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  • MEC (CCL28)

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    ENA-78 (CXCL5)

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    Eotaxin (CCL11,24,26)

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Search results

686 results found for “ttc”

Name

Description

Product #

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  • View Data Sheet

    Name :

    GLRX3 Human

    Description:

    Glutaredoxin-3 Human Recombinant

    Glutaredoxin-3, Thioredoxin-like protein 2, PKC-interacting cousin of thioredoxin, PKC-theta-interacting protein, PKCq-interacting protein, GLRX3, PICOT, TXNL2, GRX3, GRX4, GLRX4, TXNL3, FLJ11864, bA500G10.4.

    Product # :

    ENZ-482

    Price :

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    Description

    GLRX3 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 355 amino acids (1-335 a.a.) and having a molecular mass of 39.6kDa. GLRX3 is fused to a 20 amino acid His Tag at N-terminus and purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    GLRX3 solution containing 20mM Tris-HCl buffer (pH8.0), 10% glycerol and 1mM DTT.

    Purity

    Greater than 95% as determined by SDS-PAGE.

    More Info

    • Introduction

      Glutaredoxin belongs to the thiol-disulfide oxidoreductase family. Glutraredoxins catalyze the reversible reduction of protein-glutathionyl mixed disulfides to free sulfhydryl groups though a monothiol mechanism. Glutaredoxin-3 (GRX3) is an important protein involved in the regulation of signal transduction, for example during immune cell activation and development of cardiac hypertrophy, apparently in response to redox signals. GRX3 interacts with PRKCQ. GRX3 may have a role in the regulation the function of the thioredoxin system. GRX3 is expressed in the heart, spleen, testis and, to a lower extent, in the thymus and peripheral blood leukocytes. GRX3 is weakly expressed in lung, placenta, colon and small intestine.

    • Synonyms

      Glutaredoxin-3, Thioredoxin-like protein 2, PKC-interacting cousin of thioredoxin, PKC-theta-interacting protein, PKCq-interacting protein, GLRX3, PICOT, TXNL2, GRX3, GRX4, GLRX4, TXNL3, FLJ11864, bA500G10.4.

    • Physical Appearance

      Sterile filtered colorless solution.

    • Stability

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

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MAAGAAEAAV AAVEEVGSAG QFEELLRLKA KSLLVVHFWA PWAPQCAQMN EVMAELAKEL PQVSFVKLEA EGVPEVSEKY EISSVPTFLF FKNSQKIDRL DGAHAPELTK KVQRHASSGS FLPSANEHLK EDLNLRLKKL THAAPCMLFM KGTPQEPRCG FSKQMVEILH KHNIQFSSFD IFSDEEVRQG LKAYSSWPTY PQLYVSGELI GGLDIIKELE ASEELDTICP KAPKLEERLK VLTNKASVML FMKGNKQEAK CGFSKQILEI LNSTGVEYET FDILEDEEVR QGLKAYSNWP TYPQLYVKGE LVGGLDIVKE LKENGELLPI LRGEN.

    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.

    Glrx3 Human
  • View Data Sheet

    Name :

    TULP1 Human

    Description:

    Tubby Like Protein 1 Human Recombinant

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

    Product # :

    PRO-1191

    Price :

    Quantity :

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    Description

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

    Source

    E.coli.

    Formulation

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

    Purity

    Greater than 90% as determined by SDS-PAGE.

    More Info

    • Introduction

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

    • Synonyms

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

    • Physical Appearance

      Sterile Filtered colorless solution.

    • Stability

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

    • Amino Acid Sequence

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

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

    Tulp1 Human
  • View Data Sheet

    Name :

    CNOT7 Mouse

    Description:

    CCR4-NOT Transcription Complex, Subunit 7 Mouse Recombinant

    CCR4-NOT transcription complex subunit 7, Cnot7, Caf1, Pop2, AU022737.

    Product # :

    PRO-908

    Price :

    Quantity :

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    • description
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    • More Info

    Description

    CNOT7 Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 271 amino acids (1-248 a.a) and having a molecular mass of 31.1kDa.CNOT7 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    CNOT7 protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH8.0), 20% glycerol and 1mM DTT.

    Purity

    Greater than 80.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      CCR4-Not transcription complex, subunit 7 (CNOT7) is a ubiquitous transcription factor. CNOT7 is a component of the CCR4 complex which functions as a general transcription regulation complex. Furthermore, CNOT7 binds to an anti-proliferative protein, BTG1 (B-cell translocation protein 1), which negatively regulates cell proliferation.

    • Synonyms

      CCR4-NOT transcription complex subunit 7, Cnot7, Caf1, Pop2, AU022737.

    • 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 MGSMPAATVD HSQRICEVWA CNLDEEMKKI RQVIRKYNYV AMDTEFPGVV ARPIGEFRSN ADYQYQLLRC NVDLLKIIQL GLTFMNEQGE YPPGTSTWQF NFKFNLTEDM YAQDSIELLT TSGIQFKKHE EEGIETQYFA ELLMTSGVVL CEGVKWLSFH SGYDFGYLIK ILTNSNLPEE ELDFFEILRL FFPVIYDVKY LMKSCKNLKM FFEDHIDDAK YCGHLYGLGS GSSYVQNGTG NAYEEEASKQ S.

    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.

    Cnot7 Mouse
  • View Data Sheet

    Name :

    T.gondii p30

    Description:

    Toxoplasma Gondii p30 (SAG1) Recombinant

    Product # :

    TOX-264

    Price :

    Quantity :

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    • description
    • source
    • formulation
    • purity
    • More Info

    Description

    T.gondii p30 is highly conformational antigen containing 12 cysteine residues and is fused to a 6 x His tag at its C-terminus.

    Source

    Escherichia Coli.

    Formulation

    PBS, 25mM K2CO3 and 0.025% NaN3.

    Purity

    Toxoplasma protein is >95% pure as determined by 10% PAGE (coomassie staining).

    More Info

    • Introduction

      The life cycle of Toxoplasma gondii has two phases. The coccidia like takes place only in members of the Felidae family which makes these animals the parasite's primary host. The asexual part of the life cycle can take place in any warm-blooded animal, like other mammals(including felines) and birds. T. gondii constructing daughter scaffolds within the mother cell. In the intermediate hosts (including felines), the parasite invades cells, forming intracellular so-called parasitophorous vacuoles containing bradyzoites, the slowly replicating form of the parasit. Vacuoles form tissue cysts mainly within the muscles and brain. Since they are within cells, the host's immune system does not detect these cysts. Resistance to antibiotics varies, but the cysts are very difficult to eradicate entirely. Within these vacuoles T. gondii propagates by a series of binary fissions until the infected cell eventually bursts and tachyzoites are released. Tachyzoites are the motile, asexually reproducing form of the parasite. Unlike the bradyzoites, the free tachyzoites are usually efficiently cleared by the host's immune response, although some manage to infect cells and form bradyzoites, thus maintaining the infection.

