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Search results

1000 results found for “enterokinase”

Name

Description

Product #

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  • View Data Sheet

    Name :

    MAP2K6 Human

    Description:

    Mitogen-Activated Protein Kinase Kinase 6 Human Recombinant

    Mitogen-Activated Protein Kinase Kinase 6, PRKMK6, MEK6, MKK6, Stress-Activated Protein Kinase Kinase 3,MAPK/ERK Kinase 6, SAPK Kinase 3, EC 2.7.12.2, MAPKK, SAPKK, SAPKK3, MEK 6, Protein Kinase, Mitogen-Activated, Kinase 6 (MAP Kinase Kinase 6), Dual Specificity Mitogen-Activated Protein Kinase Kinase 6, Kinase 6 (MAP Kinase Kinase 6), MAP Kinase Kinase 6,Mitogen-Activated, Protein Kinase, SKK3.

    Product # :

    PKA-073

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    Description

    MAP2K6 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 283 amino acids (53-314 a.a) and having a molecular mass of 32kDa.MAP2K6 is fused to a 21 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    MAP2K6 protein solution (0.25mg/ml) containing 20mM Tris-HCl (pH8.0) and 10% glycerol.

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Mitogen-Activated Protein Kinase 6 (MAP2K6) is a part of the dual specificity protein kinase family. MAP2K6 phosphorylates and activates p38 MAP kinase in response to inflammatory cytokines or environmental stress. MAP2K6 is a vital component of the MAP kinase signal transduction pathway. MAP2K6 takes part in various cellular processes such as stress induced cell cycle arrest and apoptosis.

    • Synonyms

      Mitogen-Activated Protein Kinase Kinase 6, PRKMK6, MEK6, MKK6, Stress-Activated Protein Kinase Kinase 3,MAPK/ERK Kinase 6, SAPK Kinase 3, EC 2.7.12.2, MAPKK, SAPKK, SAPKK3, MEK 6, Protein Kinase, Mitogen-Activated, Kinase 6 (MAP Kinase Kinase 6), Dual Specificity Mitogen-Activated Protein Kinase Kinase 6, Kinase 6 (MAP Kinase Kinase 6), MAP Kinase Kinase 6,Mitogen-Activated, Protein Kinase, SKK3.

    • 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 MLEPIMELGR GAYGVVEKMR HVPSGQIMAV KRIRATVNSQ EQKRLLMDLD ISMRTVDCPF TVTFYGALFR EGDVWICMEL MDTSLDKFYK QVIDKGQTIP EDILGKIAVS IVKALEHLHS KLSVIHRDVK PSNVLINALG QVKMCDFGIS GYLVDEVAKE IDAGCKPYMA PERINPELNQ KGYSVKSDIW SLGITMIELA ILRFPYDSWG TPFQQLKQVV EEPSPQLPAD KFSAEFVDFT SQCLKKNSKE RPTYPELMQH PFF.

    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.

    Map2K6 Human
  • View Data Sheet

    Name :

    NTRK1 Rat

    Description:

    Neurotrophic Receptor Tyrosine Kinase 1 Rat Recombinant

    TRKA, TRK-A, NTRK-1.

    Product # :

    PKA-133

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    Description

    NTRK1 Rat Recombinant produced in HEK is a single, non-glycosylated polypeptide chain containing 623 amino acids (35-418 a.a) and having a molecular mass of 69 kDa. NTRK1 is fused to a 239 amino acid human IgG-His-tag at C-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    NTRK1 protein solution (1mg/ml) in Phosphate-Buffered Saline (pH 7.4) and 10% Glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    Biological Activity

    Measured by its ability to inhibit NGF-induced proliferation assay using TF1 human erythroleukemic cells in the presence of 0.5ng/ml of rat NGF. The ED50 range ≤ 5 ng/ml.

    More Info

    • Introduction

      NTRK1 plays a role in the development and survival of nerve cells (neurons), specifically those that transmit dataregarding senses such as touch, pain and temperatureie. sensory neurons. NTRK1 protein is located on surface cells, mainly such as sensory neurons. NTRK1 acts as a kinase enzyme that alters the activity of different proteins by adding anoxygen cluster and phosphorus atoms at precise positions ie. phosphorylation. NTRK1 activated by nerve growth factor beta which binds to it and signals the NTRK1 protein to phosphorylate itself. Post autophosphorylation, the activated NTRK1 protein phosphorylates other proteins which is required for cell growth and survival.

    • Synonyms

      TRKA, TRK-A, NTRK-1.

    • Physical Appearance

      Sterile filtered colorless solution.

    • Stability

      NTRK1 although stable at 4°C for 1 week, should be stored below -18°C. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze thaw cycles.

    • Amino Acid Sequence

      SCRETCCPVG PSGLRCTRAG TLNTLRGLRG AGNLTELYVE NQRDLQRLEF EDLQGLGELR SLTIVKSGLR FVAPDAFHFT PRLSHLNLSS NALESLSWKT VQGLSLQDLT LSGNPLHCSC ALLWLQRWEQ EDLCGVYTQK LQGSGSGDQF LPLGHNNSCG VPSVKIQMPN DSVEVGDDVF LQCQVEGQAL QQADWILTEL EGTATMKKSG DLPSLGLTLV NVTSDLNKKN VTCWAENDVG RAEVSVQVSV SFPASVHLGK AVEQHHWCIP FSVDGQPAPS LRWFFNGSVL NETSFIFTQF LESALTNETM RHGCLRLNQP THVNNGNYTL LAANPYGQAA ASIMAAFMDN PFEFNPEDPI PVSFSPVDTN STSRDPVEKK DETP LEPKSC 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.

    Ntrk1 Rat
  • View Data Sheet

    Name :

    PGK2 Human, Active

    Description:

    Phosphoglycerate Kinase 2 Human Recombinant, BioActive

    Phosphoglycerate kinase 2, dJ417L20.2, PGKB, PGKPSS, Phosphoglycerate kinase, testis specific

    Product # :

    PKA-125

    Price :

    Quantity :

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    Description

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

    Source

    Escherichia Coli.

    Formulation

    The PGK2 solution (0.5mg/ml) contains 20% glycerol, 20mM Tris-HCl buffer (pH 8.0), 1mM DTT and 0.1M NaCl.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Biological Activity

    Specific activity > 500unit/mg. One unit will convert 1 umole of 1,3-Bisphosphoglycerate to 3-PGA per minute at pH 8.0 at 37˚C.

    More Info

    • Introduction

      PGK2, also known as Phosphoglycerate kinase 2, is a testis-specific form of phosphoglycerate kinase.Originally, it was assumed that PGK2was a pseudogene. However, nowadays it is known that this protein is a functional phosphoglycerate kinase. During the Embden-Meyerhof-Parnas pathway of glycolysis, in thelater stages of spermatogenesis, the protein catalyses the reversible conversion of 1, 3- bisphosphoglycerate to 3-phosphoglycerate.

