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Search results

1000 results found for “ebv”

Name

Description

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  • View Data Sheet

    Name :

    UBE2L3 Human

    Description:

    Ubiquitin-Conjugating Enzyme E2L 3 Human Recombinant

    Ubiquitin-conjugating enzyme E2 L3, EC 6.3.2.19, Ubiquitin-protein ligase L3,Ubiquitin carrier protein L3, UbcH7, E2-F1, L-UBC, UbcM4.

    Product # :

    ENZ-342

    Price :

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    Description

    Ubiquitin-Conjugating Enzyme E2L 3 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 154 amino acids & having a molecular mass of 17.9 kDa.

    Source

    Escherichia Coli.

    Formulation

    The protein contains 50mM HEPES (pH-7.5) 150mM NaCl, 1mM DTT, and 10% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      Human Ubquitin-conjugating enzyme 7 (UbcH7) is a ubiquitin-conjugating enzyme (E2) mediating c-fos degradation, transcription factor NF-B maturation, and human papilloma virus-mediated p53 and Myc protein degradation, in vitro. The ubiquitin-conjugating enzymes (E2s) are essential components of the post-translational protein ubiquitination pathway, mediating the transfer of activated ubiquitin to substrate proteins. The human UBE2L1-UBE2L4 gene could potentially encode different isoforms of the UbcH7. UBE2L3 gene, located at chromosome 22q11.2, is the only identical family member with introns and encodes a polypeptide sequence identical to that of UbcH7.

    • Synonyms

      Ubiquitin-conjugating enzyme E2 L3, EC 6.3.2.19, Ubiquitin-protein ligase L3,Ubiquitin carrier protein L3, UbcH7, E2-F1, L-UBC, UbcM4.

    • 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

      MAASRRLMKE LEEIRKCGMK NFRNIQVDEA NLLTWQGLIV PDNPPYDKGA FRIEINFPAE YPFKPPKITF KTKIYHPNID EKGQVCLPVI SAENWKPATK TDQVIQSLIA LVNDPQPEHP LRADLAEEYS KDRKKFCKNA EEFTKKYGEK RPVD.

    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.

    Ube2L3 Human
  • View Data Sheet

    Name :

    GrpE E.Coli

    Description:

    HSP-70 Cofactor (HSP24) E.Coli Recombinant

    HSP24, HSPB25.3, HSP-70 Cofactor, Protein grpE, Heat shock protein B25.3, grpE, b2614, JW2594.

    Product # :

    HSP-014

    Price :

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    Description

    GrpE Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 197 amino acids and having a molecular mass of 21.8 kDa. The GrpE is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The HSP24 protein solution contains 20mM Tris-HCl pH-8 and 0.1M NaCl.

    Purity

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

    Citations

    More Info

    • Introduction

      GrpE , co-chaperone of E.coli, participates actively in the response to hyperosomotic and heat shock by preventing the aggregation of stress-denatured proteins in association with DnaK. This protein is the nucleotide exchange factor for DnaK and may function as a thermosensor. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding.

    • Synonyms

      HSP24, HSPB25.3, HSP-70 Cofactor, Protein grpE, Heat shock protein B25.3, grpE, b2614, JW2594.

    • 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

      MSSKEQKTPE GQAPEEIIMD QHEEIEAVEP EASAEQVDPR DEKIANLEAQ LAEAQTRERD GILRVKAEME NLRRRTELDI EKAHKFALEK FINELLPVID SLDRALEVAD KANPDMSAMV EGIELTLKSM LDVVRKFGVE VIAETNVPLD PNVHQAIAMV ESDDVAPGNV LGIMQKGYTL NGRTIRAAMV TVAKAKA.

    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.

    Grpe Ecoli
  • View Data Sheet

    Name :

    RAB5A Human

    Description:

    RAB5A Human Recombinant

    Ras-related protein Rab-5A, RAB5A, RAB5.

    Product # :

    PRO-590

    Price :

    Quantity :

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    Description

    RAB5A Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 215 amino acids and having a molecular mass of 23kDa.

    Source

    Escherichia Coli.

    Formulation

    The protein solution contains 20mM Tris-HCl pH-8.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      RAB5A is a member of RAS oncogene family. The small GTPase, RAB5A is a crucial regulatory component of the endocytic pathway. Activation of RAB5A is mediated by GDP-GTP exchange factors (GEFs) that generate the Rab5-GTP complex). RAB5A is required for the fusion of plasma membranes and early endosomes.

    • Synonyms

      Ras-related protein Rab-5A, RAB5A, RAB5.

    • 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).Please prevent freeze-thaw cycles.

    • Amino Acid Sequence

      MASRGATRPN GPNTGNKICQ FKLVLLGESA VGKSSLVLRF VKGQFHEFQE STIGAAFLTQTVCLDDTTVK FEIWDTAGQE RYHSLAPMYY RGAQAAIVVY DITNEESFAR AKNWVKELQRQASPNIVIAL SGNKADLANK RAVDFQEAQS YADDNSLLFM ETSAKTSMNV NEIFMAIAKKLPKNEPQNPG ANSARGRGVD LTEPTQPTRN QCCSN.

    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.

    Rab5A Human
  • View Data Sheet

    Name :

    RALA Human

    Description:

    V-ral Simian Leukemia Viral Oncogene Homolog A Human Recombinant

    Ras-related protein Ral-A, RALA, RAL, MGC48949.

    Product # :

    PRO-043

    Price :

    Quantity :

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    Description

    RALA Human Recombinant fused with a 24 amino acid His tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 227 amino acids (1-203 a.a.) and having a molecular mass of 25.8kDa. The RALA is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The RALA solution (0.5 mg/ml) contains 20mM Tris-HCl buffer (pH8.0), 10% glycerol, 2mM DTT, 100mM NaCl and 0.1mM PMSF.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      Ras-related protein Ral-A (RALA) is a member of the small GTPase superfamily, Ras family of proteins. RALA mediates a distinct downstream signaling pathway from Ras which facilitates cellular transformation. Furthermore, RALA is thought to be involved in various signaling cascades, including regulation of the cytoskeleton, vesicle trafficking, and endocytosis.

    • Synonyms

      Ras-related protein Ral-A, RALA, RAL, MGC48949.

    • 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 MGSHMAANKP KGQNSLALHK VIMVGSGGVG KSALTLQFMY DEFVEDYEPT KADSYRKKVV LDGEEVQIDI LDTAGQEDYA AIRDNYFRSG EGFLCVFSIT EMESFAATAD FREQILRVKE DENVPFLLVG NKSDLEDKRQ VSVEEAKNRA EQWNVNYVET SAKTRANVDK VFFDLMREIR ARKMEDSKEK NGKKKRKSLA KRIRERC.

    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.

