long His Tag at N-terminus and is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Cyclophilin-E solution containing 20mM Tris pH-8.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Biological Activity

    Specific activity is > 210 nmoles/min/ug, and is defined as the amount of enzyme that cleave 1umole of suc-AAFP-pNA per minute at 1C in Tris-HCl pH8.0 using chymotrypsin.

    More Info

    • Introduction

      Cyclophilin-E is a member of the peptidyl-prolyl cis-trans isomerase (PPIase) family. PPIases catalyze the cis-trans isomerization of proline imidic peptide bonds in oligopeptides and speeds up the protein folding. Cyclophilin-E contains a highly conserved cyclophilin domain in addition to a RNA-binding domain. Cyclophilin-E exhibits PPIase activity, protein folding activities and possess RNA-binding activity. Cyclophilin-E contains 2 RNA binding domains at the N-terminal region and a PPIase domain at the C-terminal region.

    • Synonyms

      Peptidyl-prolyl cis-trans isomerase E, PPIase E, Rotamase E, Cyclophilin-33, PPIE, peptidylprolyl isomerase E, CYP33, Cyclophilin E, CYP-33, MGC3736, MGC111222.

    • 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

      MRGSHHHHHH GMASMTGGQQ MGRDLYDDDD KDRWGSMATT KRVLYVGGLA EEVDDKVLHA AFIPFGDITD IQIPLDYETE KHRGFAFVEF ELAEDAAAAI DNMNESELFG RTIRVNLAKP MRIKEGSSRP VWSDDDWLKK FSGKTLEENK EEEGSEPPKA ETQEGEPIAK KARSNPQVYM DIKIGNKPAG RIQMLLRSDV VPMTAENFRC LCTHEKGFGF KGSSFHRIIP QFMCQGGDFT NHNGTGGKSI YGKKFDDENF ILKHTGPGLL SMANSGPNTN GSQFFLTCDK TDWLDGKHVV FGEVTEGLDV LRQIEAQGSK DGKPKQKVII ADCGEYV.

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    Cyclophilin E Human
  • View Data Sheet

    Name :

    NANS Human

    Description:

    N-acetylneuraminic acid synthase Human Recombinant

    Sialic acid synthase, N-acetylneuraminate synthase, N-acetylneuraminate-9-phosphate synthase, N-acetylneuraminic acid phosphate synthase, N-acetylneuraminic acid synthase, NANS, SAS.

    Product # :

    ENZ-024

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    Description

    NANS Human Recombinant fused with a 20 amino acid His tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 379 amino acids (1-359 a.a.) and having a molecular mass of 42.4kDa. The NANS is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The NANS solution (0.5 mg/ml) contains 20mM Tris-HCl buffer (pH8.0), 0.1M NaCl, 1mM DTT and 10% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      NANS is a 359 amino acid protein that contains one AFP (antifreeze proteins)-like domain and functions in the biosynthesis of sialic acids. The ubiquitously expressed NANS enzymatically catalyzes the H2O-dependent formation of N-acetylneuraminic acid (Neu5Ac) and 2-keto-3-deoxy-D-glycero-D-galacto-nononic acid (KDN), both of which are sialic acids. NANS uses N-acetylmannosamine 6-phosphate as a substrate for Neu5Ac synthesis and mannose 6-phosphate as a substrate for KDN synthesis.

    • Synonyms

      Sialic acid synthase, N-acetylneuraminate synthase, N-acetylneuraminate-9-phosphate synthase, N-acetylneuraminic acid phosphate synthase, N-acetylneuraminic acid synthase, NANS, SAS.

    • 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 MPLELELCPG RWVGGQHPCF IIAEIGQNHQ GDLDVAKRMI RMAKECGADC AKFQKSELEF KFNRKALERP YTSKHSWGKT YGEHKRHLEF SHDQYRELQR YAEEVGIFFT ASGMDEMAVE FLHELNVPFF KVGSGDTNNF PYLEKTAKKG RPMVISSGMQ SMDTMKQVYQ IVKPLNPNFC FLQCTSAYPL QPEDVNLRVI SEYQKLFPDI PIGYSGHETG IAISVAAVAL GAKVLERHIT LDKTWKGSDH SASLEPGELA ELVRSVRLVE RALGSPTKQL LPCEMACNEK LGKSVVAKVK IPEGTILTMD MLTVKVGEPK GYPPEDIFNL VGKKVLVTVE EDDTIMEELV DNHGKKIKS.

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    Nans Human
  • View Data Sheet

    Name :

    ECH1 Human

    Description:

    Enoyl CoA Hydratase 1, Peroxisomal Human Recombinant

    peroxisomal, enoyl Coenzyme A hydratase 1.

