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Search results

1000 results found for “SNRP”

Name

Description

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  • View Data Sheet

    Name :

    NOV Mouse

    Description:

    Nephroblastoma Overexpressed Mouse Recombinant

    Protein NOV homolog, NovH, CCN family member 3, Nephroblastoma-overexpressed gene protein homolog, Nov, Ccn3, C130088N23Rik.

    Product # :

    CYT-171

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    Description

    NOV Mouse Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 333 amino acids and having a molecular mass of 36.4kDa.The NOV is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    NOV protein was lyophilized from a 0.2µm filtered concentrated solution in 20mM Tris-HCl, pH 8.5 and 150mM NaCl.

    Purity

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

    Biological Activity

    The ED50 as determined by a cell proliferation assay using murine Balb/c 3T3 cells is less than 1.0 μg/ml, corresponding to a specific activity of > 1000 IU/mg.

    More Info

    • Introduction

      Nephroblastoma Overexpressed (NOV) is a member of the CCN family of secreted cysteine rich regulatory proteins. The full length NOV protein is comprised of 4 structural domains, which present distinct, and sometimes opposing, biological activities. An elevated expression of NOV is linked with certain tumors, including Wilm’s tumor and most nephroblastomas. On the other hand, in other tumor types and certain cancer cell lines, increased tumorgenicity and proliferation is associated with decreased NOV expression.

    • Synonyms

      Protein NOV homolog, NovH, CCN family member 3, Nephroblastoma-overexpressed gene protein homolog, Nov, Ccn3, C130088N23Rik.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Amino Acid Sequence

      QVSASLRCPS RCPPKCPSIS PTCAPGVRSV LDGCSCCPVC ARQRGESCSE MRPCDQSSGL YCDRSADPNN QTGICMVPEG DNCVFDGVIY RNGEKFEPNC QYFCTCRDGQ IGCLPRCQLD VLLPGPDCPA PRKVAVPGEC CEKWTCGSDE QGTQGTLGGL ALPAYRPEAT VGVEVSDSSI NCIEQTTEWS ACSKSCGMGV STRVTNRNRQ CEMVKQTRLC IVRPCEQEPE EVTDKKGKKC LRTKKSLKAI HLQFENCTSL YTYKPRFCGV CSDGRCCTPH NTKTIQVEFQ CLPGEIIKKP VMVIGTCTCY SNCPQNNEAF LQDLELKTSR GEI.

    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.

    Nov Mouse
  • View Data Sheet

    Name :

    SOD1 Human

    Description:

    Superoxide Dismutase 1 Human Recombinant

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

    Product # :

    PRO-648

    Price :

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    Description

    Recombinant Human Cu/Zn Superoxide Dismutase produced in E.Coli is a single monomeric non-glycosylated polypeptide chain containing 154 amino acids and having a total molecular mass of 15.9 kDa.The SOD1 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    SOD1 filtered solution (1mg/ml) contains 20mM Tris-HCl pH-7.5 and 10% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Biological Activity

    Specific activity is > 500 units/mg, in which one unit will inhibit the rate of reduction of cytochrome c by 50% in a coupled system, using xanthine and Xanthine oxidase at pH 7.8 at 25°C.

    More Info

    • Introduction

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

    • Synonyms

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

    • Physical Appearance

      Sterile Filtered 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

      MATKAVCVLK GDGPVQGIIN FEQKESNGPV KVWGSIKGLT EGLHGFHVHE FGDNTAGCTS AGPHFNPLSR KHGGPKDEER HVGDLGNVTA DKDGVADVSI EDSVISLSGD HCIIGRTLVV HEKADDLGKG GNEESTKTGN AGSRLACGVIGIAQ.

    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.

    Sod1 Human
  • View Data Sheet

    Name :

    SOD2 Human

    Description:

    Superoxide Dismutase-2 Human Recombinant

    MNSOD, MVCD6, IPOB, Mn superoxide dismutase, EC=1.15.1.1.

    Product # :

    PRO-819

    Price :

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    • description
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    • More Info

    Description

    SOD2 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 219 amino acids (25-222 a.a.) and having a molecular mass of 24.4kDa. SOD2 protein is fused to a 20 amino acid His-Tag at N-terminus and purified by standard chromatography.

    Source

    Escherichia Coli.

    Formulation

    SOD2 Human solution containing 20mM Tris-HCl pH-8 & 20% glycerol.

    Purity

    Greater than 95% as determined by SDS-PAGE.

    Biological Activity

    Specific activity is > 1,200 units/mg, in which one unit will inhibit the rate of reduction of cytochrome c by 50% in a coupled system, using xanthine and Xanthine oxidase at pH 7.8 at 25C in a 1.5 ml reaction volume.

    More Info

    • Introduction

      SOD2 is part of the iron/manganese superoxide dismutase family. It encodes a mitochondrial protein that forms a homotetramer and binds one manganese ion per subunit. SOD2 binds to the superoxide byproducts of oxidative phosphorylation and converts them to hydrogen peroxide and diatomic oxygen. Mutations in SOD2 gene have been associated with idiopathic cardiomyopathy (IDC), premature aging, sporadic motor neuron disease, and cancer. SOD2 destroys radicals which are usually produced within the cells and which are toxic to biological systems.

    • Synonyms

      MNSOD, MVCD6, IPOB, Mn superoxide dismutase, EC=1.15.1.1.

    • Physical Appearance

      Sterile filtered colorless solution.

    • Stability

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

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MKHSLPDLPY DYGALEPHIN AQIMQLHHSK HHAAYVNNLN VTEEKYQEAL AKGDVTAQIA LQPALKFNGG GHINHSIFWT NLSPNGGGEP KGELLEAIKR DFGSFDKFKE KLTAASVGVQ GSGWGWLGFN KERGHLQIAA CPNQDPLQGT TGLIPLLGID VWEHAYYLQY KNVRPDYLKA IWNVINWENV TERYMACKK.