    • Synonyms

      Phosphoglycerate kinase 2, dJ417L20.2, PGKB, PGKPSS, Phosphoglycerate kinase, testis specific

    • 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 Enzyme
  • View Data Sheet

    Name :

    MAPK10 Human

    Description:

    Mitogen-Activated Protein Kinase 10 Human Recombinant

    C-Jun N-Terminal Kinase 3, MAP Kinase P49 3F12, MAP Kinase 10, PRKM10, SAPK1b, JNK3A, JNK3.

    Product # :

    PKA-115

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    • description
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    Description

    MAPK10 produced in Sf9 Insect cells is a single, glycosylated polypeptide chain containing 470 amino acids (1-464 a.a.) and having a molecular mass of 53.4kDa. MAPK10 is expressed with a 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    MAPK10 is protein solution ( 0.25mg/ml) contains Phosphate Buffered Saline (pH 7.4), 30% glycerol, 1mM DTT and 0.1mM PMSF.

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      MAPK10 is part of the MAP kinase protein family. MAP Kinases perform as assimilation point for many biochemical pathways. The enzyme also takes part in wide range of cellular pathways: differentiation, proliferation, development and transcription regulation.

    • Synonyms

      C-Jun N-Terminal Kinase 3, MAP Kinase P49 3F12, MAP Kinase 10, PRKM10, SAPK1b, JNK3A, JNK3.

    • 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

      MSLHFLYYCS EPTLDVKIAF CQGFDKQVDV SYIAKHYNMS KSKVDNQFYS VEVGDSTFTV LKRYQNLKPI GSGAQGIVCA AYDAVLDRNV AIKKLSRPFQ NQTHAKRAYR ELVLMKCVNH KNIISLLNVF TPQKTLEEFQ DVYLVMELMD ANLCQVIQME LDHERMSYLL YQMLCGIKHL HSAGIIHRDL KPSNIVVKSD CTLKILDFGL ARTAGTSFMM TPYVVTRYYR APEVILGMGY KENVDIWSVG CIMGEMVRHK ILFPGRDYID QWNKVIEQLG TPCPEFMKKL QPTVRNYVEN RPKYAGLTFP KLFPDSLFPA DSEHNKLKAS QARDLLSKML VIDPAKRISV DDALQHPYIN VWYDPAEVEA PPPQIYDKQL DEREHTIEEW KELIYKEVMN SEEKTKNGVV KGQPSPSGAA VNSSESLPPS SSVNDISSMS TDQTLASDTD SSLEASAGPL GCCRHHHHHH.

    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.

    Mapk10 Human
  • View Data Sheet

    Name :

    AMPD2 Human

    Description:

    AMPD2 Human Recombinant

    (Isoform L), EC 3.5.4.6, SPG63, AMP Deaminase Isoform L, AMP Deaminase 2, AMPD Isoform L, AMPD, PCH9, AMP deaminase 2.

    Product # :

    ENZ-835

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    Description

    AMPD2 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 667 amino acids (236-879 a.a) and having a molecular mass of 77.0kDa. AMPD2 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    AMPD2 protein solution (0.25mg/ml) containing Phosphate buffered saline (pH7.4) and 10% glycerol.

    Purity

    Greater than 85% as determined by Analysis by SDS-PAGE.

    More Info

    • Introduction

      AMPD2 is significant in purine metabolism by converting AMP to IMP. AMPD2 which functions as a homotetramer, is one of the three AMP deaminases shown in mammals. More than a few transcript variants encoding differentisoforms have been discovered for AMPD2.

    • Synonyms

      (Isoform L), EC 3.5.4.6, SPG63, AMP Deaminase Isoform L, AMP Deaminase 2, AMPD Isoform L, AMPD, PCH9, AMP deaminase 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 MGSDLLDAAK SVVRALFIRE KYMALSLQSF CPTTRRYLQQ LAEKPLETRT YEQGPDTPVS ADAPVHPPAL EQHPYEHCEP STMPGDLGLG LRMVRGVVHV YTRREPDEHC SEVELPYPDL QEFVADVNVL MALIINGPIK SFCYRRLQYL SSKFQMHVLL NEMKELAAQK KVPHRDFYNI RKVDTHIHAS SCMNQKHLLR FIKRAMKRHL EEIVHVEQGR EQTLREVFES MNLTAYDLSV DTLDVHADRN TFHRFDKFNA KYNPIGESVL REIFIKTDNR VSGKYFAHII KEVMSDLEES KYQNAELRLS IYGRSRDEWD KLARWAVMHR VHSPNVRWLV QVPRLFDVYR TKGQLANFQE MLENIFLPLF EATVHPASHP ELHLFLEHVD GFDSVDDESK PENHVFNLES PLPEAWVEED NPPYAYYLYY TFANMAMLNH LRRQRGFHTF VLRPHCGEAG PIHHLVSAFM LAENISHGLL LRKAPVLQYL YYLAQIGIAM SPLSNNSLFL SYHRNPLPEY LSRGLMVSLS TDDPLQFHFT KEPLMEEYSI ATQVWKLSSC DMCELARNSV LMSGFSHKVK SHWLGPNYTK EGPEGNDIRR TNVPDIRVGY RYETLCQELA LITQAVQSEM LETIPEEAGI TMSPGPQ.

    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.

    Ampd2 Human
  • View Data Sheet

    Name :

    Tamm Horsfall

    Description:

    Recombinant Human Tamm Horsfall Glycoprotein

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


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    ENZ-1206

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    • SDS-PAGE

    Description

    Uromodulin Human Recombinant protein produced from HEK Cells, is a polypeptide chain containing 595 amino acids ( 25-613 a.a. ) and having a total Mw of 65 kDa.

    Source

    HEK293

    Formulation

    The UMOD protein was lyophilized from 0.4μm filtered solution containing 50mM NaCl, 0.02M TRIS, pH 7.5.

    Purity

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

    SDS-PAGE

    Tamm Horsfall-SDS-PAGE - Product image 1

    More Info

    • Introduction

      Uromodulin (Tamm–Horsfall protein) is produced mainly by cells in the kidney’s thick ascending limb and is the most abundant protein in normal urine.
      Uromodulin takes part in salt and water regulation, helps prevent urinary tract infections and kidney stones, and influences inflammation and immune activity in the kidney.
      Reduced Uromodulin levels is associated with chronic kidney disease.
      UMOD mutations causes unproper protein folding and thus transported incorrectly, resulting in its accumulation inside kidney tubular cells that damages the tubules and cause kidney disease (ADTKD-UMOD), associated with high uric acid, gout, and progressive kidney failure.