    Rala Human
  • View Data Sheet

    Name :

    RELM a Mouse

    Description:

    RELM-alpha Mouse Recombinant

    Resistin-like alpha, RELMalpha, Cysteine-rich secreted protein FIZZ1, Parasite-induced macrophage novel gene 1 protein, Cysteine-rich secreted protein A12-gamma, RELM-a.

    Product # :

    CYT-309

    Price :

    Quantity :

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    • description
    • source
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    • Citations

    Description

    Mouse RELM-alpha Recombinant produced in E.Coli is a monomeric, non-glycosylated, polypeptide chain containing 88 amino acids and having a molecular mass of 10 kDa. The Mouse RELM-alpha is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Sterile filtered and lyophilized from 0.5mg/ml in 10mM sodium phosphate buffer, pH 7.5.

    Purity

    Greater than 98% as determined by SDS-PAGE & RP-HPLC.

    Citations

    More Info

    • Introduction

      Bronchoalveolar lavage fluid from mice with experimentally induced allergic pulmonary inflammation contains a novel 9.4 kDa cysteine-rich secreted protein, RELM-alpha (FIZZ1, found in inflammatory zone). RELM-alpha is a secreted protein that has a restricted tissue distribution with highest levels in adipose tissue stroma. Murine RELM-alpha (FIZZ1) is the founding member of a new gene family including two other murine genes expressed, respectively, in intestinal crypt epithelium (RELM-beta) and white adipose tissue (Resistin), and two related human genes.
      RELMalpha inhibits the differentiation of 3T3-L1 preadipocytes into adipocytes but has no effect on proliferation of 3T3-L1 preadipocytes. RELMalpha is able to form heterooligomers with resistin but not RELMbeta. Since RELMalpha is expressed by adipose tissue and it is a secreted factor, our findings suggest that RELMalpha may be involved in the control of the adipogenesis as well as in the process of muscle differentiation.
      In the lung, RELM-alpha is induced by hypoxia and was renamed as hypoxia-induced mitogenic factor (HIMF). HIMF strongly activated Akt phosphorylation. The phosphatidylinositol 3-kinase (PI3K) inhibitor LY294002 (10 micromol/L) inhibited HIMF-activated Akt phosphorylation. It also inhibited HIMF stimulated RPSM proliferation. Thus, the PI3K/Akt pathway, at least in part, mediates the proliferative effect of HIMF. Further studies showed that HIMF had angiogenic and vasoconstrictive properties. HIMF increased pulmonary arterial pressure and vascular resistance. Further studies suggest that HIMF regulates apoptosis and may participate in lung alveolarization and maturation.

    • Synonyms

      Resistin-like alpha, RELMalpha, Cysteine-rich secreted protein FIZZ1, Parasite-induced macrophage novel gene 1 protein, Cysteine-rich secreted protein A12-gamma, RELM-a.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Solubility

      At 0.1mg/ml of deionized sterile water.

    • Amino Acid Sequence

      MDETIEIIVE NKVKELLANP ANYPSTVTKT LSCTSVKTMN RWASCPAGMT ATGCACGFAC GSWEIQSGDT CNCLCLLVDW TTARCCQLS.

    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.

    Relm Alpha Mouse
  • View Data Sheet

    Name :

    ECHS1 Human

    Description:

    Enoyl CoA Hydratase, Short chain, 1, Mitochondrial Human Recombinant

    Enoyl-CoA hydratase 1, SCEH.

    Product # :

    ENZ-556

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    Description

    ECHS1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 284 amino acids (28-290 a.a.) and having a molecular mass of 30.6kDa.ECHS1 is fused to a 21 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The ECHS1 protein solution (1mg/ml) contains 20mM Tris-HCl buffer (pH-8), 1mM DTT,0.1M NaCl and 20% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      ECHS1 is part of the hydratase/isomerase superfamily. ECHS1 is localized in the mitochondrial matrix and Expressed in muscle, liver and fibroblasts, with low expression in kidney and spleen, ECHS1 exists as a homohexamer that takes part in the second phase of the mitochondrial fatty acid β-oxidation pathway.

    • Synonyms

      Enoyl-CoA hydratase 1, SCEH.

    • 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 MASGANFEYI IAEKRGKNNT VGLIQLNRPK ALNALCDGLI DELNQALKIF EEDPAVGAIV LTGGDKAFAA GADIKEMQNL SFQDCYSSKF LKHWDHLTQV KKPVIAAVNG YAFGGGCELA MMCDIIYAGE KAQFAQPEIL IGTIPGAGGT QRLTRAVGKS LAMEMVLTGD RISAQDAKQA GLVSKICPVE TLVEEAIQCA EKIASNSKIV VAMAKESVNA AFEMTLTEGS KLEKKLFYST FATDDRKEGM TAFVEKRKAN FKDQ.

    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.

    Echs1 Human
  • View Data Sheet

    Name :

    CXCL13 Mouse

    Description:

    BCA-1/BLC Mouse Recombinant (CXCL13)

    C-X-C motif chemokine 13, B lymphocyte chemoattractant, CXC chemokine BLC, Small-inducible cytokine B13, Cxcl13, Blc, Scyb13.

    Product # :

    CHM-030

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    Description

    CXCL13 Mouse Recombinant (22-109) produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 88 amino acids and having a molecular mass of 10kDa.The BCA-1 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The BCA1 protein was lyophilized from a 0.2µm filtered solution in Acetonitrile and TFA.

    Purity

    Greater than 97.0% as determined by SDS-PAGE.

    Biological Activity

    The ED50, as measured by its ability to chemoattract human CXCR5-transfected mouse BaF3 cells, is less than 2µg/ml.

    Citations

    More Info

    • Introduction

      BCA-1 is a CXC chemokine that is highly expressed in thesecondary lymphoid organs, such as follicles of the spleen, lymph nodes, and Peyer's patches. CXCL13 promotes the migration of B lymphocytes (compared to T cells and macrophages), by stimulating calcium influx into, and chemotaxis of, cells expressing Burkitt's lymphoma receptor 1 (BLR1). BCA1 therefore function in the homing of B lymphocytes to follicles. Human BCA-1 shares a 64% amino acid sequence similarity with the mouse protein and 23 - 34% amino acid sequence identity with other known CXC chemokines. Recombinant or chemically synthesized BCA1 is a potent chemoattractant for B lymphocytes but not T lymphocytes, monocytes or neutrophils. BLR1, a G protein-coupled receptor originally isolated from Burkitt’s lymphoma cells, has now been shown to be the specific receptor for BCA1. Among cells of the hematopoietic lineages, the expression of BLR-1, now designated CXCR-5, is restricted to B lymphocytes and a subpopulation of T helper memory cells.

    • Synonyms

      C-X-C motif chemokine 13, B lymphocyte chemoattractant, CXC chemokine BLC, Small-inducible cytokine B13, Cxcl13, Blc, Scyb13.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized BCA1 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution BCA1 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 CXCL13 in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      ILEAHYTNLK CRCSGVISTV VGLNIIDRIQ VTPPGNGCPK TEVVIWTKMK KVICVNPRAK WLQRLLRHVQ SKSLSSTPQA PVSKRRAA.

