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Search results

1000 results found for “calmodulin”

Name

Description

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  • View Data Sheet

    Name :

    TRIM21 Human

    Description:

    Tripartite Motif Containing 21 (RO52) Human Recombinant

    52 kDa Ro protein, Sjoegren syndrome type A antigen, SS-A, Ro(SS-A), 52 kDa ribonucleoprotein autoantigen Ro/SS-A, Tripartite motif-containing protein 21, RING finger protein 81, TRIM21, RNF81, RO52, SSA1, SSA, RO-52.

    Product # :

    PRO-328

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    Description

    TRIM21 Human Recombinant produced in SF9 is a polypeptide chain having a calculated molecular mass of 52 kDa. TRIM21 is expressed with a -6x His tag at N-terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9 insect cells.

    Formulation

    TRIM21 solution is supplied in 20mM HEPES pH-7.5, 0.01mM EDTA and 0.02% SDS.

    Purity

    Greater than 95% as determined by SDS-PAGE.

    More Info

    • Introduction

      TRIM21 is a member of the tripartite motif (TRIM) family. The TRIM motif includes three zinc-binding domains, a RING, a B-box type 1 and a B-box type 2, and a coiled-coil region. The 52 kDa Ro protein is part of the RoSSA ribonucleoprotein, which includes a single polypeptide and one of four small RNA molecules. The RoSSA particle localizes to both the cytoplasm and the nucleus. Ro/SSA interacts with autoantigens in patients with Sjogren syndrome and systemic lupus erythematosus. Ribonucleoprotein particle is composed of a single polypeptide and one of four small RNA molecules. The RoSSA is present in all mammalian cells studied but has no known function. At least 2 isoforms are present in nucleated and red blood cells, and tissue specific differences in Ro/SSA proteins were identified.

    • Synonyms

      52 kDa Ro protein, Sjoegren syndrome type A antigen, SS-A, Ro(SS-A), 52 kDa ribonucleoprotein autoantigen Ro/SS-A, Tripartite motif-containing protein 21, RING finger protein 81, TRIM21, RNF81, RO52, SSA1, SSA, RO-52.

    • 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.

    Trim21 Human
  • View Data Sheet

    Name :

    PSME2 Human

    Description:

    Proteasome Activator Subunit 2 Human Recombinant

    Proteasome (prosome, macropain) activator subunit 2 (PA28 beta), PA28beta, Activator of multicatalytic protease subunit 2, Proteasome activator 28 subunit beta, 11S regulator complex subunit beta, PA28B, REG-beta, cell migration-inducing protein 22, MCP activator 31-kD subunit, proteasome activator complex subunit 2, Proteasome activator hPA28 subunit beta.

    Product # :

    PRO-975

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    Description

    PSME2 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 259 amino acids (1-239) and having a molecular mass of 29.5 kDa.PSME2 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    The PSME2 solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.1M NaCl, 1mM DTT, 0.1mM PMSF and 20% glycerol.

    Purity

    Greater than 95% as determined by SDS-PAGE.

    More Info

    • Introduction

      PSME2 is an IFN-gamma inducible proteasome activator essential for production of several key histocompatibility (MHC) class I antigens. Downregulation of PSME2 causes unusual proteasome activation and is connected to the development of intimal hyperplasia (IH) in animal models.

    • Synonyms

      Proteasome (prosome, macropain) activator subunit 2 (PA28 beta), PA28beta, Activator of multicatalytic protease subunit 2, Proteasome activator 28 subunit beta, 11S regulator complex subunit beta, PA28B, REG-beta, cell migration-inducing protein 22, MCP activator 31-kD subunit, proteasome activator complex subunit 2, Proteasome activator hPA28 subunit beta.

    • 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 MAKPCGVRLS GEARKQVEVF RQNLFQEAEE FLYRFLPQKI IYLNQLLQED SLNVADLTSL RAPLDIPIPD PPPKDDEMET DKQEKKEVPK CGFLPGNEKV LSLLALVKPE VWTLKEKCIL VITWIQHLIP KIEDGNDFGV AIQEKVLERV NAVKTKVEAF QTTISKYFSE RGDAVAKASK ETHVMDYRAL VHERDEAAYG ELRAMVLDLR AFYAELYHII SSNLEKIVNP KGEEKPSMY

    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.

    Psme2 Human
  • View Data Sheet

    Name :

    M CSF Rat HEK

    Description:

    Macrophage Colony Stimulating Factor Rat Recombinant HEK

    CSF-1, Lanimostim, MCSF, MGC31930, M-CSF.

    Product # :

    CYT-046

    Price :

    Quantity :

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    • description
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    Description

    MCSF Rat Recombinant produced in HEK-293 cells is a secreted protein (amino acids Glu33-Arg254). M-CSF is disulfide-linked homodimer containing 2 x 222 a.a chains.

    Source

    HEK293

    Formulation

    The recombinant MCSF was lyophilized after extensive dialysis against PBS.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Biological Activity

    The ED50 of 3-4ng/ml is measured by its ability to stimulate the proliferation of mouse M-NFS-60 cells.

    More Info

    • Introduction

      Granulocyte/Macrophage Colony-Stimulating Factors are cytokines that act in hematopoiesis by controlling the production, differentiation, and function of 2 related white cell populations of the blood, the granulocytes and the monocytes-macrophages. CSF-1 induces cells of the monocyte/macrophage lineage. It plays a role in immunological defenses, bone metabolism, lipoproteins clearance, fertility and pregnancy.

    • Synonyms

      CSF-1, Lanimostim, MCSF, MGC31930, M-CSF.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    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.

    M Csf Rat
  • View Data Sheet

    Name :

    MAPT Human 381a.a.

    Description:

    Microtubule-Associated Protein Tau 381 a.a. Human Recombinant

    Microtubule-associated protein tau, isoform CRA_f, Neurofibrillary tangle protein, Paired helical filament-tau, PHF-tau, MAPT, MAPTL, MTBT1, TAU, MSTD, PPND, DDPAC, MTBT2, FTDP-17, FLJ31424, MGC138549.

    Product # :

    PRO-042

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    • description
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    Description

    MAPT 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 401 amino acids (1-381 a.a.) and having a molecular mass of 41.8kDa. The NCBI Accession No. is EAW93573.1.The MAPT is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The MAPT solution (0.5 mg/ml) contains 20mM Tris-HCl Buffer (pH 7.5), 1mM DTT and 20% Glycerol.

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Microtubule-associated protein tau (MAPT or Tau) is a protein that stabilizes microtubules. MAPT is abundant in neurons in the central nervous system and is less common elsewhere. When MAPT is defective, and no longer stabilizes microtubules properly, it can result in dementias, such as Alzheimer's disease.

    • Synonyms

      Microtubule-associated protein tau, isoform CRA_f, Neurofibrillary tangle protein, Paired helical filament-tau, PHF-tau, MAPT, MAPTL, MTBT1, TAU, MSTD, PPND, DDPAC, MTBT2, FTDP-17, FLJ31424, MGC138549.