    Product # :

    ENZ-562

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    Description

    ECH1 produced in E.Coli is a single, non-glycosylated polypeptide chain containing 316 amino acids (34-328a.a.) and having a molecular mass of 34.4kDa.ECH1 is fused to a 21 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The ECH1 protein solution (1mg/1ml) is formulated in 20mM Tris-HCl buffer (pH8.0) 1mM DTT, 50mM NaCl, and 10% glycerol.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    More Info

    • Introduction

      ECH1 is a member of the hydratase/isomerase superfamily. ECH1 demonstrates high sequence similarity to enoyl-coenzyme A (CoA) hydratases of more than a few species, mostly within a conserved domain characteristic of these proteins. ECH1 contains a C-terminal peroxisomal targeting sequence, localizes to both the peroxisome and the mitochondria. peroxisomal takes part in the auxiliary step of the fatty acid beta-oxidation pathway specifically functioning to catalyze the isomerization of 3-trans, 5-cis-dienoyl-CoA to 2-trans, 4-transdienoyl-CoA.

    • Synonyms

      peroxisomal, enoyl Coenzyme A hydratase 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 MTGSSAQEAA SGVALGEAPD HSYESLRVTS AQKHVLHVQL NRPNKRNAMN KVFWREMVEC FNKISRDADC RAVVISGAGK MFTAGIDLMD MASDILQPKG DDVARISWYL RDIITRYQET FNVIERCPKP VIAAVHGGCI GGGVDLVTAC DIRYCAQDAF FQVKEVDVGL AADVGTLQRL PKVIGNQSLV NELAFTARKM MADEALGSGL VSRVFPDKEV MLDAALALAA EISSKSPVAV QSTKVNLLYS RDHSVAESLN YVASWNMSML QTQDLVKSVQ ATTENKELKT VTFSKL.

    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.

    Ech1 Human
  • View Data Sheet

    Name :

    NPM1 Human

    Description:

    Nucleophosmin Human Recombinant

    Nucleophosmin, NPM, Nucleolar phosphoprotein B23, Nucleolar protein NO38, Numatrin, NPM1, NPM, B23.

    Product # :

    PRO-1120

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    Description

    NPM1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 314 amino acids (1-294 a.a) and having a molecular mass of 34.7kDa.NPM1 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    NPM1 protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH8.0), 10% glycerol, 0.15M NaCl and 1mM DTT.

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Nucleophosmin (NPM1) is a phosphoprotein which shuffles between the nucleus and the cytoplasm. NPM1 is assumed to be involved in a number of processes including regulation of the ARF/p53 pathway. Several genes fusion partners have been described, particularly the anaplastic lymphoma kinase gene on chromosome 2. NPM1 gene mutations are linked with acute myeloid leukemia.

    • Synonyms

      Nucleophosmin, NPM, Nucleolar phosphoprotein B23, Nucleolar protein NO38, Numatrin, NPM1, NPM, B23.

    • 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 MEDSMDMDMS PLRPQNYLFG CELKADKDYH FKVDNDENEH QLSLRTVSLG AGAKDELHIV EAEAMNYEGS PIKVTLATLK MSVQPTVSLG GFEITPPVVL RLKCGSGPVH ISGQHLVAVE EDAESEDEEE EDVKLLSISG KRSAPGGGSK VPQKKVKLAA
      DEDDDDDDEE DDDEDDDDDD FDDEEAEEKA PVKKSIRDTP AKNAQKSNQN GKDSKPSSTP RSKGQESFKK QEKTPKTPKG PSSVEDIKAK MQASIEKGGS LPKVEAKFIN YVKNCFRMTD QEAIQDLWQW RKSL.

    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.

    Npm1 Human
  • View Data Sheet

    Name :

    SYT13 Human

    Description:

    Synaptotagmin XIII Human Recombinant

    Synaptotagmin XIII, KIAA1427, synaptotagmin-13, sytXIII.

    Product # :

    PRO-1550

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    Description

    SYT13 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 420 amino acids (30-426) and having a molecular mass of 46.5kDa.SYT13 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The SYT13 solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 1mM DTT, 1mM PMSF, 1mM EDTA and 30% glycerol.

    Purity

    Greater than 85% as determined by SDS-PAGE.

    More Info

    • Introduction

      SYT13 belongs to the great synaptotagmin protein family which contain 2 domains: cytoplasmic C terminus with two tandem C2 domains (C2A and C2B) and extracellular N-terminal transmembrane domain. Synaptotogmin family members have dissimilar biochemical properties and developmental profiles, and patterns of tissue distribution. Additionally, Synaptotogmins formulate homo- and heteromeric complexes with each other. Synaptotagmins operate as membrane traffickers in multicellular organisms.

    • Synonyms

      Synaptotagmin XIII, KIAA1427, synaptotagmin-13, sytXIII.