    • Stability

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

    • Applications

      Immunoassay.

    • Purification Method

      Toxoplasma protein was 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.

    Tgondii P30
  • View Data Sheet

    Name :

    CTF2P Mouse

    Description:

    Neuropoietin Mouse Recombinant

    Cardiotrophin-2, CT-2, Neuropoietin, Np, Ctf2, Gm494.

    Product # :

    CYT-1128

    Price :

    Quantity :

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    Shipped at Room temp

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    More Info

    • description
    • source
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    • biological activity
    • More Info

    Description

    Neuropoietin Mouse Recombinant produced in E.Coli is a non-glycosylated polypeptide chain containing 182 amino acids and having a molecular mass of approximately 19.7kDa.CTF2P is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Lyophilized from a 0.2μm filtered concentrated solution in 20mM Tris-HCl, pH 8.0, 0.5mM DTT and 500mM NaCl.

    Purity

    Greater than 98.0% as determined by:
    (a) Analysis by RP-HPLC.
    (b) Analysis by SDS-PAGE.

    Biological Activity

    The ED50 as determined by a cell proliferation assay using human TF-1 cells is < 200 ng/ml, corresponding to a specific activity of > 5000 IU/mg.

    More Info

    • Introduction

      CTF2P, aka Neuropoietinis a part of the IL-6 family of cytokines. CTF2P is the outcome of a gene duplication event involving cardiotrophin-1 (CT-1) and it helps to define a subfamily within the IL-6 family that includes CT-1, CLC and CTNF. CTF2P Increases the platelet count associated with splenomegaly and takes part in neuronal precursor development and maturation.

    • Synonyms

      Cardiotrophin-2, CT-2, Neuropoietin, Np, Ctf2, Gm494.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized CTF2P although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Neuropoietin should be stored at 4°C between 2-7 days and for future use below -18°C. Please prevent freeze-thaw cycles.

    • Solubility

      It is recommended to reconstitute the lyophilized Neuropoietin in sterile PBS not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      APISPSEPIG QAYSLALYMQ KNTSALLQTY LQHQGSPFSD PGFSAPELQL STLPSAAVSF KTWHAMEDAE RLSRAQGAFL ALTQHLQLVG DDQSYLNPGS PILLAQLGAA RLRAQGLLGN MAAIMTALGL PIPPEEDTLG FVPFGASAFE RKCRGYIVTR EYGHWTDRAV RDLALLKAKY SA.

    • Background

      What is the molecular weight/Mw of CTF2P Protein?
      CTF2P Protein has a total Mw of 19.7kDa.

      What is the source or expression system of CTF2P Protein?
      Escherichia Coli.

      What is the Purity of CTF2P Protein?
      CTF2P Protein is >98% pure as determined by SDS-PAGE.

      What is the Biological Activity of CTF2P Protein?
      The ED50 as determined by a cell proliferation assay using human TF-1 cells is < 200 ng/ml, corresponding to a specific activity of > 5000 IU/mg.

      What is the amino acid sequence of CTF2P Protein?
      APISPSEPIG QAYSLALYMQ KNTSALLQTY LQHQGSPFSD PGFSAPELQL STLPSAAVSF KTWHAMEDAE RLSRAQGAFL ALTQHLQLVG DDQSYLNPGS PILLAQLGAA RLRAQGLLGN MAAIMTALGL PIPPEEDTLG FVPFGASAFE RKCRGYIVTR EYGHWTDRAV RDLALLKAKY SA.

      What applications can CTF2P Protein be used in?
      CTF2P Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for CTF2P Protein?
      The endotoxin level is minimal, CTF2P 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.

    Neuropoietin Mouse
  • View Data Sheet

    Name :

    Hepsin Human

    Description:

    Hepsin Human Recombinant

    HPN, TMPRSS1, Serine protease hepsin, Transmembrane protease serine 1.

    Product # :

    PRO-2846

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    Description

    Hepsin Human Recombinant produced in Cho cells is a covalently-linked heterodimer having a total molecular mass of 43.0kDa. Hepsin is fused to a 6 amino acid His-tag at C-terminus & purified by proprietary chromatographic techniques.

    Source

    CHO cells.

    Formulation

    The Hepsin protein was Lyophilized from a 0.2µm filtered concentrated solution in 20mM Tris and 150mM NaCl, pH 8.0.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Biological Activity

    The specific activity is >20,000 pmol/min/μg and was measured by its ability to cleave tert-butoxycarbonyl-Gln-Arg-Arg-7-amino-4-methylcoumarin (Boc-QRR-AMC).

    More Info

    • Synonyms

      HPN, TMPRSS1, Serine protease hepsin, Transmembrane protease serine 1.

    • Physical Appearance

      Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Solubility

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

    • Amino Acid Sequence

      Light Chain (Non-catalytic Chain)
      RSDQEPLYPV QVSSADARLM VFDKTEGTWR LLCSSRSNAR VAGLSCEEMG FLRALTHSEL DVRTAGANGT SGFFCVDEGR LPHTQRLLE VISVCDCPRGR FLAAICQDCG RRKLPVDR.

      Heavy Chain (Catalytic Chain)
      IVGGRDTSLG RWPWQVSLRY DGAHLCGGSL LSGDWVLTAA HCFPERNRVL SRWRVFAGAV AQASPHGLQL GVQAVVYHGG YLPFRDPNSE ENSNDIALVH LSSPLPLTEY IQPVCLPAAG QALVDGKICT VTGWGNTQYY GQQAGVLQEA RVPIISNDVC NGADFYGNQI KPKMFCAGYP EGGIDACQGD SGGPFVCEDS ISRTPRWRLC GIVSWGTGCA LAQKPGVYTK VSDFREWIFQ AIKTHSEASG MVTQLHHHHH H.

    • Background

      Hepsin is a type II transmembrane serine protease expressed primarily on epithelial cells, it takes part in extracellular proteolysis by activating precursor proteins such as pro-HGF and contributes to tissue remodeling, cell signaling, and normal epithelial function. Recombinant Hepsin is used to study prostate cancer, extracellular matrix remodelling, protease signalling pathways, tumor invasion, metastasis, HGF/MET signaling, and for screening inhibitors that target serine proteases

      What is the molecular weight / Mw of Hepsin Protein?
      Hepsin Protein has a total Mw of 43kDa.