    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.

    Sod2 Human
  • View Data Sheet

    Name :

    NUDCD2 Human

    Description:

    NudC Domain Containing 2 Human Recombinant

    NudC Domain Containing 2, NudC Domain-Containing Protein 2, NudC-Like Protein 2.

    Product # :

    PRO-1881

    Price :

    Quantity :

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    Description

    NUDCD2 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 180 amino acids (1-157 a.a) and having a molecular mass of 20kDa.NUDCD2 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    NUDCD2 protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 10% glycerol and 1mM DTT.

    Purity

    Greater than 95% as determined by SDS-PAGE.

    More Info

    • Introduction

      NudC Domain Containing 2 also known as NUDCD2 contains 1 CS domain and interacts with LIS1. NUDCD2 regulates the LIS1/dynein pathway by stabilizing LIS1 with Hsp90 chaperone.

    • Synonyms

      NudC Domain Containing 2, NudC Domain-Containing Protein 2, NudC-Like Protein 2.

    • Physical Appearance

      Sterile Filtered clear solution.

    • Stability

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

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MGSMSAPFEE RSGVVPCGTP WGQWYQTLEE VFIEVQVPPG TRAQDIQCGL QSRHVALSVG GREILKGKLF DSTIADEGTW TLEDRKMVRI VLTKTKRDAA NCWTSLLESE YAADPWVQDQ MQRKLTLERF QKENPGFDFS GAEISGNYTK GGPDFSNLEK

    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.

    Nudcd2 Human
  • View Data Sheet

    Name :

    NUDT16 Human

    Description:

    Nudix Type Motif 16 Human Recombinant

    Nudix (nucleoside diphosphate linked moiety X)-Type Motif 16, FLJ31265, FLJ34034, FLJ36248, U8 snoRNA-binding protein H29K, U8 snoRNA-decapping enzyme.

    Product # :

    ENZ-053

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    • description
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    Description

    NUDT16 produced in E.Coli is a single, non-glycosylated polypeptide chain containing 215 amino acids (1-195a.a.) and having a molecular mass of 23.4kDa.NUDT16 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The NUDT16 protein solution (1mg/1ml) is formulated in 20mM Tris-HCl buffer (pH8.0) 1mM DTT, 100mM NaCl and 10% glycerol.

    Purity

    Greater than 95% as determined by SDS-PAGE.

    More Info

    • Introduction

      NUDT16 is nuclear nucleoside diphosphatase proteins restricted in foci in the nucleolus and nucleoplasm. NUDT16 is a RNA-decapping enzyme. It binds specifically to U8 snoRNA and can remove m7G and m227G caps from RNAs, rendering them substrates for 5’-3’ exonucleases for degradation in vivo.

    • Synonyms

      Nudix (nucleoside diphosphate linked moiety X)-Type Motif 16, FLJ31265, FLJ34034, FLJ36248, U8 snoRNA-binding protein H29K, U8 snoRNA-decapping enzyme.

    • 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

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MAGARRLELG EALALGSGWR HACHALLYAP DPGMLFGRIP LRYAILMQMR FDGRLGFPGG FVDTQDRSLE DGLNRELREE LGEAAAAFRV ERTDYRSSHV GSGPRVVAHF YAKRLTLEEL LAVEAGATRA KDHGLEVLGL VRVPLYTLRD GVGGLPTFLE NSFIGSAREQ LLEALQDLGL LQSGSISGLK IPAHH

    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.

    Nudt16 Human
  • View Data Sheet

    Name :

    BDNF Human, His

    Description:

    Brain-Derived Neurotrophic Factor Human Recombinant, His Tag

    Brain-Derived Neurotrophic Factor, Neurotrophin, Abrineurin, ANON2, BULN2, Brain-derived neurotrophic factor.

    Product # :

    CYT-881

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    • sds-page

    Description

    BDNF Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 140 amino acids (129-247 a.a) and having a molecular mass of 15.8kDa. BDNF is fused to a 21 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

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

    Purity

    Greater than 85% as determined by SDS-PAGE.

    sds-page

    BDNF-sds-page - Product image 1

    More Info

    • Introduction

      BDNF promotes the survival of neuronal populations that are all located either in the central nervous system or directly connected to it. BDNF is a major regulator of synaptic transmission and plasticity at adult synapses in many regions of the cns. The versatility of BDNF is emphasized by its contribution to a range of adaptive neuronal responses including long-term potentiation (ltp), long-term depression (ltd), certain forms of short-term synaptic plasticity, as well as homeostatic regulation of intrinsic neuronal excitability.

    • Synonyms

      Brain-Derived Neurotrophic Factor, Neurotrophin, Abrineurin, ANON2, BULN2, Brain-derived neurotrophic factor.

    • 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 MHSDPARRGE LSVCDSISEW VTAADKKTAV DMSGGTVTVL EKVPVSKGQL KQYFYETKCN PMGYTKEGCR GIDKRHWNSQ CRTTQSYVRA LTMDSKKRIG WRFIRIDTSC VCTLTIKRGR.

    • Background

      What is the molecular weight/Mw of BDNF Protein?
      BDNF Protein has a total Mw of 15.8kDa.

      What is the source or expression system of BDNF Protein?
      Escherichia Coli.

      What is the Purity of BDNF Protein?
      BDNF Protein is >85% pure as determined by SDS-PAGE.

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

      What is the amino acid sequence of BDNF Protein?
      MGSSHHHHHH SSGLVPRGSH MHSDPARRGE LSVCDSISEW VTAADKKTAV DMSGGTVTVL EKVPVSKGQL KQYFYETKCN PMGYTKEGCR GIDKRHWNSQ CRTTQSYVRA LTMDSKKRIG WRFIRIDTSC VCTLTIKRGR.