    • 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 MAEPRQEFEV MEDHAGTYGL GDRKDQGGYT MHQDQEGDTD AGLKESPLQT PTEDGSEEPG SETSDAKSTP TAEAEEAGIG DTPSLEDEAA GHVTQARMVS KSKDGTGSDD KKAKGADGKT KIATPRGAAP PGQKGQANAT RIPAKTPPAP KTPPSSGEPP KSGDRSGYSS PGSPGTPGSR SRTPSLPTPP TREPKKVAVV RTPPKSPSSA KSRLQTAPVP MPDLKNVKSK IGSTENLKHQ PGGGKVQIVY
      KPVDLSKVTS KCGSLGNIHH KPGGGQVEVK SEKLDFKDRV QSKIGSLDNI THVPGGGNKK IETHKLTFRE NAKAKTDHGA EIVYKSPVVS GDTSPRHLSN VSSTGSIDMV DSPQLATLAD EVSASLAKQG 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.

    Mapt Human 381Aa
  • View Data Sheet

    Name :

    HAUS1 Human

    Description:

    HAUS Augmin-Like Complex, Subunit 1 Human Recombinant

    HAUS augmin-like complex subunit 1, Coiled-coil domain-containing protein 5, Enhancer of invasion-cluster, HEI-C, HAUS1, CCDC5, HEIC, HsT1461.

    Product # :

    PRO-1077

    Price :

    Quantity :

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    Description

    HAUS1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 302 amino acids (1-278 a.a) and having a molecular mass of 34.4kDa.HAUS1 is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    HAUS1 protein solution (0.25mg/ml) containing 20mM Tris-HCl buffer (pH8.0), 50% glycerol, 0.2M NaCl and 2mM DTT.

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      HAUS augmin-like complex subunit 1 (HAUS1) is 1 of 8 subunits of the 390kDa human augmin complex/ HAUS complex. The augmin complex is a microtubule-binding complex required in microtubule generation within the mitotic spindle and is imperative to mitotic spindle compilation. HAUS1 contributes to mitotic spindle assembly, maintenance of centrosome integrity and completion of cytokinesis as part of the HAUS augmin-like complex. HAUS1 is broadly expressed, especially in the pancreas, kidney, skeletal muscle, liver and heart. However it is weakly expressed in the lung, brain and placenta. HAUS1-depleted cells hold functional cell cycle checkpoints, but the depletion reduces the G2/M cell cycle compartment and stimulates apoptosis. The HAUS1 protein level remains constant through the cell cycle.

    • Synonyms

      HAUS augmin-like complex subunit 1, Coiled-coil domain-containing protein 5, Enhancer of invasion-cluster, HEI-C, HAUS1, CCDC5, HEIC, HsT1461.

    • 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 MGSHMEPQEE RETQVAAWLK KIFGDHPIPQ YEVNPRTTEI LHHLSERNRV RDRDVYLVIE DLKQKASEYE SEAKYLQDLL MESVNFSPAN LSSTGSRYLN ALVDSAVALE TKDTSLASFI PAVNDLTSDL FRTKSKSEEI KIELEKLEKN LTATLVLEKC
      LQEDVKKAEL HLSTERAKVD NRRQNMDFLK AKSEEFRFGI KAAEEQLSAR GMDASLSHQS LVALSEKLAR LKQQTIPLKK KLESYLDLMP NPSLAQVKIE EAKRELDSIE AELTRRVDMM EL.

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    Haus1 Human
  • View Data Sheet

    Name :

    ORM1 Human, HEK

    Description:

    Orosomucoid 1 Human Recombinant, HEK

    Orosomucoid 1, ORM, AGP1, OMD 1, AGP-A, alpha-1-acid glycoprotein 1.

    Product # :

    PRO-2764

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    Description

    ORM1 Human Recombinant produced in HEK is a polypeptide chain containing 189 amino acids (19-201) and having a molecular mass of 22.4 kDa. The ORM1 is fused to a 6 a.a. amino acid His tag at C-terminus & purified by proprietary chromatographic techniques.

    Source

    HEK293

    Formulation

    The ORM1 solution (1mg/ml) contains 1x PBS pH-7 and 10% glycerol.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    More Info

    • Introduction

      The acute phase plasma protein ORM1 synthesized by the liver mediates the interaction between blood cells and endothelial cells. In addition, together with haptoglobin and C reactive protein, ORM1 regulates the extravasation of the cells through infection and inflammation. Expression of ORM1 is induced by acute-phase stimulatory mediators such as bacterial lipopolysaccharides.

    • Synonyms

      Orosomucoid 1, ORM, AGP1, OMD 1, AGP-A, alpha-1-acid glycoprotein 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

      QIPLCANLVP VPITNATLDR ITGKWFYIAS AFRNEEYNKS VQEIQATFFY FTPNKTEDTI FLREYQTRQD QCIYNTTYLN VQRENGTISR YVGGQEHFAH LLILRDTKTY MLAFDVNDEK NWGLSVYADK PETTKEQLGE FYEALDCLRI PKSDVVYTDW KKDKCEPLEK QHEKERKQEE GES HHHHHH

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    Orm1 Protein
  • View Data Sheet

    Name :

    DDR1 Human

    Description:

    Discoidin Domain Receptor Tyrosine Kinase 1 Human Recombinant

    Discoidin Domain Receptor Tyrosine Kinase 1, CD167 Antigen-Like Family Member A, Protein-Tyrosine Kinase RTK-6, Mammary Carcinoma Kinase 10, Tyrosine-Protein Kinase CAK, Cell Adhesion Kinase, Tyrosine Kinase DDR, EC 2.7.10.1, EDDR1, NTRK4, PTK3A, HGK2, RTK6, TRKE, CAK, NEP, Neurotrophic Tyrosine Kinase, Receptor, Type 4, Discoidin Domain Receptor Family, Member 1, Epithelial Discoidin Domain Receptor 1, Discoidin Receptor Tyrosine Kinase, PTK3A Protein Tyrosine Kinase 3A, Neuroepithelial Tyrosine Kinase, Protein-Tyrosine Kinase 3A, CD167a Antigen, EC 2.7.10, MCK-10, CD167, MCK10, TRK E, PTK3, DDR.

    Product # :

    PKA-103

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    Description

    DDR1 Human Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 636 amino acids (21-417a.a.) and having a molecular mass of 71.0kDa (Molecular size on SDS-PAGE will appear at approximately 70-100kDa).DDR1 is expressed with a 239 amino acid hIgG-His tag at C-Terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    DDR1 protein solution (0.5mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 10% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Discoidin Domain Receptor Tyrosine Kinase 1 (DDR1) is a transmembrane glycoprotein which is a part of the discoidin-like domain containing subfamily of receptor tyrosine kinases. DDR1 functions as cell surface receptor for fibrillar collagen and regulates cell attachment to the extracellular matrix, remodeling of the extracellular matrix, cell migration, differentiation, survival and cell proliferation. DDR1 is expressed in epithelial cells, mainly in the kidney, lung, gastrointestinal tract, and brain and is significantly overexpressed in several human tumors.

    • Synonyms

      Discoidin Domain Receptor Tyrosine Kinase 1, CD167 Antigen-Like Family Member A, Protein-Tyrosine Kinase RTK-6, Mammary Carcinoma Kinase 10, Tyrosine-Protein Kinase CAK, Cell Adhesion Kinase, Tyrosine Kinase DDR, EC 2.7.10.1, EDDR1, NTRK4, PTK3A, HGK2, RTK6, TRKE, CAK, NEP, Neurotrophic Tyrosine Kinase, Receptor, Type 4, Discoidin Domain Receptor Family, Member 1, Epithelial Discoidin Domain Receptor 1, Discoidin Receptor Tyrosine Kinase, PTK3A Protein Tyrosine Kinase 3A, Neuroepithelial Tyrosine Kinase, Protein-Tyrosine Kinase 3A, CD167a Antigen, EC 2.7.10, MCK-10, CD167, MCK10, TRK E, PTK3, DDR.