      What is the source or expression system of Hepsin Protein?
      CHO Cells

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

      What is the Biological Activity of Hepsin Protein?
      The enzymatic activity was measured by its ability to cleave tert-butoxycarbonyl-Gln-Arg-Arg-7-amino-4-methylcoumarin (Boc-QRR-AMC). The specific activity is >20,000 pmol/min/μg.

      What is the amino acid sequence of Hepsin Protein?
      Light Chain (Non-catalytic Chain)
      RSDQEPLYPV QVSSADARLM VFDKTEGTWR LLCSSRSNAR VAGLSCEEMG FLRALTHSEL DVRTAGANGT SGFFCVDEGR LPHTQRLLE VISVCDCPRGR FLAAICQDCG RRKLPVDR
      Heavy Chain (Catalytic Chain)
      IVGGRDTSLG RWPWQVSLRY DGAHLCGGSL LSGDWVLTAA HCFPERNRVL SRWRVFAGAV AQASPHGLQL GVQAVVYHGG YLPFRDPNSE ENSNDIALVH LSSPLPLTEY IQPVCLPAAG QALVDGKICT VTGWGNTQYY GQQAGVLQEA RVPIISNDVC NGADFYGNQI KPKMFCAGYP EGGIDACQGD SGGPFVCEDS ISRTPRWRLC GIVSWGTGCA LAQKPGVYTK VSDFREWIFQ AIKTHSEASG MVTQLHHHHH H

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

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

    Hepsin Human
  • View Data Sheet

    Name :

    TBC1D22B Human

    Description:

    TBC1 Domain Family, Member 22B Human Recombinant

    TBC1 Domain Family, Member 22B, C6orf197, Chromosome 6 Open Reading Frame 197, TBC1 Domain Family Member 22B, TBC1 domain family member 22B.

    Product # :

    PRO-2214

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    Description

    TBC1D22B Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 528 amino acids (1-505 a.a) and having a molecular mass of 61.5kDa. TBC1D22B is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    TBC1D22B protein solution (0.25mg/ml) containing Phosphate buffered saline (pH7.4) 30% glycerol and 1mM DTT.

    Purity

    Greater than 80% as determined by SDS-PAGE.

    More Info

    • Introduction

      TBC1 domain family member 22B, also known as TBC1D22B acts as a GTPase-activating protein for Rab family protein. The Tre-2/Bub2/Cdc16 (TBC) domain is a conserved protein motif which consists of roughly 200 amino acids and functions as a specific Rab-GAP domain. The TBC domain has more than 40 distinct TBC domain-containing proteins which have been identified in humans.

    • Synonyms

      TBC1 Domain Family, Member 22B, C6orf197, Chromosome 6 Open Reading Frame 197, TBC1 Domain Family Member 22B, TBC1 domain family member 22B.

    • Physical Appearance

      Sterile Filtered clear solution.

    • Stability

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

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MGSMAAENSK QFWKRSAKLP GSIQPVYGAQ HPPLDPRLTK NFIKERSKVN TVPLKNKKAS SFHEFARNTS DAWDIGDDEE EDFSSPSFQT LNSKVALATA AQVLENHSKL RVKPERSQST TSDVPANYKV IKSSSDAQLS RNSSDTCLRN PLHKQQSLPL RPIIPLVARI SDQNASGAPP MTVREKTRLE KFRQLLSSQN TDLDELRKCS WPGVPREVRP ITWRLLSGYL PANTERRKLT LQRKREEYFG FIEQYYDSRN EEHHQDTYRQ IHIDIPRTNP LIPLFQQPLV QEIFERILFI WAIRHPASGY VQGINDLVTP FFVVFLSEYV EEDVENFDVT NLSQDMLRSI EADSFWCMSK LLDGIQDNYT FAQPGIQKKV KALEELVSRI DEQVHNHFRR YEVEYLQFAF RWMNNLLMRE LPLRCTIRLW DTYQSEPEGF SHFHLYVCAA FLIKWRKEIL DEEDFQGLLM LLQNLPTIHW GNEEIGLLLA EAYRLKYMFA DAPNHYRR.

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    Tbc1D22B Human
  • View Data Sheet

    Name :

    THG1L Human

    Description:

    tRNA-Histidine Guanylyltransferase 1-Like Human Recombinant

    tRNA-histidine guanylyltransferase 1-like (S. cerevisiae), Interphase cytoplasmic foci protein 45, probable tRNA(His) guanylyltransferase, induced by high glucose-1, FLJ11601, FLJ20546, ICF45, IHG-1, EC 2.7.7.79, EC 2.7.7.6.

    Product # :

    ENZ-639

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    Description

    THG1L Human Recombinant produced in E. coli is a single polypeptide chain containing 292 amino acids (30-298) and having a molecular mass of 34.0 kDa.THG1L is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    The THG1L 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

      Probable tRNA (His) guanylyltransferase (THG1L) is a member of the tRNA (His) gyanylytransferase family. THG1L which is localized to the cytoplasm also found adjacent to the nuclear membrane and expressed in various tissues, including liver and lung. THG1L is expressed in a cell cycle-dependent manner and may be involved in cell cycle progression and cell proliferation. THG1L adds a GMP to the 5'-end of tRNA(His) after transcription and RNase P cleavage. This step is vital for accurate recognition of the tRNA and for the fidelity of protein synthesis. Upon DNA damage, THG1L is phosphorylated, presumably by ATM or ATR.

    • Synonyms

      tRNA-histidine guanylyltransferase 1-like (S. cerevisiae), Interphase cytoplasmic foci protein 45, probable tRNA(His) guanylyltransferase, induced by high glucose-1, FLJ11601, FLJ20546, ICF45, IHG-1, EC 2.7.7.79, EC 2.7.7.6.

    • Physical Appearance

      Sterile Filtered colorless solution.

    • Stability

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

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MGSMAKSKFE YVRDFEADDT CLAHCWVVVR LDGRNFHRFA EKHNFAKPND SRALQLMTKC AQTVMEELED IVIAYGQSDE YSFVFKRKTN WFKRRASKFM THVASQFASS YVFYWRDYFE DQPLLYPPGF DGRVVVYPSN QTLKDYLSWR QADCHINNLY NTVFWALIQQ SGLTPVQAQG RLQGTLAADK NEILFSEFNI NYNNELPMYR KGTVLIWQKV DEVMTKEIKL PTEMEGKKMA VTRTRTKPVP LHCDIIGDAF WKEHPEILDE DS.

    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.

    Thg1L Human
  • View Data Sheet

    Name :

    TNNI3 Human, (1-210)

    Description:

    Cardiac Troponin-I Human Recombinant (1-210 a.a.)

    Troponin I cardiac muscle, Cardiac troponin I, TNNI3, TNNC1, CMH7, RCM1, cTnI, CMD2A, MGC116817.

