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Search results

1000 results found for “Enterokinase”

Name

Description

Product #

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  • View Data Sheet

    Name :

    Placental Lactogen Caprine

    Description:

    Placental Lactogen Caprine Recombinant

    Chorionic Somatomammotropin Hormone 1, CSH1, CS-1, hCS, PL.

    Product # :

    CYT-510

    Price :

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    • description
    • source
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    • purity
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    • More Info

    Description

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

    Source

    Escherichia Coli.

    Formulation

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

    Purity

    Greater than 99.0% as determined by:
    (a) Gel filtration analysis.
    (b) Analysis by SDS-PAGE.

    Biological Activity

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

    More Info

    • Introduction

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

    • Synonyms

      Chorionic Somatomammotropin Hormone 1, CSH1, CS-1, hCS, PL.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized caprine recombinant placental lactogen although stable at room temperature for several weeks, should be stored desiccated below -18C. Upon reconstitution of caprine recombinant placental lactogen at > 0.1 mg/ml and up to 4 mg/ml and filter sterilization caprine recombinant placental lactogen can be stored at 4C for several weeks.

    • Solubility

      It is recommended to reconstitute the lyophilized caprine recombinant placental lactogen in sterile water or 0.4% NaHCO3 adjusted tp pH 8-9, not less than 100µg/ml, which can then be further diluted to other aqueous solutions, preferably in presence of carrier protein.

    • Amino Acid Sequence

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

    • Protein content

      UV spectroscopy at 280 nm using the absorbency value of 0.85 as the extinction coefficient for a 0.1% (1mg/ml) solution. This value is calculated by the PC GENE computer analysis program of protein sequences (IntelliGenetics).

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

    Placental Lactogen Caprine
  • View Data Sheet

    Name :

    METTL1 Human

    Description:

    Methyltransferase Like 1 Human Recombinant

    Methyltransferase-Like 1, TRM8, tRNA(m7G46)-methyltransferase, tRNA (guanine-N(7)-)-methyltransferase , C12orf1, YDL201w, D1075-like gene product, FLJ95748, EC 2.1.1.33.

    Product # :

    ENZ-054

    Price :

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    Description

    Recombinant Human METTL1 produced in E.Coli is a single, non-glycosylated polypeptide chain containing 296 amino acids (1-276a.a.) and having a molecular mass of 33.6kDa.METTL1 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The METTL1 protein solution (0.5mg/1ml) is formulated in 20mM Tris-HCl buffer (pH8.0)
    1mM DTT, 50mM NaCl and 10% glycerol.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    More Info

    • Introduction

      METTL1 is recognized as tRNA (guanine-N(7)-)-methyltransferase that is a part of the methyltransferase superfamily. METTL1 displays high sequence similarity to yeast ORF YDL201w and can be inactivated by phosphorylation. METTL1 protein has a conserved S-adenosylmethionine-binding motif and ccatalyzes the formation of N(7)-methylguanine at position 46 (m7G46) in tRNA.

    • Synonyms

      Methyltransferase-Like 1, TRM8, tRNA(m7G46)-methyltransferase, tRNA (guanine-N(7)-)-methyltransferase , C12orf1, YDL201w, D1075-like gene product, FLJ95748, EC 2.1.1.33.

    • 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 MAAETRNVAG AEAPPPQKRY YRQRAHSNPM ADHTLRYPVK PEEMDWSELY PEFFAPLTQN QSHDDPKDKK EKRAQAQVEF ADIGCGYGGL LVELSPLFPD TLILGLEIRV KVSDYVQDRI RALRAAPAGG FQNIACLRSN AMKHLPNFFY KGQLTKMFFL FPDPHFKRTK HKWRIISPTL LAEYAYVLRV GGLVYTITDV LELHDWMCTH FEEHPLFERV PLEDLSEDPV VGHLGTSTEE GKKVLRNGGK NFPAIFRRIQ DPVLQAVTSQ TSLPGH

    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.

    Mettl1 Human
  • View Data Sheet

    Name :

    TOP1 Bovine

    Description:

    DNA Topoisomerase-I Bovine

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

    Product # :

    ENZ-656

    Price :

    Quantity :

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    • More Info

    Description

    Bovine DNA Topoisomerase-I shows multiple bands between 76-109 KDa and is purified from bovine tissues by proprietary chromatographic techniques.

    Source

    Bovine tissues.

    Formulation

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

    Purity

    Greater than 95% as determined by SDS-PAGE.

    More Info

    • Introduction

      TOP1 is an important nuclear enzyme that interconverts supercoiled DNA to the necessary topological conformations for standard DNA replication and transcription. TOP1 is the target antigen for TOP1 autoantibodies. TOP1 antibodies are a specific marker in scleroderma patients (specificity 98-100%) and are related with the existence of diffuse skin involvement and pulmonary fibrosis. In human tissues top1 enzyme is primarily synthesized as a protein with a molecular weight of 100-kDa. Most of this precursor is then proteolytically processed to a 70-kDa size, from which the TOP1 antigen has derived its name.

    • Synonyms

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

    • 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.

    • Immunological Functions

      1. Binds IgG-type human auto-antibodies. 2. Standard ELISA test (checkerboard analysis of positive/negative samples) and immunodot test with positive/negative samples.

    • coating concentration

      0.5-0.8 µg/ml (depending on the type of ELISA plate and coating buffer). Suitable for labeling of functional groups.

    • Applications

      Western blot with anti TOP1 autoantibody positive sample.

    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 Bovine
  • View Data Sheet

    Name :

    GPT2 Human

    Description:

    Glutamic-Pyruvate Transaminase 2 Human Recombinant

    ALT2, AAT2, Alanine aminotransferase 2, Glutamate pyruvate transaminase 2, Glutamic--alanine transaminase 2, Glutamic--pyruvic transaminase 2.

    Product # :

    ENZ-680

    Price :

    Quantity :

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    Description

    GPT2 Human Recombinant produced in E. coli is a single polypeptide chain containing 546 amino acids (1-523) and having a molecular mass of 60.3 kDa. GPT2 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    The GPT2 solution (0.5mg/1ml) contains 20mM Tris-HCl buffer (pH 7.5), 30% glycerol, 0.2M NaCl and 2mM DTT.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    More Info

    • Introduction

      Alanine aminotransferase 2 (GPT2), catalyzes the reversible transamination among alanine and 2-oxoglutarate to create pyruvate and glutamate. GPT2 expressed mainly in muscle, fat and kidney and participates in the intermediary metabolism of glucose and amino acids. Multiple transcript variants encoding various isoforms have been found for GPT2.

