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Search results

1000 results found for “alkaline phosphatase”

Name

Description

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  • View Data Sheet

    Name :

    IDI1 Human

    Description:

    Isopentenyl-Diphosphate Delta Isomerase 1 Human Recombinant

    Isopentenyl-diphosphate Delta-isomerase 1, Isopentenyl pyrophosphate isomerase 1, IPP isomerase 1, IPPI1, IDI1, IPP1.

    Product # :

    ENZ-189

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    Description

    IDI1 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 248 amino acids (1-228) and having a molecular mass of 28.6kDa.IDI1 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    The IDI1 solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 1mM DTT, 10% glycerol and 0.1M NaCl.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      Isopentenyl-diphosphate isomerase 1 (IDI1) belongs to the IPP isomerase type I family and is involved in cholesterol biosynthesis. IDI1 is a peroxisomally-localized enzyme which catalyzes the interconversion of isopentenyl diphosphate (IPP) to its highly electrophilic isomer, dimethylallyl diphosphate (DMAPP), which is the substrate for the sequential reaction that results in the synthesis of farnesyl diphosphate and, eventually, cholesterol. Peroxisomal deficiency diseases such as Zellweger syndrome and neonatal adrenoleukodystrophy show a reduction in IPP isomerase activity.

    • Synonyms

      Isopentenyl-diphosphate Delta-isomerase 1, Isopentenyl pyrophosphate isomerase 1, IPP isomerase 1, IPPI1, IDI1, IPP1.

    • 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 MMPEINTNHL DKQQVQLLAE MCILIDENDN KIGAETKKNC HLNENIEKGL LHRAFSVFLF NTENKLLLQQ RSDAKITFPG CFTNTCCSHP LSNPAELEES DALGVRRAAQ RRLKAELGIP LEEVPPEEIN YLTRIHYKAQ SDGIWGEHEI DYILLVRKNV
      TLNPDPNEIK SYCYVSKEEL KELLKKAASG EIKITPWFKI IAATFLFKWW DNLNHLNQFV DHEKIYRM.

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

    Idi1 Human
  • View Data Sheet

    Name :

    NUDT3 Human

    Description:

    Nudix Type Motif 3 Human Recombinant

    Diphosphoinositol polyphosphate phosphohydrolase 1, DIPP-1, Diadenosine 5',5'''-P1,P6-hexaphosphate hydrolase 1, Nucleoside diphosphate-linked moiety X motif 3, Nudix motif 3, NUDT3, DIPP, DIPP1.

    Product # :

    ENZ-071

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    Description

    NUDT3 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 192 amino acids (1-172 a.a.) and having a molecular mass of 21.6kDa. The NUDT3 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The NUDT3 solution (0.5 mg/ml) contains 20mM Tris-HCl buffer (pH8.0), 0.2M NaCl, 5mM DTT and 20% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      NUDT3 is a 172 amino acid cytoplasmic protein which is a member of the nudix hydrolase family and DIPP subfamily. NUDT3 functions as a negative regulator of the ERK 1/2 pathway and hydrolyzes 5-phosphoribose 1-diphosphate. NUDT3 is a monomer which binds magnesium as a cofactor. In addition, NUDT3 is widely expressed but can be found at highest levels in the liver, pancreas, brain and heart.

    • Synonyms

      Diphosphoinositol polyphosphate phosphohydrolase 1, DIPP-1, Diadenosine 5',5'''-P1,P6-hexaphosphate hydrolase 1, Nucleoside diphosphate-linked moiety X motif 3, Nudix motif 3, NUDT3, DIPP, DIPP1.

    • 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 MMKLKSNQTR TYDGDGYKKR AACLCFRSES EEEVLLVSSS RHPDRWIVPG GGMEPEEEPS VAAVREVCEE AGVKGTLGRL VGIFENQERK HRTYVYVLIV TEVLEDWEDS VNIGRKREWF KIEDAIKVLQ YHKPVQASYF ETLRQGYSAN NGTPVVATTY SVSAQSSMSG IR.

    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.

    Nudt3 Human
  • View Data Sheet

    Name :

    ErbB3 Human, sf9

    Description:

    Tyrosine Kinase ErbB-3 Human Recombinant, sf9

    Tyrosine Kinase ErbB-3, sf9, ErbB3 sf9, Receptor tyrosine-protein kinase erbB-3, ERBB3, Proto-oncogene-like protein c-ErbB-3, Tyrosine kinase-type cell surface receptor HER3, HER3, Receptor tyrosine-protein kinase erbB-3 isoform, c-erbB-3, ErbB-3, erbB3-S, LCCS2, MDA-BF-1, p180-ErbB3, p45-sErbB3, p85-sErbB3.

    Product # :

    PKA-081

    Price :

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    Description

    ErbB3 Human Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 863 amino acids (20-643 a.a.) and having a molecular mass of 95.6kDa (Migrates at 100-150kDa on SDS-PAGE under reducing conditions).ErbB3 is expressed with a 239 amino acid hIgG-His tag at C-Terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    ErbB3 protein solution (0.25mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 10% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      ErbB3, also called Her3 (human epidermal growth factor receptor 3), is a type I membrane glycoprotein that is a member of the ErbB family of tyrosine kinase receptors. ErbB family members serve as receptors for the epidermal growth factor (EGF) family of growth factors. Among ErbB family members, ErbB3 is unique in that it contains a defective kinase domain. ErbB3 is expressed in keratinocytes, melanocytes, skeletal muscle cells, embryonic myoblasts and Schwann cells. Monomeric ErbB3 serves as a low affinity receptor for the heregulins (HRG). ErbB3 can induce specific antibody production in vivo, hence to inhibit tumor cell growth. ErbB-3 can be used to treat early, medium and advanced or post-operative breast cancer with over-expression of ErbB2. According to its mechanism of action, ErbB3 is classified as a therapeutic for cancer.