    Product # :

    PRO-2591

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    Description

    TNNI3 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 233 amino acids (1-210 a.a) and having a molecular mass of 26.4 kDa.TNNI3 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    TNNI3 protein solution (0.25mg/ml) contains 30% glycerol, 20mM Tris-HCl buffer (pH 7.5), 0.1M NaCl, 0.1mMPMSF & 1mM DTT.

    Purity

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

    More Info

    • Introduction

      Troponin I (TnI), troponin T (TnT) and troponin C (TnC) form the troponin complex of the thin filaments of striated muscle. TnI acts as the inhibitory subunit by blocking actin-myosin interactions and thereby mediating striated muscle relaxation. The TnI subfamily contains 3 genes: TnI-skeletal-fast-twitch, TnI-skeletal-slow-twitch, and TnI-cardiac. The TNNI3 gene encodes the TnI-cardiac protein and isexpressed solely in cardiac muscle tissues. Mutations in the TNNI3 gene cause familial hypertrophic cardiomyopathy type 7 (CMH7) and familial restrictive cardiomyopathy (RCM).

    • Synonyms

      Troponin I cardiac muscle, Cardiac troponin I, TNNI3, TNNC1, CMH7, RCM1, cTnI, CMD2A, MGC116817.

    • Physical Appearance

      Sterile Filtered colorless liquid formulation.

    • 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 MGSMADGSSD AAREPRPAPA PIRRRSSNYR AYATEPHAKK KSKISASRKL QLKTLLLQIA KQELEREAEERRGEKGRALS TRCQPLELAG LGFAELQDLC RQLHARVDKV DEERYDIEAK VTKNITEIAD LTQKIFDLRG KFKRPTLRRV RISADAMMQALLGARAKESL DLRAHLKQVK KEDTEKENRE VGDWRKNIDA LSGMEGRKKK FES

    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.

    Cardiac Troponin I
  • View Data Sheet

    Name :

    CNTF Human

    Description:

    Ciliary-Neurotrophic Factor Human Recombinant

    HCNTF, CNTF, Ciliary Neurotrophic Factor.

    Product # :

    CYT-272

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    Description

    Ciliary Neurotrophic Factor Recombinant Human produced in E.Coli is a single, non-glycosylated polypeptide chain containing 199 amino acids and having a molecular mass of 22706 Dalton. The CNTF is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Lyophilized from a concentrated (1mg/ml) solution in water containing 5mM sodium Phosphate buffer pH=7.5 and 5mM sodium chloride.

    Purity

    Greater than 98.0% as determined by(a) Analysis by RP-HPLC.
    (b) Analysis by SDS-PAGE.

    Biological Activity

    The ED50 as determined by the dose-dependant stimulation of TF-1 cells is < 2 ng/ml, corresponding to a Specific Activity of 500,000IU/mg.

    More Info

    • Introduction

      CNTF is a polypeptide hormone whose actions appear to be restricted to the nervous system where it promotes neurotransmitter synthesis and neurite outgrowth in certain neuronal populations. The protein is a potent survival factor for neurons and oligodendrocytes and may be relevant in reducing tissue destruction during inflammatory attacks. A mutation in this gene, which results in aberrant splicing, leads to ciliary neurotrophic factor deficiency, but this phenotype is not causally related to neurologic disease. In addition to the predominant monocistronic transcript originating from this locus, the gene is also co-transcribed with the upstream ZFP91 gene. Co-transcription from the two loci results in a transcript that contains a complete coding region for the zinc finger protein but lacks a complete coding region for ciliary neurotrophic factor.
      CNTF is a survival factor for various neuronal cell types. Seems to prevent the degeneration of motor axons after axotomy.

    • Synonyms

      HCNTF, CNTF, Ciliary Neurotrophic Factor.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Solubility

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

    • Amino Acid Sequence

      The sequence of the first five N-terminal amino acids was determined and was found to be Met-Ala-Phe-Thr-Glu.

    • Background

      Exploring the Potential of Human Recombinant Ciliary-Neurotrophic Factor: Implications and Applications

      Abstract:

      Ciliary-Neurotrophic Factor (CNTF) holds remarkable promise in neurobiology and therapeutic development due to its neuroprotective and regenerative properties. This paper delves into the significance of Human Recombinant CNTF, its production methodologies, and its potential applications in treating neurodegenerative disorders. The review sheds light on the therapeutic potential of CNTF and its role in advancing neuroregeneration research.

      Introduction:

      CNTF, a neurotrophic cytokine, is known for its pivotal role in neuronal survival and growth. The availability of Human Recombinant CNTF allows researchers to investigate its therapeutic potential and explore avenues for developing novel treatments for neurodegenerative diseases. CNTF's ability to support neuronal health and promote regeneration makes it a promising candidate for medical interventions.

      Mechanisms of Action:

      CNTF interacts with specific receptor complexes, activating various downstream signaling pathways, including Janus kinase (JAK) and Signal Transducer and Activator of Transcription (STAT) pathways. These pathways contribute to cell survival, differentiation, and axonal growth, forming the foundation for CNTF's neuroprotective effects.

      Production Methods:

      Human Recombinant CNTF is produced by introducing the CNTF gene into suitable expression systems, often employing bacterial or mammalian cells. Ensuring proper post-translational modifications is essential for maintaining the protein's biological activity and therapeutic potential.

      Therapeutic Applications:

      CNTF's neuroprotective and regenerative effects offer potential therapeutic applications in neurodegenerative disorders, such as amyotrophic lateral sclerosis (ALS), retinal degeneration, and Parkinson's disease. It holds promise for preserving and restoring neuronal function, thereby improving the quality of life for affected individuals.

      Challenges and Future Directions:

      While Human Recombinant CNTF shows great potential, challenges include precise dosing, delivery methods, and potential side effects. Further research is needed to optimize CNTF-based therapies and assess their long-term safety and efficacy in clinical settings.

      Conclusion:

      Human Recombinant Ciliary-Neurotrophic Factor emerges as a critical tool in advancing our understanding of neuroprotection and neuroregeneration. Its potential in treating neurodegenerative disorders highlights the ongoing quest for innovative therapeutic approaches that harness the body's inherent ability to heal and regenerate.

      What is the molecular weight/Mw of CNTF Protein?
      CNTF Protein has a total Mw of 22kDa.

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

      What is the Purity of CNTF Protein?
      CNTF Protein is >98% pure as determined by SDS-PAGE.

      What is the Biological Activity of CNTF Protein?
      The ED50 as determined by the dose-dependant stimulation of TF-1 cells is < 2 ng/ml, corresponding to a Specific Activity of 500,000IU/mg.

      What is the amino acid sequence of CNTF Protein?
      CNTF Protein is composed from 199 amino acids.