    • Synonyms

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

    • Physical Appearance

      Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized UMOD although stable at room temperature for 3 weeks, should be stored at -18C. Upon reconstitution UMOD 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

      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.

    • Amino Acid Sequence

      DTSEARWCSE CHSNATCTED EAVTTCTCQE GFTGDGLTCV DLDECAIPGA HNCSANSSCV NTPGSFSCVC PEGFRLSPGL GCTDVDECAE PGLSHCHALA TCVNVVGSYL CVCPAGYRGD GWHCECSPGS CGPGLDCVPE GDALVCADPC QAHRTLDEYW RSTEYGEGYA CDTDLRGWYR FVGQGGARMA ETCVPVLRCN TAAPMWLNGT HPSSDEGIVS RKACAHWSGH CCLWDASVQV KACAGGYYVY NLTAPPECHL AYCTDPSSVE GTCEECSIDE DCKSNNGRWH CQCKQDFNIT DISLLEHRLE CGANDMKVSL GKCQLKSLGF DKVFMYLSDS RCSGFNDRDN RDWVSVVTPA RDGPCGTVLT RNETHATYSN TLYLADEIII RDLNIKINFA CSYPLDMKVS LKTALQPMVS ALNIRVGGTG MFTVRMALFQ TPSYTQPYQG SSVTLSTEAF LYVGTMLDGG DLSRFALLMT NCYATPSSNA TDPLKYFIIQ DRCPHTRDST IQVVENGESS QGRFSVQMFR FAGNYDLVYL HCEVYLCDTM NEKCKPTCSG TRFRSGSVID QSRVLNLGPI TRKGVQATVH HHHHH

    • Background

      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.

      What is the molecular weight/Mw of UMOD Protein?
      UMOD Protein has a total Mw of 65kDa.

      What is the source or expression system of UMOD Protein?
      HEK293.

      What is the Purity of UMOD Protein?
      UMOD Protein is >90% pure as determined by SDS-PAGE.

      What is the Biological Activity of UMOD Protein?
      The biological functionality of UMOD Protein will be determined in the future.

      What is the amino acid sequence of UMOD Protein?
      UMOD Protein is composed from 595 amino acids.

      What applications can UMOD Protein be used in?
      UMOD Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for UMOD Protein?
      The endotoxin level is minimal, UMOD Protein was purified using conventional chromatography techniques.

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

    Tamm Horsfall
  • View Data Sheet

    Name :

    LAP3 Human

    Description:

    Leucine Aminopeptidase 3 Human Recombinant

    Leucine Aminopeptidase 3, Peptidase S, PEPS, Proline Aminopeptidase, Leucyl Aminopeptidase, Prolyl Aminopeptidase, EC 3.4.11.1, LAP-3, LAPEP, Epididymis Secretory Protein Li 106, Cytosol Aminopeptidase, EC 3.4.11.5, HEL-S-106, EC 3.4.11, LAP, Cytosol aminopeptidase, Leucine aminopeptidase 3, Leucyl aminopeptidase, Proline aminopeptidase, Prolyl aminopeptidase.

    Product # :

    ENZ-889

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    Description

    LAP3 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 539 amino acids (1-519 a.a) and having a molecular mass of 58.3kDa. LAP3 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    LAP3 protein solution (0.5mg/ml) containing 20mM Tris-HCl(pH8.5), 50% glycerol, 5mM DTT and 1mM EDTA.

    Purity

    Greater than 85% as determined by SDS-PAGE.

    More Info

    • Introduction

      Leucine Aminopeptidase 3 also known as LAP3 is a member of the peptidase M17 family. LAP3 is implicated in the processing as well as regular turnover of intracellular proteins. LAP3 catalyzes the removal of unsubstituted N-terminal amino acids from different peptides. LAP3 is responsible of releasing an N-terminal amino acid, Xaa-|-Yaa-, in which Xaa is preferably Leu, but could be other amino acids including Pro although not Arg or Lys, and Yaa may be Pro. Amino acid amides and methyl esters are as well readily hydrolyzed; however rates on arylamides are exceedingly low.

    • Synonyms

      Leucine Aminopeptidase 3, Peptidase S, PEPS, Proline Aminopeptidase, Leucyl Aminopeptidase, Prolyl Aminopeptidase, EC 3.4.11.1, LAP-3, LAPEP, Epididymis Secretory Protein Li 106, Cytosol Aminopeptidase, EC 3.4.11.5, HEL-S-106, EC 3.4.11, LAP, Cytosol aminopeptidase, Leucine aminopeptidase 3, Leucyl aminopeptidase, Proline aminopeptidase, Prolyl aminopeptidase.

    • 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 MFLLPLPAAG RVVVRRLAVR RFGSRSLSTA DMTKGLVLGI YSKEKEDDVP QFTSAGENFD KLLAGKLRET LNISGPPLKA GKTRTFYGLH QDFPSVVLVG LGKKAAGIDE QENWHEGKEN IRAAVAAGCR QIQDLELSSV EVDPCGDAQA AAEGAVLGLY EYDDLKQKKK MAVSAKLYGS GDQEAWQKGV LFASGQNLAR QLMETPANEM TPTRFAEIIE KNLKSASSKT EVHIRPKSWI EEQAMGSFLS VAKGSDEPPV FLEIHYKGSP NANEPPLVFV GKGITFDSGG ISIKASANMD LMRADMGGAA TICSAIVSAA KLNLPINIIG LAPLCENMPS GKANKPGDVV RAKNGKTIQV DNTDAEGRLI LADALCYAHT FNPKVILNAA TLTGAMDVAL GSGATGVFTN SSWLWNKLFE ASIETGDRVW RMPLFEHYTR QVVDCQLADV NNIGKYRSAG ACTAAAFLKE FVTHPKWAHL DIAGVMTNKD EVPYLRKGMT GRPTRTLIEF LLRFSQDNA.

    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.

    Lap3 Human
  • View Data Sheet

    Name :

    TOP1 Human

    Description:

    DNA Topoisomerase-I Human Recombinant

    DNA topoisomerase 1, EC 5.99.1.2, DNA topoisomerase I, TOP1, Scl-70.

    Product # :

    ENZ-306

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    Description

    DNA Topoisomerase-I Human Recombinant produced in SF9 is a glycosylated, polypeptide chain having a molecular mass of 102 kDa. The TOP1 is expressed with a -6xHis tag and purified by proprietary chromatographic techniques.

    Source

    Sf9 insect cells.

    Formulation

    TOP1 is supplied in 16mM HEPES buffer pH-7.5, 400mM sodium chloride, and 20% glycerol.