    • Synonyms

      Tyrosine Kinase ErbB-3, sf9, ErbB3 sf9, Receptor tyrosine-protein kinase erbB-3, ERBB3, Proto-oncogene-like protein c-ErbB-3, Tyrosine kinase-type cell surface receptor HER3, HER3, Receptor tyrosine-protein kinase erbB-3 isoform, c-erbB-3, ErbB-3, erbB3-S, LCCS2, MDA-BF-1, p180-ErbB3, p45-sErbB3, p85-sErbB3.

    • 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

      SEVGNSQAVC PGTLNGLSVT GDAENQYQTL YKLYERCEVV MGNLEIVLTG HNADLSFLQW IREVTGYVLV AMNEFSTLPL PNLRVVRGTQ VYDGKFAIFV MLNYNTNSSH ALRQLRLTQL TEILSGGVYI EKNDKLCHMD TIDWRDIVRD RDAEIVVKDN GRSCPPCHEV CKGRCWGPGS EDCQTLTKTI CAPQCNGHCF GPNPNQCCHD ECAGGCSGPQ DTDCFACRHF NDSGACVPRC PQPLVYNKLT FQLEPNPHTK YQYGGVCVAS CPHNFVVDQT SCVRACPPDK MEVDKNGLKM CEPCGGLCPK ACEGTGSGSR FQTVDSSNID GFVNCTKILG NLDFLITGLN GDPWHKIPAL DPEKLNVFRT VREITGYLNI QSWPPHMHNF SVFSNLTTIG GRSLYNRGFS LLIMKNLNVT SLGFRSLKEI SAGRIYISAN RQLCYHHSLN WTKVLRGPTE ERLDIKHNRP RRDCVAEGKV CDPLCSSGGC WGPGPGQCLS CRNYSRGGVC VTHCNFLNGE PREFAHEAEC FSCHPECQPM EGTATCNGSG SDTCAQCAHF RDGPHCVSSC PHGVLGAKGP IYKYPDVQNE CRPCHENCTQ GCKGPELQDC LGQTLVLIGK THLTRSPKSC DKTHTCPPCP APELLGGPSV FLFPPKPKDT LMISRTPEVT CVVVDVSHED PEVKFNWYVD GVEVHNAKTK PREEQYNSTY RVVSVLTVLH QDWLNGKEYK CKVSNKALPA PIEKTISKAK GQPREPQVYT LPPSRDELTK NQVSLTCLVK GFYPSDIAVE WESNGQPENN YKTTPPVLDS DGSFFLYSKL TVDKSRWQQG NVFSCSVMHE ALHNHYTQKS LSLSPGKHHH HHH.

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

    Erbb3 Human Sf9
  • View Data Sheet

    Name :

    CA12 Human

    Description:

    Carbonic Anhydrase XII Human Recombinant

    Carbonic anhydrase 12, Carbonate dehydratase XII, Carbonic anhydrase XII, CA-XII, Tumor antigen HOM-RCC-3.1.3, CA12, Carbonic Anhydrase XII, Carbonic anhydrase 12 isoform 1, CAXII, HsT18816.

    Product # :

    ENZ-886

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    • Citations

    Description

    CA12 Human Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 283 amino acids (25-301a.a.) and having a molecular mass of 31.94kDa (Migrates at 28-40kDa on SDS-PAGE under reducing conditions).CA12 is fused to a 6 amino acid His-tag at C-terminus & purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    CA12 protein solution (0.5mg/ml) containing Phosphate Buffer Saline (pH7.4) and 10% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    Biological Activity

    Specific activity is > 300 pmol/min/ug, and is defined as the amount of enzyme that hydrolyze 1.0 pmole of 4-nitrophenyl acetate to 4-nitrophenol per minute at pH 7.5 at 37C.

    Citations

    More Info

    • Introduction

      Carbonic anhydrase 12 (CA12) is an enzyme that belongs to the Carbonic anhydrases (CAs) family. This is a large family of zinc metalloenzymes which catalyze the reversible hydration of carbon dioxide. They are involved in various biological processes, including respiration, calcification, acid-base balance, bone resorption, and the formation of aqueous humor, cerebrospinal fluid, saliva, and gastric acid. CA12 is a type I membrane protein which is highly expressed in normal tissues, such as the kidney, colon and pancreas, and is overexpressed in 10% of clear cell renal carcinomas.

    • Synonyms

      Carbonic anhydrase 12, Carbonate dehydratase XII, Carbonic anhydrase XII, CA-XII, Tumor antigen HOM-RCC-3.1.3, CA12, Carbonic Anhydrase XII, Carbonic anhydrase 12 isoform 1, CAXII, HsT18816.

    • 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

      APVNGSKWTY FGPDGENSWS KKYPSCGGLL QSPIDLHSDI LQYDASLTPL EFQGYNLSAN KQFLLTNNGH SVKLNLPSDM HIQGLQSRYS ATQLHLHWGN PNDPHGSEHT VSGQHFAAEL HIVHYNSDLY PDASTASNKS EGLAVLAVLI EMGSFNPSYD KIFSHLQHVK YKGQEAFVPG FNIEELLPER TAEYYRYRGS LTTPPCNPTV LWTVFRNPVQ ISQEQLLALE TALYCTHMDD PSPREMINNF RQVQKFDERL VYTSFSQVQV CTAAGLSHHH HHH.

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

    Ca12 Human
  • View Data Sheet

    Name :

    CAIII Human, His

    Description:

    Carbonic Anhydrase III Human Recombinant, His Tag

    Car3, CAIII, Carbonic anhydrase 3, EC 4.2.1.1, Carbonic anhydrase III, Carbonate dehydratase III, CA-III.