    • 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

      DMKGHFDPAK CRYALGMQDR TIPDSDISAS SSWSDSTAAR HSRLESSDGD GAWCPAGSVF PKEEEYLQVD LQRLHLVALV GTQGRHAGGL GKEFSRSYRL RYSRDGRRWM GWKDRWGQEV ISGNEDPEGV VLKDLGPPMV ARLVRFYPRA DRVMSVCLRV ELYGCLWRDG LLSYTAPVGQ TMYLSEAVYL NDSTYDGHTV GGLQYGGLGQ LADGVVGLDD FRKSQELRYV WPGYDYVGWS NHSFSSGYVE MEFEFDRLRA FQAMQVHCNN MHTLGARLPG GVECRFRRGP AMAWEGEPMR HNLGGNLGDP RARAVSVPLG GRVARFLQCR FLFAGPWLLF SEISFISDVV NNSSPALGGT FPPAPWWPPG PPPTNFSSLE LEPRGQQPVA KAEGSPTALE PKSCDKTHTC PPCPAPELLG GPSVFLFPPK PKDTLMISRT PEVTCVVVDV SHEDPEVKFN WYVDGVEVHN AKTKPREEQY NSTYRVVSVL TVLHQDWLNG KEYKCKVSNK ALPAPIEKTI SKAKGQPREP QVYTLPPSRD ELTKNQVSLT CLVKGFYPSD IAVEWESNGQ PENNYKTTPP VLDSDGSFFL YSKLTVDKSR WQQGNVFSCS VMHEALHNHY TQKSLSLSPG KHHHHHH.

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    Ddr1 Human
  • View Data Sheet

    Name :

    SERTAD1 Human

    Description:

    SERTA Domain Containing 1 Human Recombinant

    SERTA domain-containing protein 1, CDK4-binding protein p34SEI1, SEI-1, Transcriptional regulator interacting with the PHD-bromodomain 1, TRIP-Br1, SERTAD1, SEI1.

    Product # :

    PRO-1157

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    Description

    SERTAD1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 260 amino acids (1-236 a.a) and having a molecular mass of 27.3kDa (Molecular weight on SDS-PAGE will appear higher).SERTAD1 is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    SERTAD1 protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH8.0), 10% glycerol and 1mM DTT.

    Purity

    Greater than 85% as determined by SDS-PAGE.

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    • Introduction

      SERTA domain-containing protein (SERTAD1) functions with E2F-responsive promoters to integrate signals provided by PHD- and/or bromodomain-containing transcription factors. SERTAD1 stimulates E2F-1/DP-1 transcriptional activity. SERTAD1 reduces the activity of cyclin D1/CDK4 resistant to the inhibitory effects of p16(INK4a). In addition, SERTAD1 interacts with the PHD-bromodomain of TIF1, TRIM28/TIF1B and p300/CBP. Furthermore, SERTAD1 binds to DP1 and interacts with CDK4.

    • Synonyms

      SERTA domain-containing protein 1, CDK4-binding protein p34SEI1, SEI-1, Transcriptional regulator interacting with the PHD-bromodomain 1, TRIP-Br1, SERTAD1, SEI1.

    • 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 MGSHMLSKGL KRKREEEEEK EPLAVDSWWL DPGHTAVAQA PPAVASSSLF DLSVLKLHHS LQQSEPDLRH LVLVVNTLRR IQASMAPAAA LPPVPSPPAA PSVADNLLAS SDAALSASMA SLLEDLSHIE GLSQAPQPLA DEGPPGRSIG GAAPSLGALD LLGPATGCLL DDGLEGLFED IDTSMYDNEL WAPASEGLKP GPEDGPGKEE APELDEAELD YLMDVLVGTQ ALERPPGPGR.

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    Sertad1 Human
  • View Data Sheet

    Name :

    BMP3 Human

    Description:

    Bone Morphogenetic protein-3 Human Recombinant

    Bone Morphogenetic Protein 3, Osteogenin, Bone Morphogenetic Protein 3 (Osteogenic), Bone Morphogenetic Protein 3A, BMP-3A, BMP-3, Bone Morphogenetic Protein-3, BMP3A, BMP3.

    Product # :

    CYT-937

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    Description

    BMP3 Human Recombinant produced in E.coli is a non-glycosylated disulfide linked homodimer containing 2 chains of 110 amino acids and having a molecular mass of 24.8kDa.The BMP-3 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    BMP-3 protein was lyophilized from a 0.2µm filtered concentrated solution in 30% Acetonitrile and 0.1% TFA.

    Purity

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

    Biological Activity

    The ED50 as determined by its ability to inhibit BMP-2-induced activity in murine MC3T3- E1 cells.

    More Info

    • Introduction

      Bone Morphogenetic Protein 3 (BMP3) is one of the BMPs, some of which are members of the TGF-beta superfamily (BMP2-7). There are more than 13 BMPs, which are involved in inducing cartilage and bone formation, embryogenesis and morphogenesis of various tissues and organs. In addition, BMPs regulate the growth, differentiation, chemotaxis, and apoptosis of various cell types. Akin to most other TGF-beta family proteins, BMPs are extremely conserved across animal species. At the amino acid sequence level, mature human and rat BMP3 are 98% identical.

    • Synonyms

      Bone Morphogenetic Protein 3, Osteogenin, Bone Morphogenetic Protein 3 (Osteogenic), Bone Morphogenetic Protein 3A, BMP-3A, BMP-3, Bone Morphogenetic Protein-3, BMP3A, BMP3.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized BMP3 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution BMP-3 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 BMP3 in sterile 4mM HCl not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      QWIEPRNCAR RYLKVDFADI GWSEWIISPK SFDAYYCSGA CQFPMPKSLK PSNHATIQSI VRAVGVVPGI PEPCCVPEKM SSLSILFFDE NKNVVLKVYP NMTVESCACR.

    • Background

      Bone Morphogenetic Protein-3 Human Recombinant: Unveiling the Potential of a Key Regulator in Tissue Regeneration

      Abstract:

      Bone Morphogenetic Protein-3 (BMP-3) human recombinant is a critical member of the bone morphogenetic protein family, known for its role in tissue development, repair, and regeneration. This research paper provides a comprehensive analysis of BMP-3, including its characteristics, signaling pathways, and potential therapeutic applications. Additionally, innovative methodologies for the production and optimization of BMP-3 human recombinant are proposed, shedding light on its future implications in the field of regenerative medicine.

      Introduction:

      Tissue regeneration is a complex biological process requiring precise molecular cues. BMP-3, a crucial member of the BMP family, plays a significant role in tissue development and regeneration. This paper explores the unique features of BMP-3 and presents novel approaches for its production and optimization, aiming to unlock its therapeutic potential in various regenerative contexts.

      Characteristics and Signaling Pathways:

      BMP-3 is a secreted protein that binds to cell surface receptors, initiating intracellular signaling cascades. It influences cell differentiation, proliferation, and extracellular matrix synthesis through both Smad-dependent and Smad-independent signaling pathways. BMP-3 signaling regulates critical processes involved in tissue regeneration, including chondrogenesis and osteogenesis.

      Production of BMP-3 Human Recombinant:

      Efficient production methodologies are essential for harnessing the therapeutic potential of BMP-3 human recombinant. Recombinant protein expression systems, such as Escherichia coli or mammalian cells, have been utilized to produce functional BMP-3. Optimization strategies, including codon optimization, signal peptide engineering, and protein folding optimization, have been employed to enhance the yield and activity of BMP-3 recombinant protein.