    • Synonyms

      ALT2, AAT2, Alanine aminotransferase 2, Glutamate pyruvate transaminase 2, Glutamic--alanine transaminase 2, Glutamic--pyruvic transaminase 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 MGSMQRAAAL VRRGCGPRTP SSWGRSQSSA AAEASAVLKV RPERSRRERI LTLESMNPQV KAVEYAVRGP IVLKAGEIEL ELQRGIKKPF TEVIRANIGD AQAMGQQPIT FLRQVMALCT YPNLLDSPSF PEDAKKRARR ILQACGGNSL GSYSASQGVN CIREDVAAYI TRRDGGVPAD PDNIYLTTGA SDGISTILKI LVSGGGKSRT GVMIPIPQYP LYSAVISELD AIQVNYYLDE ENCWALNVNE LRRAVQEAKD HCDPKVLCII NPGNPTGQVQ SRKCIEDVIH FAWEEKLFLL ADEVYQDNVY SPDCRFHSFK KVLYEMGPEY SSNVELASFH STSKGYMGEC GYRGGYMEVI NLHPEIKGQL VKLLSVRLCP PVSGQAAMDI VVNPPVAGEE SFEQFSREKE SVLGNLAKKA KLTEDLFNQV PGIHCNPLQG AMYAFPRIFI PAKAVEAAQA HQMAPDMFYC MKLLEETGIC VVPGSGFGQR EGTYHFRMTI LPPVEKLKTV LQKVKDFHIN FLEKYA.

    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.

    Gpt2 Human
  • View Data Sheet

    Name :

    MMP23B Human

    Description:

    Matrix Metallopeptidase 23B Human Recombinant

    Matrix Metallopeptidase 23B, MMP23B, MMP22, Matrix Metalloproteinase 23B, Matrix Metalloproteinase 22, Matrix Metalloproteinase In The Female Reproductive Tract, Matrix Metalloproteinase-21, Matrix Metalloproteinase-22, MIFR-1, MMP-21, MMP-22, MMP-23, MIFR, MMP23A, Matrix Metalloproteinase-23, EC 3.4.24.-, Femalysin, MMP21.

    Product # :

    ENZ-793

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    Description

    MMP23B Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 199 amino acids (79-254) and having a molecular mass of 22.6kDa.MMP23B is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The MMP23B solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.4M Urea and 10% glycerol.

    Purity

    Greater than 85% as determined by SDS-PAGE.

    More Info

    • Introduction

      Matrix Metallopeptidase 23B (MMP23B) belongs to the matrix metalloproteinase (MMP) family, and it is section of a duplicated region of chromosome 1p36.3. MMP23B is a protease. MMP23B regulates the surface expression of some potassium channels by holding them in the endoplasmic reticulum. Members of the matrix metalloproteinase (MMP) family are involved in the breakdown of extracellular matrix in normal physiological processes, such as embryonic development, reproduction, and tissue remodeling, as well as in disease processes, such as arthritis and metastasis.

    • Synonyms

      Matrix Metallopeptidase 23B, MMP23B, MMP22, Matrix Metalloproteinase 23B, Matrix Metalloproteinase 22, Matrix Metalloproteinase In The Female Reproductive Tract, Matrix Metalloproteinase-21, Matrix Metalloproteinase-22, MIFR-1, MMP-21, MMP-22, MMP-23, MIFR, MMP23A, Matrix Metalloproteinase-23, EC 3.4.24.-, Femalysin, MMP21.

    • 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 MGSYTLTPAR LRWDHFNLTY RILSFPRNLL SPRETRRALA AAFRMWSDVS PFSFREVAPE QPSDLRIGFY PINHTDCLVS ALHHCFDGPT GELAHAFFPP HGGIHFDDSE YWVLGPTRYS WKKGVWLTDL VHVAAHEIGH ALGLMHSQHG RALMHLNATL RGWKALSQDE LWGLHRLYG.

    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.

    Mmp23B Human
  • View Data Sheet

    Name :

    IMMP2L Human

    Description:

    IMP2 Inner Mitochondrial Membrane Peptidase-Like Human Recombinant

    IMP2 Inner Mitochondrial Membrane Peptidase-Like (S. Cerevisiae), IMP2, IMP2 Inner Mitochondrial Membrane Protease-Like (S. Cerevisiae), IMMP2L Intronic Transcript 1 (Non-Protein Coding), Mitochondrial Inner Membrane Protease Subunit, Inner Mitochondrial Membrane Peptidase 2 Like, IMP2-Like Protein, EC 3.4.21.- , IMMP2L-IT1, IMP2-LIKE, EC 3.4.21, Mitochondrial inner membrane protease subunit 2.

    Product # :

    ENZ-822

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    Description

    IMMP2L Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 161 amino acids (38-175aa) and having a molecular mass of 18.0kDa. IMMP2L is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    IMMP2L protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 50% glycerol and 1mM DTT.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      IMP2 Inner Mitochondrial Membrane Peptidase-Like (IMMP2L) is implicated in processing the signal peptide sequences, IMMP2L is used to direct mitochondrial proteins to the mitochondria. IMMP2L resides in the mitochondria and is one of the essential proteins for the catalytic activity of the mitochondrial inner membrane peptidase (IMP) complex. Two variants which encode the same protein have been found for IMMP2L.

    • Synonyms

      IMP2 Inner Mitochondrial Membrane Peptidase-Like (S. Cerevisiae), IMP2, IMP2 Inner Mitochondrial Membrane Protease-Like (S. Cerevisiae), IMMP2L Intronic Transcript 1 (Non-Protein Coding), Mitochondrial Inner Membrane Protease Subunit, Inner Mitochondrial Membrane Peptidase 2 Like, IMP2-Like Protein, EC 3.4.21.- , IMMP2L-IT1, IMP2-LIKE, EC 3.4.21, Mitochondrial inner membrane protease subunit 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 MGSRVEGASM QPSLNPGGSQ SSDVVLLNHW KVRNFEVHRG DIVSLVSPKN PEQKIIKRVI ALEGDIVRTI GHKNRYVKVP RGHIWVEGDH HGHSFDSNSF GPVSLGLLHA HATHILWPPE RWQKLESVLP PERLPVQREE E.

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

    Immp2L Human
  • 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 :

    XYLT2 Human

    Description:

    Xylosyltransferase 2 Human Recombinant

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

    Product # :

    ENZ-1086

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    Description

    XYLT2 Human Recombinant is a single, glycosylated polypeptide chain containing 839 amino acids (Gly37-Arg865, luminal domain, isoform 1, natural variant with Thr305) and having a molecular mass of 94.0kDa. XYLT2 is fused to an N-terminal linker (2 extra a.a), C-terminal linker (2 extra a.a) and C-terminal His-tag (6 extra a.a).

    Source

    HEK293 Cells.

    Formulation

    XYLT2 filtered (0.4 µm) and lyophilized in 0.05 M PBS and 0.075 M NaCl, pH 7.4.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      XYLT2 or Xylosyltransferase 2 is an enzyme which is expressed in ubiquitous and is part of the glycosyltransfe-rases family. XYLT2 promotes proteoglycans formation by attaching GAG chains to the substrate protein via transfer of xylose molecule from the donor (nucleoside diphosphate) to the protein’s serine residues. XYLT2 is present in the ER and the cis part of the Golgi, furthermore the protein is released to the extracellular matrix.