    Purity

    Greater than 95% as determined by SDS-PAGE.

    More Info

    • Introduction

      DNA toposisomerase I is a key nuclear enzyme that interconverts supercoiled DNA to the required topological conformations for normal DNA replication and transcription. This enzyme is the target antigen for the so-called Scl-70 autoantibodies. Scl-70 antibodies are a specific marker in Scleroderma patients (specificity 98-100%) and are associated with the presence of diffuse skin involvement and pulmonary fibrosis.
      In human tissues the DNA topoisomerase I is initially synthesized as a protein with 100 kDa molecular weight. Most of this precursor is then proteolytically processed to a species with 70 kDa molecular weight from which the Scl-70 antigen has derived its name.

    • Synonyms

      DNA topoisomerase 1, EC 5.99.1.2, DNA topoisomerase I, TOP1, Scl-70.

    • 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. 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.

    Top1 Human
  • View Data Sheet

    Name :

    PSAT1 Human

    Description:

    Phosphoserine Aminotransferase 1 Human Recombinant

    Phosphoserine aminotransferase, Phosphohydroxythreonine aminotransferase, PSAT, PSAT1, PSA, EPIP.

    Product # :

    ENZ-209

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    Description

    PSAT1 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 394 amino acids (1-370) and having a molecular mass of 42.9kDa.PSAT1 is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The PSAT1 solution (1mg/ml) contains 20mM Tris-HCl buffer (pH8.0), 20% glycerol and 1mM DTT.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Phosphoserine aminotransferase (PSAT1) catalyzes the conversion of 3-phosphohydroxypyruvate into 3-phosphoserine which is dephosphorylated consequently by phosphoserine phosphatase to form L-serine. PSAT1 is probably a phosphoserine aminotransferase, based on similarity to proteins in mouse, rabbit, and Drosophila. PSAT1 is expressed at high levels in the brain, liver, kidney and pancreas, and very weakly expressed in the thymus, prostate, testis and colon. Defects in the PSAT1 gene are the cause of phosphoserine aminotransferase deficiency (PSATD). PSATD is distinguished biochemically by low plasma and cerebrospinal fluid concentrations of serine and glycine and clinically by intractable seizures, acquired microcephaly, hypertonia, and psychomotor retardation.

    • Synonyms

      Phosphoserine aminotransferase, Phosphohydroxythreonine aminotransferase, PSAT, PSAT1, PSA, EPIP.

    • 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 MGSHMDAPRQ VVNFGPGPAK LPHSVLLEIQ KELLDYKGVG ISVLEMSHRS SDFAKIINNT ENLVRELLAV PDNYKVIFLQ GGGCGQFSAV PLNLIGLKAG RCADYVVTGA WSAKAAEEAK KFGTINIVHP KLGSYTKIPD PSTWNLNPDA SYVYYCANET VHGVEFDFIP DVKGAVLVCD MSSNFLSKPV DVSKFGVIFA GAQKNVGSAG VTVVIVRDDL LGFALRECPS VLEYKVQAGN SSLYNTPPCF SIYVMGLVLE WIKNNGGAAA MEKLSSIKSQ TIYEIIDNSQ GFYVCPVEPQ NRSKMNIPFR IGNAKGDDAL EKRFLDKALE LNMLSLKGHR SVGGIRASLY NAVTIEDVQK LAAFMKKFLE MHQL.

    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.

    Psat1 Human
  • View Data Sheet

    Name :

    PCYT2 Human

    Description:

    Phosphate Cytidylyltransferase 2 Human Recombinant

    MEA-phosphate cytidylyltransferase, CTP:phospho MEA cytidylyltransferase, Phosphoryl MEA transferase, PCYT2, ET.

    Product # :

    ENZ-221

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    Description

    PCYT2 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 409 amino acids (1-389) and having a molecular mass of 45.9kDa.PCYT2 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The PCYT2 solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH8.0), 20% glycerol, 0.1M NaCl, 1mM DTT and 0.1mM PMSF.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      PCYT2 is a member of the cytidylyltransferase family. PCYT2 is an enzyme which catalyzes the formation of CDP-MEA from CTP and phospho MEA in the Kennedy pathway of phospholipid synthesis. PCYT2 has the strongest expression in the liver, heart, and skeletal muscle.

    • Synonyms

      MEA-phosphate cytidylyltransferase, CTP:phospho MEA cytidylyltransferase, Phosphoryl MEA transferase, PCYT2, ET.

    • 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 MIRNGRGAAG GAEQPGPGGR RAVRVWCDGC YDMVHYGHSN QLRQARAMGD YLIVGVHTDE EIAKHKGPPV FTQEERYKMV QAIKWVDEVV PAAPYVTTLE TLDKYNCDFC VHGNDITLTV DGRDTYEEVK QAGRYRECKR TQGVSTTDLV GRMLLVTKAH HSSQEMSSEY REYADSFGKC PGGRNPWTGV SQFLQTSQKI IQFASGKEPQ PGETVIYVAG AFDLFHIGHV DFLEKVHRLA ERPYIIAGLH FDQEVNHYKG KNYPIMNLHE RTLSVLACRY VSEVVIGAPY AVTAELLSHF KVDLVCHGKT EIIPDRDGSD PYQEPKRRGI FRQIDSGSNL TTDLIVQRII TNRLEYEARN QKKEAKELAF LEAARQQAAQ PLGERDGDF.

    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.

    Pcyt2 Human
  • View Data Sheet

    Name :

    DYRK1A Human

    Description:

    Dual-Specificity Tyrosine-(Y)-Phosphorylation Regulated 1A Human Recombinant

    Dual Specificity Yak1-related kinase, Dyrk; PSK47, Dual specificity tyrosine-phosphorylation-regulated kinase 1A, Dual specificity YAK1-related kinase, Protein kinase minibrain homolog, RP86, Dyrk1a, MNBH.

    Product # :

    PKA-310

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    Description

    DYRK1A Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 343 amino acids (159-479a.a) and having a molecular mass of 39.4kDa. DYRK1A is fused to a 22 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The DYRK1A solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 10% glycerol and 0.4M Urea.

    Purity

    Greater than 80% as determined by SDS-PAGE.

    More Info

    • Introduction

      Dual-Specificity Tyrosine-(Y)-Phosphorylation Regulated 1A (DYRK1A) belongs to the dual-specificity tyrosine phosphorylation-regulated kinase (DYRK) family. DYRK1A includes a nuclear targeting signal sequence, a leucine zipper motif and a protein kinase domain. DYRK1A catalyzes its autophosphorylation on serine/threonine and tyrosine residues and takes part in a signaling pathway regulating cell proliferation. DYRK1A has a substrate preference for proline at position P+1 and arginine at position P-3.