      Potential Therapeutic Applications:

      BMP-3 human recombinant holds significant promise in the field of regenerative medicine. It plays a crucial role in bone and cartilage regeneration, making it a potential candidate for the treatment of skeletal disorders and tissue injuries. Additionally, BMP-3 signaling influences tissue remodeling and wound healing, suggesting its broader therapeutic applications in other regenerative processes.

      Conclusion:

      BMP-3 human recombinant represents a key regulator in tissue regeneration, with immense potential in regenerative medicine. Optimizing production methodologies and further unraveling its signaling mechanisms will enhance its therapeutic applications. With its implications in bone and cartilage regeneration and its role in tissue remodeling, BMP-3 human recombinant emerges as a promising tool for promoting tissue repair and regeneration.

      What is the molecular weight/Mw of BMP3 Protein?
      BMP3 Protein has a total Mw of 24.8kDa.

      What is the source or expression system of BMP3 Protein?
      Escherichia Coli.

      What is the Purity of BMP3 Protein?
      BMP3 Protein is >95% pure as determined by SDS-PAGE.

      What is the Biological Activity of BMP3 Protein?
      The ED50 as determined by its ability to inhibit BMP-2-induced activity in murine MC3T3- E1 cells.

      What is the amino acid sequence of BMP3 Protein?
      QWIEPRNCAR RYLKVDFADI GWSEWIISPK SFDAYYCSGA CQFPMPKSLK PSNHATIQSI VRAVGVVPGI PEPCCVPEKM SSLSILFFDE NKNVVLKVYP NMTVESCACR.

      What applications can BMP3 Protein be used in?
      BMP3 Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for BMP3 Protein?
      The endotoxin level is minimal, BMP3 Protein was purified using conventional chromatography techniques.

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    Bmp3 Human
  • View Data Sheet

    Name :

    PDCL Human

    Description:

    Phosducin-Like Human Recombinant

    Phosducin-like protein, PHLP, DKFZp564M1863.

    Product # :

    PRO-1141

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    Description

    PDCL Human Recombinant produced in E. coli is a single polypeptide chain containing 325 amino acids (1-301) and having a molecular mass of 36.8 kDa.PDCL is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

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

    Purity

    Greater than 90% as determined by SDS-PAGE.

    More Info

    • Introduction

      Phosducin-like protein (PDCL) is a member of the phosducin family. PDCL is a putative modulator of heterotrimeric G proteins. PDCL shares broad amino acid sequence homology with phosducin, a phosphoprotein expressed in the retina and pineal gland. Both PDCL and phosphoducin regulate G-protein signaling by binding to the beta-gamma subunits of G proteins.

    • Synonyms

      Phosducin-like protein, PHLP, DKFZp564M1863.

    • 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 MGSHMTTLDD KLLGEKLQYY YSSSEDEDSD HEDKDRGRCA PASSSVPAEA ELAGEGISVN TGPKGVINDW RRFKQLETEQ REEQCREMER LIKKLSMTCR SHLDEEEEQQ KQKDLQEKIS GKMTLKEFAI MNEDQDDEEF LQQYRKQRME EMRQQLHKGP QFKQVFEISS GEGFLDMIDK EQKSIVIMVH IYEDGIPGTE AMNGCMICLA AEYPAVKFCK VKSSVIGASS QFTRNALPAL LIYKGGELIG NFVRVTDQLG DDFFAVDLEA FLQEFGLLPE KEVLVLTSVR NSATCHSEDS DLEID

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    Pdcl Human
  • View Data Sheet

    Name :

    FCER1A Human, HEK

    Description:

    Fc-Epsilon RI-Alpha Human Recombinant, HEK

    FCERIA, FCERA, Fc epsilon receptor Ia, Fcepsilon RI-alpha, Fc epsilon RI alpha chain, FcERI, High affinity immunoglobulin epsilon receptor subunit alpha isoform1, IgE Fc receptor subunit alpha, FCER1A, FCE1A.

    Product # :

    PRO-2779

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    Description

    FCER1A Human Recombinant produced in HEK293 Cells is a single, glycosylated polypeptide chain containing 186 amino acids (26-205aa) and having a molecular mass of 21.8kDa. FCER1A is fused to a 6 His-tag at C-terminus & purified by proprietary chromatographic techniques.

    Source

    HEK293.

    Formulation

    FCER1A protein solution (1mg/ml) containing 10% Glycerol and Phosphate-Buffered Saline (pH 7.4).

    Purity

    Greater than 90% as determined by SDS-PAGE.

    Biological Activity

    The ED50 range ≤ 0.01 ug/ml and is measured by its binding ability in a functional ELISA with Human IgE.

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    • Synonyms

      FCERIA, FCERA, Fc epsilon receptor Ia, Fcepsilon RI-alpha, Fc epsilon RI alpha chain, FcERI, High affinity immunoglobulin epsilon receptor subunit alpha isoform1, IgE Fc receptor subunit alpha, FCER1A, FCE1A.

    • 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

      VPQKPKVSLN PPWNRIFKGE NVTLTCNGNN FFEVSSTKWF HNGSLSEETN SSLNIVNAKF EDSGEYKCQH QQVNESEPVY LEVFSDWLLL QASAEVVMEG QPLFLRCHGW RNWDVYKVIY YKDGEALKYW YENHNISITN ATVEDSGTYY CTGKVWQLDY ESEPLNITVI KAPREKYWLQ HHHHHH

    • Background

      The FCER1A gene encodes the alpha subunit of the high-affinity immunoglobulin E (IgE) receptor, known as FCER1A. This receptor is primarily expressed on mast cells and basophils, and its activation plays a pivotal role in allergic and inflammatory responses. This research aims to explore the significance of FCER1A and its potential implications in allergic disorders and immune-mediated diseases. By investigating the functions and regulation of FCER1A, we can gain insights into its role in immune responses and identify potential therapeutic targets.

      The FCER1A receptor is responsible for the binding of IgE antibodies, initiating a cascade of signaling events upon allergen exposure. Crosslinking of IgE-bound FCER1A leads to the release of various inflammatory mediators, such as histamine, cytokines, and leukotrienes, which contribute to the clinical manifestations of allergic reactions. Understanding the molecular mechanisms underlying FCER1A activation and downstream signaling is crucial for comprehending allergic diseases.

      In addition to its role in allergies, FCER1A has been implicated in immune-mediated inflammatory diseases, including asthma, atopic dermatitis, and autoimmune conditions. Dysregulation of FCER1A expression and signaling pathways can lead to exaggerated immune responses and chronic inflammation. Investigating the genetic and epigenetic factors influencing FCER1A expression and the interplay between FCER1A and other immune molecules can provide valuable insights into disease pathogenesis.

      This research will delve into the molecular mechanisms governing FCER1A expression, activation, and downstream signaling pathways. The paper will explore the regulatory effects of FCER1A on mast cell and basophil activation, the release of inflammatory mediators, and the recruitment of other immune cells. Additionally, it will examine the impact of FCER1A dysregulation in allergic and immune-mediated diseases and discuss the potential of FCER1A as a therapeutic target for intervention.

      The study will also investigate the diagnostic and prognostic value of FCER1A in various allergic and immune disorders. Understanding the expression patterns and alterations of FCER1A in different diseases and patient populations may aid in disease stratification, treatment selection, and monitoring of treatment response.