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

      What is the endotoxin level for BDNF Protein?
      The endotoxin level is minimal, BDNF 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.

    Bdnf Human His
  • View Data Sheet

    Name :

    SUMO3 Human

    Description:

    Small Ubiquitin-Related Modifier 3 Human Recombinant

    SUMO-3, SMT3A, SMT3H1, SMT3 homolog 1, Small Ubiquitin-related modifier 3, Ubiquitin-like protein SMT3A.

    Product # :

    PRO-267

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    Description

    SUMO3 produced in E.Coli is a single, non-glycosylated polypeptide chain containing 112 amino acids (1-92a.a.) and having a molecular mass of 12.6kDa (molecular weight on SDS-PAGE will appear higher).SUMO3 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The SUMO3 protein solution (1mg/1ml) is formulated in 20mM Tris-HCl buffer (pH8.0) 0.1M NaCl,1mM DTT and 20% glycerol.

    Purity

    Greater than 95% as determined by SDS-PAGE.

    More Info

    • Introduction

      SUMO3 belongs to the SUMO protein family and operates like ubiquitin. Nevertheless, unlike ubiquitin that targets proteins for degradation, SUMO3 protein takes part in several cellular processes, like nuclear transport, transcriptional regulation, apoptosis, and protein stability. SUMO3 regulates amyloid beta generation and is crucial in the onset or progression of Alzheimer’s disease.

    • Synonyms

      SUMO-3, SMT3A, SMT3H1, SMT3 homolog 1, Small Ubiquitin-related modifier 3, Ubiquitin-like protein SMT3A.

    • 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 MSEEKPKEGV KTENDHINLK VAGQDGSVVQ FKIKRHTPLS KLMKAYCERQ GLSMRQIRFR FDGQPINETD TPAQLEMEDE DTIDVFQQQT GG

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    Sumo3 Human
  • View Data Sheet

    Name :

    FABP1 Mouse

    Description:

    Fatty Acid Binding Protein-1 Mouse Recombinant

    Fatty acid-binding protein 1 liver, L-FABP, FABPL, FABP-1, FABP1, Z-protein.

    Product # :

    PRO-1121

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    Description

    Fatty Acid Binding Protein-1 Recombinant Mouse produced in E.Coli is a single, non-glycosylated polypeptide chain containing 127 amino acids and having a molecular mass of 14.2kDa. The FABP1 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

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

    Purity

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

    More Info

    • Introduction

      FABP1 (Fatty acid binding protein1) encodes the fatty acid binding protein found in liver. FABP1 is composed of ten antiparallel beta strands that form a barrel with a bigger binding pocket than the other FABPs allowing it to accommodate two fatty acid. This protein binds free fatty acids and their coenzyme A derivatives, bilirubin, and some other small molecules in the cytoplasm; it may be involved in intracellular lipid transport and metabolism.

    • Synonyms

      Fatty acid-binding protein 1 liver, L-FABP, FABPL, FABP-1, FABP1, Z-protein.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized FABP1 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution FABP1 should be stored at 4°C between 2-7 days and for future use below -18°C.Please prevent freeze-thaw cycles.

    • Solubility

      It is recommended to reconstitute the lyophilized FABP1 in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      MNFSGKYQLQ SQENFEPFMK AIGLPEDLIQ KGKDIKGVSE IVHEGKKIKL TITYGPKVVR NEFTLGEECE LETMTGEKVK AVVKLEGDNK MVTTFKGIKS VTELNGDTIT NTMTLGDIVY KRVSKRI.

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    Fabp1 Mouse
  • View Data Sheet

    Name :

    TAGLN3 Human

    Description:

    Transgelin-3 Human Recombinant

    Transgelin 3, NP22, NP25, Neuronal protein 22, Neuronal protein NP25.

    Product # :

    PRO-946

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    Description

    TAGLN3 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 219 amino acids (1-199) and having a molecular mass of 24.6 kDa.The TAGLN3 is fused to a 20 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    The TAGLN3 solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 1mM DTT and 20% glycerol.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    More Info

    • Introduction

      TAGLN3 holds a putative Actin-binding domain, two potential phosphorylation sites, two EF-hand motifs and a calponin-homology (CH) domain. TAGLN3 is homologic to transgelin and calponin, two cytoskeleton-interacting proteins. TAGLN3 is a member of the calponin family, and is co-localized with Actin and tubulin, which indicates that TAGLN3 has a part in neuronal plasticity or as a signaling protein. As a result of a wide-ranging expression pattern, TAGLN3 is able to take different roles in the developing and adult brain.

    • Synonyms

      Transgelin 3, NP22, NP25, Neuronal protein 22, Neuronal protein NP25.

    • 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 MANRGPSYGL SREVQEKIEQ KYDADLENKL VDWIILQCAE DIEHPPPGRA HFQKWLMDGT VLCKLINSLY PPGQEPIPKI SESKMAFKQM EQISQFLKAA ETYGVRTTDI FQTVDLWEGK DMAAVQRTLM ALGSVAVTKD DGCYRGEPSW FHRKAQQNRR GFSEEQLRQG QNVIGLQMGS NKGASQAGMT GYGMPRQIM

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    Tagln3 Human
  • View Data Sheet

    Name :

    PDPN Human

    Description:

    Podoplanin Human Recombinant

    Podoplanin, Glycoprotein 36, PA2.26 antigen, T1A, GP36, GP40, Gp38, OTS8, T1A2, HT1A-1, PA2.26, T1-alpha, PDPN.