    • 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 MGSCRHMHPK KGLLPRDQDP DLEKAKPSLL GSAQQFNVKK STEPVQPRAL LKFPDIYGPR PAVTAPEVIN YADYSLRSTE EPTAPASPQP PNDSRLKRQV TEELFILPQN GVVEDVCVME TWNPEKAASW NQAPKLHYCL DYDCQKAELF VTRLEAVTSN HDGGCDCYVQ GSVANRTGSV EAQTALKKRQ LHTTWEEGLV LPLAEEELPT ATLTLTLRTC DRFSRHSVAG ELRLGLDGTS VPLGAAQWGE LKTSAKEPSA GAGEVLLSIS YLPAANRLLV VLIKAKNLHS NQSKELLGKD VSVKVTLKHQ ARKLKKKQTK RAKHKINPVW NEMIMFELPD DLLQASSVEL EVLGQDDSGQ SCALGHCSLG LHTSGSERSH WEEMLKNPRR QIAMWHQLHL

    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.

    Syt13 Human
  • View Data Sheet

    Name :

    C12ORF5 Human

    Description:

    Chromosome 12 Open Reading Frame 5 Human

    Fructose-2,6-bisphosphatase TIGAR, TP53-induced glycolysis and apoptosis regulator, TIGAR, C12orf5.

    Product # :

    PRO-1791

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    Description

    TIGAR Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 270 amino acids and having a molecular mass of 30.1kDa. The TIGAR is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    TIGAR was Lyophilized from a 0.2 µm filtered concentrated solution in 20mM Tris-HCl, pH8.5, 150mM NaCl.

    Purity

    Greater than 95.0% as determined by:
    (a) Analysis by RP-HPLC.
    (b) Analysis by SDS-PAGE.

    More Info

    • Introduction

      TIGAR is a p53-inducible enzyme which catalyzes the hydrolysis of fructose-2-6 bisphosphate (F-2-6-BP) to fructose-6-phosphate and inorganic phosphate. F-2-6-BP is an influential activator of 6-phosphofructose-1 kinase (the rate limiting enzyme of glycolysis). By lowering the intracellular level of F-2-6-BP, TIGAR expression leads to increased glucose processing through the pentose phosphate pathway, the main cellular source for NADPH.

    • Synonyms

      Fructose-2,6-bisphosphatase TIGAR, TP53-induced glycolysis and apoptosis regulator, TIGAR, C12orf5.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized TIGAR stable at room temperature for 3 weeks, should be stored desiccated below -18C. Upon reconstitution TIGAR should be stored at 4C between 2-7 days and for future use below -18C. 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 TIGAR in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      MARFALTVVR HGETRFNKEK IIQGQGVDEP LSETGFKQAA AAGIFLNNVK FTHAFSSDLM RTKQTMHGIL ERSKFCKDMT VKYDSRLRER KYGVVEGKAL SELRAMAKAA REECPVFTPP GGETLDQVKM RGIDFFEFLC QLILKEADQK EQFSQGSPSN CLETSLAEIF PLGKNHSSKV NSDSGIPGLA ASVLVVSHGA YMRSLFDYFL TDLKCSLPAT LSRSELMSVT PNTGMSLFII NFEEGREVKP TVQCICMNLQ DHLNGLTETR

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    Tigar Human
  • View Data Sheet

    Name :

    PEX26 Human

    Description:

    Peroxisomal Biogenesis Factor 26 Human Recombinant

    PBD7A, PBD7B, PEX26M1T, Pex26pM1T, Peroxisome assembly protein 26, PEX26.

    Product # :

    PRO-1544

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    Description

    PEX26 Human Recombinant produced in E. coli is a single polypeptide chain containing 269 amino acids (1-246) and having a molecular mass of 29.3kDa. PEX26 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The PEX26 solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 20% glycerol and 1mM DTT.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    More Info

    • Introduction

      Peroxisomal Biogenesis Factor 26 (PEX26) which is a part of the peroxin-26 gene family is probably required for protein import into peroxisomes. PEX26 attaches PEX1 and PEX6 to peroxisome membranes to form heteromeric AAA ATPase complexes needed for the import of proteins into peroxisomes. Deficiencies in this gene are the cause of peroxisome biogenesis disorder complementation group 8. PBD is a group of peroxisomal disorders evolving from a failure of protein import into the peroxisomal membrane or matrix.

    • Synonyms

      PBD7A, PBD7B, PEX26M1T, Pex26pM1T, Peroxisome assembly protein 26, PEX26.

    • 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 MGSMKSDSST SAAPLRGLGG PLRSSEPVRA VPARAPAVDL LEEAADLLVV HLDFRAALET CERAWQSLAN HAVAEEPAGT SLEVKCSLCV VGIQALAEMD RWQEVLSWVL QYYQVPEKLP PKVLELCILL YSKMQEPGAV LDVVGAWLQD PANQNLPEYG ALAEFHVQRV LLPLGCLSEA EELVVGSAAF GEERRLDVLQ AIHTARQQQK QEHSGSEEAQ KPNLEGSVSH KFLSLPMLVR QLWDSAVSH.

    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.