    • Background

      What is the molecular weight/Mw of CXCL13 MOUSE Protein?
      CXCL13 MOUSE Protein has a total Mw of 10kDa.

      What is the source or expression system of CXCL13 MOUSE Protein?
      Escherichia Coli.

      What is the Purity of CXCL13 MOUSE Protein?
      CXCL13 MOUSE Protein is >97% pure as determined by SDS-PAGE.

      What is the Biological Activity of CXCL13 MOUSE Protein?
      The ED50, as measured by its ability to chemoattract human CXCR5-transfected mouse BaF3 cells, is less than 2µg/ml.

      What is the amino acid sequence of CXCL13 MOUSE Protein?
      ILEAHYTNLK CRCSGVISTV VGLNIIDRIQ VTPPGNGCPK TEVVIWTKMK KVICVNPRAK WLQRLLRHVQ SKSLSSTPQA PVSKRRAA.

      What applications can CXCL13 MOUSE Protein be used in?
      CXCL13 MOUSE Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for CXCL13 MOUSE Protein?
      The endotoxin level is minimal, CXCL13 MOUSE Protein was purified using conventional chromatography techniques.

      Who supplies recombinant CXCL13 MOUSE that is in stock and available to order?
      ProSpec has the protein in stock and available for immediate delivery.

      Where can I order bulk mg quantities of CXCL13 MOUSE?
      ProSpec supplies bulk mg quantities at affordable prices that meets research and academic budgets.

    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.

    Bca 1 Mouse
  • View Data Sheet

    Name :

    Bcl XL Mouse

    Description:

    B-Cell Leukemia/Lymphoma XL Mouse Recombinant

    BclXL, Bcl-X(L), Bcl-XL.

    Product # :

    PRO-1362

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    Description

    Bcl-XL Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 211 amino acids, having an MW of 23.7kDa.The Bcl-XL is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Bcl-XL Mouse 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.

    Citations

    More Info

    • Introduction

      Bcl-XL is a transmembrane protein located in the mitochondrial membranes of cells that are long-lived and postmitotic, such as adult brain cells. It plays arole in the signal transduction pathway of the FAS-Ligand. Bcl-XL is an anti-apoptotic protein which is a member of the Bcl-2 family which are able to form heterodimers, and this is an significant event in the regulation of apoptosis. BCL-XL is involved in the survival of cancer cells.
      Bcl-xL is the leading monitor of apoptosis/active cell suicide. Bcl-xL has cell death repressor activity and therefore acts as a survival protein.

    • Synonyms

      BclXL, Bcl-X(L), Bcl-XL.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Amino Acid Sequence

      SQSNRELVVD FLSYKLSQKG YSWSQFSDVE ENRTEAPEET EAERETPSAI NGNPSWHLAD SPAVNGATGH SSSLDAREVI PMAAVKQALR EAGDEFELRY RRAFSDLTSQ LHITPGTAYQ SFEQVVNELF RDGVNWGRIV AFFSFGGALC VESVDKEMQV LVSRIASWMA TYLNDHLEPW IQENGGWDTF VDLYGNNAAA ESRKGQERFN R.

    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.

    Bcl Xl Mouse
  • View Data Sheet

    Name :

    Influenza-B Victoria

    Description:

    Influenza-B Virus Victoria/504/00

    Product # :

    IHA-018

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    Description

    Allantoic fluid of 10 days old embryonated eggs, inoculated with influenza B virus, strain B/Victoria/504/00. The Influenza B Virus was purified by Ultracentrifugation with 10-40 % sucrose gradient.

    Formulation

    The B/ Victoria /53/99 solution contains STE, 0.1% sodium azide (NaN3) and 0.005% thimerosal.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      Influenzavirus B is a genus in the virusfamily Orthomyxoviridae. The only species in this genus is called "Influenza B virus". Influenza B virus only infects humansand seals. This limited host range is apparently in contrast with those caused by the similar Influenza virus Aas both mutate by both genetic drift and reassortment. Influenza-B virus evolves slower than A viruses and faster than C viruses. Influenza-B virus mutates at a rate 2-3 times lower than type A. However, influenza B mutates enough that lasting immunity is not possible. The Influenza B virus capsidis enveloped while its virionconsists of a matrix protein + envelope + nucleoprotein complex + nucleocapsid, and a polymerasecomplex. Influenza B is sometimes spherical and sometimes filamentous. Its 500 or so surface projections are made of hemagglutinin and neuraminidase.
      The Influenza B virus is 14648 nucleotideslong and consists of eight segments of linear negative-sense, single-stranded RNA. The multipartite genome is encapsidated, each segment in a separate nucleocapsid, and the nucleocapsids are surrounded by one envelope.

    • Physical Appearance

      Sterile Filtered colorless solution.

    • Stability

      B/Victoria/504/00 although stable 4°C for 4 weeks, should be stored below -18°C. Please prevent freeze-thaw cycles.

    • Applications

      Serological studies of influenza B virus, immunogen for antibody production.

    • Inactivation

      Thimerosal and beta propiolactone treatmentThis product has been treated in a manner consistent with methods of inactivation. Generally accepted good laboratory practices appropriate to microbiological/viral safe handling practices and techniques are required at work.

    • Immunological Activity

      Tested with anti-influenza B monoclonal antibodies in ELISA.

    • Note

      Contains thimerosal (0.005%) and sodium azide (0.1%) as preservative. Although the amounts are very small, appropriate care must be taken when handling this product.

    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.

    Influenza B Victoria
  • View Data Sheet

    Name :

    UBE2H Human

    Description:

    Ubiquitin-Conjugating Enzyme E2H Human Recombinant

    Ubiquitin-conjugating enzyme E2 H, UbcH2, Ubiquitin carrier protein H, Ubiquitin-conjugating enzyme E2-20K, Ubiquitin-protein ligase H, UBE2H, GID3, UBC8, UBCH.

    Product # :

    ENZ-603

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    Description

    UBE2H Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 206 amino acids (1-183) and having a molecular mass of 23.1kDa.UBE2H is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The UBE2H solution (1mg/ml) contains 20mM Tris-HCl buffer, pH8.0, 10% glycerol, 1mM DTT and 50mM NaCl.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      Ubiquitin-conjugating enzyme E2 H (UBE2H) is a member of the ubiquitin-conjugating enzyme family. Protein modification with ubiquitin is a vital cellular apparatus for directing abnormal or short-lived proteins for degradation. Ubiquitination requires at least 3 classes of enzymes: ubiquitin-activating enzymes (E1s) ubiquitin-conjugating enzymes (E2s) and ubiquitin-protein ligases (E3s). UBE2H receives ubiquitin from the E1 complex and catalyzes its covalent attachment to other proteins. UBE2H protein sequence is 100% identical to the mouse homolog and 98% identical to the frog and zebrafish homologs.