    Product # :

    PRO-626

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    Description

    PDPN Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 130 amino acids (99-207 a.a) and having a molecular mass of 13.4kDa. PDPN is fused to a 21 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The protein solution contains 20mM Tris-HCl pH7.5 & 0.1M NaCl.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Podoplanin is a small mucin-like type-1 transmembrane protein, typically expressed in various specialized cell types throughout the body. Podoplanin is a type-I integral membrane glycoprotein with diverse distribution in human tissues. PDPN physiological function is related to its mucin-type character. The homologous protein in other species has been described as a differentiation antigen and influenza-virus receptor.
      PDPN is expressed in lymphatic progenitor cells and afterwards during mouse development in lymphatic endothelial cells. Podoplanin is a specific marker for lymph vessel endothelial cells. Over-expression of podoplanin significantly elevates endothelial cell adhesion, migration, and tube formation. Inhibition of Podoplanin expression decreases cell adhesion in human dermal lymphatic endothelial cells. Podoplanin is used as a specific marker for lymphatic endothelium in histopathology.
      Podoplanin expression is increased in nearly all human colon, rectum, and small intestine tumors. AGGRUS may serve as a diagnostic marker that distinguishes seminomas, the majority of which over express the protein, from embryonal carcinoma in testicular germ cell tumors.

    • Synonyms

      Podoplanin, Glycoprotein 36, PA2.26 antigen, T1A, GP36, GP40, Gp38, OTS8, T1A2, HT1A-1, PA2.26, T1-alpha, PDPN.

    • 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 MASTGQPEDD TETTGLEGGV AMPGAEDDVV TPGTSEDRYK SGLTTLVATS VNSVTGIRIE DLPTSESTVH AQEQSPSATA SNVATSHSTE KVDGDTQTTV EKDGLSTVTL.

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    Pdpn Human
  • View Data Sheet

    Name :

    PFN1 Rat

    Description:

    Profilin-1 Rat Recombinant

    Profilin-1, Profilin I.

    Product # :

    PRO-2231

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    Description

    PFN1 Rat Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 164 amino acids (1-140 a.a) and having a molecular mass of 17.5kDa. PFN1 is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    PFN1 protein solution (1mg/ml) containing Phosphate Buffered Saline (pH 7.4) and 10% glycerol 1mM DTT.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Profilin-1 also known as Pfn1 is a ubiquitous actin monomer-binding protein which is a member of the profilin family. Pfn1 significantly enhances skin wound healing in-vitro as well as in-vivo which is mediated by purinergic receptors. Furthermore, Pfn1 is also active in endothelial cell migration and vessel sprouting. Pfn1 is considered to regulate actin polymerization in response to extracellular signals.

    • Synonyms

      Profilin-1, Profilin I.

    • Physical Appearance

      Sterile Filtered colorless solution.

    • Stability

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

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MGSHMAGWNA YIDSLMADGT CQDAAIVGYK DSPSVWAAVP GKTFVSITPA EVGVLVGKDR SSFFVNGLTL GGQKCSVIRD SLLQDGEFTM DLRTKSTGGA PTFNVTVTMT AKTLVLLMGK EGVHGGLINK KCYEMASHLR RSQY.

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    Pfn1 Rat
  • View Data Sheet

    Name :

    KCNIP3 Human

    Description:

    Kv Channel Interacting Protein 3 Human Recombinant

    Calsenilin, A-type potassium channel modulatory protein 3, DRE-antagonist modulator, Kv channel-interacting protein 3, KCNIP3, CSEN, DREAM, KCHIP3, MGC18289.

    Product # :

    PRO-009

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    Description

    KCNIP3 Human Recombinant fused with a 20 amino acid His tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 276 amino acids (1-256 a.a.) and having a molecular mass of 31.4kDa. The KCNIP3 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The KCNIP3 solution (1 mg/ml) contains 20mM Tris-HCl buffer(pH 8.0), 10% glycerol, 2mM DTT and 0.1M NaCl.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      KCNIP3 belongs to a family of voltage-gated potassium (Kv) channel-interacting proteins, which belong to the recoverin branch of the EF-hand superfamily. KCNIP family members are small calcium binding proteins containing EF-hand-like domains. KCNIP3 also functions as a calcium-regulated transcriptional repressor, and interacts with presenilins. Mutations in the presenilin genes are implicated in Alzheimer's disease.

    • Synonyms

      Calsenilin, A-type potassium channel modulatory protein 3, DRE-antagonist modulator, Kv channel-interacting protein 3, KCNIP3, CSEN, DREAM, KCHIP3, MGC18289.

    • 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 MQPAKEVTKA SDGSLLGDLG HTPLSKKEGI KWQRPRLSRQ ALMRCCLVKW ILSSTAPQGS DSSDSELELS TVRHQPEGLD QLQAQTKFTK KELQSLYRGF KNECPTGLVD EDTFKLIYAQ FFPQGDATTY AHFLFNAFDA DGNGAIHFED FVVGLSILLR GTVHEKLKWA FNLYDINKDG YITKEEMLAI MKSIYDMMGR HTYPILREDA PAEHVERFFE KMDRNQDGVV TIEEFLEACQ KDENIMSSMQ LFENVI.

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    Kcnip3 Human
  • View Data Sheet

    Name :

    KDSR Human

    Description:

    3-Ketodihydrosphingosine Reductase Human Recombinant

    3-ketodihydrosphingosine reductase, KDS reductase, 3-dehydrosphinganine reductase, Follicular variant translocation protein 1, FVT-1, KDSR, FVT1, DHSR, SDR35C1, FLJ36555, FLJ92680.

    Product # :

    ENZ-092

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    Description

    KDSR Human Recombinant fused with a 21 amino acid His tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 266 amino acids (26-270 a.a.) and having a molecular mass of 29kDa. The KDSR is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The KDSR solution (0.5 mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 1mM DTT, 10% glycerol, 0.1M NaCl and 0.1mM PMSF.