      By unraveling the molecular mechanisms underlying FCER1A's functions in allergic and inflammatory responses, this research aims to contribute to our understanding of immune-mediated diseases. Furthermore, it highlights the potential of FCER1A as a target for therapeutic interventions and emphasizes the need for further investigations to develop novel treatments and improve patient outcomes.

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    Fcer1A Protein
  • View Data Sheet

    Name :

    IMPAD1 Mouse Bioactive

    Description:

    Inositol Monophosphatase Domain Containing 1 Mouse Recombinant Bioactive

    Inositol monophosphatase 3, IMP 3, IMPase 3, Golgi 3-prime phosphoadenosine 5-prime phosphate 3-prime phosphatase, Golgi-resident PAP phosphatase, gPAPP, Inositol monophosphatase domain-containing protein 1, Inositol-1(or 4)-monophosphatase 3, Myo-inositol monophosphatase A3.

    Product # :

    PRO-2380

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    Description

    IMPAD1 Mouse Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 332 amino acids (34-356a.a.) and having a molecular mass of 36.2kDa. (Molecular size on SDS-PAGE will appear at approximately 28-40kDa). IMPAD1 is expressed with a 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    IMPAD1 protein solution (0.5mg/ml) containing Phosphate Buffered Saline (pH 7.4) and 10% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Biological Activity

    Specific activity is > 5,000 pmol/min/ug and is defined as the amount of enzyme that hydrolyze Adenosine 3, 5-diphosphate per minute at pH 7.5 at 25C.

    More Info

    • Introduction

      Inositol monophosphatase 3 (IMPAD1) belongs to the inositol monophosphatase family. IMPAD1 is restricted to the Golgi apparatus and catalyzes the hydrolysis of phosphoadenosine phosphate (PAP) to adenosine monophosphate (AMP). IMPAD1 gene mutations cause the GRAPP type chondrodysplasia with joint dislocations, and a pseudogene of the IMPAD1 gene is located on the long arm of chromosome 1.

    • Synonyms

      Inositol monophosphatase 3, IMP 3, IMPase 3, Golgi 3-prime phosphoadenosine 5-prime phosphate 3-prime phosphatase, Golgi-resident PAP phosphatase, gPAPP, Inositol monophosphatase domain-containing protein 1, Inositol-1(or 4)-monophosphatase 3, Myo-inositol monophosphatase A3.

    • 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

      ADPGRFSLFG LGSEPAAGEA EVASDGGTVD LREMLAVAVL AAERGGDEVR RVRESNVLHE KSKGKTREGA DDKMTSGDVL SNRKMFYLLK TAFPNVQINT EEHVDASDKE VIVWNRKIPE DILKEIAAPK EVPAESVTVW IDPLDATQEY TEDLRKYVTT MVCVAVNGKP VLGVIHKPFS EYTAWAMVDG GSNVKARSSY NEKTPKIIVS RSHAGMVKQV ALQTFGNQTS IIPAGGAGYK VLALLDVPDM TQEKADLYIH VTYIKKWDIC AGNAILKALG GHMTTLNGEE ISYTGSDGIE GGLLASIRMN HQALVRKLPD LEKSGHHHHH HH.

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    Impad1 Mouse Bioactive
  • View Data Sheet

    Name :

    KLK7 Human, sf9

    Description:

    Kallikrein-7 Human Recombinant, sf9

    Kallikrein Related Peptidase 7, Kallikrein 7 (Chymotryptic, Stratum Corneum), Stratum Corneum Chymotryptic Enzyme, Serine Protease 6, PRSS6, SCCE, HK7, Kallikrein-Related Peptidase 7, Signal Protein, EC 3.4.21.117, EC 3.4.21, HSCCE.

    Product # :

    ENZ-962

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    Description

    KLK7 produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 190 amino acids (1-181 a.a.) and having a molecular mass of 20.9kDa (Migrates at 28-40kDa on SDS-PAGE under reducing conditions). KLK7 is expressed with a 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    KLK7 protein solution (0.5mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 10% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      KLK7 catalyzes the degradation of intercellular cohesive structures in the cornified layer of the skin in the continuous shedding of cells from the skin surface. Specific for amino acid residues with aromatic side chains in the P1 position. KLK7 cleaves insulin B chain at ''6-Leu- -Cys-7'', ''16-Tyr- -Leu-17'', ''25-Phe- -Tyr-26'' and ''26-Tyr--Thr-27''. KLK7 is involved in the activation of precursors to inflammatory cytokines.

    • Synonyms

      Kallikrein Related Peptidase 7, Kallikrein 7 (Chymotryptic, Stratum Corneum), Stratum Corneum Chymotryptic Enzyme, Serine Protease 6, PRSS6, SCCE, HK7, Kallikrein-Related Peptidase 7, Signal Protein, EC 3.4.21.117, EC 3.4.21, HSCCE.

    • 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

      ADPMNEYTVH LGSDTLGDRR AQRIKASKSF RHPGYSTQTH VNDLMLVKLN SQARLSSMVK KVRLPSRCEP PGTTCTVSGW GTTTSPDVTF PSDLMCVDVK LISPQDCTKV YKDLLENSML CAGIPDSKKN ACNGDSGGPL VCRGTLQGLV SWGTFPCGQP NDPGVYTQVC KFTKWINDTM KKHRHHHHHH.

    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.

    Klk7 Human Sf9
  • View Data Sheet

    Name :

    POP7 Human

    Description:

    Processing Of Precursor 7 Human Recombinant

    Ribonuclease P protein subunit p20, RNaseP protein p20, Ribonucleases P/MRP protein subunit POP7 homolog, hPOP7, POP7, RPP20, 0610037N12Rik, RPP2.

    Product # :

    PRO-2015

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    Description

    POP7 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 165 amino acids (1-140 a.a.) and having a molecular mass of 18.3kDa.POP7 is fused to a 25 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    POP7 protein solution (0.25mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 50% glycerol, 2mM DTT and 2mM EDTA.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Processing Of Precursor 7, also known as POP7, is a part of the histone-like Alba family. POP7 is a part of ribonuclease P which is a protein complex that generates mature tRNA molecules by cleaving their 5'-ends. POP7 is also a part of RNase MRP complex, which cleaves pre-rRNA sequences.

    • Synonyms

      Ribonuclease P protein subunit p20, RNaseP protein p20, Ribonucleases P/MRP protein subunit POP7 homolog, hPOP7, POP7, RPP20, 0610037N12Rik, RPP2.

    • 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 MGSEFMAENR EPRGAVEAEL DPVEYTLRKR LPSRLPRRPN DIYVNMKTDF KAQLARCQKL LDGGARGQNA CSEIYIHGLG LAINRAINIA LQLQAGSFGS LQVAANTSTV ELVDELEPET DTREPLTRIR NNSAIHIRVF RVTPK.

    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.

    Pop7 Human
  • View Data Sheet

    Name :

    VAMP2 Human, (1-94)

    Description:

    Synaptobrevin-2 Human Recombinant, (1-94)

    Vesicle Associated Membrane Protein 2, Vesicle-Associated Membrane Protein 2, Synaptobrevin 2, VAMP-2, SYB2, Synaptobrevin-2.

    Product # :

    PRO-2644

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    Description

    VAMP2 Human Recombinant produced in e.coli is a single, non-glycosylated polypeptide chain containing 118 amino acids (1-94 a.a) and having a molecular mass of 12.8kDa. VAMP2 is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.Coli

    Formulation

    The VAMP2 solution (0.5mg/1ml) contains 0.1mM PMSF, 10% glycerol and Phosphate-Buffered Saline (pH 7.4).