    • Synonyms

      Ubiquitin-conjugating enzyme E2 H, UbcH2, Ubiquitin carrier protein H, Ubiquitin-conjugating enzyme E2-20K, Ubiquitin-protein ligase H, UBE2H, GID3, UBC8, UBCH.

    • 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 MGSMSSPSPG KRRMDTDVVK LIESKHEVTI LGGLNEFVVK FYGPQGTPYE GGVWKVRVDL PDKYPFKSPS IGFMNKIFHP NIDEASGTVC LDVINQTWTA LYDLTNIFES FLPQLLAYPN PIDPLNGDAA AMYLHRPEEY KQKIKEYIQK YATEEALKEQ EEGTGDSSSE SSMSDFSEDE AQDMEL.

    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.

    Ube2H Human
  • View Data Sheet

    Name :

    Zika Ectodomain

    Description:

    Zika Ectodomain Recombinant

    Product # :

    ZKV-006

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    Description

    Recombinant Zika Ectodomain is a glycosylated protein, produced using baculovirus vectors in insect cells and its Mw is approximately 45kDa.The Zika Ectodomain is a recombinant protein of the ectodomain of the envelope protein from the Suriname Zika virus strain.

    Source

    Baculovirus Insect Cells.

    Formulation

    The Zika Ectodomain solution 10mM Sodium phosphate, pH 7.2, 150mM NaCl.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      Zika virus (ZIKV) belongs to the family Flaviviridae and the genus Flavivirus, it is transmitted by daytime-active Aedes mosquitoes, such as A. aegypti and A. albopictus. The Zika virus is related to the dengue, yellow fever, Japanese encephalitis, and West Nile viruses. Much like the other flaviviruses, Zika virus is enveloped and icosahedral and has a nonsegmented, single-stranded, positive-sense RNA genome. Zika fever is an infection, which often causes no symptoms or only mild ones, like a mild form of dengue fever, and it is treated by rest. As of February 2016, there has been mounting evidence that Zika fever in pregnant women can cause abnormal brain development in their fetuses by mother-to-child transmission, which may result in miscarriage or microcephaly, however it is not yet known whether Zika virus causes microcephaly. Furthermore, a connection has been established with neurologic conditions in infected adults, including Guillain–Barre syndrome.

    • Physical Appearance

      Sterile Filtered solution.

    • Stability

      Zika Ectodomain should be stored at 4°C. Do not freeze!

    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.

    Zika Ectodomain
  • View Data Sheet

    Name :

    MUSTN1 Human

    Description:

    Musculoskeletal, Embryonic Nuclear Protein 1 Human Recombinant

    Musculoskeletal, Embryonic Nuclear Protein 1, MUSTANG, Musculoskeletal Embryonic Nuclear Protein 1, Musculoskeletal Temporally Activated Novel, MUSTN1.

    Product # :

    PRO-2061

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    Description

    MUSTN1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 105 amino acids (1-82 a.a) and having a molecular mass of 11.3kDa. MUSTN1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    MUSTN1 protein solution (0.25 mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 10% glycerol and 1mM DTT.

    Purity

    Greater than 80.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      Musculoskeletal, Embryonic Nuclear Protein 1, also known as MUSTN1 is a member of the MUSTANG family. MUSTN1 is implicated in the development andregeneration of the musculoskeletal system.

    • Synonyms

      Musculoskeletal, Embryonic Nuclear Protein 1, MUSTANG, Musculoskeletal Embryonic Nuclear Protein 1, Musculoskeletal Temporally Activated Novel, MUSTN1.

    • 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 MGSMSQAGAQ EAPIKKKRPP VKEEDLKGAR GNLTKNQEIK SKTYQVMREC EQAGSAAPSV FSRTRTGTET VFEKPKAGPT KSVFG.

    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.

    Mustn1 Human
  • View Data Sheet

    Name :

    BMP 4 Human

    Description:

    Bone Morphogenetic Protein-4 Human Recombinant

    BMP4, ZYME, BMP2B, BMP2B1.

    Product # :

    CYT-361

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    Description

    Bone Morphogenetic Protein-4 Human Recombinant produced in E.Coli is a monomeric, non-glycosylated, Polypeptide chain containing 116 amino acids and having a molecular mass of 13kDa. The BMP-4 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    BMP-4 was lyophilized from a 0.2µm filtered concentrated (1mg/ml) solution in 20mM Na2CO3 buffer, pH 9.0.

    Purity

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

    Citations

    More Info

    • Introduction

      The protein encoded by this gene is a member of the bone morphogenetic protein family which is part of the transforming growth factor-beta superfamily. The superfamily includes large families of growth and differentiation factors. Bone morphogenetic proteins were originally identified by an ability of demineralized bone extract to induce endochondral osteogenesis in vivo in an extraskeletal site. This particular family member plays an important role in the onset of endochondral bone formation in humans, and a reduction in expression has been associated with a variety of bone diseases, including the heritable disorder Fibrodysplasia Ossificans Progressiva. Alternative splicing in the 5' untranslated region of this gene has been described and three variants are described, all encoding an identical protein.

    • Synonyms

      BMP4, ZYME, BMP2B, BMP2B1.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized Bone Morphogenetic Protein-4 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution BMP4 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 Bone Morphogenetic Protein-4 in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      SPKHHSQRAR KKNKNCRRHS LYVDFSDVGW NDWIVAPPGY QAFYCHGDCP FPLADHLNST NHAIVQTLVN SVNSSIPKAC CVPTELSAIS MLYLDEYDKV VLKNYQEMVV EGCGCR.

    • Background

      What You Should Know About Bone Morphogenetic Protein-4 (BMP-4) Human Recombinant

      As part of the transforming growth factor-beta (TGF-β) superfamily, Bone morphogenetic protein-4 (BMP-4) participates in multiple developmental processes, from embryogenesis to bone and cartilage formation.

      Since this signaling protein is involved in many physiological processes, its laboratory-produced version has been studied for different medical applications. Additionally, a reduction in BMP-4 expression has been associated with multiple diseases, leading to further research into its potential therapeutic benefits.

      Are you interested in learning more about Bone Morphogenetic Protein-4 (BMP-4) human recombinant? Read on to find more information!

      How Does Bone Morphogenetic Protein-4 (BMP-4) Work?

      Bone Morphogenetic Protein-4 (BMP-4) regulates microRNAs miR-494 and miR-126-5p expression, controlling endothelial cells' involvement and function in angiogenesis. As such, it has diverse effects on cell growth, differentiation, and survival.

      The Role of BMP-4

      This protein emits signals that promote the formation of different tissues and organs, including the bones and cartilage, kidneys, teeth, and the neural tube. In other words, it's essential for the development of the heart, skeleton, and central nervous system.