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

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

    • Protein content

      CNTF quantitation was carried out by two independent methods1. UV spectroscopy at 280 nm using the absorbency value of 1.28 as the extinction coefficient for a 0.1% (1mg/ml) solution. This value is calculated by the PC GENE computer analysis program of protein sequences (IntelliGenetics). 2. Analysis by RP-HPLC, using a standard solution of CNTF Recombinant as a Reference Standard.

    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.

    Cntf Human
  • View Data Sheet

    Name :

    CTHRC1 Human, HEK

    Description:

    Collagen Triple Helix Repeat Containing 1 Human Recombinant, HEK

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

    Product # :

    PRO-2028

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    Description

    CTHRC1 Human Recombinant produced in HEK cells is a single, glycosylated, polypeptide chain (Ser31-Lys243) containing a total of 219 amino acids, having a calculated molecular mass of 23.9kDa and fused to a 6 aa His tag at C-Terminus.

    Source

    HEK 293.

    Formulation

    CTHRC1 was filtered (0.4µm) and lyophilized in phosphate buffered saline pH 7.5.

    Purity

    Greater than 95.0% 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

      Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Solubility

      It is recommended to add deionized water to prepare a working stock solution of approximately 0.5 mg/ml and let the lyophilized pellet dissolve completely. CTHRC1 is not sterile! Please filter the product by an appropriate sterile filter before using it in the cell culture.

    • Amino Acid Sequence

      SEIPKGKQKA QLRQREVVDL YNGMCLQGPA GVPGRDGSPG ANGIPGTPGI PGRDGFKGEK GECLRESFEE SWTPNYKQCS WSSLNYGIDL GKIAECTFTK MRSNSALRVL FSGSLRLKCR NACCQRWYFT FNGAECSGPL PIEAIIYLDQ GSPEMNSTIN IHRTSSVEGL CEGIGAGLVD VAIWVGTCSD YPKGDASTGW NSVSRIIIEE LPK HHHHHH.

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    Cthrc1 Human Hek
  • View Data Sheet

    Name :

    CUEDC1 Human

    Description:

    CUE Domain Containing 1 Human Recombinant

    CUE Domain Containing 1, CUE Domain-Containing Protein 1.

    Product # :

    PRO-1822

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    Description

    CUEDC1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 409 amino acids (1-386 a.a) and having a molecular mass of 44.6kDa.CUEDC1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    CUEDC1 protein solution (0.25mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 20% glycerol and 1mM DTT.

    Purity

    Greater than 85% as determined by SDS-PAGE.

    More Info

    • Introduction

      CUE Domain Containing 1, also know as CUEDC1 contains 1 CUE domain. The CUE domain is structurally associated to the ubiquitin-binding UBA domain and exists as a domain-swapped dimer which makes additional contacts with ubiquitin, and as a result, binds ubiquitin with higher affinity. The CUE domain is discovered in proteins with diverse functions including protein sorting and degradation of misfolded proteins in the endoplasmic reticulum.

    • Synonyms

      CUE Domain Containing 1, CUE Domain-Containing Protein 1.

    • Physical Appearance

      Sterile Filtered clear solution.

    • Stability

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

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MGSMTSLFRR SSSGSGGGGT AGARGGGGGT AAPQELNNSR PARQVRRLEF NQAMDDFKTM FPNMDYDIIE CVLRANSGAV DATIDQLLQM NLEGGGSSGG VYEDSSDSED SIPPEILERT LEPDSSDEEP PPVYSPPAYH MHVFDRPYPL APPTPPPRID ALGSGAPTSQ RRYRNWNPPL LGNLPDDFLR ILPQQLDSIQ GNAGGPKPGS GEGCPPAMAG PGPGDQESRW KQYLEDERIA LFLQNEEFMK ELQRNRDFLL ALERDRLKYE SQKSKSSSVA VGNDFGFSSP VPGTGDANPA VSEDALFRDK LKHMGKSTRR KLFELARAFS EKTKMRKSKR KHLLKHQSLG AAASTANLLD DVEGHACDED FRGRRQEAPK VEEGLREGQ

    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.

    Cuedc1 Human
  • View Data Sheet

    Name :

    Tetanus antibody

    Description:

    Tetanus toxoid scFv Recombinant antibody

    Product # :

    ANT-195

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    Description

    Tetanus toxin is the neurotoxin produced by the vegetative spore of Clostridium tetani in anaerobic conditions, causing tetanus.Recombinant Anti Tetanus produced in E.Coli is a non-glycosylated, polypeptide chain containing a hexahistidine tag and having a molecular weight of 37 kDa.Tetanus Antibody is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Tetanus is supplied in 1x PBS (pH 7.4) and 0.09% azide

    Purity

    Greater than 95.0% as determined byAnalysis by RP-HPLC.
    Analysis by SDS-PAGE.

    More Info

    • Physical Appearance

      Sterile Filtered clear solution.

    • Stability

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

    • Type

      Antibody Recombinant.

    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.

    Tetanus Antibody
  • View Data Sheet

    Name :

    POMC Human

    Description:

    Proopiomelanocortin Human Recombinant

    Pro-opiomelanocortin, POMC, LPH, MSH, NPP, POC, ACTH, CLIP.

    Product # :

    PRO-236

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    Description

    POMC produced in E.Coli is a single, non-glycosylated polypeptide chain containing 262 amino acids (27-267 a.a) and having a molecular mass of 28.9kDa (molecular weight on SDS-PAGE will appear higher).POMC is fused to a 21 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    POMC protein solution (0.25mg/ml) containing 20mM Tris-HCl buffer (pH 8.5), 1mM DTT, 50% glycerol, 0.1mM PMSF, 0.1M Imidazole and 0.2M NaCl.

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Pro-opiomelanocortin preproprotein (POMC) is a polypeptide hormone precursor which experiences extensive, tissue-specific, post-translational processing via cleavage by subtilisin-like enzymes known as prohormone convertases. POMC regulates the corticosteroid production in the adrenal cortex. Furthermore, POMC is cleaved into ten hormone chains named NPP, g-MSH, ACTH, a-MSH, CLIP, Lipotropin b, Lipotropin g, b-MSH,b endorphin and Met-enkephalin. POMC gene defects are the cause of POMC deficiency, which is characterized by red hair and adrenal insufficiency.

    • Synonyms

      Pro-opiomelanocortin, POMC, LPH, MSH, NPP, POC, ACTH, CLIP.