    • Synonyms

      Dual Specificity Yak1-related kinase, Dyrk; PSK47, Dual specificity tyrosine-phosphorylation-regulated kinase 1A, Dual specificity YAK1-related kinase, Protein kinase minibrain homolog, RP86, Dyrk1a, MNBH.

    • 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 RSYEIDSLIG KGSFGQVVKA YDRVEQEWVA IKIIKNKKAF LNQAQIEVRL LELMNKHDTE MKYYIVHLKR HFMFRNHLCL VFEMLSYNLY DLLRNTNFRG VSLNLTRKFA QQMCTALLFL ATPELSIIHC DLKPENILLC NPKRSAIKIV DFGSSCQLGQ RIYQYIQSRF YRSPEVLLGM PYDLAIDMWS LGCILVEMHT GEPLFSGANE VDQMNKIVEV LGIPPAHILD QAPKARKFFE KLPDGTWSLK KTKDGKREYK PPGTRKLHNI LGVETGGPGG RRAGESGHTV ADYLKFKDLI LRMLDYDPKT RIQPYYALQH SFF.

    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.

    Dyrk1A Human
  • View Data Sheet

    Name :

    PRKAG1 Human

    Description:

    Protein Kinase, AMP-Activated, Gamma 1 Human Recombinant

    Protein Kinase AMP-Activated Gamma 1 Non-Catalytic Subunit, 5'-AMP-Activated Protein Kinase Subunit Gamma-1, AMPK Gamma1 Chain, AMPKg.

    Product # :

    PKA-305

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    Description

    PRKAG1 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 354 amino acids (1-331) and having a molecular mass of 40.0kDa.PRKAG1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The PRKAG1 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.

    More Info

    • Introduction

      PRKAG1 is a regulatory subunit of the AMP-activated protein kinase (AMPK). AMPK is a heterotrimer comprised of an alpha catalytic subunit, and non-catalytic beta and gamma subunits. AMPK is a vital energy-sensing enzyme which supervises cellular energy status. PRKAG1 is one of the gamma regulatory subunits of AMPK. Alternatively spliced transcript variants encoding dissimilar isoforms were found.

    • Synonyms

      Protein Kinase AMP-Activated Gamma 1 Non-Catalytic Subunit, 5'-AMP-Activated Protein Kinase Subunit Gamma-1, AMPK Gamma1 Chain, AMPKg.

    • 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 MGSMETVISS DSSPAVENEH PQETPESNNS VYTSFMKSHR CYDLIPTSSK LVVFDTSLQV KKAFFALVTN GVRAAPLWDS KKQSFVGMLT ITDFINILHR YYKSALVQIY ELEEHKIETW REVYLQDSFK PLVCISPNAS LFDAVSSLIR NKIHRLPVID PESGNTLYIL THKRILKFLK LFITEFPKPE FMSKSLEELQ IGTYANIAMV RTTTPVYVAL GIFVQHRVSA LPVVDEKGRV VDIYSKFDVI NLAAEKTYNN LDVSVTKALQ HRSHYFEGVL KCYLHETLET IINRLVEAEV HRLVVVDEND VVKGIVSLSD ILQALVLTGG EKKP

    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.

    Prkag1 Human
  • View Data Sheet

    Name :

    UBE2G2 Human

    Description:

    Ubiquitin-Conjugating Enzyme E2G2 Human Recombinant

    Ubiquitin-conjugating enzyme E2 G2, E2 ubiquitin-conjugating enzyme G2, Ubiquitin carrier protein G2, Ubiquitin-protein ligase G2, UBE2G2, Ubiquitin-Conjugating Enzyme E2G2, Ubiquitin-conjugating enzyme E2 G2 isoform 1, UBC7.

    Product # :

    ENZ-884

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    Description

    UBE2G2 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 188 amino acids (1-165a.a.) and having a molecular mass of 21kDa.UBE2G2 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    UBE2G2 protein solution (1mg/ml) containing Phosphate buffered saline (pH7.4), 10% glycerol and 1mM DTT.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Ubiquitin-Conjugating Enzyme E2G2 (UBE2G2) is a protein coding gene which is a part of the E2 ubiquitin-conjugating enzyme family. UBE2G2 accepts ubiquitin from the E1 complex and catalyzes its covalent attachment to various proteins. UBE2G2 is ubiquitously expressed mainly in adult muscle. UBE2G2 also takes part in endoplasmic reticulum-associated degradation (ERAD).

    • Synonyms

      Ubiquitin-conjugating enzyme E2 G2, E2 ubiquitin-conjugating enzyme G2, Ubiquitin carrier protein G2, Ubiquitin-protein ligase G2, UBE2G2, Ubiquitin-Conjugating Enzyme E2G2, Ubiquitin-conjugating enzyme E2 G2 isoform 1, UBC7.

    • 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 MGSMAGTALK RLMAEYKQLT LNPPEGIVAG PMNEENFFEW EALIMGPEDT CFEFGVFPAI LSFPLDYPLS PPKMRFTCEM FHPNIYPDGR VCISILHAPG DDPMGYESSA ERWSPVQSVE KILLSVVSML AEPNDESGAN VDASKMWRDD REQFYKIAKQ IVQKSLGL.

    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.

    Ube2G2 Human
  • View Data Sheet

    Name :

    DECR1 Human

    Description:

    2,4-Dienoyl CoA Reductase 1 Human Recombinant

    2,4-dienoyl-CoA reductase, mitochondrial, 2,4-dienoyl-CoA reductase [NADPH], 4-enoyl-CoA reductase [NADPH], DECR1, DECR, NADPH, SDR18C1.

    Product # :

    ENZ-102

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    Description

    DECR1 Human Recombinant fused to 21 amino acid His Tag at N-terminal produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 322 amino acids (35-335 a.a.) and having a molecular mass of 34.4kDa. The DECR1 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The DECR1 solution contains 20mM Tris-HCl buffer (pH 8.0), 10% glycerol and 1mM DTT.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      DECR1 is a mitochondrial protein which exists as a homotetramer and is a member of a family of short-chain dehydrogenases/reductases. DECR1 acts as an auxiliary enzyme of beta-oxidation andt partakes in the metabolism of unsaturated fatty enoyl-CoA esters. in particular, DECR1 uses NADP+ to catalyze the reduction of 2,4-dienoyl-CoA to yield trans-3-enoyl-CoA that can subsequently be used as an intermediate in the Krebs cycle. Furthermore, DECR1 is believed to work as a tumor suppressor, possibly downregulating the expression of Neu and slowing the rate of tumorigenesis.