      However, the role of BMP-4 goes beyond these processes. It participates in different physiological activities, such as:

      • Embryonic development
      • Wound healing
      • Bone remodeling
      • Immune response modulation
      • Tissue repair
      • Cardiac development and function

      What Is Bone Morphogenetic Protein-4 (BMP-4) Human Recombinant?

      To replicate the effects of the BMP4 found in humans and explore its possible therapeutic applications, many laboratories have started producing this protein in Chinese hamster ovary (CHO) cells.

      As mentioned, decreased BMP-4 expression has been associated with different diseases, including bone disorders, fibrosis, and cancer, which can cause other conditions, such as organ dysfunction.

      More research is needed, but BMP-4 human recombinant (rhBMP4) produced in CHO has the potential to address these diseases and could be used for other medical applications. These are some examples:

      • Cancer therapy
      • Development of engineered tissues and organs
      • Bone regeneration for the treatment of osteoporosis and nonunion fractures
      • Bone growth and fusion in spinal fusion surgeries (the U.S. Food and Drug Administration approved some bone morphogenetic proteins for these procedures)
      • Promotion of tissue repair and regeneration

      Final Thoughts BMP-4

      Although BMP-4 human recombinant produced in CHO offers potential benefits, several challenges remain, including possible side effects, as high doses can cause inflammation, bone overgrowth, and other issues.

      However, the long-term effects of rhBMP4 are still under investigation. Further research will provide solutions to address these challenges and allow experts to explore this laboratory-produced protein's power in different medical fields.

      What is the molecular weight/Mw of BMP4 Protein?
      BMP4 Protein has a total Mw of 13kDa.

      What is the source or expression system of BMP4 Protein?
      Escherichia Coli.

      What is the Purity of BMP4 Protein?
      BMP4 Protein is >95% pure as determined by SDS-PAGE.

      What is the Biological Activity of BMP4 Protein?
      The biological functionality of BMP4 Protein will be determined in the future.

      What is the amino acid sequence of BMP4 Protein?
      SPKHHSQRAR KKNKNCRRHS LYVDFSDVGW NDWIVAPPGY QAFYCHGDCP FPLADHLNST NHAIVQTLVN SVNSSIPKAC CVPTELSAIS MLYLDEYDKV VLKNYQEMVV EGCGCR.

      What applications can BMP4 Protein be used in?
      BMP4 Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for BMP4 Protein?
      The endotoxin level is minimal, BMP4 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.

    Bmp4 Human
  • View Data Sheet

    Name :

    Dengue Envelope-1 15kDa

    Description:

    Dengue Virus Subtype 1 Envelope 15kDa, C-Terminal (Domain III) Recombinant

    Product # :

    DEN-011

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    Description

    The E.coli derived recombinant 15kDa protein is genetically engineered peptide which is derived from C terminus of Dengue Type-1 envelope. The expressed protein contains neutralizing epitopes and receptor binding domain, it has been used in the study for vaccine development. A 6 x His Tag is fused at its C-terminus.

    Source

    Escherichia Coli.

    Formulation

    1xPBS, 0.02% sodium nitrate and 25mM k2CO3.

    Purity

    Protein is >95% pure as determined by 12% PAGE (coomassie staining).

    Citations

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    • Introduction

      Caused by one of four closely related virus serotypes of the genus Flavivirus, family Flaviviridae, each serotype is sufficiently different that there is no cross-protection and epidemics caused by multiple serotypes (hyperendemicity) can occur. In cell culture experiments and mice Morpholino antisense oligos have shown specific activity against Dengue virus.

    • Stability

      Dengue Envelope-ST1 D-III although stable at 4°C for 1 week, should be stored below -18°C. Please prevent freeze thaw cycles.

    • Applications

      Each laboratory should determine an optimum working titer for use in its particular application.

    • Purification Method

      Purified by proprietary chromatographic technique.

    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.

    Dengue Envelope 3 St1
  • View Data Sheet

    Name :

    Norovirus Group-2 P-Domain

    Description:

    Norovirus Group-2 Capsid P-Domain Recombinant

    Product # :

    NRV-216

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    Description

    The Recombinant Norovirus Group-2 Capsid P-Domain, E.Coli derived, VA387 Strain contains a.a. from 225-520 having a Mw of 30kDa. The protein is fused to a 6xHis tag at N-terminal and purified by chromatography techniques. P-domain (225-520 a.a.) forms P1- P2-P1 structure. P-domain has a receptor binding region to recognize human histo-blood group antigens (HBGAs). P-domain expressed in bacteria can spontaneously form a P dime and a P particle aggregated by 12 P dimmers. P-particle displays an enhanced binding activity to HBGAs higher than virus-like particle (VLP) formed by the full length capsid.

    Source

    Escherichia Coli.

    Formulation

    Phosphate buffer and 17mM K2CO3.

    Purity

    Protein is >95% pure as determined by 12% PAGE (coomassie staining).

    Citations

    More Info

    • Introduction

      Human norovirus is classified into two groups, group 1& group 2. Norwalk virus is the species which belongs to group 1 and was discovered in 1968 at Ohio. Norovirus is a familiar virus which causes human gastroenteritis with the following symptoms vomiting, diarrhea and sickness. CDC report revealed that there are 19-21 million Americans infected by Nororvirus annually with 800 deaths, 1 in 15 people with infection. Around the world, this virus affects about 267 million people and causes over 200,000 deaths each year; these losses are mostly in less developed countries and in the very young, elderly and immuno-suppressed population, though, most cases are self-limited with a full recovery within just a few days. Norovirus is extremely contagious and can spread from human to human through infected food, water or contaminated surfaces. The outbreaks usually occur from November-April, while the peak is in January. Norovirus is a positive sense RNA virus with 7.5 kb nucleotides, encoding a major structural protein VP1 with 50-55kDa. The full length of VP1 capsid comprises the internal N-terminal, Hinge, shell (S) and protruding (P) domains. P domain from 225 to 520 forms P1- P2-P1 structure. Moreover, P domain has a receptor binding region which recognizes human histo-blood group antigens (HBGAs). P domain expressed in bacteria can spontaneously form a P dime as well as a P particle aggregated by 12 P dimmers. P particle displays an increased binding activity to HBGAs higher than virus-like particle (VLP) formed by the full-length capsid. For norovirus vaccine development, we consider P domain as a good candidate.

    • Physical Appearance

      Sterile Filtered clear solution.

    • Stability

      The Recombinant Norovirus Group-2 P-Domain although stable at 4°C for 1 week, should be stored below -18°C. Please prevent 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.