    Product # :

    ENZ-270

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    Description

    Carbonic anhydrase III Human Recombinant produced in E.Coli, and having a molecular mass of 33.9 kDa. CAIII is expressed with an amino-terminal hexahistidine tag.The CA-III is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Supplied in 10mM Tris-HCl (pH 8), 250mM NaCl, 0.5mM DTT, 1.5mM Cysteine, and 50% Glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      Carbonic anhydrase (carbonate dehydratase) is a family of metalloenzymes (enzymes that contain one or more metal atoms as a functional component of the enzyme) that catalyze the rapid (and reversible) conversion of carbon dioxide to bicarbonate and protons, a reaction that occurs rather slowly in the absence of a catalyst. Carbonic anhydrase greatly increases the rate of the reaction, with typical catalytic rates of the different forms of this enzyme ranging between 104 and 106 reactions per second. The active site of most carbonic anhydrases contains a zincion. CAIII is a cytoplasmic isoenzyme, but is released into the circulation following injury.

    • Synonyms

      Car3, CAIII, Carbonic anhydrase 3, EC 4.2.1.1, Carbonic anhydrase III, Carbonate dehydratase III, CA-III.

    • Physical Appearance

      Sterile Filtered blue 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.

    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.

    Caiii Human
  • View Data Sheet

    Name :

    PGK2 Human

    Description:

    Phosphoglycerate Kinase 2 Human Recombinant

    Phosphoglycerate kinase 2, Phosphoglycerate kinase testis specific, PGK2, PGKB, PGKPS, dJ417L20.2.

    Product # :

    PKA-017

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    Description

    PGK2 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 437 amino acids (1-417 a.a.) and having a molecular mass of 46.9kDa.PGK2 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    PGK2 protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH8.0), 20% glycerol, 1mM DTT and 0.1M NaCl.

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      PGK2 is a testis-specific form of phosphoglycerate kinase. Originally presumed to be a pseudogene, the PGK2 protein is actually a functional phosphoglycerate kinase which catalyzes the reversible conversion of 1,3-bisphosphoglycerate to 3-phosphoglycerate, during the Embden-Meyerhof-Parnas pathway of glycolysis, in the later stages of spermatogenesis. The PGK2 gene is intronless, results from retrotransposition of the phosphoglycerate kinase 1 gene, and is expressed specifically in the testis.

    • Synonyms

      Phosphoglycerate kinase 2, Phosphoglycerate kinase testis specific, PGK2, PGKB, PGKPS, dJ417L20.2.

    • 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 MSLSKKLTLD KLDVRGKRVI MRVDFNVPMK KNQITNNQRI KASIPSIKYC LDNGAKAVVL MSHLGRPDGV PMPDKYSLAP VAVELKSLLG KDVLFLKDCV GAEVEKACAN PAPGSVILLE NLRFHVEEEG KGQDPSGKKI KAEPDKIEAF RASLSKLGDV YVNDAFGTAH RAHSSMVGVN LPHKASGFLM KKELDYFAKA LENPVRPFLA ILGGAKVADK IQLIKNMLDK VNEMIIGGGM AYTFLKVLNN MEIGASLFDE EGAKIVKDIM AKAQKNGVRI TFPVDFVTGD KFDENAQVGK ATVASGISPG WMGLDCGPES NKNHAQVVAQ ARLIVWNGPL GVFEWDAFAK GTKALMDEIV KATSKGCITV IGGGDTATCC AKWNTEDKVS HVSTGGGASL ELLEGKILPG VEALSNM.

    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.

    Pgk2 Human
  • View Data Sheet

    Name :

    GLUL Human, Active

    Description:

    Glutamine Synthetase Human Recombinant, Active

    Glutamine synthetase, GLUL Active, GLUL, Glutamine Synthetase, Active, GLNS, GS, PIG43, PIG59, Glutamate decarboxylase (EC:4.1.1.15), Glutamate--ammonia ligase.

    Product # :

    ENZ-974

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    Description

    GLUL Recombinant Human produced in E.Coli is a single, non-glycosylated polypeptide chain containing 373 amino acids (1-373) and having a molecular mass of 42kDa.

    Source

    Escherichia Coli.

    Formulation

    GLUL protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH8.0), 10% glycerol 1mM DTT and 0.1mM PMSF.

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

    Biological Activity

    Specific activity is > 2.000 pmol/min/ug, and is defined as the amount of enzyme that convert L-glutamate to L-glutamine per miunte at pH 7.5 at 37C in coupled system with PK/LDH.

    Citations

    More Info

    • Introduction

      GLUL catalyzes the synthesis of glutamine from glutamate and ammonia. Glutamine is a major source of energy and that takes part in cell proliferation, inhibition of apoptosis, and cell signaling. GLUL is expressed during early fetal stages, and has a role in maintaining body pH by removing ammonia from circulation. Mutations in GLUL gene are related with congenital glutamine deficiency.

    • Synonyms

      Glutamine synthetase, GLUL Active, GLUL, Glutamine Synthetase, Active, GLNS, GS, PIG43, PIG59, Glutamate decarboxylase (EC:4.1.1.15), Glutamate--ammonia ligase.

    • 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

      MTTSASSHLN KGIKQVYMSL PQGEKVQAMY IWIDGTGEGL RCKTRTLDSE PKCVEELPEW NFDGSSTLQS EGSNSDMYLV PAAMFRDPFR KDPNKLVLCE VFKYNRRPAE TNLRHTCKRI MDMVSNQHPW FGMEQEYTLM GTDGHPFGWP SNGFPGPQGP YYCGVGADRA YGRDIVEAHY RACLYAGVKI AGTNAEVMPA QWEFQIGPCE GISMGDHLWV ARFILHRVCE DFGVIATFDP KPIPGNWNGA GCHTNFSTKA MREENGLKYI EEAIEKLSKR HQYHIRAYDP KGGLDNARRL TGFHETSNIN DFSAGVANRS ASIRIPRTVG QEKKGYFEDR RPSANCDPFS VTEALIRTCL LNETGDEPFQ YKN.

    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.

    Glul Human Active
  • View Data Sheet

    Name :

    UMOD Porcine

    Description:

    Uromodulin Porcine

    Tamm-Horsfall urinary glycoprotein, THP, FJHN, HNFJ, THGP, MCKD2, ADMCKD2, UMOD, Uromodulin.

    Product # :

    ENZ-733

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    Description

    Porcine Uromodulin is a 97kDa glycoprotein which is produced in the thick ascending limb of Henle´s loop and early distal convoluted tubules of the nephron.