    • 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 MWCLESSQCQ DLTTESNLLE CIRACKPDLS AETPMFPGNG DEQPLTENPR KYVMGHFRWD RFGRRNSSSS GSSGAGQKRE DVSAGEDCGP LPEGGPEPRS DGAKPGPREG KRSYSMEHFR WGKPVGKKRR PVKVYPNGAE DESAEAFPLE FKRELTGQRL
      REGDGPDGPA DDGAGAQADL EHSLLVAAEK KDEGPYRMEH FRWGSPPKDK RYGGFMTSEK SQTPLVTLFK NAIIKNAYKK GE.

    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.

    Pomc Human
  • View Data Sheet

    Name :

    TPM3 Human

    Description:

    Tropomyosin-3 Human Recombinant

    Tropomyosin alpha-3 chain, Gamma-tropomyosin, Tropomyosin-3, Tropomyosin-5, hTM5, TPM3, TM3, TM5, TRK, CFTD, NEM1, TM-5, TM30, TM30nm, TPMsk3, hscp30, OK/SW-cl.5.

    Product # :

    PRO-1020

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    Description

    TPM3 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 272 amino acids (1-248 a.a.) and having a molecular mass of 31.6kDa. TPM3 is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    TPM3 protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 1mM DTT, 10% glycerol, 0.1M NaCl.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    More Info

    • Introduction

      Tropomyosin alpha-3 chain (TPM3) belongs to the tropomyosin family of actin-binding proteins involved in the contractile system of striated and smooth muscles and the cytoskeleton of non-muscle cells. Tropomyosins are dimers of coiled-coil proteins which polymerize end-to-end along the major groove in most actin filaments. Tropomyosins give stability to the filaments and regulate access of other actin-binding proteins. In muscle cells, tropomyosins regulate muscle contraction by controlling the binding of myosin heads to the actin filament. Mutations in the TPM3 gene cause autosomal dominant nemaline myopathy, and oncogenes formed by chromosomal translocations involving this locus are linked with cancer.

    • Synonyms

      Tropomyosin alpha-3 chain, Gamma-tropomyosin, Tropomyosin-3, Tropomyosin-5, hTM5, TPM3, TM3, TM5, TRK, CFTD, NEM1, TM-5, TM30, TM30nm, TPMsk3, hscp30, OK/SW-cl.5.

    • 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 MGSHMAGITT IEAVKRKIQV LQQQADDAEE RAERLQREVE GERRAREQAE AEVASLNRRI QLVEEELDRA QERLATALQK LEEAEKAADE SERGMKVIEN RALKDEEKME LQEIQLKEAK HIAEEADRKY EEVARKLVII EGDLERTEER AELAESRCRE MDEQIRLMDQ NLKCLSAAEE KYSQKEDKYE EEIKILTDKL KEAETRAEFA ERSVAKLEKT IDDLEDKLKC TKEEHLCTQR MLDQTLLDLN EM.

    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.

    Tpm3 Human
  • View Data Sheet

    Name :

    CRYGC Human

    Description:

    Crystallin, Gamma C Human Recombinant

    Crystallin, gamma C, Gamma-crystallin 2-1, Gamma-crystallin 3, CRYG3, CCL.

    Product # :

    PRO-1095

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    Description

    CRYGC Human Recombinant produced in E. coli is a single polypeptide chain containing 198 amino acids (1-174) and having a molecular mass of 23.5kDa.CRYGC is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    The CRYGC solution (1mg/1ml) contains 20mM Tris-HCl buffer (pH 8.0), 200mM NaCl, 2mM DTT and 10% glycerol.

    Purity

    Greater than 95% as determined by SDS-PAGE.

    More Info

    • Introduction

      CRYGC is a member of the beta/gamma-crystallin family. Mammalian lens crystallins are distributed into alpha, beta, and gamma families; beta and gamma crystallins are also considered as a superfamily. Gamma-crystallins are a homogeneous group of extremely symmetrical, monomeric proteins usually missing connecting peptides and terminal extensions and are differentially regulated after early development. Three pseudogenes (gamma-E,F,G) and four gamma-crystallin genes (gamma-A,B,C,D) are structured in a genomic sector as a gene cluster. Gamma-crystallins are involved in cataract formation as a result of aging or mutations in specific genes. Mutations in CRYGC result in cataract Coppock-like (CCL) and cataract autosomal dominant (ADC).

    • Synonyms

      Crystallin, gamma C, Gamma-crystallin 2-1, Gamma-crystallin 3, CRYG3, CCL.

    • 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 MGSHMGKITF YEDRAFQGRS YETTTDCPNL QPYFSRCNSI RVESGCWMLY ERPNYQGQQY LLRRGEYPDY QQWMGLSDSI RSCCLIPQTV SHRLRLYERE DHKGLMMELS EDCPSIQDRF HLSEIRSLHV LEGCWVLYEL PNYRGRQYLL RPQEYRRCQD WGAMDAKAGS LRRVVDLY

    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.

    Crygc Human
  • View Data Sheet

    Name :

    CTNNBIP1 Human

    Description:

    Catenin, Beta Interacting Protein 1 Human Recombinant

    ICAT, MGC15093, CNBP1, CTNNBIP1, Beta-catenin-interacting protein 1, Inhibitor of beta-catenin and Tcf-4.

    Product # :

    PRO-850

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    Description

    CTNNBIP1 Recombinant E.coli produced in E.Coli is a single, non-glycosylated polypeptide chain containing 101 amino acids (1-81 a.a.) and having a molecular mass of 11.3 kDa. The CTNNBIP1 is fused to a 20 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    CTNNBIP1 Human solution containing 20mM Tris-HCl pH-7.5, 2mM DTT, 0.1M NaCl & 20% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      CTNNBIP1 binds CTNNB1 and avoids interaction between CTNNB1 and TCF (T-cell transcription factor) family members. CTNNBIP1 is a negative regulator of the Wnt signaling pathway.

    • Synonyms

      ICAT, MGC15093, CNBP1, CTNNBIP1, Beta-catenin-interacting protein 1, Inhibitor of beta-catenin and Tcf-4.

    • Physical Appearance

      Sterile filtered colorless solution.

    • Stability

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

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MNREGAPGKS PEEMYIQQKV RVLLMLRKMG SNLTASEEEF LRTYAGVVNS QLSQLPPHSI DQGAEDVVMA FSRSETEDRR Q.

    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.

    Ctnnbip1 Human
  • View Data Sheet

    Name :

    CUEDC2 Human

    Description:

    CUE Domain Containing 2 Human Recombinant

    CUE domain-containing protein 2, CUEDC2, C10orf66, HOYS6, bA18I14.5.

    Product # :

    PRO-1680

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    Description

    CUEDC2 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 310 amino acids (1-287) and having a molecular mass of 34 kDa.CUEDC2 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The CUEDC2 solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 20% glycerol and 1mM DTT.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      CUE Domain Containing 2 also known as CUEDC2 is a part of the CUEDC2 family and contains 1 CUE domain. CUEDC2 down-regulates ESR1 protein levels through the ubiquitination-proteasome pathway and controls PGR protein levels through a parallel mechanism.