    Norovirus Group 2 P Domain
  • View Data Sheet

    Name :

    CES1 Human

    Description:

    Carboxylesterase 1 Human Recombinant

    Liver carboxylesterase 1 isoform a, CES1, ACAT, CE-1, CEH, CES2, hCE-1, HMSE, HMSE1, PCE-1, REH, SES1, TGH, Acyl-coenzyme A:cholesterol acyltransferase, Brain carboxylesterase hBr1.

    Product # :

    ENZ-1099

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    Description

    CES1 Human produced in Sf9 Insect cells is a single, glycosylated polypeptide chain containing 559 amino acids (19-568 a.a.) and having a molecular mass of 61.7kDa (Molecular size on SDS-PAGE will appear at approximately 50-70kDa).CES1 is expressed with a 9 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    CES1 protein solution (0.5mg/ml) contains 25mM Sodium Acetate (pH 4.0), 10% glycerol, 0.1M NaCl and 0.1mM PMSF.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      CES1 is a part of the alpha/beta fold hydrolase familyand participates in the detoxification of xenobiotics and in the activation of ester and amide prodrugs. CES1hydrolyzes aromatic and aliphatic esters, although it has no catalytic activity toward amides or a fatty acyl-CoA ester. CES1hydrolyzes the methyl ester group of cocaine to form benzoylecgonine and catalyzes the transesterification of cocaine to form cocaethylene. CES1also plays a role in detoxification in the lung and protection of the central nervous system from ester or amide compounds.CES1 is found in most tissues, mainly in the liver.

    • Synonyms

      Liver carboxylesterase 1 isoform a, CES1, ACAT, CE-1, CEH, CES2, hCE-1, HMSE, HMSE1, PCE-1, REH, SES1, TGH, Acyl-coenzyme A:cholesterol acyltransferase, Brain carboxylesterase hBr1.

    • 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

      ADLGHPSSPP VVDTVHGKVL GKFVSLEGFA QPVAIFLGIP FAKPPLGPLR FTPPQPAEPW
      SFVKNATSYP PMCTQDPKAG QLLSELFTNR KENIPLKLSE DCLYLNIYTP ADLTKKNRLP
      VMVWIHGGGL MVGAASTYDG LALAAHENVV VVTIQYRLGI WGFFSTGDEH SRGNWGHLDQ
      VAALRWVQDN IASFGGNPGS VTIFGESAGG ESVSVLVLSP LAKNLFHRAI SESGVALTSV
      LVKKGDVKPL AEQIAITAGC KTTTSAVMVH CLRQKTEEEL LETTLKMKFL SLDLQGDPRE
      SQPLLGTVID GMLLLKTPEE LQAERNFHTV PYMVGINKQE FGWLIPMQLM SYPLSEGQLD
      QKTAMSLLWK SYPLVCIAKE LIPEATEKYL GGTDDTVKKK DLFLDLIADV MFGVPSVIVA
      RNHRDAGAPT YMYEFQYRPS FSSDMKPKTV IGDHGDELFS VFGAPFLKEG ASEEEIRLSK
      MVMKFWANFA RNGNPNGEGL PHWPEYNQKE GYLQIGANTQ AAQKLKDKEV AFWTNLFAKK AVEKPPQTEH IELHHHHHH.

    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.

    Ces1 Human
  • View Data Sheet

    Name :

    4-1BBR Mouse

    Description:

    4-1BB Receptor Mouse Recombinant

    Tumor necrosis factor receptor superfamily member 9, 4-1BB ligand receptor, T-cell antigen 4-1BB, CD137.

    Product # :

    CYT-916

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    Description

    4-1BBR produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 172 amino acids (24-187 a.a.) and having a molecular mass of 18.6kDa (Migrates at 18-28kDa on SDS-PAGE under reducing conditions). 4-1BBR is expressed with an 8 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    4-1BBR 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.

    Citations

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    • Introduction

      The protein encoded by this gene is a member of the TNF-receptor superfamily. This receptor contributes to the clonal expansion, survival, and development of T cells. It can also induce proliferation in peripheral monocytes, enhance T cell apoptosis induced by TCR/CD3 triggered activation, and regulate CD28 co-stimulation to promote Th1 cell responses. The expression of this receptor is induced by lymphocyte activation. TRAF adaptor proteins have been shown to bind to this receptor and transduce the signals leading to activation of NF-kappaB.

    • Synonyms

      Tumor necrosis factor receptor superfamily member 9, 4-1BB ligand receptor, T-cell antigen 4-1BB, CD137.

    • 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

      VQNSCDNCQP GTFCRKYNPV CKSCPPSTFS SIGGQPNCNI CRVCAGYFRF KKFCSSTHNA ECECIEGFHC LGPQCTRCEK DCRPGQELTK QGCKTCSLGT FNDQNGTGVC RPWTNCSLDG RSVLKTGTTE KDVVCGPPVV SFSPSTTISV TPEGGPGGHS LQVLLEHHHH HH.

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

    4-1BBR Mouse
  • View Data Sheet

    Name :

    MUCL1 Human

    Description:

    Mucin-Like 1 Human Recombinant

    Mucin-Like 1, Small Breast Epithelial Mucin, SBEM, Mucin-Like Protein 1, Protein BS106, Mucin-like protein 1.

    Product # :

    PRO-2124

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    Description

    MUCL1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 93 amino acids (21-90 a.a) and having a molecular mass of 9.3kDa. MUCL1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    MUCL1 protein solution (0.25mg/ml) containing Phosphate buffer saline (pH 7.4) and 10% glycerol.

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

    Citations

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    • Introduction

      Mucin-Like 1, also known as MUCL1 takes a part as a marker for the diagnosis of metastatic breast cancer. MUCL1 is expressed in mammary, salivary glands as well as in prostate.

    • Synonyms

      Mucin-Like 1, Small Breast Epithelial Mucin, SBEM, Mucin-Like Protein 1, Protein BS106, Mucin-like 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 MGSNPTTAAP ADTYPATGPA DDEAPDAETT AAATTATTAA PTTATTAAST TARKDIPVLP KWVGDLPNGR VCP.

    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.

    Mucl1 Human
  • View Data Sheet

    Name :

    BGN Human, Sf9

    Description:

    Biglycan Human Recombinant, Sf9

    BGN, DSPG1, MRLS, PG-S1, PGI, SEMDX, SLRR1A, Biglycan, Bone/cartilage proteoglycan I, Biglycan Proteoglycan, MRLS.

    Product # :

    PRO-2536

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    Description

    BGN produced in Sf9 Insect cells is a single, glycosylated polypeptide chain containing 340 amino acids (38-368 a.a.) and having a molecular mass of 38.3kDa (Molecular size on SDS-PAGE will appear at approximately 40-57kDa). BGN is expressed with a 9 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Insect cells.

    Formulation

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

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    Biological Activity

    The ED50 for this effect is ≤ 20 ug/ml. The specific activity is measured by inhibiting the cell growth using 3T3‑ L1 mouse embryonic  fibroblast  adipose-like cells.