    • Synonyms

      2,4-dienoyl-CoA reductase, mitochondrial, 2,4-dienoyl-CoA reductase [NADPH], 4-enoyl-CoA reductase [NADPH], DECR1, DECR, NADPH, SDR18C1.

    • 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 MNTEALQSKF FSPLQKAMLP PNSFQGKVAF ITGGGTGLGK GMTTLLSSLG AQCVIASRKM DVLKATAEQI SSQTGNKVHA IQCDVRDPDM VQNTVSELIK VAGHPNIVIN NAAGNFISPT ERLSPNAWKT ITDIVLNGTA FVTLEIGKQL IKAQKGAAFL SITTIYAETG SGFVVPSASA KAGVEAMSKS LAAEWGKYGM RFNVIQPGPI KTKGAFSRLD PTGTFEKEMI GRIPCGRLGT VEELANLAAF LCSDYASWIN GAVIKFDGGE EVLISGEFND LRKVTKEQWD TIEELIRKTK GS.

    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.

    Decr1 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 :

    PGAM2 Human

    Description:

    Phosphoglycerate Mutase 2 Human Recombinant

    Phosphoglycerate mutase 2, BPG-dependent PGAM 2, Muscle-specific phosphoglycerate mutase, Phosphoglycerate mutase isozyme M, PGAM-M, PGAM2, PGAMM, GSD10.

    Product # :

    ENZ-578

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    Description

    PGAM2 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 273 amino acids (1-253) and having a molecular mass of 30.9kDa.PGAM2 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The PGAM2 solution (1mg/ml) contains 20mM Tris-HCl buffer (pH8.0), 20% glycerol, 0.1M NaCl and 1mM DTT.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Phosphoglycerate mutase 2 (PGAM2) is a member of the phosphoglycerate mutase family. PGAM is a dimeric enzyme which contains in separate tissues, different proportions of a slow-migrating muscle (MM) isozyme, a fast-migrating brain (BB) isozyme, and a hybrid form (MB). PGAM (Phosphoglycerate mutase) catalyzes the reversible reaction of 3-phosphoglycerate (3-PGA) to 2-phosphoglycerate (2-PGA) in the glycolytic pathway. PGAM2 gene mutations cause muscle phosphoglycerate mutase efficiency, otherwise known as glycogen storage disease X.

    • Synonyms

      Phosphoglycerate mutase 2, BPG-dependent PGAM 2, Muscle-specific phosphoglycerate mutase, Phosphoglycerate mutase isozyme M, PGAM-M, PGAM2, PGAMM, GSD10.

    • 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 MATHRLVMVR HGESTWNQEN RFCGWFDAEL SEKGTEEAKR GAKAIKDAKM EFDICYTSVL KRAIRTLWAI LDGTDQMWLP VVRTWRLNER HYGGLTGLNK AETAAKHGEE QVKIWRRSFD IPPPPMDEKH PYYNSISKER RYAGLKPGEL PTCESLKDTI ARALPFWNEE IVPQIKAGKR VLIAAHGNSL RGIVKHLEGM SDQAIMELNL PTGIPIVYEL NKELKPTKPM QFLGDEETVR KAMEAVAAQG KAK.

    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.

    Pgam2 Human
  • View Data Sheet

    Name :

    RNLS Human

    Description:

    Renalase Human Recombinant

    Renalase FAD-Dependent Amine Oxidase, Chromosome 10 Open Reading Frame 59, Monoamine Oxidase-C, C10orf59, FLJ11218, Renalase, MAO-C, EC 1.4.-.-.

    Product # :

    ENZ-653

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    Description

    RNLS Human Recombinant produced in E. coli is a single polypeptide chain containing 349 amino acids (18-342) and having a molecular mass of 38.8 kDa.RNLS is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    The RNLS solution contains 20mM Tris-HCl buffer (pH 8.0), 2M Urea and 10% glycerol.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    More Info

    • Introduction

      Renalase (RNLS) is a flavin adenine dinucleotide-dependent amine oxidase which is secreted into the blood from the kidney. RNLS acts as a hormone which metabolizes circulating catecholamines that have an active role in the sympathetic and parasympathetic nervous systems. High catecholamine concentration activates plasma RNLS and promotes its secretion and synthesis.

    • Synonyms

      Renalase FAD-Dependent Amine Oxidase, Chromosome 10 Open Reading Frame 59, Monoamine Oxidase-C, C10orf59, FLJ11218, Renalase, MAO-C, EC 1.4.-.-.

    • 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 MGSMALLRRQ TSGPLYLAVW DKAEDSGGRM TTACSPHNPQ CTADLGAQYI TCTPHYAKKH QRFYDELLAY GVLRPLSSPI EGMVMKEGDC NFVAPQGISS IIKHYLKESG AEVYFRHRVT QINLRDDKWE VSKQTGSPEQ FDLIVLTMPV PEILQLQGDI TTLISECQRQ QLEAVSYSSR YALGLFYEAG TKIDVPWAGQ YITSNPCIRF VSIDNKKRNI ESSEIGPSLV IHTTVPFGVT YLEHSIEDVQ ELVFQQLENI LPGLPQPIAT KCQKWRHSQV TNAAANCPGQ MTLHHKPFLA CGGDGFTQSN FDGCITSALC VLEALKNYI

    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.

    Rnls Human
  • View Data Sheet

    Name :

    REXO2 Human

    Description:

    RNA Exonuclease 2 Human Recombinant

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

    Product # :

    ENZ-715

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    Description

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

    Source

    Escherichia Coli.

    Formulation

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

    Purity

    Greater than 90% as determined by SDS-PAGE.

    More Info

    • Introduction

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

    • Synonyms

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

    • Physical Appearance

      Sterile Filtered colorless solution.

    • Stability

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

    • Amino Acid Sequence

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

    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.

    Rexo2 Human
  • View Data Sheet

    Name :

    FUT5 Human

    Description:

    Fucosyltransferase 5 Human Recombinant

    FUT-5

    Product # :

    ENZ-1199

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    Description

    The FUT5 Human is created as a recombinant protein with a 4kda N-terminal fusion of His Tag. The FUT5 His-Tagged Fusion Protein produced in E. coli, is a 30kDa protein containing 172 amino acid residues of the FUT5 Human, 203-374 amino acids.

    Source

    Escherichia Coli.

    Formulation

    Each mg was lyophilized with 1xPBS, 0.4% SDS and 4mM DTT.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    More Info

    • Synonyms

      FUT-5

    • Physical Appearance

      Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Store lyophilized FUT5 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

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

    • Background

      Fucosyltransferase 5 also known as FUT5 is a glycosyltransferase which takes part in the biosynthesis of glycolipids and glycoproteins. FUT5 mainly catalyzes the transfer of fucose (a monosaccharide) to the type 2 chain of oligosaccharides (Galβ1-4GlcNAc). FUT5 takes an important part in various biological processes which include regulation of inflammation, cell-cell interactions and immune response modulation. FUT5 is expressed mainly in tissues such as the pancreas, liver and various immune cells.