    • Synonyms

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

    • 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

      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. XYLT2 is not sterile! Please filter the product by an appropriate sterile filter before using it in the cell culture.

    • Amino Acid Sequence

      ASGLEEDEAG EKGRQRKPRP LDPGEGSKDT DSSAGRRGST GRRHGRWRGR AESPGVPVAK VVRAVTSRQR ASRRVPPAPP PEAPGRQNLS GAAAGEALVG AAGFPPHGDT GSVEGAPQPT DNGFTPKCEI VGKDALSALA RASTKQCQQE IANVVCLHQA GSLMPKAVPR HCQLTGKMSP GIQWDESQAQ QPMDGPPVRI AYMLVVHGRA IRQLKRLLKA VYHEQHFFYI HVDKRSDYLH REVVELAQGY DNVRVTPWRM VTIWGGASLL TMYLRSMRDL LEVPGWAWDF FINLSATDYP TRTNEELVAF LSKNRDKNFL KSHGRDNSRF IKKQGLDRLF HECDSHMWRL GERQIPAGIV VDGGSDWFVL TRSFVEYVVY TDDPLVAQLR QFYTYTLLPA ESFFHTVLEN SLACETLVDN NLRVTNWNRK LGCKCQYKHI VDWCGCSPND FKPQDFLRLQ QVSRPTFFAR KFESTVNQEV LEILDFHLYG SYPPGTPALK AYWENTYDAA DGPSGLSDVM LTAYTAFARL SLHHAATAAP PMGTPLCRFE PRGLPSSVHL YFYDDHFQGY LVTQAVQPSA QGPAETLEMW LMPQGSLKLL GRSDQASRLQ SLEVGTDWDP KERLFRNFGG LLGPLDEPVA VQRWARGPNL TATVVWIDPT YVVATSYDIT VDTETEVTQY KPPLSRPLRP GPWTVRLLQF WEPLGETRFL VLPLTFNRKL PLRKDDASWL HAGPPHNEYM EQSFQGLSSI LNLPQPELAE EAAQRHTQLT GPALEAWTDR ELSSFWSVAG LCAIGPSPCP SLEPCRLTSW SSLSPDPKSE LGPVKADGRL RKLHHHHHH.

    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.

    Xylt2 Human
  • View Data Sheet

    Name :

    HARS Human, His

    Description:

    Histidyl-tRNA Synthetase Human Recombinant, His Tag

    Histidyl-tRNA synthetase cytoplasmic, Histidine--tRNA ligase, HisRS, HARS, HRS, FLJ20491.

    Product # :

    ENZ-001

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    Description

    HARS Human Recombinant fused with a 23 amino acid His tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 532 amino acids (1-509 a.a.) and having a molecular mass of 59.4kDa. The HARS is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

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

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Histidyl-tRNA synthetase (HARS) functions to catalyze the aminoacylation of tRNAs by their corresponding amino acids. HARS is a member of the class II family of aminoacyl-tRNA synthetases. HARS is responsible for the synthesis of histidyl-transfer RNA, which is vital for the incorporation of histidine into proteins. HARS is a frequent target of autoantibodies in the human autoimmune disease polymyositis/dermatomyositis.

    • Synonyms

      Histidyl-tRNA synthetase cytoplasmic, Histidine--tRNA ligase, HisRS, HARS, HRS, FLJ20491.

    • 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 MGSMAERAAL EELVKLQGER VRGLKQQKAS AELIEEEVAK LLKLKAQLGP DESKQKFVLK TPKGTRDYSP RQMAVREKVF DVIIRCFKRH GAEVIDTPVF ELKETLMGKY GEDSKLIYDL KDQGGELLSL RYDLTVPFAR YLAMNKLTNI KRYHIAKVYR RDNPAMTRGR YREFYQCDFD IAGNFDPMIP DAECLKIMCE ILSSLQIGDF LVKVNDRRIL DGMFAICGVS DSKFRTICSS VDKLDKVSWE EVKNEMVGEK GLAPEVADRI GDYVQQHGGV SLVEQLLQDP KLSQNKQALE GLGDLKLLFE YLTLFGIDDK ISFDLSLARG LDYYTGVIYE AVLLQTPAQA GEEPLGVGSV AAGGRYDGLV GMFDPKGRKV PCVGLSIGVE RIFSIVEQRL EALEEKIRTT ETQVLVASAQ KKLLEERLKL VSELWDAGIK AELLYKKNPK LLNQLQYCEE AGIPLVAIIG EQELKDGVIK LRSVTSREEV DVRREDLVEE IKRRTGQPLC IC.

    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.

    Hars Human
  • View Data Sheet

    Name :

    PRSS3 Human

    Description:

    Protease Serine 3 Human Recombinant

    Protease Serine 3 (Mesotrypsin), Protease Serine 4 (Trypsin 4, Brain), Brain Trypsinogen, Mesotrypsinogen, Trypsin III, Trypsinogen IV, Trypsinogen 5, Pancreatic Trypsinogen III, MTG, TRY3, PRSS4, T9, EC 3.4.21.

    Product # :

    ENZ-735

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    Description

    PRSS3 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 247 amino acids (81-304) and having a molecular mass of 26.0kDa.PRSS3 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The PRSS3 solution contains 20mM Tris-HCl buffer (pH 8.0), 0.4M Urea and 10% glycerol.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    More Info

    • Introduction

      PRSS3 is a trypsinogen, and a member of the trypsin family of serine proteases. PRSS3 is expressed in the pancreas and brain and is unaffected by common trypsin inhibitors. It is active on peptide linkages involving the carboxyl group of lysine or arginine. PRSS3 is restricted to the locus of T cell receptor beta variable orphans on chromosome 9. 4 different isoforms encoded by 4 transcript variants were identified for this gene.

    • Synonyms

      Protease Serine 3 (Mesotrypsin), Protease Serine 4 (Trypsin 4, Brain), Brain Trypsinogen, Mesotrypsinogen, Trypsin III, Trypsinogen IV, Trypsinogen 5, Pancreatic Trypsinogen III, MTG, TRY3, PRSS4, T9, EC 3.4.21.

    • 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 MGSIVGGYTC EENSLPYQVS LNSGSHFCGG SLISEQWVVS AAHCYKTRIQ VRLGEHNIKV LEGNEQFINA AKIIRHPKYN RDTLDNDIML IKLSSPAVIN ARVSTISLPT APPAAGTECL ISGWGNTLSF GADYPDELKC LDAPVLTQAE CKASYPGKIT NSMFCVGFLE GGKDSCQRDS GGPVVCNGQL QGVVSWGHGC AWKNRPGVYT KVYNYVDWIK DTIAANS

    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.