    Purity

    KDSR purity was found to be greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      3-ketodihydrosphingosine reductase (KDSR) is a 332 amino acid multi-pass membrane protein which localizes to the ER and is a member of the short-chain dehydrogenases/reductases (SDR) family. KDSR is a secreted protein that is weakly expressed in hematopoietic tissue. Furthermore, KDSR catalyzes the reduction of 3-ketodihydrosphingosine (KDS) to dihydrosphingosine (DHS). The putative active site residues of KDSR are found on the cytosolic side of the endoplasmic reticulum membrane. Chromosomal rearrangement in the KDSR gene is a cause of follicular lymphoma, aka type II chronic lymphatic leukemia.

    • Synonyms

      3-ketodihydrosphingosine reductase, KDS reductase, 3-dehydrosphinganine reductase, Follicular variant translocation protein 1, FVT-1, KDSR, FVT1, DHSR, SDR35C1, FLJ36555, FLJ92680.

    • Physical Appearance

      The KDSR is supplied as a 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 MKPLALPGAH VVVTGGSSGI GKCIAIECYK QGAFITLVAR NEDKLLQAKK EIEMHSINDK QVVLCISVDV SQDYNQVENV IKQAQEKLGP VDMLVNCAGM AVSGKFEDLE VSTFERLMSI NYLGSVYPSR AVITTMKERR VGRIVFVSSQ AGQLGLFGFT AYSASKFAIR GLAEALQMEV KPYNVYITVA YPPDTDTPGF AEENRTKPLE TRLISETTSV CKPEQVAKQI VKDAIQGNFN SSLGSD.

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    Kdsr Human
  • View Data Sheet

    Name :

    PNOC Human

    Description:

    Prepronociceptin Human Recombinant

    Prepronociceptin, Nocistatin, OFQ, Pre-Pro-N/OFQ, Pronociceptin, Orphanin FQ, Nociceptin, PpN/OFQ, N/OFQ, PPNOC.

    Product # :

    PRO-1442

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    Description

    PNOC Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 180 amino acids (20-176) and having a molecular mass of 20.6kDa. PNOC is fused to a 23 amino acid His-tag at N-terminus.

    Source

    Escherichia Coli.

    Formulation

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

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Prepronociceptin (PNOC) is the ligand of the opioid receptor-like receptor (OPRL1). PNOC functions as a transmitter in the brain by modulating nociceptive and locomotor behavior. The PNOC protein may also be involved in neuronal differentiation and development.

    • Synonyms

      Prepronociceptin, Nocistatin, OFQ, Pre-Pro-N/OFQ, Pronociceptin, Orphanin FQ, Nociceptin, PpN/OFQ, N/OFQ, PPNOC.

    • 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 MGSSCQRDCL TCQEKLHPAL DSFDLEVCIL ECEEKVFPSP LWTPCTKVMA RSSWQLSPAA PEHVAAALYQ PRASEMQHLR RMPRVRSLFQ EQEEPEPGME EAGEMEQKQL QKRFGGFTGA RKSARKLANQ KRFSEFMRQY LVLSMQSSQR RRTLHQNGNV.

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    Pnoc Human
  • View Data Sheet

    Name :

    CEBP Alpha Human

    Description:

    CCAAT/enhancer binding protein CEBP Alpha Human Recombinant

    CCAAT/enhancer-binding protein alpha, C/EBP alpha, CEBPA, CEBP.

    Product # :

    PRO-433

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    Description

    CEBP-a Human Recombinant His-Tag fusion protein produced in E.Coli is a single, non-glycosylated polypeptide chain containing amino acids 126 (aa 270-358) and having a molecular mass of 14.5 kDa. The Human CEBP-a Human is fused to a 37 amino acids His-Tag at N-terminus and is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The protein contains 20mM Tris-HCl pH7.5, 0.1M NaCl and 5mM b-Mercaptoethanol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      CCAAT/enhancer binding protein(C/EBP) a is a family of transcription factors that all contain a highly conserved, basic-leucine zipper domain at the C-terminus that is involved in dimerization and DNA binding. C/EBP family of transcription factors regulates viral and cellular CCAAT/enhancer element-mediated transcription. C/EBP family consist of several related proteins, C/EBP a,b,g,d, that form homodimers and that form heterodimers with each other. C/EBP proteins contain the bZIP region, which is characterized by two motifs in the C-terminal half of the protein; a basic region involved in DNA binding and a leucine zipper motif involved in dimerization. C/EBPs differ significantly in their physiological functions and in their downstream target genes. For example, mice lacking C/EBPa die shortly after birth due to severe hypoglycemia and the absence of glycogen storage in liver, whereas knockout of C/EBPb causes defects in female reproduction.

    • Synonyms

      CCAAT/enhancer-binding protein alpha, C/EBP alpha, CEBPA, CEBP.

    • Physical Appearance

      Sterile filtered colorless solution.

    • Stability

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

    • Amino Acid Sequence

      MRGSHHHHHH GMASMTGGQQ MGRDLYDDDD KDRWGSMGAG KAKKSVDKNS NEYRVRRERN NIAVRKSRDK AKQRNVETQQ KVLELTSDND RLRKRVEQLS RELDTLRGIF RQLPESSLVKAMGNCA.

    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.

    Cebpa Human
  • View Data Sheet

    Name :

    TULP1 Human

    Description:

    Tubby Like Protein 1 Human Recombinant

    Tubby like protein 1, TUBL1, RP14, LCA15, tubby-related protein 1.