    Citations

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    • Introduction

      Biglycan (BGN) is a small cellular or pericellular matrix proteoglycan which takes part in assembly of collagen fibrils and muscle regeneration. BGN is closely correlated in structure to two other small proteoglycans, decorin and fibromodulin. BGN interacts with several proteins involved in muscular dystrophy, including alpha-dystroglycan, alpha- and gamma-sarcoglycan and collagen VI. BGN is also critical for the assembly of the dystrophin-associated protein complex.

    • Synonyms

      BGN, DSPG1, MRLS, PG-S1, PGI, SEMDX, SLRR1A, Biglycan, Bone/cartilage proteoglycan I, Biglycan Proteoglycan, MRLS.

    • 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

      ADPDEEASGA DTSGVLDPDS VTPTYSAMCP FGCHCHLRVV QCSDLGLKSV PKEISPDTTL LDLQNNDISE LRKDDFKGLQ HLYALVLVNN KISKIHEKAF SPLRKLQKLY ISKNHLVEIP PNLPSSLVEL RIHDNRIRKV PKGVFSGLRN MNCIEMGGNP LENSGFEPGA FDGLKLNYLR ISEAKLTGIP KDLPETLNEL HLDHNKIQAI ELEDLLRYSK LYRLGLGHNQ IRMIENGSLS FLPTLRELHL DNNKLARVPS GLPDLKLLQV VYLHSNNITK VGVNDFCPMG FGVKRAYYNG ISLFNNPVPY WEVQPATFRC VTDRLAIQFG NYKKHHHHHH.

    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.

    Biglycan Human
  • View Data Sheet

    Name :

    Erythropoietin Human, Active

    Description:

    Erythropoietin Receptor Human Recombinant, Active

    EPO-R, EPOR, Erythropoietin Receptor.

    Product # :

    CYT-997

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    Description

    EPOR produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 232 amino acids (25-250a.a.) and having a molecular mass of 25.6kDa (Molecular size on SDS-PAGE will appear at approximately 28-40kDa).EPOR is expressed with a 6 amino acid His-tag at C-Terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

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

    Purity

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

    Biological Activity

    Measured by its ability to inhibit EPO dependent proliferation assay using TF-1 human erythroleukemic cells. The ED50 for this effect less or equal to 70ng/ml.

    Citations

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    • Introduction

      Erythropoietin receptor, also known as EPOR arbitrates erythropoietin-induced erythroblast proliferation as well as differentiation. During EPO binding, EPOR activates Jak2 tyrosine kinase which activates various intracellular pathways including: Ras/MAP kinase, phosphatidylinositol 3-kinase and STAT transcription factors. Furthermore, stimulated EPOR has a function in erythroid cell survival. Mutations in EPOR may possibly produce erythroleukemia and familial erythrocytosis. In addition, dysregulation of EPOR can affect on the growth of selected tumors.

    • Synonyms

      EPO-R, EPOR, Erythropoietin Receptor.

    • 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

      APPPNLPDPK FESKAALLAA RGPEELLCFT ERLEDLVCFW EEAASAGVGP GNYSFSYQLE DEPWKLCRLH QAPTARGAVR FWCSLPTADT SSFVPLELRV TAASGAPRYH RVIHINEVVL LDAPVGLVAR LADESGHVVL RWLPPPETPM TSHIRYEVDV SAGNGAGSVQ RVEILEGRTE CVLSNLRGRT RYTFAVRARM AEPSFGGFWS AWSEPVSLLT PSDLDPHHHH HH.

    • Background

      What is the molecular weight/Mw of ERYTHROPOIETIN Protein?
      ERYTHROPOIETIN Protein has a total Mw of 25.6kDa.

      What is the source or expression system of ERYTHROPOIETIN Protein?
      Sf9, Baculovirus cells.

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

      What is the Biological Activity of ERYTHROPOIETIN Protein?
      Measured by its ability to inhibit EPO dependent proliferation assay using TF-1 human erythroleukemic cells. The ED50 for this effect less or equal to 70ng/ml.

      What is the amino acid sequence of ERYTHROPOIETIN Protein?
      APPPNLPDPK FESKAALLAA RGPEELLCFT ERLEDLVCFW EEAASAGVGP GNYSFSYQLE DEPWKLCRLH QAPTARGAVR FWCSLPTADT SSFVPLELRV TAASGAPRYH RVIHINEVVL LDAPVGLVAR LADESGHVVL RWLPPPETPM TSHIRYEVDV SAGNGAGSVQ RVEILEGRTE CVLSNLRGRT RYTFAVRARM AEPSFGGFWS AWSEPVSLLT PSDLDPHHHH HH.

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

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

    Epor Human Sf9
  • View Data Sheet

    Name :

    VAMP2 Mouse

    Description:

    Synaptobrevin-2 Recombinant Mouse

    Vesicle-associated membrane protein 2, VAMP-2, Synaptobrevin-2, Vamp2, Syb2.

    Product # :

    PRO-2415

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    Description

    VAMP2 Mouse 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

    Escherichia Coli.

    Formulation

    VAMP2 protein solution (1mg/ml) containing Phosphate Buffered Saline (pH7.4), 1mM EDTA, 0.1mM PMSF and 10% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      Synaptobrevin 2 which is an 18 kDa integral membrane protein localized to the cytoplasmic surface of synaptic vesicle, consists of a proline-rich N-terminal region, a highly conserved hydrophilic domain, followed by a transmembrane anchor and a C-terminal. Synaptobrevin 2 is predominantly expressed in Langerhans islets and glomerular cells. The N-terminal domain of the protein (residues 1-89) forms a specific SNARE complex with the target membrane-associated t- or Q-SNAREs syntaxin 1 and SNAP-25.

    • Synonyms

      Vesicle-associated membrane protein 2, VAMP-2, Synaptobrevin-2, Vamp2, Syb2.

    • 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 MGSHMSATAA TVPPAAPAGE GGPPAPPPNL TSNRRLQQTQ AQVDEVVDIM RVNVDKVLER DQKLSELDDR ADALQAGASQ FETSAAKLKR KYWWKNLK.

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    Vamp2 Mouse 3
  • View Data Sheet

    Name :

    RPL30 Human

    Description:

    Ribosomal Protein L30 Human Recombinant

    60S ribosomal protein L30, RPL30, Ribosomal Protein L30, L30.

    Product # :

    PRO-1659

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    Description

    RPL30 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 138 amino acids (1-115 a.a) and having a molecular mass of 15.2kDa.RPL30 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    RPL30 protein solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.2M NaCl, 40% glycerol and 2mM DTT.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      Ribosomal Protein L30 (RPL30) is a member of the L30E family of ribosomal proteins. RPL30 is a ribosomal protein which is a component of the 60S subunit. RPL30 is located in the cytoplasm. The RPL30 gene is co-transcribed with the U72 small nucleolar RNA gene, which is located in its 4th intron.