    Source

    Porcine Urine.

    Formulation

    The UMOD protein was lyophilized from 0.4µm filtered solution at a concentration of 0.5mg/ml containing deionized water.

    Citations

    More Info

    • Introduction

      Uromodulin is the most abundant protein in normal urine. Its secretion in urine follows proteolytic cleavage of the ectodomain of its glycosyl phosphatidylinosital-anchored counterpart that is situated on the luminal cell surface of the loop of Henle. Uromodulin plays a role as a constitutive inhibitor of calcium crystallization in renal fluids. Secretion of uromodulin in urine provides protection against urinary tract infections caused by uropathogenic bacteria. Defects in Uromodulin expression are associated with the autosomal dominant renal disorders medullary cystic kidney disease-2 (MCKD2) and familial juvenile hyperuricemic nephropathy (FJHN). These disorders are characterized by juvenile onset of hyperuricemia, gout, and progressive renal failure. While several transcript variants may exist for this gene, the full-length natures of only two have been described to date. UMOD is involved in regulating the circulating activity of cytokines as it binds to il-1, il-2 and tnf with high affinity.

    • Synonyms

      Tamm-Horsfall urinary glycoprotein, THP, FJHN, HNFJ, THGP, MCKD2, ADMCKD2, UMOD, Uromodulin.

    • Physical Appearance

      Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Store lyophilized protein at -20°C. Aliquot the product after reconstitution to avoid repeated freezing/thawing cycles. Reconstituted protein can be stored at 4°C for a limited period of time; it does not show any change after two weeks at 4°C.

    • Solubility

      Add deionized water to prepare a working stock solution of approximately 0.5mg/mL and let the lyophilized pellet dissolve completely. Product is not sterile! Please filter the product by an appropriate sterile filter before using it in the cell culture.

    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.

    Umod Porcine
  • View Data Sheet

    Name :

    GSK3B Human, sf9

    Description:

    Glycogen synthase kinase-3 beta, sf9 Human Recombinant

    Glycogen synthase kinase-3 beta, GSK-3 beta, Serine/threonine-protein kinase GSK3B.

    Product # :

    PKA-084

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    Description

    GSK3B produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 426 amino acids (1-420a.a.) and having a molecular mass of 47.5kDa. GSK3B is expressed with a 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    GSK3B protein solution (0.25mg/ml) contains Phosphate Buffered Saline (pH7.4), 0.5mM PMSF and 30% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      GSK3B is a serine-threonine kinase that belongs to the glycogen synthase kinase subfamily. GSK3B is involved in energy metabolism, neuronal cell development, and body pattern formation. Polymorphisms in the GSK3B gene have been implicated in modifying risk of Parkinson disease, and studies in mice show that overexpression of the GSK3B gene may be significant to the pathogenesis of Alzheimer disease.

    • Synonyms

      Glycogen synthase kinase-3 beta, GSK-3 beta, Serine/threonine-protein kinase GSK3B.

    • 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

      MSGRPRTTSF AESCKPVQQP SAFGSMKVSR DKDGSKVTTV VATPGQGPDR PQEVSYTDTK VIGNGSFGVV YQAKLCDSGE LVAIKKVLQD KRFKNRELQI MRKLDHCNIV RLRYFFYSSG EKKDEVYLNL VLDYVPETVY RVARHYSRAK QTLPVIYVKL YMYQLFRSLA YIHSFGICHR DIKPQNLLLD PDTAVLKLCD FGSAKQLVRG EPNVSYICSR YYRAPELIFG ATDYTSSIDV WSAGCVLAEL LLGQPIFPGD SGVDQLVEII KVLGTPTREQ IREMNPNYTE FKFPQIKAHP WTKVFRPRTP PEAIALCSRL LEYTPTARLT PLEACAHSFF DELRDPNVKL PNGRDTPALF NFTTQELSSN PPLATILIPP HARIQAAAST PTNATAASDA NTGDRGQTNN AASASASNST HHHHHH.

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    Gsk3B Human Sf9
  • View Data Sheet

    Name :

    GSTM1 Human

    Description:

    Glutathione S-Transferase M1 Human Recombinant

    GST1, GSTM1-1, GSTM1a-1a, GSTM1b-1b, GTH4, GTM1, H-B, MU, MU-1, GST HB subunit 4, GST class-mu 1.

    Product # :

    ENZ-780

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    Description

    GSTM1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 203 amino acids (1-181 a.a) and having a molecular mass of 23.6kDa.GSTM1 is fused to a 22 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    GSTM1 protein solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.4M Urea and 10% glycerol.

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      Cytosolic and membrane-bound types of GST are encoded by 2 different supergene families. There are 8 classes of the soluble cytoplasmic mammalian GST: alpha, kappa, mu, omega, pi, sigma, theta and zeta. The mu class of enzymes functions in the detoxification of electrophilic compounds, including carcinogens, therapeutic drugs, environmental toxins and products of oxidative stress, by conjugation with glutathione. The genes encoding the mu class of enzymes are arranged in a gene cluster on chromosome 1p13.3 and aare highly polymorphic. These genetic differences can change an individual's resistance to carcinogens and toxins as well as affect the toxicity and efficacy of certain drugs. Null mutations of this class mu gene have been linked with the rise in a number of cancers.

    • Synonyms

      GST1, GSTM1-1, GSTM1a-1a, GSTM1b-1b, GTH4, GTM1, H-B, MU, MU-1, GST HB subunit 4, GST class-mu 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 RSMPMILGYW DIRGLAHAIR LLLEYTDSSY EEKKYTMGDA PDYDRSQWLN EKFKLGLDFP NLPYLIDGAH KITQSNAILC YIARKHNLCG ETEEEKIRVD ILENQTMDNH MQLGMICYNP EFEKLKPKYL EELPEKLKLY SEFLGKRPWF AGNKGLEKIS AYMKSSRFLP RPVFSKMAVW GNK.

    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.