    Product # :

    PRO-1191

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    Description

    TULP1 Human Recombinant produced in E. coli is a single polypeptide chain containing 276 amino acids (290-542) and having a molecular mass of 31.1 kDa.TULP1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    The TULP1 solution (1mg/1ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.2M NaCl, 5mM DTT, 2mM EDTA and 50% glycerol.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    More Info

    • Introduction

      Tubby-related protein 1 (TULP1) belongs to the TULP family of 4 proteins (TUB and TULP1, -2, and -3), categorized structurally by the highly conserved C-terminal half of the protein. Tubby-like gene family (TULPs) members are found in plants, vertebrates, and invertebrates and encode proteins of unknown function. TULP proteins share a conserved C-terminal region of roughly 200 amino acid residues. In the retina, TULP1 is observed exclusively in the photoreceptor cells, localizing predominantly in the inner segments and connecting cilium and to a lesser degree in the perinuclear cytoplasm and synaptic termini. TULP1 gene mutations are linked with retinitis pigmentosa.

    • Synonyms

      Tubby like protein 1, TUBL1, RP14, LCA15, tubby-related protein 1.

    • Physical Appearance

      Sterile Filtered colorless solution.

    • Stability

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

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MGSEPREFVL RPAPQGRTVR CRLTRDKKGM DRGMYPSYFL HLDTEKKVFL LAGRKRKRSK TANYLISIDP TNLSRGGENF IGKLRSNLLG NRFTVFDNGQ NPQRGYSTNV ASLRQELAAV IYETNVLGFR GPRRMTVIIP GMSAENERVP IRPRNASDGL LVRWQNKTLE SLIELHNKPP VWNDDSGSYT LNFQGRVTQA SVKNFQIVHA DDPDYIVLQF GRVAEDAFTL DYRYPLCALQ AFAIALSSFD GKLACE

    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.

    Tulp1 Human
  • View Data Sheet

    Name :

    LITAF Human

    Description:

    Lipopolysaccharide-Induced TNF Factor Human Recombinant

    Lipopolysaccharide-induced TNF-alpha factor, PIG7, SIMPLE, Lipopolysaccharide-induced tumor necrosis factor-alpha factor, LPS-induced TNF-alpha factor, p53-induced gene 7 protein, Small integral membrane protein of lysosome/late endosome, LITAF.

    Product # :

    PRO-1350

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    Description

    LITAF Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 181 amino acids (1-161) and having a molecular mass of 19.2 kDa. LITAF is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The LITAF solution (0.25mg/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

      Lipopolysaccharide-induced TNF-alpha factor (LITAF) is a small integral membrane protein of lysosome/late endosome. The expression of inflammatory cytokines such as TNF-alpha in Lipopolysaccharide-induced processes is mediated by LITAF. LITAF connects to STAT6B, which belongs to the STAT6 family forming a complex on the TNF-alpha promoter that modifies TNF activity. High levels of expression of LITAF mRNA are observed mostly in the placenta, peripheral blood leukocytes, lymph nodes and spleen.

    • Synonyms

      Lipopolysaccharide-induced TNF-alpha factor, PIG7, SIMPLE, Lipopolysaccharide-induced tumor necrosis factor-alpha factor, LPS-induced TNF-alpha factor, p53-induced gene 7 protein, Small integral membrane protein of lysosome/late endosome, LITAF.

    • 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 MSVPGPYQAA TGPSSAPSAP PSYEETVAVN SYYPTPPAPM PGPTTGLVTG PDGKGMNPPS YYTQPAPIPN NNPITVQTVY VQHPITFLDR PIQMCCPSCN KMIVSQLSYN AGALTWLSCG SLCLLGCIAG CCFIPFCVDA LQDVDHYCPN CRALLGTYKR L.

    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.

    Litaf Human
  • View Data Sheet

    Name :

    GSTP1 Mouse

    Description:

    Glutathione S-Transferase pi 1 Mouse Recombinant

    Glutathione S-transferase P 1, Gst P1, GST YF-YF, GST class-pi, GST-piB, Preadipocyte growth factor.

    Product # :

    ENZ-909

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    Description

    GSTP1 Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 233 amino acids (1-210 a.a) and having a molecular mass of 26kDa. GSTP1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    GSTP1 protein solution (1mg/ml) containing Phosphate Buffered Saline (pH 7.4) and 10% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    Biological Activity

    Specific activity is > 40 units/mg, and is defined as the amount of enzyme that conjugate 1.0 umole of 1-chloro-2,4-dinitrobenzene (CDNB) with reduced glutathione per minute at pH 6.5 at 25C.

    More Info

    • Introduction

      GSTP1 is a polymorphic gene encoding active, functionally different GSTP1 variant proteins that are believed to function in xenobiotic metabolism and have a part in susceptibility to cancer, and other diseases. GSTP1 is a glutathione S-transferase belonging to the pi class. GST family enzymes play a significant role in detoxification by catalyzing the conjugation of many hydrophobic and electrophilic compounds with reduced glutathione. Based upon the biochemical, immunologic and structural properties of the soluble GSTs they are grouped into 4 main classes: alpha, mu, pi, and theta. The GSTP1 enzyme acts by catalyzing the reaction of glutathione with an acceptor molecule to form a Sulfur-substituted glutathione. The reactions employing glutathione contribute the transformation of a broad range of electrophiles, including reactive products of lipid, protein, carcinogens, therapeutic drugs, environmental toxins, and products of oxidative stress.
      The GSTP1 inactivation through CpG hypermethylation is frequent in pituitary adenomas and may be a factor in aggressive pituitary tumor behavior. GSTP1 is may be a transcriptional target of the p53 tumor suppressor gene. Single-nucleotide polymorphism in GSTP1 is linked to modified protein binding, which influence GSTP1's contribution to carcinogen and drug metabolism, and possibly disease pathogenesis and/or drug response. GST-pi might have central roles in proliferation of androgen-independent human prostate cancer cells.

    • Synonyms

      Glutathione S-transferase P 1, Gst P1, GST YF-YF, GST class-pi, GST-piB, Preadipocyte growth factor.

