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Search results

1000 results found for “transforming growth factor”

Name

Description

Product #

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  • View Data Sheet

    Name :

    ING1 Human

    Description:

    Inhibitor of Growth Family, Member 1 Human Recombinant

    Inhibitor Of Growth Family, Member 1, Growth Inhibitory Protein ING1, Tumor Suppressor ING1, Growth Inhibitor ING1, Inhibitor Of Growth Protein 1, Inhibitor Of Growth 1, P24ING1c,P33ING1b, P47ING1a, P33ING1, P33, P47, ING1 .

    Product # :

    PRO-2130

    Price :

    Quantity :

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    • source
    • formulation
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    • More Info

    Description

    ING1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 302 amino acids (1-279 a.a) and having a molecular mass of 34.3kDa.ING1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    ING1 protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH 8.0) and 10% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Inhibitor of Growth Family Member 1, also known as ING1 is a tumor suppressor protein which is able to induce cell growth arrest and apoptosis. ING1 is a nuclear protein which physically act together with the tumor suppressor protein TP53 and is a component of the p53 signaling pathway. In addition, Reduced expression and rearrangement of ING1 have been identified in various cancers. Multiple alternatively spliced transcript variants encoding distinct isoforms have been described for ING1.

    • Synonyms

      Inhibitor Of Growth Family, Member 1, Growth Inhibitory Protein ING1, Tumor Suppressor ING1, Growth Inhibitor ING1, Inhibitor Of Growth Protein 1, Inhibitor Of Growth 1, P24ING1c,P33ING1b, P47ING1a, P33ING1, P33, P47, ING1 .

    • 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 MGSMLSPANG EQLHLVNYVE DYLDSIESLP FDLQRNVSLM REIDAKYQEI LKELDECYER FSRETDGAQK RRMLHCVQRA LIRSQELGDE KIQIVSQMVE LVENRTRQVD SHVELFEAQQ ELGDTAGNSG KAGADRPKGE AAAQADKPNS KRSRRQRNNE NRENASSNHD HDDGASGTPK EKKAKTSKKK KRSKAKAERE ASPADLPIDP NEPTYCLCNQ VSYGEMIGCD NDECPIEWFH FSCVGLNHKP KGKWYCPKCR GENEKTMDKA LEKSKKERAY NR.

    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.

    Ing1 Human
  • View Data Sheet

    Name :

    MLLT11 Human

    Description:

    Myeloid/Lymphoid Leukemia Translocated To 11 Human Recombinant

    AF1Q, RP11-316M1.10, Protein AF1q, MLLT11.

    Product # :

    PRO-1991

    Price :

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    Description

    MLLT11 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 113 amino acids (1-90 a.a) and having a molecular mass of 12.4kDa. MLLT11 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    MLLT11 protein solution (0.25mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.4M Urea and 10% glycerol.

    Purity

    Greater than 80.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Myeloid/Lymphoid Leukemia Translocated To 11 (MLLT11) is a part of the Mixed-Lineage Leukemia protein family. MLLT11 which takes part in leukemogenesis and in the progression of severe monocytic leukemia (AML) is located on chromosome 11q23. MLLT11 which is also expressed in embryonic brain cortex is upregulated during neuronal differentiation and is taking part in the evolution of the central nervous system.

    • Synonyms

      AF1Q, RP11-316M1.10, Protein AF1q, MLLT11.

    • 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 MGSMRDPVSS QYSSFLFWRM PIPELDLSEL EGLGLSDTAT YKVKDSSVGK MIGQATAADQ EKNPEGDGLL EYSTFNFWRA PIASIHSFEL DLL.

    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.

    Mllt11 Human
  • View Data Sheet

    Name :

    CDNF Rat

    Description:

    CDNF Rat Recombinant

    Cerebral neurotrophic factor, ARMET-like protein 1, Arginine-rich protein mutated in early stage tumors-like 1, Conserved neurotrophic factor, Cdnf, Armetl1.