    • Synonyms

      CUE domain-containing protein 2, CUEDC2, C10orf66, HOYS6, bA18I14.5.

    • 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 MGSMELERIV SAALLAFVQT HLPEADLSGL DEVIFSYVLG VLEDLGPSGP SEENFDMEAF TEMMEAYVPG FAHIPRGTIG DMMQKLSGQL SDARNKENLQ PQSSGVQGQV PISPEPLQRP EMLKEETRSS AAAAADTQDE ATGAEEELLP GVDVLLEVFP TCSVEQAQWV LAKARGDLEE AVQMLVEGKE EGPAAWEGPN QDLPRRLRGP QKDELKSFIL QKYMMVDSAE DQKIHRPMAP KEAPKKLIRY IDNQVVSTKG ERFKDVRNPE AEEMKATYIN LKPARKYRFH.

    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.

    Cuedc2 Human
  • View Data Sheet

    Name :

    SEPSECS Human

    Description:

    Selenocysteinyl-tRNA(Sec) synthase Human Recombinant

    SLA, SLA/LP autoantigen, SLA-p35, Selenocysteinyl-tRNA(Sec) synthase, Selenocysteine synthase, Liver-pancreas antigen, Soluble liver antigen, Sec synthase, UGA suppressor tRNA-associated protein.

    Product # :

    ENZ-033

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    Description

    SEPSECS produced in E.Coli is a single, non-glycosylated polypeptide chain containing 521 amino acids (1-501a.a.) and having a molecular mass of 57.9kDa.SEPSECS is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The SEPSECS protein solution (0.5mg/1ml) is formulated in 20mM Tris-HCl buffer (pH8.0) 1mM DTT, 100mM NaCl and 10% glycerol.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    More Info

    • Introduction

      SEPSECS catalyzes the last step of sec synthesis by way of converting O-phosphoseryl-tRNA(sec) to selenocysteinyl-tRNA(sec) using selenophosphate as the selenium donor. Furthermore, SEPSECS protein is considered a specific marker of autoimmune hepatitis.

    • Synonyms

      SLA, SLA/LP autoantigen, SLA-p35, Selenocysteinyl-tRNA(Sec) synthase, Selenocysteine synthase, Liver-pancreas antigen, Soluble liver antigen, Sec synthase, UGA suppressor tRNA-associated protein.

    • 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 MNRESFAAGE RLVSPAYVRQ GCEARRSHEH LIRLLLEKGK CPENGWDEST LELFLHELAI MDSNNFLGNC GVGEREGRVA SALVARRHYR FIHGIGRSGD ISAVQPKAAG SSLLNKITNS LVLDIIKLAG VHTVANCFVV PMATGMSLTL CFLTLRHKRP KAKYIIWPRI DQKSCFKSMI TAGFEPVVIE NVLEGDELRT DLKAVEAKVQ ELGPDCILCI HSTTSCFAPR VPDRLEELAV ICANYDIPHI VNNAYGVQSS KCMHLIQQGA RVGRIDAFVQ SLDKNFMVPV GGAIIAGFND SFIQEISKMY PGRASASPSL DVLITLLSLG SNGYKKLLKE RKEMFSYLSN QIKKLSEAYN ERLLHTPHNP ISLAMTLKTL DEHRDKAVTQ LGSMLFTRQV SGARVVPLGS MQTVSGYTFR GFMSHTNNYP CAYLNAASAI GMKMQDVDLF IKRLDRCLKA VRKERSKESD DNYDKTEDVD IEEMALKLDN VLLDTYQDAS S.

    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.

    Sepsecs Human
  • View Data Sheet

    Name :

    THTPA Human

    Description:

    Thiamine Triphosphatase Human Recombinant

    MGC2652, THTP, THTPASE.

    Product # :

    ENZ-249

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    Description

    Recombinant Human THTPA produced in E.Coli is a single, non-glycosylated polypeptide chain containing 250 amino acids (1-230 a.a.) and having a molecular mass of 27.7 kDa. THTPA is fused to a 20 amino acid His-Tag at N-Terminus and purified by conventional chromatography techniques.

    Source

    Escherichia Coli.

    Formulation

    The THTPA 1mg/ml protein solution contains 20mM Tris-HCL buffer, pH-8, 1mM DTT and 10% Glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      THTPA enzyme is part of the THTPase family. THTPA is localized to the cytoplasm and expressed at small quantities in a variety of tissues, including testis, uterus, prostate, bladder, lung and kidney. THTPA is a hydrolase that catalyzes the H2O-dependent hydrolysis of thiamine triphosphate (THTP) to thiamine diphosphate (THDP), the main form of thiamine within the cell. THTPA occurs as a monomer and is activated at an optimal pH of 8.5.

    • Synonyms

      MGC2652, THTP, THTPASE.

    • Physical Appearance

      Sterile filtered colorless solution.

    • Stability

      Store THTPA 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 MAQGLIEVER KFLPGPGTEE RLQELGGTLE YRVTFRDTYY DTPELSLMQA DHWLRRREDS GWELKCPGAA GVLGPHTEYK ELTAEPTIVA QLCKVLRADG LGAGDVAAVL GPLGLQEVAS FVTKRSAWKL VLLGADEEEP QLRVDLDTAD FGYAVGEVEA LVHEEAEVPT ALEKIHRLSS MLGVPAQETA PAKLIVYLQR FRPQDYQRLL EVNSSRERPQ ETEDPDHCLG.

    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.

    Thtpa Human
  • View Data Sheet

    Name :

    CD207 Human

    Description:

    CD207 Human Recombinant

    C-type lectin domain family 4 member K, CLEC4K, Langerin, CD207.

    Product # :

    PRO-2204

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    Description

    CD207 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 287 amino acids (65-328 a.a) and having a molecular mass of 32.2kDa.CD207 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    CD207 protein solution (1mg/ml) containing 20mM Tris 8.0 and 10% glycerol.

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      CD207 (C-type lectin domain family 4 member K) is expressed in Langerhans cells which are immature dendritic cells of the epidermis and mucosa. Moreover, CD207 is expressed in several other dendritic cell types including dermal CD103+ DCs and splenic CD8+ DCs. Langerin is localized in the Birbeck granules, the organelles present in the cytoplasm of Langerhans cells and comprised of superimposed and zippered membranes. CD207 is a C-type lectin with mannose binding specificity, and it has been suggested that mannose binding by the CD207 protein leads to internalization of antigen into Birbeck granules thus providing access to a nonclassical antigen-processing pathway.