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Synaptobrevin-2 or VAMP2 is a protein that has a proline-rich N-terminal part, highly conserved hydrophilic domain, a transmembrane anchor and a C-terminal.VAMP2 found in the transmembrane region of the cell, in the cytoplasmic surface of the synaptic vesicle. The protein is mainly found in the Langerhans islets in the pancreas and glomerular cells in the kidney. A SNARE complex is created within the protein’s N-terminal domain and the target membrane-associated T.

    • Synonyms

      Vesicle Associated Membrane Protein 2, Vesicle-Associated Membrane Protein 2, Synaptobrevin 2, VAMP-2, SYB2, Synaptobrevin-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 MGSHMSATAA TAPPAAPAGE GGPPAPPPNL TSNRRLQQTQ AQVDEVVDIM RVNVDKVLER DQKLSELDDR ADALQAGASQ FETSAAKLKR KYWWKNLK.

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    Synaptobrevin 2 Human
  • View Data Sheet

    Name :

    YOD1 Human

    Description:

    YOD1 Human Recombinant

    DUBA8, OTUD2, PRO0907, RP11-164O23.1, Ubiquitin thioesterase OTU1, DUBA-8, HIN-7, HsHIN7, OTU domain-containing protein 2.

    Product # :

    ENZ-696

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    Description

    YOD1 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 371 amino acids (1-348) and having a molecular mass of 40.7kDa.YOD1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The YOD1 solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 30% glycerol and 1mM DTT.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      YOD1 is a Hydrolase which removes conjugated ubiquitin from proteins and takes part in endoplasmic reticulum-associated degradation (ERAD) for misfolded lumenal proteins. YOD1 is a highly conserved deubiquitinating enzyme belonging to the ovarian tumor (otubain) family, whose function has yet to be determined in mammalian cells. YOD1 is a component of a multiprotein complex with p97 as its nucleus, proposing a functional link to a pathway responsible for the dislocation of misfolded proteins from the endoplasmic reticulum. YOD1 variant xpression deprived of its deubiquitinating activity compels a halt on the dislocation reaction, as concluded by the stabilization of various dislocation substrates.

    • Synonyms

      DUBA8, OTUD2, PRO0907, RP11-164O23.1, Ubiquitin thioesterase OTU1, DUBA-8, HIN-7, HsHIN7, OTU domain-containing protein 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 MGSMFGPAKG RHFGVHPAPG FPGGVSQQAA GTKAGPAGAW PVGSRTDTMW RLRCKAKDGT HVLQGLSSRT RVRELQGQIA AITGIAPGGQ RILVGYPPEC LDLSNGDTIL EDLPIQSGDM LIIEEDQTRP RSSPAFTKRG ASSYVRETLP VLTRTVVPAD NSCLFTSVYY VVEGGVLNPA CAPEMRRLIA QIVASDPDFY SEAILGKTNQ EYCDWIKRDD TWGGAIEISI LSKFYQCEIC VVDTQTVRID RFGEDAGYTK RVLLIYDGIH YDPLQRNFPD PDTPPLTIFS SNDDIVLVQA LELADEARRR RQFTDVNRFT LRCMVCQKGL TGQAEAREHA KETGHTNFGE V.

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    Yod1 Human
  • View Data Sheet

    Name :

    PSMA5 Human

    Description:

    Proteasome Subunit Alpha Type 5 Human Recombinant

    Proteasome subunit alpha type-5, Macropain zeta chain, Multicatalytic endopeptidase complex zeta chain, Proteasome zeta chain, PSMA5, PSC5, ZETA.

    Product # :

    ENZ-213

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    Description

    PSMA5 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 277 amino acids (1-241) and having a molecular mass of 30.5kDa.PSMA5 is fused to a 36 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    The PSMA5 solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 2mM DTT, 10% glycerol and 100mM NaCl.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    More Info

    • Introduction

      Proteasome subunit alpha type-5 (PSMA5) is a member of the peptidase T1A family. The proteasome is a multicatalytic proteinase complex which is distinguished by its ability to cleave peptides with Arg, Phe, Tyr, Leu, and Glu adjacent to the leaving group at neutral or slightly basic pH. Proteasomes are spread throughout eukaryotic cells at a high concentration and cleave peptides in an ATP/ubiquitin-dependent process in a non-lysosomal pathway. PSMA5 interacts with PLK1. The PSMA5 peptidase has a very wide-ranging specificity for cleavage of peptide bonds.

    • Synonyms

      Proteasome subunit alpha type-5, Macropain zeta chain, Multicatalytic endopeptidase complex zeta chain, Proteasome zeta chain, PSMA5, PSC5, ZETA.

    • 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 KDRWGSMFLT RSEYDRGVNT FSPEGRLFQV EYAIEAIKLG STAIGIQTSE GVCLAVEKRI TSPLMEPSSI EKIVEIDAHI GCAMSGLIAD AKTLIDKARV ETQNHWFTYN ETMTVESVTQ AVSNLALQFG EEDADPGAMS RPFGVALLFG GVDEKGPQLF HMDPSGTFVQ CDARAIGSAS EGAQSSLQEV YHKSMTLKEA IKSSLIILKQ VMEEKLNATN IELATVQPGQ NFHMFTKEEL EEVIKDI.

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    Psma5 Human
  • View Data Sheet

    Name :

    GDF7 Human

    Description:

    Growth and Differentiation factor 7 Human Recombinant

    Growth Differentiation Factor 7, GDF-7, Growth/Differentiation Factor 7, BMP12, GDF7.

    Product # :

    CYT-870

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    Description

    GDF7 Human Recombinant (322-450) produced in E.Coli is a disulfide-linked homodimeric, non-glycosylated, polypeptide chain containing 129 amino acids and having a molecular mass of 28kDa.The GDF-7 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Lyophilized from a 0.2µm filtered solution in HCl.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Biological Activity

    The ED50, as determined by inducing alkaline phosphatase production by mouse ATDC5 cells, is less than 1.25µg/ml.

    More Info

    • Introduction

      Growth Differentiation Factor-7 (GDF-7) belongs to the BMP family of TGF-b superfamily proteins. GDF7 elicits its bioactivity via a heterodimeric receptor complex comprised of a type 1 (BMPR-IB) and a type II (BMPR-II or Activin RII) serine/threonine kinase receptor. GDF7 signaling results in the phosphorylation and activation of Smad proteins. GDF-7 is also involved in tendon and ligament formation and repair. In addition, GDF7 regulates bone formation, mesenchymal stem cell differentiation, neuronal differentiation, and axon guidance.

    • Synonyms

      Growth Differentiation Factor 7, GDF-7, Growth/Differentiation Factor 7, BMP12, GDF7.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized GDF7 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution GDF-7 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 GDF-7 in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      TALAGTRTAQ GSGGGAGRGH GRRGRSRCSR KPLHVDFKEL GWDDWIIAPL DYEAYHCEGL CDFPLRSHLE PTNHAIIQTL LNSMAPDAAP ASCCVPARLS PISILYIDAA NNVVYKQYED MVVEACGCR.

    • Background

      What is the molecular weight/Mw of GDF7 Protein?
      GDF7 Protein has a total Mw of 28kDa.

      What is the source or expression system of GDF7 Protein?
      Escherichia Coli.