    Pex26 Human
  • View Data Sheet

    Name :

    GCAT Human

    Description:

    Glycine C-Acetyltransferase Human Recombinant

    2-amino-3-ketobutyrate coenzyme A ligase mitochondrial, AKB ligase, EC 2.3.1.29, Aminoacetone synthase, Glycine acetyltransferase, GCAT, KBL.

    Product # :

    ENZ-705

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    Description

    GCAT Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 419 amino acids (22-419 a.a) and having a molecular mass of 45kDa.GCAT is fused to a 21 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    GCAT protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.4M urea and 10% glycerol.

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

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    • Introduction

      L-threonine to glycine degradation consists of a two-step biochemical pathway which involvs the enzymes L-threonine dehydrogenase and 2-amino-3-ketobutyrate coenzyme A ligase. L-Threonine is initially converted into 2-amino-3-ketobutyrate by L-threonine dehydrogenase. Glycine C-Acetyltransferase (GCAT) is the 2nd enzyme in this pathway, which subsequently catalyzes the reaction between 2-amino-3-ketobutyrate and coenzyme A to form glycine and acetyl-CoA. The GCAT enzyme is regard as a class II pyridoxal-phosphate-dependent aminotransferase. GCAT is strongly expressed in the heart, brain, liver and pancreas. GCAT is also found in lung.

    • Synonyms

      2-amino-3-ketobutyrate coenzyme A ligase mitochondrial, AKB ligase, EC 2.3.1.29, Aminoacetone synthase, Glycine acetyltransferase, GCAT, KBL.

    • 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 MSALAQLRGI LEGELEGIRG AGTWKSERVI TSRQGPHIRV DGVSGGILNF CANNYLGLSS HPEVIQAGLQ ALEEFGAGLS SVRFICGTQS IHKNLEAKIA RFHQREDAIL YPSCYDANAG LFEALLTPED AVLSDELNHA SIIDGIRLCK AHKYRYRHLD MADLEAKLQE AQKHRLRLVA TDGAFSMDGD IAPLQEICCL ASRYGALVFM DECHATGFLG PTGRGTDELL GVMDQVTIIN STLGKALGGA SGGYTTGPGP LVSLLRQRAR PYLFSNSLPP AVVGCASKAL DLLMGSNTIV QSMAAKTQRF RSKMEAAGFT ISGASHPICP VMLGDARLAS RMADDMLKRG IFVIGFSYPV VPKGKARIRV QISAVHSEED IDRCVEAFVE VGRLHGALP.

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    Gcat Human
  • View Data Sheet

    Name :

    TPX E.coli

    Description:

    Thiol Peroxidase E.Coli Recombinant

    Thiol peroxidase, Scavengase P20, tpx, yzzJ, b1324, JW1317.

    Product # :

    ENZ-135

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    Description

    TPX produced in E.Coli is a single, non-glycosylated polypeptide chain containing 188 amino acids (1-168 a.a.) and having a molecular mass of 19.9kDa.TPX is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The Recombinant TPX solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0) 10% glycerol, 2mM DTT and 0.1M NaCl.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Lipid hydroperoxide peroxidase (TPX) belongs to the peroxiredoxin family of antioxidant enzymes, which reduce hydrogen peroxide and alkyl hydroperoxides. TPX has an imperative role in thioredoxin peroxidase activity.

    • Synonyms

      Thiol peroxidase, Scavengase P20, tpx, yzzJ, b1324, JW1317.

    • Physical Appearance

      Sterile filtered liquid formulation 1 mg/ml.

    • Stability

      TPX E.Coli Recombinant although stable at 4°C for 1 week, should be stored below -18°C. Please prevent freeze thaw cycles.

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MSQTVHFQGN PVTVANSIPQ AGSKAQTFTL VAKDLSDVTL GQFAGKRKVL NIFPSIDTGV CAASVRKFNQ LATEIDNTVV LCISADLPFA QSRFCGAEGL NNVITLSTFR NAEFLQAYGV AIADGPLKGL AARAVVVIDE NDNVIFSQLV DEITTEPDYE AALAVLKA.

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    Tpx Ecoli
  • View Data Sheet

    Name :

    COPS8 Human

    Description:

    COP9 Constitutive Photomorphogenic 8 Human Recombinant

    COP9 signalosome complex subunit 8, SGN8, Signalosome subunit 8, COP9 homolog, hCOP9, JAB1-containing signalosome subunit 8, COPS8, CSN8, COP9.

    Product # :

    PRO-983

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    Description

    COPS8 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 229 amino acids (1-209) and having a molecular mass of 25.3kDa.COPS8 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The COPS8 solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.4M Urea and 10% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      COP9 signalosome complex subunit 8 isoform 1 (COPS8) is one of the 8 subunits of COP9 signalosome, which is a much conserved protein complex that functions as an imperative regulator in multiple signaling pathways. The structure and function of COP9 signalosome is analogous to that of the 19S regulatory particle of 26S proteasome. COP9 signalosome interacts with SCF-type E3 ubiquitin ligases and acts as a positive regulator of E3 ubiquitin ligases.