    • Synonyms

      C-type lectin domain family 4 member K, CLEC4K, Langerin, CD207.

    • 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 MGSPRFMGTI SDVKTNVQLL KGRVDNISTL DSEIKKNSDG MEAAGVQIQM VNESLGYVRS QFLKLKTSVE KANAQIQILT RSWEEVSTLN AQIPELKSDL EKASALNTKI RALQGSLENM SKLLKRQNDI LQVVSQGWKY FKGNFYYFSL IPKTWYSAEQ FCVSRNSHLT SVTSESEQEF LYKTAGGLIY WIGLTKAGME GDWSWVDDTP FNKVQSARFW IPGEPNNAGN NEHCGNIKAP SLQAWNDAPC DKTFLFICKR PYVPSEP.

    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.

    Cd207 Human
  • View Data Sheet

    Name :

    LCN1 Human

    Description:

    Lipocalin-1 Human Recombinant

    Lipocalin-1, PMFA, TLC, TP, VEGP, Tear lipocalin, Tear prealbumin, Von Ebner gland protein, VEG protein.

    Product # :

    ENZ-825

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    Description

    LCN1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 183 amino acids (19-176 a.a) and having a molecular mass of 20.1kDa. LCN1 is fused to a 25 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    LCN1 protein solution (1mg/ml) containing Phosphate buffered saline (pH7.4), 10% glycerol and 1mM DTT.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Lipocalin-1 (LCN1) belongs to the lipocalin family of small secretory proteins. Lipocalins are extracellular transport proteins, which bind to various hydrophobic ligands. LCN1 protein is the principal lipid binding protein in tears and is overproduced in response to numerous stimuli including infection and stress. LCN1 is a marker for chromosome aneuploidy as well as an autoantigen in Sjogren's syndrome.

    • Synonyms

      Lipocalin-1, PMFA, TLC, TP, VEGP, Tear lipocalin, Tear prealbumin, Von Ebner gland protein, VEG protein.

    • 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 MGSHMHHLLA SDEEIQDVSG TWYLKAMTVD REFPEMNLES VTPMTLTTLE GGNLEAKVTM LISGRCQEVK AVLEKTDEPG KYTADGGKHV AYIIRSHVKD HYIFYCEGEL HGKPVRGVKL VGRDPKNNLE ALEDFEKAAG ARGLSTESIL IPRQSETCSP GSD.

    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.

    Lcn1 Human
  • View Data Sheet

    Name :

    TSSK6 Human

    Description:

    Testis Specific Serine Kinase 6 Human Recombinant

    TSSK6, Testis-Specific Serine Kinase 6, Cancer/Testis Antigen 72, SSTK, Small Serine/Threonine Kinase, CT72, TSK-6, TSSK4, Serine/Threonine Protein Kinase SSTK, Testis-Specific Serine/Threonine-Protein Kinase 6, EC 2.7.11.1, TSSK-6, Serine/Threonine-Protein Kinase SSTK, Testis-Specific Kinase 6.

    Product # :

    PKA-220

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    • More Info

    Description

    TSSK6 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 296 amino acids (1-273) and having a molecular mass of 32.7kDa.TSSK6 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The TSSK6 solution (1mg/ml) contains 20mM Tris-HCl buffer (pH8.0), 10% glycerol and 0.4M Urea.

    Purity

    Greater than 80.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Testis-specific serine/threonine-protein kinase 6 (TSSK6) is an intronless gene, which belongs to the CAMK Ser/Thr protein kinase family. The TSSK6 protein contains one protein kinase domain. TSSK6 is highly expressed in the testis and lowly expressed in the colon, prostate, thymus, small intestine, and peripheral blood leukocytes. TSSK6 interacts with the heatshock proteins HSPA8, HSPCB, and HAPA1A; these interactions seem to be essential for TSSK6 kinase activity. TSSK6 plays a role in DNA condensation during postmeiotic chromatin remodeling. In addition, TSSK6 is required for sperm production and function.

    • Synonyms

      TSSK6, Testis-Specific Serine Kinase 6, Cancer/Testis Antigen 72, SSTK, Small Serine/Threonine Kinase, CT72, TSK-6, TSSK4, Serine/Threonine Protein Kinase SSTK, Testis-Specific Serine/Threonine-Protein Kinase 6, EC 2.7.11.1, TSSK-6, Serine/Threonine-Protein Kinase SSTK, Testis-Specific Kinase 6.

    • Physical Appearance

      Sterile Filtered colorless solution.

    • Stability

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

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MGSMSGDKLL SELGYKLGRT IGEGSYSKVK VATSKKYKGT VAIKVVDRRR APPDFVNKFL PRELSILRGV RHPHIVHVFE FIEVCNGKLY IVMEAAATDL LQAVQRNGRI PGVQARDLFA QIAGAVRYLH DHHLVHRDLK CENVLLSPDE RRVKLTDFGF GRQAHGYPDL STTYCGSAAY ASPEVLLGIP YDPKKYDVWS MGVVLYVMVT GCMPFDDSDI AGLPRRQKRG VLYPEGLELS ERCKALIAEL LQFSPSARPS AGQVARNCWL RAGDSG.

    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.

    Tssk6 Human
  • View Data Sheet

    Name :

    TXN1 Human, His

    Description:

    Thioredoxin Human Recombinant, His Tag

    Thioredoxin, ATL-derived factor, ADF, Surface-associated sulphydryl protein, SASP, TXN, TRDX, TRX, TRX1, MGC61975, DKFZp686B1993.

    Product # :

    PRO-804

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    Quantity :

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    More Info

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

    Description

    Thioredoxin Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 125 amino acids (1-105 a.a.) and having a molecular mass of 13.9 kDa (Molecular weight on SDS-PAGE will appear higher). TXN protein is fused to a 20 amino acid His-Tag at N-terminus and purified by standard chromatography.

    Source

    Escherichia Coli.

    Formulation

    TXN1 solution containing 1x PBS pH 7.4.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Biological Activity

    Specific activity is 7-10 A650/min/mg, obtained by measuring the increase of insulin precipitation in absorbance at 650 nm resulting from the reduction of insulin.

    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. 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. Trx also provides control over a number of transcription factors affecting cell proliferation and death through a mechanism referred to as redox regulation.

    • Synonyms

      Thioredoxin, ATL-derived factor, ADF, Surface-associated sulphydryl protein, SASP, TXN, TRDX, TRX, TRX1, MGC61975, DKFZp686B1993.

    • 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 MVKQIESKTA FQEALDAAGD KLVVVDFSAT WCGPCKMIKP FFHSLSEKYS NVIFLEVDVD DCQDVASECE VKCMPTFQFF KKGQKVGEFS GANKEKLEAT INELV.

    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.

    Txn1 Human His
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