      What is the Purity of GDF7 Protein?
      GDF7 Protein is >95% pure as determined by SDS-PAGE.

      What is the Biological Activity of GDF7 Protein?
      The ED50, as determined by inducing alkaline phosphatase production by mouse ATDC5 cells, is less than 1.25µg/ml.

      What is the amino acid sequence of GDF7 Protein?
      TALAGTRTAQ GSGGGAGRGH GRRGRSRCSR KPLHVDFKEL GWDDWIIAPL DYEAYHCEGL CDFPLRSHLE PTNHAIIQTL LNSMAPDAAP ASCCVPARLS PISILYIDAA NNVVYKQYED MVVEACGCR.

      What applications can GDF7 Protein be used in?
      GDF7 Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for GDF7 Protein?
      The endotoxin level is minimal, GDF7 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.

    Gdf7 Human
  • View Data Sheet

    Name :

    TXN1 E.Coli

    Description:

    Thioredoxin E.Coli Recombinant

    Thioredoxin-1, Trx-1, trxA, fipA, tsnC, b3781, JW5856.

    Product # :

    PRO-334

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    Description

    Recombinant Thioredoxin was purified from E. coli harboring its gene.

    Source

    Escherichia Coli.

    Formulation

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

    Purity

    Greater than 90.0% as determined by:
    (a) Analysis by RP-HPLC.
    (b) Analysis by SDS-PAGE.

    Biological Activity

    TRX activity is assayed by measuring the change in absorbance at 650 nm at 25°C using 0.13µM bovine insulin containing 0.33mM DTT (pH 6.5).
    The specific activity was found to be 3IU/mg.

    More Info

    • Introduction

      Thioredoxins are small disulphide-containing redox proteins (within the conserved Cys-Gly-Pro-Cys active site) that have been found in all the kingdoms of living organisms. Thioredoxin contains a single disulfide active site and serves as a general protein disulphide oxidoreductase. Thioredoxins are involved in the first unique step in DNA synthesis. It interacts with a broad range of proteins by a redox mechanism based on reversible oxidation of two cysteine thiol groups to a disulphide, accompanied by the transfer of two electrons and two protons. The net result is the covalent interconversion of a disulphide and a dithiol. Trx also provides control over a number of transcription factors affecting cell proliferation and death through a mechanism referred to as redox regulation. It has been suggested that thioredoxin may catalyze the formation of correct disulfides during protein folding because of its ability to act as an efficient oxidoreductant. This could be especially useful in refolding proteins expressed in E. coli. To this end, thioredoxin has been shown to act as a protein disulfide isomerase.Its Molecular Weight is 11.9kDa. and the pI is 4.67.

    • Synonyms

      Thioredoxin-1, Trx-1, trxA, fipA, tsnC, b3781, JW5856.

    • Physical Appearance

      Sterile Lyophilized Powder.

    • Stability

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

    • Solubility

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

    • Amino Acid Sequence

      HMSDKIIHL TDDSFDTDVLKADGAIL VDFW AEWCGPCKMIAPILDEI GKLTVAKLNIDQNPGTAPKYGIRGIPTLLLFKNGEVAATKVGAL DANLA.

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

    Thioredoxin 1
  • View Data Sheet

    Name :

    CCL14 Human (66 a.a.)

    Description:

    HCC-1 Human Recombinant (CCL14) (66 a.a.)

    Small inducible cytokine A14, CCL14, Chemokine CC-1/CC-3, HCC-1/HCC-3, HCC-1(1-74), NCC-2, chemokine (C-C motif) ligand 14, CC-1, CC-3, CKb1, MCIF, SY14, HCC-1, HCC-3, SCYL2, SCYA14.

    Product # :

    CHM-006

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    Description

    HCC-1 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 66 amino acids and having a molecular mass of 7.8kDa. The HCC-1 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The CCL14 protein was lyophilized from a 0.2µm filtered concentrated solution in 1×PBS, pH 7.4 and 5% trehalose.

    Purity

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

    Biological Activity

    The Biological activity is determined by its ability to chemoattract human monocytes using a concentration range of 5.0-20.0 ng/ml.

    More Info

    • Introduction

      Chemokine (C-C motif) ligand 14 (CCL14) is a small cytokine belonging to the CC chemokine family. It is also commonly known as HCC-1. It is produced as a protein precursor that is procesed to generate a mature active protein containing 74 amino acids that and is 46% identical in amino acid composition to CCL3 and CCL4. This chemokine is expressed in various tissues including spleen, bone marrow, liver, muscle, and gut. CCL13 activates monocytes, but does not induce their chemotaxis. Human CCL13 is located on chromosome 17 within a cluster of other chemokines belonging to the CC family.

    • Synonyms

      Small inducible cytokine A14, CCL14, Chemokine CC-1/CC-3, HCC-1/HCC-3, HCC-1(1-74), NCC-2, chemokine (C-C motif) ligand 14, CC-1, CC-3, CKb1, MCIF, SY14, HCC-1, HCC-3, SCYL2, SCYA14.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized HCC1 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution CCL14 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 HCC-1 in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      GPYHPSECCF TYTTYKIPRQ RIMDYYETNS QCSKPGIVFI TKRGHSVCTN PSDKWVQDYI KDMKEN.

    • Background

      What is the molecular weight/Mw of CCL14 HUMAN (66 A.A.) Protein?
      CCL14 HUMAN (66 A.A.) Protein has a total Mw of 7.8kDa.

      What is the source or expression system of CCL14 HUMAN (66 A.A.) Protein?
      Escherichia Coli.

      What is the Purity of CCL14 HUMAN (66 A.A.) Protein?
      CCL14 HUMAN (66 A.A.) Protein is >97% pure as determined by SDS-PAGE.

      What is the Biological Activity of CCL14 HUMAN (66 A.A.) Protein?
      The Biological activity is determined by its ability to chemoattract human monocytes using a concentration range of 5.0-20.0 ng/ml.

      What is the amino acid sequence of CCL14 HUMAN (66 A.A.) Protein?
      GPYHPSECCF TYTTYKIPRQ RIMDYYETNS QCSKPGIVFI TKRGHSVCTN PSDKWVQDYI KDMKEN.

      What applications can CCL14 HUMAN (66 A.A.) Protein be used in?
      CCL14 HUMAN (66 A.A.) Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for CCL14 HUMAN (66 A.A.) Protein?
      The endotoxin level is minimal, CCL14 HUMAN (66 A.A.) Protein was purified using conventional chromatography techniques.


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    Hcc 1 Human 66 Aa
  • View Data Sheet

    Name :

    Activin A Human

    Description:

    Activin A Human Recombinant

    Activin Beta-A chain, Erythroid differentiation protein, EDF, FRP, Activin-A, Inhibin-B, Inihibin-Beta A chain.

    Product # :

    CYT-569

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    • sds-page

    Description

    Activin-A Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 137 amino acids (311-426) and having a molecular mass of 15.2kDa.Activin-A is fused to a 21 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Activin-A protein solution (1mg/ml) contains 20mM Tris pH 8.0 and 10% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    sds-page

    Activin A Human sds-page - Product image 1

    More Info

    • Introduction

      Inhibins are dimeric peptide hormones produced by female ovarian granulose cells and male Sertoli cells as well as a variety of other tissues. Inhibins have two isoforms, A and B, with the same alpha subunit but different beta subunits. Inhibin A is a dimer of alpha and beta A subunits, inhibin B is a dimer of alpha and beta B subunits.
      Inhibins are thought to inhibit the production of follicle-stimulating hormone (FSH) by the pituitary gland. In addition, Inhibins are also thought to play a role in the control of gametogenesis, and embryonic and fetal development.