    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.

    Fut5 Human
  • View Data Sheet

    Name :

    MMP9 Mouse

    Description:

    Matrix Metalloproteinase-9 Mouse Recombinant

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

    Product # :

    ENZ-1177

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    Description

    MMP9 Mouse produced in Sf9 Insect cells is a single, glycosylated polypeptide chain containing 717 amino acids (20-730 a.a.) and having a molecular mass of 79.3 kDa. MMP9 is expressed with a 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    MMP9 Mouse protein solution (0.25mg/ml) contains 20mM Tris-HCl pH-7.5, 10mM CaCl2, 100mM NaCl, 0.05% Brij35 and 10% glycerol.

    Purity

    Greater than 85% as determined by SDS-PAGE.

    Biological Activity

    Defined as the amount of enzyme that cleaves 1pmol of Mca-PLGLDpa-AR-NH2 per minute at pH 7.5 at 25C. Specific activity is > 500 pmol/min/ug.

    More Info

    • Introduction

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

    • Synonyms

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

    • Physical Appearance

      Sterile Filtered colorless solution.

    • Stability

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

    • Amino Acid Sequence

      APYQRQPTFV VFPKDLKTSN LTDTQLAEAY LYRYGYTRAA QMMGEKQSLR PALLMLQKQL SLPQTGELDS QTLKAIRTPR CGVPDVGRFQ TFKGLKWDHH NITYWIQNYS EDLPRDMIDD AFARAFAVWG EVAPLTFTRV YGPEADIVIQ FGVAEHGDGY PFDGKDGLLA HAFPPGAGVQ GDAHFDDDEL WSLGKGVVIP TYYGNSNGAP CHFPFTFEGR SYSACTTDGR NDGTPWCSTT ADYDKDGKFG FCPSERLYTE HGNGEGKPCV FPFIFEGRSY SACTTKGRSD GYRWCATTAN YDQDKLYGFC PTRVDATVVG GNSAGELCVF PFVFLGKQYS SCTSDGRRDG RLWCATTSNF DTDKKWGFCP DQGYSLFLVA AHEFGHALGL DHSSVPEALM YPLYSYLEGF PLNKDDIDGI QYLYGRGSKP DPRPPATTTT EPQPTAPPTM CPTIPPTAYP TVGPTVGPTG APSPGPTSSP SPGPTGAPSP GPTAPPTAGS SEASTESLSP ADNPCNVDVF DAIAEIQGAL HFFKDGWYWK FLNHRGSPLQ GPFLTARTWP ALPATLDSAF EDPQTKRVFF FSGRQMWVYT GKTVLGPRSL DKLGLGPEVT HVSGLLPRRL GKALLFSKGR VWRFDLKSQK VDPQSVIRVD KEFSGVPWNS HDIFQYQDKA YFCHGKFFWR VSFQNEVNKV DHEVNQVDDV GYVTYDLLQC P-HHHHHH

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

    Mmp9 Mouse
  • View Data Sheet

    Name :

    Phosphotransacetylase

    Description:

    Phosphotransacetylase Bacillus S. Recombinant

    Phosphate Acetyltransferase, EC 2.3.1.8, Phosphotransacetylase, phosphoacylase.

    Product # :

    ENZ-1205

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    Description

    Phosphotransacetylase Bacillus Stearothermophilus Recombinant produced in E.Coli is a single, non glycosylated polypeptide chain containing 325 amino acids and having a total molecular mass of 34.7kDa.
    Phosphotransacetylase Recombinant is purified by proprietary chromatographic techniques.

    Source

    E.Coli

    Formulation

    The protein was lyophilized with 0.15M NaCl and 20mM Tris pH-8.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Biological Activity

    Phosphotransacetylase activity is assessed by using the DTNB spectrophotometric method which was found to be greater than 3,000 Units/mg.

    More Info

    • Introduction

      Phosphotransacetylase (PTA) is a metabolic enzyme (EC 2.3.1.8) that catalyzes the reversible conversion: acetyl-CoA + Pi ⇄ acetyl-phosphate + CoA. The reversible reaction of acetyl-CoA to acetate node and back, is useful in R&D and biotech assays such as Metabolic engineering, Synthetic biology, Production of biopolymers, Enzymatic synthesis of acetyl-phosphate, bacterial signaling
      and Fermentation.  Phosphotransacetylase controls acetate formation and manipulates acetyl-CoA flux thus is widely used in protein expression, metabolic engineering, and synthetic pathways.

    • Synonyms

      Xylosyltransferase 2, Peptide O-xylosyltransferase 1, Xylosyltransferase II, XT-II, XylT-II, XYLT2, XT2.

    • Physical Appearance

      Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized Phosphate Acetyltransferase although stable at room temperature for 3 weeks, should be stored desiccated below -18C. Upon reconstitution Phosphate Acetyltransferase 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 Phosphate Acetyltransferase in
      sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be
      further diluted to other aqueous solutions.

    • Amino Acid Sequence

      TTDLFTALKA KVTGTARKIV FPEGTDDRIL TAASRLATEQ VLQPIVLGDE QAIRVKAAAL GLPLEGVEIV NPRRYGGFDE LVSAFVERRK GKVTEETARE LLFDENYFGT MLVYMGAADG LVSGAAHSTA DTVRPALQII KTKPGVGKTS GVFIMVRGDE KYVFADCAIN IAPNSQDLAE IAVESARTAK MFGLKPRVAL LSFSTKGSAS SPETEKVVEA VRLAKEMAPD LILDGEFQFD AAFVPEVAKK KAPDSVIQGD ANVFIFPSLE AGNIGYKIAQ RLGGFEAVGP ILQGLNKPVN DLSRGCSAED AYKLALITAA QSLGE

    • Unit Definition

      1 unit will convert 1umole of Coenzyme A to acetyl coenzyme A /min/pH-7.5/30˚C using acetyl phosphate as substrate

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    Phosphotransacetylase
  • View Data Sheet

    Name :

    DCXR Human, Bioactive

    Description:

    Dicarbonyl/L-Xylulose Reductase Human Recombinant, Bioactive

    DCR, HCR2, HCRII, KIDCR, P34H, SDR20C1, Dicarbonyl/L-Xylulose Reductase, EC=1.1.1.10, Carbonyl reductase II, Kidney dicarbonyl reductase, Sperm surface protein P34H.