    Prss3 Human
  • View Data Sheet

    Name :

    Streptolysin-O

    Description:

    Streptolysin-O Streptococcus Pyogenes Recombinant

    Streptolysin O, Thiol-activated cytolysin, slo.

    Product # :

    PRO-2302

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    Description

    Recombinant Streptococcus Pyogenes Streptolysin-O produced in E.coli is a single, non-glycosylated, polypeptide chain containing 538 amino acids and having a molecular mass of 60.1kDa.The Streptolysin-O is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Streptolysin-O protein was lyophilized from a 0.2µm filtered concentrated solution in PBS, pH 7.4.

    Purity

    Greater than 97.0% as determined by
    (a) Analysis by RP-HPLC.
    (b) Analysis by SDS-PAGE.

    More Info

    • Introduction

      Streptolysin-O is a sulfhydryl-activated toxin which causes cytolysis by forming pores in cholesterol containing host membranes. After binding to target membranes, the Streptolysin-O protein undergoes a major conformation change, leading to its insertion in the host membrane and creation of an oligomeric pore complex. Cholesterol may be needed for binding to host membranes, membrane insertion and pore formation. Streptolysin-O can be reversibly inactivated by oxidation.

    • Synonyms

      Streptolysin O, Thiol-activated cytolysin, slo.

    • Physical Appearance

      Sterile Filtered white lyophilized powder.

    • Stability

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

    • Solubility

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

    • Amino Acid Sequence

      NKQNTASTET TTTNEQPKPE SSELTTEKAG QKTDDMLNSN DMIKLAPKEM PLESAEKEEK KSEDKKKSEE DHTEEINDKI YSLNYNELEV LAKNGETIEN FVPKEGVKKA DKFIVIERKK KNINTTPVDI SIIDSVTDRT YPAALQLANK GFTENKPDAV VTKRNPQKIH IDLPGMGDKA TVEVNDPTYA NVSTAIDNLV NQWHDNYSGG NTLPARTQYT ESMVYSKSQI EAALNVNSKI LDGTLGIDFK SISKGEKKVM IAAYKQIFYT VSANLPNNPA DVFDKSVTFK ELQRKGVSNE APPLFVSNVA YGRTVFVKLE TSSKSNDVEA AFSAALKGTD VKTNGKYSDI LENSSFTAVV LGGDAAEHNK VVTKDFDVIR NVIKDNATFS RKNPAYPISY TSVFLKNNKI AGVNNRTEYV ETTSTEYTSG KINLSHQGAY VAQYEILWDE INYDDKGKEV ITKRRWDNNW YSKTSPFSTV IPLGANSRNI RIMARECTGL AWEWWRKVID ERDVKLSKEI NVNISGSTLS PYGSITYK.

    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.

    Streptolysin O
  • View Data Sheet

    Name :

    ACP6 Human

    Description:

    Acid Phosphatase-6 Human Recombinant

    Acid Phosphatase 6, Lysophosphatidic, Acid Phosphatase-Like Protein 1, PACPL1, ACPL1, LPAP, Lysophosphatidic Acid Phosphatase Type 6, Lysophosphatidic Acid Phosphatase 6, Acid Phosphatase Like 1, EC 3.1.3.2, Lysophosphatidic acid phosphatase type 6.

    Product # :

    ENZ-865

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    Description

    ACP6 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 419 amino acids (33-428a.a) and having a molecular mass of 47.7kDa. ACP6 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    ACP6 protein solution (1mg/ml) containing Phosphate buffered saline (pH7.4), 30% glycerol and 1mM DTT.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Biological Activity

    Specific activity is > 1000 units/mg, and is defined as the amount of enzyme which hydrolyze 1.0 nmoles of p-nitrophenyl phosphate (pNPP) per minute at PH 5.0 at 37C.

    More Info

    • Introduction

      Acid Phosphatase-6, also known as ACP6 is Hydrolyzes lysophosphatidic acid (LPA) which contains a medium length fatty acid chain to the corresponding monoacylglycerol. ACP6 shows highest activity with lysophosphatidic acid which contains myristate (C14:0), monounsaturated oleate (C18:1) or palmitate (C16:0), and lower activity with C18:0 as well as C6:0 lysophosphatidic acid.

    • Synonyms

      Acid Phosphatase 6, Lysophosphatidic, Acid Phosphatase-Like Protein 1, PACPL1, ACPL1, LPAP, Lysophosphatidic Acid Phosphatase Type 6, Lysophosphatidic Acid Phosphatase 6, Acid Phosphatase Like 1, EC 3.1.3.2, Lysophosphatidic acid phosphatase type 6.

    • 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 MGSELQEADG QCPVDRSLLK LKMVQVVFRH GARSPLKPLP LEEQVEWNPQ LLEVPPQTQF DYTVTNLAGG PKPYSPYDSQ YHETTLKGGM FAGQLTKVGM QQMFALGERL RKNYVEDIPF LSPTFNPQEV FIRSTNIFRN LESTRCLLAG LFQCQKEGPI IIHTDEADSE VLYPNYQSCW SLRQRTRGRR QTASLQPGIS EDLKKVKDRM GIDSSDKVDF FILLDNVAAE QAHNLPSCPM LKRFARMIEQ RAVDTSLYIL PKEDRESLQM AVGPFLHILE SNLLKAMDSA TAPDKIRKLY LYAAHDVTFI PLLMTLGIFD HKWPPFAVDL TMELYQHLES KEWFVQLYYH GKEQVPRGCP DGLCPLDMFL NAMSVYTLSP EKYHALCSQT QVMEVGNEE.

    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.

    Acp6 Human
  • View Data Sheet

    Name :

    GPT2 Mouse, Active

    Description:

    Glutamic-Pyruvate Transaminase 2, Active Mouse Recombinant

    ALT2, AAT2, Alanine aminotransferase 2, Glutamate pyruvate transaminase 2, Glutamic--alanine transaminase 2, Glutamic--pyruvic transaminase 2.

    Product # :

    ENZ-1110

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    Description

    GPT2 Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 542 amino acids (1-522 aa) and having a molecular mass of 60.1kDa.GPT2 is fused to a 20 amino acid His tag at N-terminus and purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The GPT2 solution (1 mg/ml) contains 2mM DTT, 20% Glycerol and 20mM Tris-HCl (pH7.5).

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

    Biological Activity

    Specific activity is > 50 units/mg. Measured by the amount of enzyme that cleaves 1umole of L-Alanineto L-Glutamate per minute at pH7.5 at 37C˚.

    More Info

    • Introduction

      Glutamic-Pyruvate Transaminase 2 (GPT2) catalyzes the reversible transamination among alanine and 2-oxoglutarate to create pyruvate and glutamate. GPT2 expressed mainly in muscle, fat and kidney and participates in the intermediary metabolism of glucose and amino acids.