    Gstm1 Human
  • View Data Sheet

    Name :

    DARS Human

    Description:

    Aspartyl-tRNA Synthetase Human Recombinant

    Aspartyl-tRNA synthetase, Cell proliferation-inducing gene 40 protein, AspRS, aspartate tRNA ligase 1 cytoplasmic, EC 6.1.1.12.

    Product # :

    ENZ-591

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    Description

    DARS Recombinant produced in E. coli is a single polypeptide chain containing 521 amino acids (1-501) and having a molecular mass of 59.3kDa.DARS is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    The DARS solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 150mM Nacl, 1mM DTT and 40% glycerol.

    Purity

    Greater than 85% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      DARS uses a 2 step reaction to catalyze the specific attachment of an amino acid to its cognate tRNA: the amino acid (AA) is first activated by ATP to form AA-AMP and then transferred to the acceptor end of the tRNA.

    • Synonyms

      Aspartyl-tRNA synthetase, Cell proliferation-inducing gene 40 protein, AspRS, aspartate tRNA ligase 1 cytoplasmic, EC 6.1.1.12.

    • 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 MPSASASRKS QEKPREIMDA AEDYAKERYG ISSMIQSQEK PDRVLVRVRD LTIQKADEVV WVRARVHTSR AKGKQCFLVL RQQQFNVQAL VAVGDHASKQ MVKFAANINK ESIVDVEGVV RKVNQKIGSC TQQDVELHVQ KIYVISLAEP RLPLQLDDAV RPEAEGEEEG RATVNQDTRL DNRVIDLRTS TSQAVFRLQS GICHLFRETL INKGFVEIQT PKIISAASEG GANVFTVSYF KNNAYLAQSP QLYKQMCICA DFEKVFSIGP VFRAEDSNTH RHLTEFVGLD IEMAFNYHYH EVMEEIADTM VQIFKGLQER FQTEIQTVNK QFPCEPFKFL EPTLRLEYCE ALAMLREAGV EMGDEDDLST PNEKLLGHLV KEKYDTDFYI LDKYPLAVRP FYTMPDPRNP KQSNSYDMFM RGEEILSGAQ RIHDPQLLTE RALHHGIDLE KIKAYIDSFR FGAPPHAGGG IGLERVTMLF LGLHNVRQTS MFPRDPKRLT P.

    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.

    Dars 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.

    Citations

    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 :

    TPMT Human

    Description:

    Thiopurine S-methyltransferase Human Recombinant

    TPMT, Thiopurine S-methyltransferase, EC 2.1.1.67, Thiopurine methyltransferase.

    Product # :

    PKA-255

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    Description

    TPMT Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 245 amino acids (1-245) and having a molecular mass of 28 kDa. Thiopurine S-methyltransferase is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    1 mg/ml solution containing 20mM Tris 8.0, 0.2mM PMSF and 2mM EDTA.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      TPMT, thiopurine S-methyltransferase, is a cytosolic enzyme that metabolizes thiopurine drugs via S-adenosyl-L-methionine as the S-methyl donor and S-adenosyl-L-homocysteine as a byproduct. TPMT activity exhibits autosomal codominant genetic polymorphism, and patients inheriting TPMT-deficiency are at high risk of potentially fatal hematopoietic toxicity.

    • Synonyms

      TPMT, Thiopurine S-methyltransferase, EC 2.1.1.67, Thiopurine methyltransferase.

    • 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

      MDGTRTSLDI EEYSDTEVQK NQVLTLEEWQ DKWVNGKTAF HQEQGHQLLK KHLDTFLKGKSGLRVFFPLC GKAVEMKWFA DRGHSVVGVE ISELGIQEFF TEQNLSYSEE PITEIPGTKVFKSSSGNISL YCCSIFDLPR TNIGKFDMIW DRGALVAINP GDRKCYADTM FSLLGKKFQY LLCVLSYDPT KHPGPPFYVP HAEIERLFGK ICNIRRLEKV DAFEERHKSW GIDCLFEKLYLLTEK.

    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.

    Tpmt Human
  • View Data Sheet

    Name :

    GGH Human

    Description:

    Gamma-Glutamyl Hydrolase Human Recombinant

    Gamma-glutamyl hydrolase (conjugase, folylpolygammaglutamyl hydrolase), Gamma-Glu-X carboxypeptidase, gamma-glutamyl hydrolase, Conjugase, GH, EC 3.4.19.9.

    Product # :

    ENZ-242

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    Description

    GGH Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 315 amino acids (25-318) and having a molecular mass of 35.9kDa.GGH is fused to a 21 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    The GGH solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 100mM NaCl, 1mM DTT and 10% glycerol.

    Purity

    Greater than 95% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      GGH is a homodimeric protein which catalyzes the cleavage of the gamma-glutamyl chain of folylpoly-gamma-glutamyl substrates. GGH is a vital enzyme in folyl and antifolyl poly-gamma-glutamate metabolism and it has a significant part in the bioavailability of dietary pteroylpolyglutamates and in the metabolism of antifolates and pteroylpolyglutamates.

    • Synonyms

      Gamma-glutamyl hydrolase (conjugase, folylpolygammaglutamyl hydrolase), Gamma-Glu-X carboxypeptidase, gamma-glutamyl hydrolase, Conjugase, GH, EC 3.4.19.9.

    • 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 MRPHGDTAKK PIIGILMQKC RNKVMKNYGR YYIAASYVKY LESAGARVVP VRLDLTEKDY EILFKSINGI LFPGGSVDLR RSDYAKVAKI FYNLSIQSFD DGDYFPVWGT CLGFEELSLL ISGECLLTAT DTVDVAMPLN FTGGQLHSRM FQNFPTELLL SLAVEPLTAN FHKWSLSVKN FTMNEKLKKF FNVLTTNTDG KIEFISTMEG YKYPVYGVQW HPEKAPYEWK NLDGISHAPN AVKTAFYLAE FFVNEARKNN HHFKSESEEE KALIYQFSPI YTGNISSFQQ CYIFD

    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.