    • 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 MGSMPPYTIV YFPVRGRCEA MRMLLADQGQ SWKEEVVTID TWMQGLLKPT CLYGQLPKFE DGDLTLYQSN AILRHLGRSL GLYGKNQREA AQMDMVNDGV EDLRGKYVTL IYTNYENGKN DYVKALPGHL KPFETLLSQN QGGKAFIVGD QISFADYNLL DLLLIHQVLA PGCLDNFPLL SAYVARLSAR PKIKAFLSSP EHVNRPINGN GKQ.

    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.

    Gstp1 Mouse
  • View Data Sheet

    Name :

    MAPKSP1 Human

    Description:

    MAPK Scaffold Protein 1 Human Recombinant

    MAPBP, MP1, MAPK Scaffold Protein 1, Interacting Protein 1, MEK binding partner 1, Mitogen-Activated Protein Kinase kinase 1.

    Product # :

    PRO-034

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    Description

    MAPKSP1 produced in E.Coli is a single, non-glycosylated polypeptide chain containing 144 amino acids (1-124a.a.) and having a molecular mass of 15.8kDa.MAPKSP1 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The MAPKSP1 protein solution (0.5mg/1ml) is formulated in 20mM Tris-HCl buffer (pH8.0) 5mM DTT, 100mM NaCl and 20% glycerol.

    Purity

    Greater than 95% as determined by SDS-PAGE.

    More Info

    • Introduction

      MAPKSP1 is a scaffold protein which operates in the extracellular signal-regulated kinase (ERK) cascade. MAPKSP1 protein is restricted to late endosomes by the mitogen-activated protein-binding protein-interacting protein, and binds specifically to MAP kinase kinase MAP2K1/MEK1, MAP kinase MAPK3/ERK1, and MAP kinase MAPK1/ERK2.

    • Synonyms

      MAPBP, MP1, MAPK Scaffold Protein 1, Interacting Protein 1, MEK binding partner 1, Mitogen-Activated Protein Kinase kinase 1.

    • Physical Appearance

      Sterile Filtered clear solution.

    • Stability

      Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time.Please avoid freeze thaw cycles.

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MADDLKRFLY KKLPSVEGLH AIVVSDRDGV PVIKVANDNA PEHALRPGFL STFALATDQG SKLGLSKNKS IICYYNTYQV VQFNRLPLVV SFIASSSANT GLIVSLEKEL APLFEELRQV VEVS

    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.

    Mapksp1 Human
  • View Data Sheet

    Name :

    COPS8 Human

    Description:

    COP9 Constitutive Photomorphogenic 8 Human Recombinant

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

    Product # :

    PRO-983

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    Description

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

    Source

    Escherichia Coli.

    Formulation

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

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

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

    • Synonyms

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

    • Physical Appearance

      Sterile Filtered colorless solution.

    • Stability

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

    • Amino Acid Sequence

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

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

    Cops8 Human
  • View Data Sheet

    Name :

    VPS25 Human

    Description:

    Vacuolar Protein Sorting 25 Human Recombinant

    Vacuolar protein sorting 25 homolog (S. cerevisiae), vacuolar protein-sorting-associated protein 25, ELL-associated protein of 20 kDa, ESCRT-II complex subunit VPS25, Dermal papilla-derived protein 9, DERP9, EAP20, FAP20, MGC10540.

    Product # :

    PRO-1054

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    Description

    VPS25 Human Recombinant produced in E. coli is a single polypeptide chain containing 200 amino acids (1-176) and having a molecular mass of 23.3kDa.VPS25 is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    The VPS25 solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 100mM Nacl, and 20% glycerol.

    Purity

    Greater than 85% as determined by SDS-PAGE.

    More Info

    • Introduction

      VPS25 contains the ESCRT-II complex (endosomal sorting complex required for transport II), that is needed for sorting of endosomal cargo proteins into MVBs and multivesicular body (MVB) formation. The MVB pathway facilitates transport of transmembrane proteins into the lumen of the lysosome for degradation. The ESCRT-II complex takes part in the recruitment of the ESCRT-III complex which is involved in transcription regulation, probably through its collaboration with ELL.

    • Synonyms

      Vacuolar protein sorting 25 homolog (S. cerevisiae), vacuolar protein-sorting-associated protein 25, ELL-associated protein of 20 kDa, ESCRT-II complex subunit VPS25, Dermal papilla-derived protein 9, DERP9, EAP20, FAP20, MGC10540.

    • 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 MGSHMAMSFE WPWQYRFPPF FTLQPNVDTR QKQLAAWCSL VLSFCRLHKQ SSMTVMEAQE SPLFNNVKLQ RKLPVESIQI VLEELRKKGN LEWLDKSKSS FLIMWRRPEE WGKLIYQWVS RSGQNNSVFT LYELTNGEDT EDEEFHGLDE ATLLRALQAL QQEHKAEIIT VSDGRGVKFF

    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.

    Vps25 Human
  • View Data Sheet

    Name :

    XAF1 Human

    Description:

    XIAP Associated Factor 1 Human Recombinant

    XIAP Associated Factor 1, BIRC4-Binding Protein, BIRC4BP, XIAPAF1, XIAP-Associated Factor 1, BIRC4 Binding Protein, HSXIAPAF1, XAF1.

    Product # :

    PRO-1963

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    Description

    XAF1 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 161 amino acids (1-125) and having a molecular mass of 18.6 kDa.XAF1 is fused to a 36 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The XAF1 solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 30% glycerol, 0.15M NaCl and 1mM DTT.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      XIAP Associated Factor 1 (XAF1) is a protein which binds to and counteracts the inhibitory effect of a member of the IAP (inhibitor of apoptosis) protein family. IAP proteins bind to and inhibit caspases which are activated in the course of apoptosis. The ratio of IAPs and proteins which interfere with their activity, such as the XAF1 protein, influence the progress of the apoptosis signaling pathway. Additionally, XAF1 inhibits anti-caspase activity of BIRC4. XAF1 induces cleavage and inactivation of BIRC4 independent of caspase activation. Furthermore, XAF1 mediates TNF-alpha-induced apoptosis and is involved in apoptosis in trophoblast cells.