    • Synonyms

      ALT2, AAT2, Alanine aminotransferase 2, Glutamate pyruvate transaminase 2, Glutamic--alanine transaminase 2, Glutamic--pyruvic transaminase 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 MQRAAVLVRR GSCPRASGPW GRSHSSAAAE ASAALKVRPE
      RSPRDRILTL ESMNPQVKAV EYAVRGPIVL KAGEIEMELQ RGIKKPFTEV IRANIGDAHA
      MGQQPITFLR QVMALCTYPN LLNSPSFPED AKKRARRILQ ACGGNSLGSY SASQGVNCIR
      EDVAAFITRR DGVPADPDNI YLTTGASDGI STILKLLVSG GGKSRTGVMI PIPQYPLYSA
      VISELDAVQV NYYLDEENCW ALNVDELRRA LRQAKDHCDP KVLCIINPGN PTGQVQSRKC
      IEDVIHFAWE EKLFLLADEV YQDNVYSPDC RFHSFKKVLY QMGHEYSSNV ELASFHSTSK
      GYMGECGYRG GYMEVINLHP EIKGQLVKLL SVRLCPPVSG QAAMDIVVNP PEPGEESFEQ
      FSREKEFVLG NLAKKAKLTE DLFNQVPGIQ CNPLQGAMYA FPRILIPAKA VEAAQSHKMA
      PDMFYCMKLL EETGICVVPG SGFGQREGTY HFRMTILPPV DKLKTVLHKV KDFHLKFLEQ YS

    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.

    Gpt 2 Mouse
  • View Data Sheet

    Name :

    MMP9 Mouse

    Description:

    Matrix Metalloproteinase-9 Mouse Recombinant

    AW743869, Matrix metalloproteinase-9, 92 kDa type IV collagenase, Gelatinase B, GELB, Mmp9, MANDP2, B/MMP, B/MMP9, Clg4, Clg4b, Gel B, MMP-9, pro-MMP-9, 92 kDa gelatinase.

    Product # :

    ENZ-1191

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    Description

    MMP9 Mouse Recombinant produced in HEK cells is a single, glycosylated, polypeptide chain (20-730 a.a) containing a total of 717 amino acids, having a molecular mass of 79.3kDa. MMP9 is fused to a 6 amino acid His-tag at C-terminus,and is purified by proprietary chromatographic techniques.

    Source

    HEK293 Cells.

    Formulation

    MMP9 protein solution (1mg/ml) containing 10% glycerol, 20mM Tris-HCl (pH 7.5), 1mM CaCl2 and 0.1M NaCl.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    Biological Activity

    Specific activity is greater than 1,500 pmol/min/ug and is defined by the amount of enzyme that cleaves 1pmole of  Mca-PLGLDpa-AR-NH2 per minute at pH 7.5 at 37˚C.

    More Info

    • Synonyms

      AW743869, Matrix metalloproteinase-9, 92 kDa type IV collagenase, Gelatinase B, GELB, Mmp9, MANDP2, B/MMP, B/MMP9, Clg4, Clg4b, Gel B, MMP-9, pro-MMP-9, 92 kDa gelatinase.

    • 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

      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 PHHHHHH.

    • Background

      The MMP9 mouse recombinant, a variant of the matrix metalloproteinase 9 enzyme, has emerged as a crucial focus of biomedical research due to its diverse biological functions and potential implications in various physiological and pathological processes. Matrix metalloproteinase 9 (MMP9) is a key enzyme involved in extracellular matrix remodeling, cell migration, and tissue homeostasis. The MMP9 mouse recombinant, generated through recombinant DNA technology, offers a valuable tool for investigating the molecular characteristics and biological roles of this enzyme.

      Understanding the molecular characteristics of MMP9 is vital to unravel its functional significance. MMP9 belongs to the matrix metalloproteinase family, characterized by their ability to degrade various components of the extracellular matrix. MMP9 exhibits unique structural features, including a catalytic domain, a hemopexin-like domain, and a prodomain that regulates its activation. These characteristics contribute to the complexity of MMP9 and its involvement in multiple physiological and pathological processes.

      MMP9 plays diverse roles in different biological contexts. It is involved in tissue remodeling processes, such as embryogenesis, wound healing, and tissue repair. Additionally, MMP9 participates in inflammatory responses, immune cell recruitment, and angiogenesis. The precise mechanisms underlying these functions are still being elucidated, highlighting the need for further investigation.

      The MMP9 mouse recombinant offers exciting prospects for research and therapeutic applications. By utilizing this recombinant protein, scientists can investigate the role of MMP9 in disease progression, explore its interactions with other molecules, and potentially develop targeted therapies. MMP9 has been implicated in various diseases, including cancer metastasis, cardiovascular disorders, and neurodegenerative conditions, making it a promising candidate for therapeutic interventions.

      This research aims to provide a comprehensive analysis of the MMP9 mouse recombinant, focusing on its molecular characteristics, biological roles, and potential therapeutic implications. By shedding light on the intricate nature of MMP9, we aim to contribute to a deeper understanding of its functional significance and pave the way for future research and therapeutic advancements.

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    Mmmp9 Mouse
  • View Data Sheet

    Name :

    NMNAT1 Mouse

    Description:

    Nicotinamide Nucleotide Adenylyltransferase 1 Mouse Recombinant

    Nicotinamide/nicotinic acid mononucleotide adenylyltransferase 1, NMNAT1, NMN/NaMN adenylyltransferase 1, Nicotinamide mononucleotide adenylyltransferase 1, NMN adenylyltransferase, Nicotinate-nucleotide adenylyltransferase 1, NaMN adenylyltransferase 1, D4Cole1e, Nmnat.

    Product # :

    ENZ-1049

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    Description

    NMNAT1 Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 308 amino acids (1-285 a.a) and having a molecular mass of 34.7kDa. NMNAT1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    NMNAT1 protein solution (1mg/ml) containing Phosphate Buffered Saline (pH7.4), 20% glycerol and 1mM EDTA.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      NMNAT1 enzyme is vital for NAD biosynthesis, catalyzing the condensation of nicotinamide mononucleotide (NMN) or nicotinic acid mononucleotide (NaMN) with the AMP moiety of ATP to form NAD or NaAD. NMNAT1 is widely expressed with high levels in skeletal muscle, heart, liver and kidney. This protein appears to have the ability to protect against axonal degeneration following mechanical or toxic insults.

    • Synonyms

      Nicotinamide/nicotinic acid mononucleotide adenylyltransferase 1, NMNAT1, NMN/NaMN adenylyltransferase 1, Nicotinamide mononucleotide adenylyltransferase 1, NMN adenylyltransferase, Nicotinate-nucleotide adenylyltransferase 1, NaMN adenylyltransferase 1, D4Cole1e, Nmnat.