    Product # :

    ENZ-1029

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    Description

    DCXR Recombinant Human produced in E.Coli is a single, non-glycosylated polypeptide chain containing 264 amino acids (1-244 a.a.) and having a molecular mass of 28 kDa. The DCXR is fused to a 20 amino acids His-Tag at N-terminus and purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The DCXR (0.5mg/ml) solution containing 20mM Tris-HCl buffer (pH 8.0), 1mM DTT, 20% glycerol and 50mM NaCl.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Biological Activity

    Specific activity is > 1,800 pmol/min/ug and is defined as the amount of enzyme that oxidize 1pmole of xylitol to L-xylulose per minute at pH 10.0 at 37C.

    More Info

    • Introduction

      DCXR catalyzes the NADPH-dependent reduction of numerous pentoses, tetroses, trioses, alpha-dicarbonyl molecules and L-xylulose. DCXR takes part in the uronate cycle of glucose metabolism. DCXR participates in the water absorption and cellular osmoregulation in the proximal renal tubules by producing xylitol, an osmolyte, thus preventing osmolytic stress from occurring in the renal tubules.

    • Synonyms

      DCR, HCR2, HCRII, KIDCR, P34H, SDR20C1, Dicarbonyl/L-Xylulose Reductase, EC=1.1.1.10, Carbonyl reductase II, Kidney dicarbonyl reductase, Sperm surface protein P34H.

    • 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 MELFLAGRRV LVTGAGKGIG RGTVQALHAT GARVVAVSRT QADLDSLVRE CPGIEPVCVD LGDWEATERA LGSVGPVDLL VNNAAVALLQ PFLEVTKEAF DRSFEVNLRA VIQVSQIVAR GLIARGVPGA IVNVSSQCSQ RAVTNHSVYC STKGALDMLT KVMALELGPH KIRVNAVNPT VVMTSMGQAT WSDPHKAKTM LNRIPLGKFA EVEHVVNAIL FLLSDRSGMT TGSTLPVEGG FWAC.

    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.

    Dcxr Human Bioactive
  • View Data Sheet

    Name :

    FARS2 Human

    Description:

    Phenylalanyl-tRNA Synthetase 2 Human Recombinant

    Phenylalanyl-tRNA synthetase mitochondrial, Phenylalanine--tRNA ligase, PheRS, FARS2, FARS1, HSPC320, dJ520B18.2.

    Product # :

    ENZ-111

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    • description
    • source
    • formulation
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    • More Info

    Description

    FARS2 produced in E.Coli is a single, non-glycosylated polypeptide chain containing 436 amino acids (37-451 a.a.) and having a molecular mass of 50.6kDa.FARS2 is fused to a 21 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    FARS2 solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 1mM DTT, 30% glycerol, 1mM EDTA and 0.1M NaCl.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Phenylalanyl-tRNA synthetase 2 mitochondrial (FARS2) is a member of the class II aminoacyl- tRNA synthetase family. FARS2 is a mitochondrial matrix protein. FARS2 when acting as a monomer, catalyzes the ATP-dependent conversion of L-phenylalanine and tRNA (Phe) to L-phenlalanyltRNA (Phe), an event which is vital for proper translation and protein expression.

    • Synonyms

      Phenylalanyl-tRNA synthetase mitochondrial, Phenylalanine--tRNA ligase, PheRS, FARS2, FARS1, HSPC320, dJ520B18.2.

    • 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 MPAAECATQR APGSVVELLG KSYPQDDHSN LTRKVLTRVG RNLHNQQHHP LWLIKERVKE HFYKQYVGRF GTPLFSVYDN LSPVVTTWQN FDSLLIPADH PSRKKGDNYY LNRTHMLRAH TSAHQWDLLH AGLDAFLVVG DVYRRDQIDS QHYPIFHQLE AVRLFSKHEL FAGIKDGESL QLFEQSSRSA HKQETHTMEA VKLVEFDLKQ TLTRLMAHLF GDELEIRWVD CYFPFTHPSF EMEINFHGEW LEVLGCGVME QQLVNSAGAQ DRIGWAFGLG LERLAMILYD IPDIRLFWCE DERFLKQFCV SNINQKVKFQ PLSKYPAVIN DISFWLPSEN YAENDFYDLV RTIGGDLVEK VDLIDKFVHP KTHKTSHCYR ITYRHMERTL SQREVRHIHQ ALQEAAVQLL GVEGRF.

    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.

    Fars2 Human
  • View Data Sheet

    Name :

    CTSZ Human, Sf9

    Description:

    Cathepsin-Z Human Recombinant, Sf9

    Cathepsin Z, Cathepsin X, Cysteine-Type Carboxypeptidase, Lysosomal Carboxypeptidase B, Carboxypeptidase LB, Cathepsin B2, Cathepsin IV, Cathepsin Z1, Cathepsin P, Cathepsin Y, EC 3.4.18.1, Preprocathepsin P, CTSX.

    Product # :

    ENZ-1097

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    • description
    • source
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    • More Info

    Description

    CTSZ produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 288 amino acids (24-303.a.) and having a molecular mass of 32.5kDa. (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 10% glycerol & Phosphate Buffered Saline (pH 7.4).

    Purity

    Greater than 95% as determined by SDS-PAGE.

    Biological Activity

    The specific activity is determent as the ability of 1 unit to convert 1.0 pmole of Mca-PLGL-Dpa-AR-NH2 to MCA- Pro-Leu-OH per minute at pH 3.5 at 25C and is > 1,400 pmol/min/ug.

    More Info

    • Introduction

      Cathepsin-Z (CTSZ) is a lysosomal cysteine proteinase and a member of the peptidase C1 family. CTSZ, which is known also 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 as other members of this family, takes part in tumorigenesis.

    • Synonyms

      Cathepsin Z, Cathepsin X, Cysteine-Type Carboxypeptidase, Lysosomal Carboxypeptidase B, Carboxypeptidase LB, Cathepsin B2, Cathepsin IV, Cathepsin Z1, Cathepsin P, Cathepsin Y, EC 3.4.18.1, Preprocathepsin P, CTSX.

    • 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

      GLYFRRGQTC YRPLRGDGLA PLGRSTYPRP HEYLSPADLP KSWDWRNVDG VNYASITRNQ
      HIPQYCGSCW AHASTSAMAD RINIKRKGAW PSTLLSVQNV IDCGNAGSCE GGNDLSVWDY
      AHQHGIPDET CNNYQAKDQE CDKFNQCGTC NEFKECHAIR NYTLWRVGDY GSLSGREKMM
      AEIYANGPIS CGIMATERLA NYTGGIYAEY QDTTYINHVV SVAGWGISDG TEYWIVRNSW
      GEPWGERGWL RIVTSTYKDG KGARYNLAIE EHCTFGDPIV LEHHHHHH

    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.

    Cathepsin Z Protein
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