    Ggh Human
  • View Data Sheet

    Name :

    CDK16 Human

    Description:

    Cyclin-dependent kinase 16 Human Recombinant

    Cyclin-Dependent Kinase 16, PCTK1, Serine/Threonine-Protein Kinase,  Serine/Threonine-Protein Kinase PCTAIRE-1, Cell Division Protein Kinase 16, PCTAIRE Protein Kinase 1, PCTAIRE, PCTGAIRE, EC 2.7.11.22, EC 2.7.11, PCTAIRE-Motif Protein Kinase 1, PCTAIRE1.

    Product # :

    PKA-324

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    Description

    CDK16 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 362 amino acids (158-496aa) and having a molecular mass of 41.1kDa.CDK16 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    CDK16 protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.1M NaCl and 10% glycerol.

    Purity

    Greater than 95% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      CDK16 is a member of the CDK family of serine/threonine protein kinases which are known to regulate the cell cycle. These proteins have a core kinase domain flanked by unique amino- and carboxy- terminal domains. CDK16, which is expressed mainly in mammalian brain, cooperates with an assortment of proteins, and is a part of a multiple signal transduction cascade.

    • Synonyms

      Cyclin-Dependent Kinase 16, PCTK1, Serine/Threonine-Protein Kinase, Serine/Threonine-Protein Kinase PCTAIRE-1, Cell Division Protein Kinase 16, PCTAIRE Protein Kinase 1, PCTAIRE, PCTGAIRE, EC 2.7.11.22, EC 2.7.11, PCTAIRE-Motif Protein Kinase 1, PCTAIRE1.

    • 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).Please avoid freeze thaw cycles.

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MGSGFGKLET YIKLDKLGEG TYATVYKGKS KLTDNLVALK EIRLEHEEGA PCTAIREVSL LKDLKHANIV TLHDIIHTEK SLTLVFEYLD KDLKQYLDDC GNIINMHNVK LFLFQLLRGL AYCHRQKVLH RDLKPQNLLI NERGELKLAD FGLARAKSIP TKTYSNEVVT LWYRPPDILL GSTDYSTQID MWGVGCIFYE MATGRPLFPG STVEEQLHFI FRILGTPTEE TWPGILSNEE FKTYNYPKYR AEALLSHAPR LDSDGADLLT KLLQFEGRNR ISAEDAMKHP FFLSLGERIH KLPDTTSIFA LKEIQLQKEA SLRSSSMPDS GRPAFRVVDT EF

    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.

    Cdk16 Human
  • View Data Sheet

    Name :

    TrxR Yeast

    Description:

    Thioredoxin Reductase (NADPH) Yeast Recombinant

    Thioredoxin Reductase (NADPH), NTR, TrxR.

    Product # :

    ENZ-278

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    Description

    Thioredoxin Reductase (NADPH) Yeast Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain having a molecular mass of 36 kDa. Thioredoxin Reductase is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Each mg of protein contains 20mM phosphate buffer pH 7.4.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Biological Activity

    The specific activity was found to be 5.8 IU/mg.

    Citations

    More Info

    • Introduction

      Thioredoxin reductase (TrxR/NTR), an enzyme belonging to the flavoprotein family of pyridine nucleotide-disulfide oxidoreductases. Thioredoxin reductase (TrxR), a component of the thioredoxin system, including thioredoxin (Trx) and NADPH, catalyzes the transfer of electrons from NADPH to Trx, acts as a reductant of disulfide-containing proteins and participates in the defense system against oxidative stresses.

    • Synonyms

      Thioredoxin Reductase (NADPH), NTR, TrxR.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      NTR although stable at 4°C for 3 weeks, should be stored desiccated below -18°C. Please prevent freeze thaw cycles.

    • Solubility

      It is recommended to reconstitute the lyophilized NTR in sterile 18MΩ-cm H2O.

    • Unit Definition

      One unit equals the change in absorbance at 412 nm per minute at 25°C using 0.2mM NADPH containing 5mM DTNB (pH 7.0).

    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.

    Thioredoxin Reductase Yeast
  • View Data Sheet

    Name :

    UBE2E1 Human

    Description:

    Ubiquitin Conjugating Enzyme E2E1 Human Recombinant

    Ubiquitin carrier protein E1, Ubiquitin-conjugating enzyme E2E 1 (homologous to yeast UBC4/5), Ubiquitin-protein ligase E1, UBCH6, EC 6.3.2.19.

    Product # :

    ENZ-647

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    Description

    UBE2E1 Human Recombinant produced in E. coli is a single polypeptide chain containing 216 amino acids (1-193) and having a molecular mass of 23.8 kDa.UBE2E1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    The UBE2E1 solution (1mg/1ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl and 20% glycerol.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      UBE2E1 belongs to the E2 ubiquitin-conjugating enzyme family. UBE2E1 accepts ubiquitin from the E1 complex and catalyzes its covalent attachment to other proteins. UBE2E1 catalyzes the covalent attachment of ISG15 to other proteins. UBE2E1 mediates the selective degradation of short-lived and abnormal proteins. In vitro, UBE2E1 also catalyzes 'Lys-48'-linked polyubiquitination.

    • Synonyms

      Ubiquitin carrier protein E1, Ubiquitin-conjugating enzyme E2E 1 (homologous to yeast UBC4/5), Ubiquitin-protein ligase E1, UBCH6, EC 6.3.2.19.

    • 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 MGSMSDDDSR ASTSSSSSSS SNQQTEKETN TPKKKESKVS MSKNSKLLST SAKRIQKELA DITLDPPPNC SAGPKGDNIY EWRSTILGPP GSVYEGGVFF LDITFTPEYP FKPPKVTFRT RIYHCNINSQ GVICLDILKD NWSPALTISK VLLSICSLLT DCNPADPLVG SIATQYMTNR AEHDRMARQW TKRYAT

    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.

    Ube2E1 Human
  • 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.