    • Physical Appearance

      Sterile filtered colourless 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 MGSMDSSKKT EVVLLACGSF NPITNMHLRL FELAKDYMHA TGKYSVIKGI ISPVGDAYKK KGLIPAHHRI IMAELATKNS HWVEVDTWES LQKEWVETVK VLRYHQEKLA TGSCSYPQSS PALEKPGRKR KWADQKQDSS PQKPQEPKPT GVPKVKLLCG ITNDISSTKI RRALRRGQSI RYLVPDLVQE YIEKHELYNT ESEGRNAGVT LAPLQRNAAE AKHNHSTL.

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    Nmnat1 Mouse
  • View Data Sheet

    Name :

    PPIL1 Human

    Description:

    Peptidylprolyl Isomerase (Cyclophilin)-Like 1 Human Recombinant

    Peptidyl-Prolyl Cis-Trans Isomerase-Like 1, PPIL-1, CYPL1, hCyPX, MGC678, PPIase, CGI-124, PPIL1.

    Product # :

    ENZ-388

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    • sds-page

    Description

    PPIL1 Human Recombinant protein produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 174 amino acids (1-166) and having a molecular mass of 19.3 kDa. PPIL1 is fused to 8 amino acid His Tag at C-terminus and is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    PPIL1 solution containing 20 mM Tris-HCl buffer (pH 8.0) and 20% glycerol

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Biological Activity

    Specific activity is > 300 nmoles/min/mg, and is defined as the amount of enzyme that cleaves 1umole of suc-AAFP-pNA per minute at 25C in Tris-Hcl pH8.0 using chymotrypsin.

    sds-page

    PPIL1 Human SDS-PAGE - Product image 1

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    • Introduction

      PPIL1 belongs to the cyclophilin family of peptidylprolyl isomerases (PPIases).
      The cyclophilins are a well conserved, ubiquitous family, members of which take an significant part in protein folding, immunosuppression by cyclosporin A, and infection of HIV-1 virions. PPIL1 protein increases the folding of proteins and catalyze the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. PPIL1 is involved in proliferation of cancer cells through modulation of phosphorylation of stathmin. PPIL1 is a novel molecular target for colon-cancer therapy.

    • Synonyms

      Peptidyl-Prolyl Cis-Trans Isomerase-Like 1, PPIL-1, CYPL1, hCyPX, MGC678, PPIase, CGI-124, PPIL1.

    • 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

      MAAIPPDSWQ PPNVYLETSM GIIVLELYWK HAPKTCKNFA ELARRGYYNG TKFHRIIKDF MIQGGDPTGT GRGGASIYGK QFEDELHPDL KFTGAGILAM ANAGPDTNGS QFFVTLAPTQ WLDGKHTIFG RVCQGIGMVN RVGMVETNSQ DRPVDDVKII KAYPSGLEHH HHHH.

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    Ppil1 Human
  • View Data Sheet

    Name :

    SMS Human

    Description:

    Spermine Synthase Human Recombinant

    Spermine synthase, SPMSY, Spermidine aminopropyltransferase, SMS, SRS, SpS, MRSR.

    Product # :

    ENZ-230

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    Description

    SMS Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 390 amino acids (1-366) and having a molecular mass of 43.8kDa.SMS is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

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

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Spermine synthase (SMS) is amember of the spermidine/spermine synthase family. SMS is an enzyme which converts spermidine into spermine. The SMS enzyme is essential for normal viability, growth and fertility involved in polyamine metabolism. Defects in the SMS gene are the cause of Snyder-Robinson syndrome (SRS), also known as X-linked mental retardation Snyder-Robinson type. SRS is categorized by moderate intellectual deficit, hypotonia, an unsteady gait, osteoporosis, kyphoscoliosis and facial asymmetry, its transmission is X-linked recessive.

    • Synonyms

      Spermine synthase, SPMSY, Spermidine aminopropyltransferase, SMS, SRS, SpS, MRSR.

    • 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 MGSHMAAARH STLDFMLGAK ADGETILKGL QSIFQEQGMA ESVHTWQDHG YLATYTNKNG SFANLRIYPH GLVLLDLQSY DGDAQGKEEI DSILNKVEER MKELSQDSTG RVKRLPPIVR GGAIDRYWPT ADGRLVEYDI DEVVYDEDSP YQNIKILHSK QFGNILILSG DVNLAESDLA YTRAIMGSGK EDYTGKDVLI LGGGDGGILC EIVKLKPKMV TMVEIDQMVI DGCKKYMRKT CGDVLDNLKG DCYQVLIEDC IPVLKRYAKE GREFDYVIND LTAVPISTSP EEDSTWEFLR LILDLSMKVL KQDGKYFTQG NCVNLTEALS LYEEQLGRLY CPVEFSKEIV CVPSYLELWV FYTVWKKAKP.

    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.

    Sms Human
  • View Data Sheet

    Name :

    ACAT1 Human

    Description:

    Acetyl-Coenzyme A acetyltransferase 1 Human Recombinant

    Acetyl-CoA acetyltransferase, mitochondrial, EC 2.3.1.9, Acetoacetyl-CoA thiolase, T2, ACAT1, ACAT, MAT, THIL.

    Product # :

    ENZ-665

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    Description

    ACAT1 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 417 amino acids (34-427) and having a molecular mass of 43.8 kDa.ACAT1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    The ACAT1 solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 7.5), 0.1M NaCl, 10% glycerol and 1mM DTT.

    Purity

    Greater than 95% as determined by SDS-PAGE.

    More Info

    • Introduction

      Acetoacetyl-CoA thiolase (ACAT1) is an enzyme member of the membrane-bound acyltransferase family and Sterol o-acyltransferase subfamily. The ACAT1 enzyme catalyzes the reversible formation of acetoacetyl-CoA from 2 molecules of acetyl-CoA. ACAT1 plays a part in lipoprotein compilation and dietary cholesterol absorption. Added to its acyltransferase activity, ACAT1 acts as a ligase.

    • Synonyms

      Acetyl-CoA acetyltransferase, mitochondrial, EC 2.3.1.9, Acetoacetyl-CoA thiolase, T2, ACAT1, ACAT, MAT, THIL.

    • 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 MGSVSKPTLK EVVIVSATRT PIGSFLGSLS LLPATKLGSI AIQGAIEKAG IPKEEVKEAY MGNVLQGGEG QAPTRQAVLG AGLPISTPCT TINKVCASGM KAIMMASQSL MCGHQDVMVA GGMESMSNVP YVMNRGSTPY GGVKLEDLIV KDGLTDVYNK
      IHMGSCAENT AKKLNIARNE QDAYAINSYT RSKAAWEAGK FGNEVIPVTV TVKGQPDVVV KEDEEYKRVD FSKVPKLKTV FQKENGTVTA ANASTLNDGA AALVLMTADA AKRLNVTPLA RIVAFADAAV EPIDFPIAPV YAASMVLKDV GLKKEDIAMW EVNEAFSLVV LANIKMLEID
      PQKVNINGGA VSLGHPIGMS GARIVGHLTH ALKQGEYGLA SICNGGGGAS AMLIQKL.