    Product # :

    CYT-730

    Price :

    Quantity :

    Shipping Method :

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    More Info

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

    Description

    CDNF Rat Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 163 amino acids and having a molecular mass of 18.8kDa.The CDNF is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    CDNF protein was lyophilized from a 0.2µm filtered concentrated solution in 1xPBS, pH 7.4.

    Purity

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

    Biological Activity

    CDNF Rat is able to enhance neurite outgrowth of E16-E18 rat embryonic cortical neurons when immobilized at 5-25 µg/mL on a nitrocellulose-coated microplate.

    More Info

    • Introduction

      CDNF is a member of the ARMET family and acts as a trophic factor for neurons. CDNF inhibits the 6-hydroxy (6-OHDA)-induced degeneration of neurons. When CDNF controlled after 6-OHDA-lesioning, it reestablishes the function and inhibits the degeneration of neurons in substantia nigra. CDNF is universally expressed in neuronal and non-neuronal tissues. The highest levels in the brain are found in the optic nerve and corpus callosum.

    • Synonyms

      Cerebral neurotrophic factor, ARMET-like protein 1, Arginine-rich protein mutated in early stage tumors-like 1, Conserved neurotrophic factor, Cdnf, Armetl1.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Amino Acid Sequence

      QGLEAGVRSR ADCEVCKEFL NRFYNSLLTR GIDFSVDTIE EELISFCADT KGKENRLCYY LGATKDSATK ILGEVTRPMS VHMPTVKICE KLKKMDSQIC ELKYEKKLDL ESVDLWKMRV AELKQILHSW GEECRACAEK HDYVNLIKEL APKYVETRPQ TEL.

    • Background

      What is the molecular weight/Mw of CDNF Protein?
      CDNF Protein has a total Mw of 18.8kDa.

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

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

      What is the Biological Activity of CDNF Protein?
      CDNF Rat is able to enhance neurite outgrowth of E16-E18 rat embryonic cortical neurons when immobilized at 5-25 µg/mL on a nitrocellulose-coated microplate.

      What is the amino acid sequence of CDNF Protein?
      QGLEAGVRSR ADCEVCKEFL NRFYNSLLTR GIDFSVDTIE EELISFCADT KGKENRLCYY LGATKDSATK ILGEVTRPMS VHMPTVKICE KLKKMDSQIC ELKYEKKLDL ESVDLWKMRV AELKQILHSW GEECRACAEK HDYVNLIKEL APKYVETRPQ TEL.

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

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

    Cdnf Rat
  • View Data Sheet

    Name :

    TBPL1 Human

    Description:

    TBP-Like 1 Human Recombinant

    TATA box-binding protein-like protein 1, TBP-like protein 1, 21 kDa TBP-like protein, Second TBP of unique DNA protein, STUD, TATA box-binding protein-related factor 2, TBP-related factor 2, TBP-like factor, TBP-related protein, TBPL1, TLF, TLP, TLP21, TRF2, TRP, MGC:8389, MGC:9620.

    Product # :

    PRO-736

    Price :

    Quantity :

    Shipping Method :

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    • description
    • source
    • formulation
    • purity
    • More Info

    Description

    TBPL1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 209 amino acids (1-186 a.a) and having a molecular mass of 23.3kDa.TBPL1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    TBPL1 protein solution (0.25mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.2M NaCl, 50% glycerol, 2mM DTT and 1mM EDTA.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      TBP-Like 1 (TBPL1) is a member of the TBP family. The TATA box-binding protein (TBP) is an indispensable component of the basal transcriptional machinery. TBPL1 is crucial for spermiogenesis and supposed to be significant in expression of developmentally regulated genes.