    • Synonyms

      COP9 signalosome complex subunit 8, SGN8, Signalosome subunit 8, COP9 homolog, hCOP9, JAB1-containing signalosome subunit 8, COPS8, CSN8, COP9.

    • 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 MPVAVMAESA FSFKKLLDQC ENQELEAPGG IATPPVYGQL LALYLLHNDM NNARYLWKRI PPAIKSANSE LGGIWSVGQR IWQRDFPGIY TTINAHQWSE TVQPIMEALR DATRRRAFAL VSQAYTSIIA DDFAAFVGLP VEEAVKGILE QGWQADSTTR
      MVLPRKPVAG ALDVSFNKFI PLSEPAPVPP IPNEQQLARL TDYVAFLEN.

    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.

    Cops8 Human
  • View Data Sheet

    Name :

    YWHAE Human

    Description:

    Tyr-3/Trp- 5 Monooxygenase Activation Protein Epsilon Human Recombinant

    YWHAE, MDS, MDCR, KCIP-1, 14-3-3E, 14-3-3 Epsilon, FLJ45465, Tyr-3/Trp- 5 Monooxygenase Activation Protein Epsilon.

    Product # :

    PKA-253

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    Description

    YWHAE Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 255 amino acids (1-255) and having a molecular mass of 29 kDa. YWHAE is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    YWHAE solution containing 20mM Tris 7.5.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      The 14-3-3 family of proteins plays a key regulatory role in signal transduction, checkpoint control, apoptotic and nutrient-sensing pathways. 14-3-3 proteins are highly conserved and ubiquitously expressed. There are at least seven isoforms, β, γ, ε, σ, ζ, τ and η that have been identified in mammals. The 14-3-3 epsilon, a subtype of the 14-3-3 family of proteins, was thought to be brain and neuron-specific. It has been shown to interact with CDC25 phosphatases, RAF1 and IRS1 proteins, suggesting its role in diverse biochemical activities related to signal transduction, such as cell division and regulation of sensitivity. It has also been implicated in the pathogenesis of small cell lung cancer.

    • Synonyms

      YWHAE, MDS, MDCR, KCIP-1, 14-3-3E, 14-3-3 Epsilon, FLJ45465, Tyr-3/Trp- 5 Monooxygenase Activation Protein Epsilon.

    • Physical Appearance

      Sterile filtered colorless solution.

    • Stability

      YWHAE Human Recombinant although stable at 4°C for 1 week, should be stored below -18°C. Please prevent freeze thaw cycles.

    • Amino Acid Sequence

      MDDREDLVYQ AKLAEQAERY DEMVESMKKV AGMDVELTVE ERNLLSVAYK NVIGARRASWRIISSIEQKE ENKGGEDKLK MIREYRQMVE TELKLICCDI LDVLDKHLIP AANTGESKVFYYKMKGDYHR YLAEFATGND RKEAAENSLV AYKAASDIAM TELPPTHPIR LGLALNFSVFYYEILNSPDR ACRLAKAAFD DAIAELDTLS EESYKDSTLI MQLLRDNLTL WTSDMQGDGE EQNKEALQDV EDENQ.

    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.

    Ywhae Human
  • View Data Sheet

    Name :

    ECI1 Human

    Description:

    Enoyl-CoA Delta Isomerase 1 Human Recombinant

    Enoyl-CoA delta isomerase 1, mitochondrial, 3,2-trans-enoyl-CoA isomerase, Enoyl-CoA Delta Isomerase 1, Delta(3),Delta(2)-enoyl-CoA isomerase, D3,D2-enoyl-CoA isomerase, Dodecenoyl-CoA isomerase, ECI1, DCI.

    Product # :

    ENZ-758

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    Description

    ECI1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 284 amino acids (42-302 a.a.) and having a molecular mass of 31.1kDa. ECI1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    ECI1 protein solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 10% glycerol and 1mM DTT.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Enoyl-CoA Delta Isomerase 1 (ECI1) is a main mitochondrial enzyme which takes part in beta-oxidation of unsaturated fatty acids. ECI1 is a member of the hydratase/isomerase superfamily. ECI1 catalyzes the transformation of 3-cis and 3-trans-enoyl-CoA esters to the 2-trans-enoylCoA intermediates.

    • Synonyms

      Enoyl-CoA delta isomerase 1, mitochondrial, 3,2-trans-enoyl-CoA isomerase, Enoyl-CoA Delta Isomerase 1, Delta(3),Delta(2)-enoyl-CoA isomerase, D3,D2-enoyl-CoA isomerase, Dodecenoyl-CoA isomerase, ECI1, DCI.