    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.

    Acat1 Human
  • View Data Sheet

    Name :

    UBE2D1 Human

    Description:

    Ubiquitin Conjugating Enzyme E2D1 Human Recombinant

    Ubiquitin-conjugating enzyme E2 D1, Stimulator of Fe transport, SFT, UBC4/5 homolog, UbcH5, Ubiquitin carrier protein D1, Ubiquitin-conjugating enzyme E2(17)KB 1, Ubiquitin-conjugating enzyme E2-17 kDa 1, Ubiquitin-protein ligase D1, UBE2D1, SFT, UBC5A, UBCH5A, E2(17)KB1.

    Product # :

    ENZ-116

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    Description

    UBE2D1 produced in E.Coli is a single, non-glycosylated polypeptide chain containing 170 amino acids (1-147 a.a.) and having a molecular mass of 19kDa.UBE2D1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    UBE2D1 solution (1mg/ml) containing 20mM Tris-HCl buffer (pH8.0), 40% glycerol and 0.1M NaCl.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

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    • Introduction

      UBE2D1 is a member of the ubiquitin-conjugating enzyme family. Ubiquitination involves at least 3 classes of enzymes: ubiquitin-activating enzymes (E1s), ubiquitin-conjugating enzymes (E2s) and ubiquitin-protein ligases (E3s). UBE2D1 is strongly related to a stimulator of iron transport (SFT), and is up-regulated in hereditary hemochromatosis. In addition, UBE2D1 functions in the ubiquitination of the tumor-suppressor protein p53 and the hypoxia-inducible transcription factor HIF1alpha by interacting with the E1 ubiquitin-activating enzyme and the E3 ubiquitin-protein ligases.

    • Synonyms

      Ubiquitin-conjugating enzyme E2 D1, Stimulator of Fe transport, SFT, UBC4/5 homolog, UbcH5, Ubiquitin carrier protein D1, Ubiquitin-conjugating enzyme E2(17)KB 1, Ubiquitin-conjugating enzyme E2-17 kDa 1, Ubiquitin-protein ligase D1, UBE2D1, SFT, UBC5A, UBCH5A, E2(17)KB1.

    • Physical Appearance

      Sterile filtered colorless solution.

    • Stability

      UBE2D1 Human Recombinant although stable at 4°C for 1 week, should be stored below -18°C. Please prevent freeze thaw cycles.

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MGSMALKRIQ KELSDLQRDP PAHCSAGPVG DDLFHWQATI MGPPDSAYQG GVFFLTVHFP TDYPFKPPKI AFTTKIYHPN INSNGSICLD ILRSQWSPAL TVSKVLLSIC SLLCDPNPDD PLVPDIAQIY KSDKEKYNRH AREWTQKYAM.

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    Ube2D1 Human
  • View Data Sheet

    Name :

    CA13 Human

    Description:

    Carbonic Anhydrase XIII Human Recombinant

    Carbonic Anhydrase XIII, Carbonate Dehydratase XIII, EC 4.2.1.1, CA-XIII, Carbonic, Anhydrase 13, CAXIII.

    Product # :

    ENZ-902

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    Description

    CA13 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 285 amino acids (1-262a.a) and having a molecular mass of 31.8kDa.CA13 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    CA13 protein solution (0.5mg/ml) containing Phosphate buffered saline (pH7.4),10% glycerol and 1mM DTT.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    Biological Activity

    Specific activity is > 2,500 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.

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    • Introduction

      Carbonic Anhydrase XIII, also known as CA13 is a member of the alpha-carbonic anhydrase family, which catalyzes the rapid interconversion of carbon dioxide and water tobicarbonate and protons, a reversible reaction which occurs relatively slowly in the absence of catalyst. Furthermore, the active siteof nearly all carbonic anhydrases contains a zinc ion; they have been classified as metalloenzymes. At least fivedistinct CA families (?, ?, ?, ? and ?) have been found. These families have no significant a.a sequence resemblance and in just about allcases are considered to be an example of convergent evolution. The ?-CAs have been demonstrated in humans.

    • Synonyms

      Carbonic Anhydrase XIII, Carbonate Dehydratase XIII, EC 4.2.1.1, CA-XIII, Carbonic, Anhydrase 13, CAXIII.

    • 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 SSGLVPRGSP MGSMSRLSWG YREHNGPIHW KEFFPIADGD QQSPIEIKTK EVKYDSSLRP LSIKYDPSSA KIISNSGHSF NVDFDDTENK SVLRGGPLTG SYRLRQVHLH WGSADDHGSE HIVDGVSYAA ELHVVHWNSD KYPSFVEAAH EPDGLAVLGV FLQIGEPNSQ LQKITDTLDS IKEKGKQTRF TNFDLLSLLP PSWDYWTYPG SLTVPPLLES VTWIVLKQPI NISSQQLAKF RSLLCTAEGE AAAFLVSNHR PPQPLKGRKV RASFH.

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    Ca13 Human
  • View Data Sheet

    Name :

    FOLH1 Human

    Description:

    Folate Hydrolase 1 Human Recombinant

    Glutamate carboxypeptidase 2 isoform 1,Cell growth-inhibiting gene 27 protein, Folate hydrolase 1, Folylpolygamma-glutamate carboxypeptidase, Glutamate carboxypeptidase II, Membrane glutamate carboxypeptidase, Nacetylated-alpha-linked acidic dipeptidase I, Prostate-specific membrane antigen, Pteroylpoly-gamma glutamate carboxypeptidase, Folh1, FGCP, FOLH, GCP2, GCPII, mGCP, NAALAD1, NAALAdase, PSM, PSMA

    Product # :

    ENZ-1170

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    Description

    FOLH1 produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 717 amino acids (44-750 a.a) and having a molecular mass of 80.7kDa.FOLH1 is expressed with a 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    FOLH1 protein solution (0.25mg/ml) contains Phosphate buffered saline (pH 7.4) and 20% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

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    • Introduction

      FOLH1, also known as glutamate carboxypeptidase 2 (GCPII), is a single pass type 2 membrane protein which belongs to the peptidase M28 family. FOLH1 is highly produced in prostate epithelium. FOLH1 is also found in ovary, live, stomach, small intestine colon, urinary bladder, kidney, testis, and the capillary endothelium of a variety of tumours. Therefore, it plays a role in directed imaging and therapy of recurrent of metastatic disease. FOLH1 is a zinc metalloenzyme that resides in membranes and catalyses the hydrolysis of N-acetylaspartylglutamate to glutamate and N-acetylaspartate.