    • Synonyms

      XIAP Associated Factor 1, BIRC4-Binding Protein, BIRC4BP, XIAPAF1, XIAP-Associated Factor 1, BIRC4 Binding Protein, HSXIAPAF1, XAF1.

    • Physical Appearance

      Sterile Filtered colorless solution.

    • Stability

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

    • Amino Acid Sequence

      MRGSHHHHHH GMASMTGGQQ MGRDLYDDDD KDRWGSMEGD FSVCRNCKRH VVSANFTLHE AYCLRFLVLC PECEEPVPKE TMEEHCKLEH QQVGCTMCQQ SMQKSSLEFH KANECQERPV ECKFCKLDMQ LSKLELHESY CGSRTELCQG CGQFIMHRML A.

    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.

    Xaf1 Human
  • View Data Sheet

    Name :

    RBBP4 Human

    Description:

    Retinoblastoma Binding Protein 4 Human Recombinant

    Histone-binding protein RBBP4, Chromatin assembly factor 1 subunit C, CAF-1 subunit C, Chromatin assembly factor I p48 subunit, CAF-I 48 kDa subunit, CAF-I p48, Nucleosome-remodeling factor subunit RBAP48, Retinoblastoma-binding protein 4, RBBP-4, Retinoblastoma-binding protein p48, RBBP4, RBAP48, NURF55.

    Product # :

    PRO-1168

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    Description

    RBBP4 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 449 amino acids (1-425 a.a) and having a molecular mass of 50.2kDa.RBBP4 is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    RBBP4 protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.1M NaCl, 10% glycerol and 1mM EDTA.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    More Info

    • Introduction

      Retinoblastoma binding protein 4 (RBBP4) is a ubiquitously expressed nuclear protein which is a member of a highly conserved subfamily of WD-repeat proteins. RBBP4 is present in protein complexes involved in histone acetylation and chromatin assembly. In addition, RBBP4 is part of co-repressor complexes, which is a fundamental component of transcriptional silencing. RBBP4 is observed among several cellular proteins which bind directly to a retinoblastoma protein to regulate cell proliferation. RBBP4 also is a part of the Mi-2 complex which is implicated in chromatin remodeling and transcriptional repression connected with histone deacetylation.

    • Synonyms

      Histone-binding protein RBBP4, Chromatin assembly factor 1 subunit C, CAF-1 subunit C, Chromatin assembly factor I p48 subunit, CAF-I 48 kDa subunit, CAF-I p48, Nucleosome-remodeling factor subunit RBAP48, Retinoblastoma-binding protein 4, RBBP-4, Retinoblastoma-binding protein p48, RBBP4, RBAP48, NURF55.

    • 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 MGSHMADKEA AFDDAVEERV INEEYKIWKK NTPFLYDLVM THALEWPSLT AQWLPDVTRP EGKDFSIHRL VLGTHTSDEQ NHLVIASVQL PNDDAQFDAS HYDSEKGEFG GFGSVSGKIE IEIKINHEGE VNRARYMPQN PCIIATKTPS SDVLVFDYTK HPSKPDPSGE CNPDLRLRGH QKEGYGLSWN PNLSGHLLSA SDDHTICLWD ISAVPKEGKV VDAKTIFTGH TAVVEDVSWH LLHESLFGSV ADDQKLMIWD TRSNNTSKPS HSVDAHTAEV NCLSFNPYSE FILATGSADK TVALWDLRNL KLKLHSFESH KDEIFQVQWS PHNETILASS GTDRRLNVWD LSKIGEEQSP EDAEDGPPEL LFIHGGHTAK ISDFSWNPNE PWVICSVSED NIMQVWQMAE NIYNDEDPEG SVDPEGQGS.

    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.

    Rbbp4 Human
  • View Data Sheet

    Name :

    RBP4 Human

    Description:

    Retinol Binding Protein-4 Human Recombinant

    Retinol Binding Protein 4, RBP-4, RBP4, Plasma retinol-binding protein, PRBP, RBP.

    Product # :

    CYT-535

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    Description

    RBP-4 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain (19-201 a.a.) containing 184 amino acids and having a molecular mass of 21 kDa.The Retinol Binding Protein-4 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    1 mg/ml in PBS pH-7.4.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Retinol binding protein 4(RBP4) belongs to the lipocalin family and is the specific carrier for retinol (vitamin A alcohol) in the blood. This protein was found to be expressed and secreted by adipose tissue, and was strongly associated with insulin resistance. It delivers retinol from the liver stores to the peripheral tissues. In plasma, the RBP-retinol complex interacts with transthyretin which prevents its loss by filtration through the kidney glomeruli.
      RBP4 delivers retinol from the liver to the peripheral tissues. In plasma, the rbp-retinol complex interacts with transthyretin, this prevents its loss by filtration through the kidney glomeruli.

    • Synonyms

      Retinol Binding Protein 4, RBP-4, RBP4, Plasma retinol-binding protein, PRBP, RBP.

    • 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

      MERDCRVSSF RVKENFDKAR FSGTWYAMAK KDPEGLFLQD NIVAEFSVDE TGQMSATAKGRVRLLNNWDV CADMVGTFTD TEDPAKFKMK YWGVASFLQK GNDDHWIVDT DYDTYAVQYS CRLLNLDGTC ADSYSFVFSR DPNGLPPEAQ KIVRQRQEEL CLARQYRLIV HNGYCDGRSE RNLL.

    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.

    Rbp4 Human
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