    Citations

    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 :

    PTRH2 Human

    Description:

    Peptidyl-tRNA Hydrolase 2 Human Recombinant

    Peptidyl-tRNA hydrolase 2, mitochondrial, PTH 2, Bcl-2 inhibitor of transcription 1, PTRH2, BIT1, PTH2, CGI-147, FLJ32471, PTRH2.

    Product # :

    ENZ-045

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    Description

    PTRH2 Human Recombinant fused with a 21 amino acid His tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 137 amino acids (64-179 a.a.) and having a molecular mass of 14.9kDa. The PTRH2 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The PTRH2 solution (1 mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 10% glycerol and 1mM DTT.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      Peptidyl-tRNA hydrolase 2 (PTRH2) is a mitochondrial protein. PTRH2 is released during apoptosis from the mitochondria to the cytoplasm. When in the cytoplasm, PTRH2 regulates the function of 2 transcriptional regulators, TLE5 and TLE1, thus promoting caspase-independent cell death. Natural substrates for PTRH2 may be petidyl-tRNAs which drop off the ribosome during protein synthesis.

    • Synonyms

      Peptidyl-tRNA hydrolase 2, mitochondrial, PTH 2, Bcl-2 inhibitor of transcription 1, PTRH2, BIT1, PTH2, CGI-147, FLJ32471, PTRH2.

    • 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 MEYKMILVVR NDLKMGKGKV AAQCSHAAVS AYKQIQRRNP EMLKQWEYCG QPKVVVKAPD EETLIALLAH AKMLGLTVSL IQDAGRTQIA PGSQTVLGIG PGPADLIDKV TGHLKLY.

    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.

    Ptrh2 Human
  • View Data Sheet

    Name :

    MAPK14 Human

    Description:

    Mitogen-Activated Protein Kinase 14 Human Recombinant

    Mitogen-activated protein kinase 14, Mitogen-activated protein kinase p38 alpha, CSBP1, CSBP2, Mxi2, PRKM14, MAP kinase p38 alpha, MAX-interacting protein 2, EXIP, PRKM15, p38, Cytokine suppressive anti-inflammatory drug-binding protein, MAP kinase MXI2, Stress-activated protein kinase 2a, RK, CSAID binding protein, p38alpha Exip, SAPK2A, EC 2.7.11, EC 2.7.11.24.

    Product # :

    PKA-014

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    Description

    MAPK14 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 383 amino acids (1-360 a.a.) and having a molecular mass of 43.7kDa.MAPK14 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    MAPK14 protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH8.0), 1mM DTT, 100mM NaCl and 10% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE analysis.

    Citations

    More Info

    • Introduction

      MAPK14 belongs to the MAP kinase family and is most associated with p38 MAP kinases(MAPKs). MAPKs are activated mainly as a reaction to cellular stress and inflammatory cytokines, and inhibitors that target the MAPK14 and MAPK11 have demonstrated ability to cure inflammatory disease. The substrates of this kinase contain transcription regulator ATF2, MEF2C, and MAX, cell cycle regulator CDC25B, and tumor suppressor p53, which demonstrate the parts of MAPK14 in stress-related transcription, cell cycle regulation and genotoxic stress response.

    • Synonyms

      Mitogen-activated protein kinase 14, Mitogen-activated protein kinase p38 alpha, CSBP1, CSBP2, Mxi2, PRKM14, MAP kinase p38 alpha, MAX-interacting protein 2, EXIP, PRKM15, p38, Cytokine suppressive anti-inflammatory drug-binding protein, MAP kinase MXI2, Stress-activated protein kinase 2a, RK, CSAID binding protein, p38alpha Exip, SAPK2A, EC 2.7.11, EC 2.7.11.24.

    • 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 MGSMSQERPT FYRQELNKTI WEVPERYQNL SPVGSGAYGS VCAAFDTKTG LRVAVKKLSR PFQSIIHAKR TYRELRLLKH MKHENVIGLL DVFTPARSLE EFNDVYLVTH LMGADLNNIV KCQKLTDDHV QFLIYQILRG LKYIHSADII HRDLKPSNLA VNEDCELKIL DFGLARHTDD EMTGYVATRW YRAPEIMLNW MHYNQTVDIW SVGCIMAELL TGRTLFPGTD HIDQLKLILR LVGTPGAELL KKISSESARN YIQSLTQMPK MNFANVFIGA NPLAVDLLEK MLVLDSDKRI TAAQALAHAY FAQYHDPDDE PVADPYDQSF ESRDLLIDEW KSLTYDEVIS FVPPPLDQEE MES.

    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.

    Mapk14 Human
  • View Data Sheet

    Name :

    RNASE3 Human

    Description:

    Ribonuclease 3 Human Recombinant

    ECP, RNS3, Ribonuclease 3, Eosinophil cationic protein, RNASE3, RNASE3.

    Product # :

    ENZ-668

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    Description

    RNASE3 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 171 amino acids (28-160) and having a molecular mass of 19.9kDa. RNASE3 is fused to a 38 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The RNASE3 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.

    Citations

    More Info

    • Introduction

      Ribonuclease 3 (RNASE3) is cytotoxin and helminthotoxin with low-efficiency ribonuclease activity. RNASE3 possesses a broad diversity of biological activities. RNASE3 protein has shown antibacterial activity such as cytoplasmic membrane depolarization of preferentially Gram-negative and Gram-positive strains and promotes E. coli outer membrane detachment, alteration of the overall cell shape and partial loss of cell content.

    • Synonyms

      ECP, RNS3, Ribonuclease 3, Eosinophil cationic protein, RNASE3, RNASE3.

    • 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 KDRWGSHMRP PQFTRAQWFA IQHISLNPPR CTIAMRAINN YRWRCKNQNT FLRTTFANVV NVCGNQSIRC PHNRTLNNCH RSRFRVPLLH CDLINPGAQN ISNCRYADRP GRRFYVVACD NRDPRDSPRY PVVPVHLDTT I.

    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.

    Rnase3 Human
  • View Data Sheet

    Name :

    CTSZ Mouse

    Description:

    Cathepsin-Z Mouse Recombinant

    Cathepsin Z, CTSZ.