    • Synonyms

      Glutamate carboxypeptidase 2 isoform 1,Cell growth-inhibiting gene 27 protein, Folate hydrolase 1, Folylpolygamma-glutamate carboxypeptidase, Glutamate carboxypeptidase II, Membrane glutamate carboxypeptidase, Nacetylated-alpha-linked acidic dipeptidase I, Prostate-specific membrane antigen, Pteroylpoly-gamma glutamate carboxypeptidase, Folh1, FGCP, FOLH, GCP2, GCPII, mGCP, NAALAD1, NAALAdase, PSM, PSMA

    • 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

      ADPMKSSNEA TNITPKHNMK AFLDELKAEN IKKFLYNFTQ IPHLAGTEQN FQLAKQIQSQ WKEFGLDSVE LAHYDVLLSY PNKTHPNYIS IINEDGNEIF NTSLFEPPPP GYENVSDIVP PFSAFSPQGM PEGDLVYVNY ARTEDFFKLE RDMKINCSGK IVIARYGKVF RGNKVKNAQL AGAKGVILYS DPADYFAPGV KSYPDGWNLP GGGVQRGNIL NLNGAGDPLT PGYPANEYAY RRGIAEAVGL PSIPVHPIGY YDAQKLLEKM GGSAPPDSSW RGSLKVPYNV GPGFTGNFST QKVKMHIHST NEVTRIYNVI GTLRGAVEPD RYVILGGHRD SWVFGGIDPQ SGAAVVHEIV RSFGTLKKEG WRPRRTILFA SWDAEEFGLL GSTEWAEENS RLLQERGVAY INADSSIEGN YTLRVDCTPL MYSLVHNLTK ELKSPDEGFE GKSLYESWTK KSPSPEFSGM PRISKLGSGN DFEVFFQRLG IASGRARYTK NWETNKFSGY PLYHSVYETY ELVEKFYDPM FKYHLTVAQV RGGMVFELAN SIVLPFDCRD YAVVLRKYAD KIYSISMKHP QEMKTYSVSF DSLFSAVKNF TEIASKFSER LQDFDKSNPI VLRMMNDQLM FLERAFIDPL GLPDRPFYRH VIYAPSSHNK YAGESFPGIY DALFDIESKV DPSKAWGEVK RQIYVAAFTV QAAAETLSEV AHHHHHH

    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.

    Folh1 Human
  • View Data Sheet

    Name :

    GPT2 Mouse

    Description:

    Glutamic-Pyruvate Transaminase 2 Mouse Recombinant

    ALT2, AAT2, Alanine aminotransferase 2, Glutamate pyruvate transaminase 2, Glutamic--alanine transaminase 2, Glutamic--pyruvic transaminase 2.

    Product # :

    ENZ-1096

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    Description

    GPT2 Mouse Recombinant produced in E. coli is a single polypeptide chain containing 522 amino acids (1-522) and having a molecular mass of 60.1 kDa. Mouse GPT2 is fused to a 21 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    The GPT2 solution (1mg/1ml) contains 20mM Tris-HCl buffer (pH 7.5), 20% glycerol, and 2mM DTT.

    Purity

    Greater than 85% as determined by SDS-PAGE.

    Biological Activity

    Greater than 50units/mg, and is defined as the amount of enzyme that cleaves 1umole of L-Alanine to L-Glutamate per minute at pH7.5 at 37℃.

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    • Introduction

      Glutamic-Pyruvate Transaminase 2 (GPT2) catalyzes the reversible transamination among alanine and 2-oxoglutarate to create pyruvate and glutamate. GPT2 expressed mainly in muscle, fat and kidney and participates in the intermediary metabolism of glucose and amino acids.

    • Synonyms

      ALT2, AAT2, Alanine aminotransferase 2, Glutamate pyruvate transaminase 2, Glutamic--alanine transaminase 2, Glutamic--pyruvic transaminase 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 MQRAAVLVRR GSCPRASGPW GRSHSSAAAE ASAALKVRPE RSPRDRILTL ESMNPQVKAV EYAVRGPIVL KAGEIEMELQ RGIKKPFTEV IRANIGDAHA MGQQPITFLR QVMALCTYPN LLNSPSFPED AKKRARRILQ ACGGNSLGSY SASQGVNCIR EDVAAFITRR DGVPADPDNI YLTTGASDGI STILKLLVSG GGKSRTGVMI PIPQYPLYSA VISELDAVQV NYYLDEENCW ALNVDELRRA LRQAKDHCDP KVLCIINPGN PTGQVQSRKC IEDVIHFAWE EKLFLLADEV YQDNVYSPDC RFHSFKKVLY QMGHEYSSNV ELASFHSTSK GYMGECGYRG GYMEVINLHP EIKGQLVKLL SVRLCPPVSG QAAMDIVVNP PEPGEESFEQ FSREKEFVLG NLAKKAKLTE DLFNQVPGIQ CNPLQGAMYA FPRILIPAKA VEAAQSHKMA PDMFYCMKLL EETGICVVPG SGFGQREGTY HFRMTILPPV DKLKTVLHKV KDFHLKFLEQ.

    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.

    Gpt2 Mouse
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    Name :

    ProMMP 9 Human

    Description:

    Pro-Matrix Metalloproteinase-9 Human Recombinant

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

    Product # :

    ENZ-439

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    Description

    Pro-MMP-9 Human Recombinant produced in E.Coli is single, a non-glycosylated, Polypeptide chain containing 688 amino acids fragment (20-707) corresponding to the pro form of the protein minus the signal peptide, having a total molecular mass of 78.59kDa and fused with a 4.5kDa amino-terminal hexahistidine tag. The Pro-MMP-9 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Pro-MMP-9 protein is supplied in 1x PBS and 50% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Matrix metalloproteinases are a family of zinc and calcium-dependent endopeptidases that break down extracellular matrix proteins. The MMP9 is secreted as a 92kDa zymogen. Cleavage of ProMMP-9 results in the active enzyme, having a molecular weight of approximately 82kDa. MMP9 is composed of the following domains: a gelatin-binding domain consisting of three fibronectin type II units, a catalytic domain containing the zinc-binding site, a proline-rich type V collagen-homologous domain and a hemopexin-like domain. MMP9 is produced by the several cell types: monocytes, macrophages, neutrophils, keratinocytes, fibroblasts, osteoclasts and endothelial cells. MMP9 is involved in inflammatory responses, tissue remodeling, wound healing, tumor growth and metastasis. MMP9 may also play an important part in local proteolysis of the extracellular matrix and in leukocyte migration, as well as in bone osteoclastic resorption. MMP9 cleaves type IV and type V collagens into large C-terminal three quarter fragments and shorter N-terminal one quarter fragments. MMP9 can also degrade fibronectin but not laminin or Pz-peptide.
      MMP9 defects may be a cause of susceptibility to intervertebral disc disease (IDD), also known as lumbar disk herniation (LDH).

    • Synonyms

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

    • 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. Please avoid 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.

    Prommp 9 Human
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