    • 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 MGSFGSQRVL VEPDAGAGVA VMKFKNPPVN SLSLEFLTEL VISLEKLEND KSFRGVILTS DRPGVFSAGL DLTEMCGRSP AHYAGYWKAV QELWLRLYQS NLVLVSAING ACPAGGCLVA LTCDYRILAD NPRYCIGLNE TQLGIIAPFW LKDTLENTIG HRAAERALQL GLLFPPAEAL QVGIVDQVVP EEQVQSTALS AIAQWMAIPD HARQLTKAMM RKATASRLVT QRDADVQNFV SFISKDSIQK SLQMYLERLK EEKG.

    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.

    Eci1 Human
  • View Data Sheet

    Name :

    YWHAE Human, His

    Description:

    Tyr-3/Trp-5 Monooxygenase Activation Protein, Epsilon Human Recombinant, His Tag

    YWHAE, MDS, MDCR, KCIP-1, 14-3-3E, 14-3-3 Epsilon, FLJ45465, Tyr-3/Trp- 5 Monooxygenase Activation Protein Epsilon, HEL2, KCIP-1, MDCR, MDS.

    Product # :

    PKA-095

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    • More Info

    Description

    YWHAE Human Recombinant produced in E. coli is a single polypeptide chain containing 275 amino acids (1-255) and having a molecular mass of 31.3kDa. YWHAE is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The YWHAE solution (1mg/1ml) contains phosphate buffered Saline (pH7.4), 1mM DTT and 10% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      The 14-3-3 family of proteins plays a key regulatory role in signal transduction, checkpoint control, apoptotic and nutrient-sensing pathways. 14-3-3 proteins are highly conserved and ubiquitously expressed. There are at least seven isoforms, β, γ, ε, σ, ζ, τ and η that have been identified in mammals. The 14-3-3 epsilon, a subtype of the 14-3-3 family of proteins, was thought to be brain and neuron-specific. It has been shown to interact with CDC25 phosphatases, RAF1 and IRS1 proteins, suggesting its role in diverse biochemical activities related to signal transduction, such as cell division and regulation of insulin sensitivity. It has also been implicated in the pathogenesis of small cell lung cancer.

    • Synonyms

      YWHAE, MDS, MDCR, KCIP-1, 14-3-3E, 14-3-3 Epsilon, FLJ45465, Tyr-3/Trp- 5 Monooxygenase Activation Protein Epsilon, HEL2, KCIP-1, MDCR, MDS.

    • 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 MDDREDLVYQ AKLAEQAERY DEMVESMKKV AGMDVELTVE ERNLLSVAYK NVIGARRASW RIISSIEQKE ENKGGEDKLK MIREYRQMVE TELKLICCDI LDVLDKHLIP AANTGESKVF YYKMKGDYHR YLAEFATGND RKEAAENSLV AYKAASDIAM TELPPTHPIR LGLALNFSVF YYEILNSPDR ACRLAKAAFD DAIAELDTLS EESYKDSTLI MQLLRDNLTL WTSDMQGDGE EQNKEALQDV EDENQ.

    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.

    Ywhae Human His
  • View Data Sheet

    Name :

    SOD Human His

    Description:

    Superoxide Dismutase Human Recombinant His Tag

    Superoxide dismutase [Cu-Zn], EC 1.15.1.1, SOD1, SOD, ALS, ALS1, IPOA.

    Product # :

    PRO-1239

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    • source
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    • biological activity
    • More Info

    Description

    SOD Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 189 amino acids with a 10 × His at N-terminus and having a molecular mass of 40.0kDa.The SOD Human is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Lyophilized from a 0.2um filtered concentrated solution in PBS, pH 7.4.

    Purity

    Greater than 95.0% as determined by SDS-PAGE and HPLC analyses.

    Biological Activity

    Fully biologically active when compared to standard. The specific activity was tested by Pyrogallic Acid method and was found to be more than 10,000Units/mg.

    More Info

    • Introduction

      Human Cu/Zn Superoxide Dismutase (SOD1) catalyzes the reaction between superoxide anions and hydrogen to yield molecular oxygen and hydrogen peroxide. The enzyme protects the cell against dangerous levels of superoxide. SOD1 binds copper and zinc ions and is 1 of 3 isozymes accountable for destroying free superoxide radicals in the body. The encoded protein neutralizes supercharged oxygen molecules, which can damage cells if their levels are not controlled. Mutations in SOD1 cause a form of familial amyotrophic lateral sclerosis.

    • Synonyms

      Superoxide dismutase [Cu-Zn], EC 1.15.1.1, SOD1, SOD, ALS, ALS1, IPOA.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized SOD Human although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution SOD Human should be stored at 4°C between 2-7 days and for future use below -18°C.Please prevent freeze-thaw cycles.

    • Solubility

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

    • Amino Acid Sequence

      MGHHHHHHHH HHSSGHIEGR HMTYARAAAR QARALEATKA VCVLKGDGPV QGIINFEQKE SNGPVKVWGS IKGLTEGLHG FHVHEFGDNT AGCTSAGPHF NPLSRKHGGP KDEERHVGDL GNVTADKDGV ADVSIEDSVI SLSGDHCIIG RTLVVHEKAD DLGKGGNEES TKTGNAGSRL ACGVIGIAQ

    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.