    • Synonyms

      60S ribosomal protein L30, RPL30, Ribosomal Protein L30, L30.

    • 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 MGSMVAAKKT KKSLESINSR LQLVMKSGKY VLGYKQTLKM IRQGKAKLVI LANNCPALRK SEIEYYAMLA KTGVHHYSGN NIELGTACGK YYRVCTLAII DPGDSDIIRS MPEQTGEK.

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    Rpl30 Human
  • View Data Sheet

    Name :

    BCL10 Human

    Description:

    B-cell CLL/Lymphoma 10 Human Recombinant

    B-cell CLL/lymphoma 10, B-cell lymphoma/leukemia 10, Mammalian CARD-containing adapter molecule E10, CARD-containing molecule enhancing NF-kappa-B, CED-3/ICH-1 prodomain homologous E10-like regulator, CARD-containing apoptotic signaling protein, caspase-recruiting domain-containing protein, Cellular homolog of vCARMEN, cellular-E10, c-E10, CARD-like apoptotic protein, cCARMEN, mE10, CLAP, CIPER, Bcl-10.

    Product # :

    PRO-1058

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    Description

    BCL10 Human Recombinant produced in E. coli is a single polypeptide chain containing 257 amino acids (1-233) and having a molecular mass of 28.8kDa (molecular weight on SDS-PAGE will appear higher).BCL10 is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    The BCL10 solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 50mM NaCl, 1mM DTT and 10% glycerol.

    Purity

    Greater than 85% as determined by SDS-PAGE.

    Citations

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    • Introduction

      BCL10 holds a caspase recruitment domain (CARD), and is known as an inducer of apoptosis and as NF-kappaB activator. BCL10 cooperates with other CARD domain containing proteins such as CARD9, 10, 11 and 14, which operates as upstream regulators in NF-kappaB signaling. BCL10 is known to create a complex with MALT1, a protein encoded by another gene and is translocated in MALT lymphoma. MALT1 and BCL10 protein synergize the activation of NF-kappaB, and the deregulation of either of them facilitates the same pathogenetic process which leads to the malignancy.

    • Synonyms

      B-cell CLL/lymphoma 10, B-cell lymphoma/leukemia 10, Mammalian CARD-containing adapter molecule E10, CARD-containing molecule enhancing NF-kappa-B, CED-3/ICH-1 prodomain homologous E10-like regulator, CARD-containing apoptotic signaling protein, caspase-recruiting domain-containing protein, Cellular homolog of vCARMEN, cellular-E10, c-E10, CARD-like apoptotic protein, cCARMEN, mE10, CLAP, CIPER, Bcl-10.

    • 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 MGSHMEPTAP SLTEEDLTEV KKDALENLRV YLCEKIIAER HFDHLRAKKI LSREDTEEIS CRTSSRKRAG KLLDYLQENP KGLDTLVESI RREKTQNFLI QKITDEVLKL RNIKLEHLKG LKCSSCEPFP DGATNNLSRS NSDESNFSEK LRASTVMYHP EGESSTTPFF STNSSLNLPV LEVGRTENTI FSSTTLPRPG DPGAPPLPPD LQLEEEGTCA NSSEMFLPLR SRTVSRQ.

    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.

    Bcl10 Human
  • View Data Sheet

    Name :

    ENTPD3 Human, sf9 Bioactive

    Description:

    Ectonucleoside Triphosphate Diphosphohydrolase 3 Human Recombinant, sf9 Bioactive

    Ectonucleoside Triphosphate Diphosphohydrolase 3, Ecto-ATP Diphosphohydrolase 3, CD39 Antigen-Like 3, Ecto-ATPDase 3, Ecto-Apyrase 3, Ecto-ATPase 3, EC 3.6.1.5, NTPDase 3, CD39L3, HB6, NTPDase-3, EC 3.6.1, Ectonucleoside triphosphate diphosphohydrolase 3, NTPDase 3, CD39 antigen-like 3, Ecto-ATP diphosphohydrolase 3, Ecto-ATPDase 3, Ecto-ATPase 3, Ecto-apyrase 3, HB6.

    Product # :

    ENZ-1020

    Price :

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    More Info

    • description
    • source
    • formulation
    • purity
    • biological activity
    • More Info
    • Citations

    Description

    ENTPD3 Human Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 451 amino acids (44-485a.a.) and having a molecular mass of 50.7kDa (Molecular size on SDS-PAGE will appear at approximately 50-70kDa).ENTPD3 is expressed with a 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    ENTPD3 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.

    Biological Activity

    Specific activity is > 250,000 pmol/min/ug, and is defined as the amount of enzyme that hydrolyze ATP per minute at pH 7.5 at 37C.

    Citations

    More Info

    • Introduction

      Ectonucleoside Triphosphate Diphosphohydrolase 3, also known as ENTPD3, which owns a threefold preference for the hydrolysis of ATP over ADP is similar to E-type nucleotidases (NTPases). ENTPD3 is a protein coding gene which contains four apyrase-conserved areas which is characteristic of NTPases.

    • Synonyms

      Ectonucleoside Triphosphate Diphosphohydrolase 3, Ecto-ATP Diphosphohydrolase 3, CD39 Antigen-Like 3, Ecto-ATPDase 3, Ecto-Apyrase 3, Ecto-ATPase 3, EC 3.6.1.5, NTPDase 3, CD39L3, HB6, NTPDase-3, EC 3.6.1, Ectonucleoside triphosphate diphosphohydrolase 3, NTPDase 3, CD39 antigen-like 3, Ecto-ATP diphosphohydrolase 3, Ecto-ATPDase 3, Ecto-ATPase 3, Ecto-apyrase 3, HB6.

    • 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

      ADLQIHKQEV LPPGLKYGIV LDAGSSRTTV YVYQWPAEKE NNTGVVSQTF KCSVKGSGIS SYGNNPQDVP RAFEECMQKV KGQVPSHLHG STPIHLGATA GMRLLRLQNE TAANEVLESI QSYFKSQPFD FRGAQIISGQ EEGVYGWITA NYLMGNFLEK NLWHMWVHPH GVETTGALDL GGASTQISFV AGEKMDLNTS DIMQVSLYGY VYTLYTHSFQ CYGRNEAEKK FLAMLLQNSP TKNHLTNPCY PRDYSISFTM GHVFDSLCTV DQRPESYNPN DVITFEGTGD PSLCKEKVAS IFDFKACHDQ ETCSFDGVYQ PKIKGPFVAF AGFYYTASAL NLSGSFSLDT FNSSTWNFCS QNWSQLPLLL PKFDEVYARS YCFSANYIYH LFVNGYKFTE ETWPQIHFEK EVGNSSIAWS LGYMLSLTNQ IPAESPLIRL PIEPPHHHHHH.

    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.

    Entpd3 Human Sf9 Bioactive
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