    • Synonyms

      Activin Beta-A chain, Erythroid differentiation protein, EDF, FRP, Activin-A, Inhibin-B, Inihibin-Beta A chain.

    • 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 MGLECDGKVN ICCKKQFFVS FKDIGWNDWI IAPSGYHANY CEGECPSHIA GTSGSSLSFH STVINHYRMR GHSPFANLKS CCVPTKLRPM SMLYYDDGQN IIKKDIQNMI VEECGCS.

    • Background

      What is the molecular weight / Mw of Activin A Protein?
      Activin A Protein has a total Mw of 15.2 kDa.

      What is the source or expression system of Activin A Protein?
      E.Coli

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

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

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

      What is the amino acid sequence of ACTIVIN A Protein?MGSSHHHHHH SSGLVPRGSH MGLECDGKVN ICCKKQFFVS FKDIGWNDWI IAPSGYHANY CEGECPSHIA GTSGSSLSFH STVINHYRMR GHSPFANLKS CCVPTKLRPM SMLYYDDGQN IIKKDIQNMI VEECGCS

      What applications can ACTIVIN-A Protein be used in?

      ACTIVIN A Protein can probably be used in western blot, ELISA and Lateral Flow.

    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.

    Activin A Human
  • View Data Sheet

    Name :

    CTHRC1 Human

    Description:

    Collagen Triple Helix Repeat Containing 1 Human Recombinant

    Collagen Triple Helix Repeat Containing 1, Protein NMTC1, CTHRC1.

    Product # :

    PRO-2027

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    Description

    CTHRC1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 234 amino acids (31-243 a.a) and having a molecular mass of 25.3kDa.CTHRC1 is fused to a 21 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    CTHRC1 protein solution (1mg/ml) containing 20mM Tris-HCl (pH 8.0) and 10% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Collagen triple helix repeat-containing protein 1 (CTHRC1) functions as a negative regulator of collagen matrix deposition. CTHRC1 is a secreted 28kDa protein which is glycosylated and highly conserved from lower chordates to mammals. CTHRC1 is highly connected with calcified tissues and cartilaginous matrix, but not with endothelial cells. CTHRC1 is detected qualitatively in plasma of healthy human subjects. CTHRC1 plasma levels are also significantly elevated during pregnancy, in diabetes, in inflammatory and infectious conditions, in subjects with acute myeloid leukemia but not in subjects with solid cancers. The hormonal functions of CTHRC1 include regulation of lipid storage and cellular glycogen levels with potentially far-reaching implications for cell metabolism and physiology. CTHRC1 gene deletion leads to fatty liver (steatosis) formation in mice while others exhibited inactivation of the CTHRC1 gene also results in low bone mass.

    • Synonyms

      Collagen Triple Helix Repeat Containing 1, Protein NMTC1, CTHRC1.

    • 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 MSEIPKGKQK AQLRQREVVD LYNGMCLQGP AGVPGRDGSP GANGIPGTPG IPGRDGFKGE KGECLRESFE ESWTPNYKQC SWSSLNYGID LGKIAECTFT KMRSNSALRV LFSGSLRLKC RNACCQRWYF TFNGAECSGP LPIEAIIYLD QGSPEMNSTI NIHRTSSVEG LCEGIGAGLV DVAIWVGTCS DYPKGDASTG WNSVSRIIIE ELPK.

    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.

    Cthrc1 Human
  • View Data Sheet

    Name :

    DCUN1D2 Human

    Description:

    DCN1 Defective in Cullin Neddylation 1 Domain Containing 2 Human Recombinant

    DCN1-like protein 2, DCUN1 domain-containing protein 2, Defective in cullin neddylation protein 1-like protein 2, DCUN1D2, C13orf17, DCUN1L2.

    Product # :

    PRO-899

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    Description

    DCUN1D2 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 279 amino acids (1-259 a.a.) and having a molecular mass of 32.3kDa.DCUN1D2 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    DCUN1D2 protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 1mM DTT, 30% glycerol and 0.1M NaCl.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      DCN1-like protein 2 (DCUN1D2) which contains one DCUN1 domain and 1 UBA-like domain, may have a role in the neddylation of cullins which regulate SCF-type ubiquitin ligase complexes. The gene encoding Dcun1D2 is located on human chromosome 13. Chromosome 13 contains major tumor suppressor genes, including BRCA2 and RB1, which are linked with breast cancer susceptibility and retinoblastoma, respectively.

    • Synonyms

      DCN1-like protein 2, DCUN1 domain-containing protein 2, Defective in cullin neddylation protein 1-like protein 2, DCUN1D2, C13orf17, DCUN1L2.

    • 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 MHKLKSSQKD KVRQFMACTQ AGERTAIYCL TQNEWRLDEA TDSFFQNPDS LHRESMRNAV DKKKLERLYG RYKDPQDENK IGVDGIQQFC DDLSLDPASI SVLVIAWKFR AATQCEFSRK EFLDGMTELG CDSMEKLKAL LPRLEQELKD TAKFKDFYQF
      TFTFAKNPGQ KGLDLEMAVA YWKLVLSGRF KFLDLWNTFL MEHHKRSIPR DTWNLLLDFG NMIADDMSNY DEEGAWPVLI DDFVEYARPV VTGGKRSLF.

    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.

    Dcun1D2 Human
  • View Data Sheet

    Name :

    APMAP Human

    Description:

    Adipocyte Plasma Membrane Associated Protein Human Recombinant

    Adipocyte Plasma Membrane Associated Protein, Protein BSCv, C20orf3, Adipocyte Plasma Membrane-Associated Protein, Chromosome 20 Open Reading Frame 3, BSCv, APMAP.

    Product # :

    PRO-2170

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    Description

    APMAP Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 378 amino acids (62-416 a.a) and having a molecular mass of 42.2kDa.APMAP is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

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

    Purity

    Greater than 85% as determined by SDS-PAGE.

    More Info

    • Introduction

      Adipocyte plasma membrane-associated protein, also known as APMAP, is a member of the strictosidine synthase family. APMAP exhibits strong arylesterase activity with beta-naphthyl acetate in addition to phenyl acetate and takes part in adipocyte differentiation.

    • Synonyms

      Adipocyte Plasma Membrane Associated Protein, Protein BSCv, C20orf3, Adipocyte Plasma Membrane-Associated Protein, Chromosome 20 Open Reading Frame 3, BSCv, APMAP.

    • 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 MGSESPIDPQ PLSFKEPPLL LGVLHPNTKL RQAERLFENQ LVGPESIAHI GDVMFTGTAD GRVVKLENGE IETIARFGSG PCKTRDDEPV CGRPLGIRAG PNGTLFVADA YKGLFEVNPW KREVKLLLSS ETPIEGKNMS FVNDLTVTQD GRKIYFTDSS SKWQRRDYLL LVMEGTDDGR LLEYDTVTRE VKVLLDQLRF PNGVQLSPAE DFVLVAETTM ARIRRVYVSG LMKGGADLFV ENMPGFPDNI RPSSSGGYWV GMSTIRPNPG FSMLDFLSER PWIKRMIFKL FSQETVMKFV PRYSLVLELS DSGAFRRSLH DPDGLVATYI SEVHEHDGHL
      YLGSFRSPFL CRLSLQAV

    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.

    Apmap Human
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