    Sod Human His
  • View Data Sheet

    Name :

    NDUFAF2 Human

    Description:

    NADH Dehydrogenase 1 Alpha Subcomplex, Assembly Factor 2 Human Recombinant

    Mimitin mitochondrial, B17.2-like, B17.2L, Myc-induced mitochondrial protein, MMTN, NADH dehydrogenase [ubiquinone] 1 alpha subcomplex assembly factor 2, NDUFA12-like protein, NDUFAF2, NDUFA12L, mimitin.

    Product # :

    ENZ-150

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    • More Info

    Description

    NDUFAF2 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 189 amino acids (1-169 a.a.) and having a molecular mass of 22kDa.NDUFAF2 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    NDUFAF2 protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 1mM DTT, 20% glycerol and 200mM NaCl.

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Mimitin (NDUFAF2) is a member of the complex I NDUFA12 subunit family.NADH dehydrogenase is an enzyme located in the inner mitochondrial membrane, which catalyzes the transfer of electrons from NADH to coenzyme Q (CoQ). NDUFAF2 is the "entry enzyme" of oxidative phosphorylation in the mitochondria. Mimitin protein functions as a molecular chaperone for mitochondrial complex I assembly.

    • Synonyms

      Mimitin mitochondrial, B17.2-like, B17.2L, Myc-induced mitochondrial protein, MMTN, NADH dehydrogenase [ubiquinone] 1 alpha subcomplex assembly factor 2, NDUFA12-like protein, NDUFAF2, NDUFA12L, mimitin.

    • 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 MGWSQDLFRA LWRSLSREVK EHVGTDQFGN KYYYIPQYKN WRGQTIREKR IVEAANKKEV DYEAGDIPTE WEAWIRRTRK TPPTMEEILK NEKHREEIKI KSQDFYEKEK LLSKETSEEL LPPPVQTQIK GHASAPYFGK EEPSVAPSST GKTFQPGSWM PRDGKSHNQ.

    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.

    Ndufaf2 Human
  • View Data Sheet

    Name :

    BCAT2 Human

    Description:

    Branched Chain Amino-Acid Transaminase 2 Human Recombinant

    Branched-chain-amino-acid aminotransferase mitochondrial, BCAT(m), Placental protein 18, PP18, BCAT2, BCATM, BCT2, ECA40, BCAM.

    Product # :

    ENZ-606

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    Description

    BCAT2 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 390 amino acids (28-392) and having a molecular mass of 43.9kDa.BCAT2 is fused to a 25 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The BCAT2 solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 7.5), 10% glycerol, 0.2M NaCl and 1mM DTT.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Branched Chain Amino-Acid Transaminase 2 (BCAT2) is a member of the class-IV pyridoxal-phosphate-dependent aminotransferase family. BCAT2 is a branched chain aminotransferase found in mitochondria. BCAT2 forms a dimer which catalyzes the first step in the production of the branched chain amino acids leucine, isoleucine, and valine. In addition, BCAT2 may actn as a transporter of branched chain alpha-keto acids.

    • Synonyms

      Branched-chain-amino-acid aminotransferase mitochondrial, BCAT(m), Placental protein 18, PP18, BCAT2, BCATM, BCT2, ECA40, BCAM.

    • 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 MGSHMASSSF KAADLQLEMT QKPHKKPGPG EPLVFGKTFT DHMLMVEWND KGWGQPRIQP FQNLTLHPAS SSLHYSLQLF EGMKAFKGKD QQVRLFRPWL NMDRMLRSAM RLCLPSFDKL ELLECIRRLI EVDKDWVPDA AGTSLYVRPV LIGNEPSLGV SQPTRALLFV ILCPVGAYFP GGSVTPVSLL ADPAFIRAWV GGVGNYKLGG NYGPTVLVQQ EALKRGCEQV LWLYGPDHQL TEVGTMNIFV YWTHEDGVLE LVTPPLNGVI LPGVVRQSLL DMAQTWGEFR VVERTITMKQ LLRALEEGRV REVFGSGTAC QVCPVHRILY KDRNLHIPTM ENGPELILRF QKELKEIQYG IRAHEWMFPV.

    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.

    Bcat2 Human
  • View Data Sheet

    Name :

    NFNB E.Coli

    Description:

    Dihydropteridine Reductase E.Coli Recombinant

    DPRA, NFSB, NFSI, NTR.