    Product # :

    ENZ-934

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    Description

    CTSZ produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 292 amino acids (23-306a.a.) and having a molecular mass of 32.8kDa. (Molecular size on SDS-PAGE will appear at approximately 28-40kDa). CTSZ is expressed with an 8 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

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

    Purity

    Greater than 95% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      Cathepsin-Z (CTSZ) is a lysosomal cysteine proteinase and member of the peptidase C1 family. CTSZ, which has been also known as cathepsin X and cathepsin P, exhibits carboxy-monopeptidase and carboxy-dipeptidase activities. CTSZ is expressed ubiquitously in cancer cell lines and primary tumors and, similar to other members of this family, takes part in tumorigenesis.

    • Synonyms

      Cathepsin Z, CTSZ.

    • 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).Please avoid freeze thaw cycles.

    • Amino Acid Sequence

      ARARLYFRSG QTCYHPIRGD QLALLGRRTY PRPHEYLSPA DLPKNWDWRN VNGVNYASVT RNQHIPQYCG SCWAHGSTSA MADRINIKRK GAWPSILLSV QNVIDCGNAG SCEGGNDLPV WEYAHKHGIP DETCNNYQAK DQDCDKFNQC GTCTEFKECH TIQNYTLWRV GDYGSLSGRE KMMAEIYANG PISCGIMATE MMSNYTGGIY AEHQDQAVIN HIISVAGWGV SNDGIEYWIV RNSWGEPWGE KGWMRIVTST YKGGTGDSYN LAIESACTFG DPIVLEHHHH HH.

    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.

    Ctsz Mouse
  • View Data Sheet

    Name :

    UBE2I Human

    Description:

    Ubiquitin-Conjugating Enzyme E2I Human Recombinant

    SUMO-conjugating enzyme UBC9, EC 6.3.2.-, SUMO-protein ligase, Ubiquitin-conjugating enzyme E2 I, Ubiquitin-protein ligase I, Ubiquitin carrier protein I, Ubiquitin carrier protein 9, p18, UBC9, C358B7.1.

    Product # :

    ENZ-341

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    Description

    UBE2I Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 158 amino acids (1-158 aa) & having a molecular mass of 18.0 kDa. UBE2I is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    UBE2I (1mg/ml) contains 50mM HEPES (pH7.4) 150mM NaCl, 1mM DTT and 10% glycerol.

    Purity

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

    Citations

    More Info

    • Introduction

      Human Ubc9 is homologous to ubiquitin-conjugating enzymes (E2s). However, instead of conjugating ubiquitin, it conjugates a ubiquitin homologue, small ubiquitin-like modifier 1(SUMO-1). And hUbc9 retains striking structural and functional conservation with yeast Ubc9. The ubiquitin-dependent protein degradation system has been recognized as a complete enzymatic pathway that is responsible for the selective degradation of abnormal and short-lived proteins. The conjugation of ubiquitin requires the activities of ubiquitin-activating (E1) and –conjugating (E2) enzymes.

    • Synonyms

      SUMO-conjugating enzyme UBC9, EC 6.3.2.-, SUMO-protein ligase, Ubiquitin-conjugating enzyme E2 I, Ubiquitin-protein ligase I, Ubiquitin carrier protein I, Ubiquitin carrier protein 9, p18, UBC9, C358B7.1.

    • 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

      MSGIALSRLA QERKAWRKDH PFGFVAVPTK NPDGTMNLMN WECAIPGKKG TPWEGGLFKL RMLFKDDYPS SPPKCKFEPP LFHPNVYPSG TVCLSILEED KDWRPAITIK QILLGIQELL NEPNIQDPAQ AEAYTIYCQN RVEYEKRVRA QAKKFAPS.

    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.

    Ube2I Human
  • View Data Sheet

    Name :

    LDHA Mouse

    Description:

    Lactate Dehydrogenase A Mouse Recombinant

    L-lactate dehydrogenase A chain, LDH-A, LDH muscle subunit, LDH-M.

    Product # :

    ENZ-952

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    • Citations

    Description

    LDHA Mouse Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 340 amino acids (1-332a.a.) and having a molecular mass of 37.5kDa (Molecular size on SDS-PAGE will appear at approximately 28-40kDa). LDHA is expressed with an 8 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    LDHA 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 > 250 units/mg, and is defined as the Amount of enzyme that convert 1.0 umole of pyruvate to L-lactate and per minute at pH 7.5 at 37C.

    Citations

    More Info

    • Introduction

      LDHA catalyzes the conversion of L-lactate and NAD to pyruvate and NADH in the final step of anaerobic glycolysis. LDHA is localized primarily in muscle tissue and is part of the lactate dehydrogenase family. Mutations in LDHA have been linked to exertional myoglobinuria. LDH1 is decreased in essential thrombocythemia. LDHA is induced through a non-genomic pathway of estrogen action. Reduction in LDH-A activity results in stimulation of mitochondrial respiration and decrease of mitochondrial membrane potential.

    • Synonyms

      L-lactate dehydrogenase A chain, LDH-A, LDH muscle subunit, LDH-M.

    • 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

      MATLKDQLIV NLLKEEQAPQ NKITVVGVGA VGMACAISIL MKDLADELAL VDVMEDKLKG EMMDLQHGSL FLKTPKIVSS KDYCVTANSK LVIITAGARQ QEGESRLNLV QRNVNIFKFI IPNIVKYSPH CKLLIVSNPV DILTYVAWKI SGFPKNRVIG SGCNLDSARF RYLMGERLGV HALSCHGWVL GEHGDSSVPV WSGVNVAGVS LKSLNPELGT DADKEQWKEV HKQVVDSAYE VIKLKGYTSW AIGLSVADLA ESIMKNLRRV HPISTMIKGL YGINEDVFLS VPCILGQNGI SDVVKVTLTP EEEARLKKSA DTLWGIQKEL QFLEHHHHHH.

    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.

    Ldha Mouse
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