    Product # :

    ENZ-423

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    Description

    NFNB Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 237 amino acids (1-217 a.a.) and having a molecular mass of 26 kDa. The NFNB is fused to a 20 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    1mg/ml solution containing 20mM Tris pH-8, 1mM DTT, 0.05M NaCl & 10% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      NFNB demonstrates the capability to reduce quinines. NFNB enzyme activates prodrugs in antibody directed enzyme prodrug therapy. NFNB reduces nitrofurazone, quinones and anti-tumor agent CB1954 (5-(aziridin-1-yl)-2,4-dinitrobenzamide). The reduction of CB1954 results in the generation of cytotoxic species.

    • Synonyms

      DPRA, NFSB, NFSI, NTR.

    • 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 MDIISVALKR HSTKAFDASK KLTPEQAEQI KTLLQYSPSS TNSQPWHFIV ASTEEGKARV AKSAAGNYVF NERKMLDASH VVVFCAKTAM DDVWLKLVVD QEDADGRFAT PEAKAANDKG RKFFADMHRK DLHDDAEWMA KQVYLNVGNF LLGVAALGLD AVPIEGFDAA ILDAEFGLKE KGYTSLVVVP VGHHSVEDFN ATLPKSRLPQ NITLTEV.

    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.

    Nfnb Ecoli
  • View Data Sheet

    Name :

    CCNI Human

    Description:

    Cyclin-I Human Recombinant

    Cyclin-I, CCNI, CYC1, CYI.

    Product # :

    PKA-318

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    • More Info

    Description

    CCNI Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 400 amino acids (1-377 a.a) and having a molecular mass of 44.9kDa.CCNI is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    CCNI protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH8.0), 10% glycerol and 0.4M Urea.

    Purity

    Greater than 85% as determined by SDS-PAGE.

    More Info

    • Introduction

      CCN1 is a part of the extremely conserved cyclin family, whose members are characterized by a remarkable periodicity in protein abundance through the cell cycle. Cyclins which function as regulators of CDK kinases, shows the highest similarity with cyclin G. Different cyclins display diverse expression and degradation patterns which contribute to the chronological coordination of every mitotic event. The transcript of CCN1was found to be expressed continually during cell cycle progression.

    • Synonyms

      Cyclin-I, CCNI, CYC1, CYI.

    • 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 MGSMKFPGPL ENQRLSFLLE KAITREAQMW KVNVRKMPSN QNVSPSQRDE VIQWLAKLKY QFNLYPETFA LASSLLDRFL ATVKAHPKYL SCIAISCFFL AAKTVEEDER IPVLKVLARD SFCGCSSSEI LRMERIILDK LNWDLHTATP LDFLHIFHAI AVSTRPQLLF SLPKLSPSQH LAVLTKQLLH CMACNQLLQF RGSMLALAMV SLEMEKLIPD WLSLTIELLQ KAQMDSSQLI HCRELVAHHL STLQSSLPLN SVYVYRPLKH TLVTCDKGVF RLHPSSVPGP DFSKDNSKPE VPVRGTAAFY HHLPAASGCK QTSTKRKVEE MEVDDFYDGI KRLYNEDNVS ENVGSVCGTD LSRQEGHASP CPPLQPVSVM.

    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.

    Ccni Human
  • View Data Sheet

    Name :

    CDC123 Human

    Description:

    Cell Division Cycle 123 Human Recombinant

    C10orf7, D123, Cell division cycle protein 123 homolog, Protein D123, HT-1080, PZ32, Chromosome 10 Open Reading Frame 7.

    Product # :

    PRO-1463

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    Description

    CDC123 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 359 amino acids (1-336 a.a) and having a molecular mass of 41.5kDa.CDC123 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    CDC123 protein solution (0. 5mg/ml) containing 20mM Tris-HCl buffer (pH8.0), 20% glycerol, 0.1M NaCl and 2mM DTT.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      CDC123 is a member of the CDC123 family. CDC123is required for S phase entry of the cell cycle. It is also broadly expressed in spleen,thymus, prostate, testis, ovary, small intestine, colon and leukocytes with the uppermost expression in testis.

    • Synonyms

      C10orf7, D123, Cell division cycle protein 123 homolog, Protein D123, HT-1080, PZ32, Chromosome 10 Open Reading Frame 7.

    • 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 MGSMKKEHVL HCQFSAWYPF FRGVTIKSVI LPLPQNVKDY LLDDGTLVVS GRDDPPTHSQ PDSDDEAEEI QWSDDENTAT LTAPEFPEFA TKVQEAINSL GGSVFPKLNW SAPRDAYWIA MNSSLKCKTL SDIFLLFKSS DFITRDFTQP FIHCTDDSPD PCIEYELVLR KWCELIPGAE FRCFVKENKL IGISQRDYTQ YYDHISKQKE EIRRCIQDFF KKHIQYKFLD EDFVFDIYRD SRGKVWLIDF NPFGEVTDSL LFTWEELISE NNLNGDFSEV DAQEQDSPAF RCTNSEVTVQ PSPYLSYRLP KDFVDLSTGE DAHKLIDFLK LKRNQQEDD

    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.

    Cdc123 Human
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