    • Synonyms

      TATA box-binding protein-like protein 1, TBP-like protein 1, 21 kDa TBP-like protein, Second TBP of unique DNA protein, STUD, TATA box-binding protein-related factor 2, TBP-related factor 2, TBP-like factor, TBP-related protein, TBPL1, TLF, TLP, TLP21, TRF2, TRP, MGC:8389, MGC:9620.

    • 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 MGSMDADSDV ALDILITNVV CVFRTRCHLN LRKIALEGAN VIYKRDVGKV LMKLRKPRIT ATIWSSGKII CTGATSEEEA KFGARRLARS LQKLGFQVIF TDFKVVNVLA VCNMPFEIRL PEFTKNNRPH ASYEPELHPA VCYRIKSLRA TLQIFSTGSI TVTGPNVKAV ATAVEQIYPF VFESRKEIL.

    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.

    Tbpl1 Human
  • View Data Sheet

    Name :

    Activin-A Human Plant-Active

    Description:

    Activin-A Human Recombinant, Plant-Active

    Inhba, Inhibin beta A, FSH releasing protein.

    Product # :

    CYT-414

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    Description

    Active form Activin-A Human Recombinant produced in Plant is a homodimeric, glycosylated, polypeptide chain containing 2 x 116 amino acids and having a molecular weight of 27.4kDa.The Active form Activin-A is fused to a 6-His tag at N-terminus and purified by standard chromatographic techniques.

    Source

    Nicotiana benthamiana.

    Formulation

    Active form Activin-A was lyophilized from a concentrated 1mg/ml protein solution containing 50mM Tris-HCl pH-7.4

    Purity

    Greater than 98% as obsereved by SDS-PAGE.

    Biological Activity

    The biological activity of INHBA is measured by its ability to inhibit mouse plasmacytoma cell line (MPC-11) cells proliferation ([3H]thymidine incorporation). ED50<5ng/ml.

    More Info

    • Introduction

      Activins are homodimers or heterodimers of the different β subunit isoforms, part of the TGFβ family. Mature Activin A has two 116 amino acids residues βA subunits (βA-βA). Activin displays an extensive variety of biological activities, including mesoderm induction, neural cell differentiation, bone remodelling, haematopoiesis, and reproductive physiology. Activins takes part in the production and regulation of hormones such as FSH, LH, GnRH and ACTH. Cells that are identified to express Activin A include fibroblasts, endothelial cells, hepatocytes, vascular smooth muscle cells, macrophages, keratinocytes, osteoclasts, bone marrow monocytes, prostatic epithelium, neurons, chondrocytes, osteoblasts, Leydig cells, Sertoli cells, and ovarian granulosa cells.

    • Synonyms

      Inhba, Inhibin beta A, FSH releasing protein.

    • Physical Appearance

      Lyophilized freeze dried powder.

    • Stability

      For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA). Repeated freezing and thawing is not recommended.

    • Solubility

      INHBA protein should be reconstituted in distilled water to a concentration of 50 ug /ml. Due to the protein nature, dimmers and multimers may be observed.

    • Amino Acid Sequence

      HHHHHHGLECDGKVNICCKKQFFVSFKDIGWNDWIIAPSG
      YHANYCEGECPSHIAGTSGSSLSFHSTVINHYRMRGHSPFA
      NLKSCCVPTKLRPMSMLYYDDGQNIIKKDIQNMIVEECGCS.

    • Background

      What is the molecular weight / Mw of Activin A Protein?
      Activin A Protein has a total Mw of 27.4 kDa.

      What is the source or expression system of Activin A Protein?
      Nicotiana benthamiana.

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

      What is the Biological Activity of Activin A Protein?
      The biological activity of INHBA is measured by its ability to inhibit mouse plasmacytoma cell line (MPC-11) cells proliferation ([3H]thymidine incorporation). ED50<5ng/ml.

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

      What is the amino acid sequence of ACTIVIN A Protein?HHHHHHGLECDGKVNICCKKQFFVSFKDIGWNDWIIAPSGYHANYCEGECPSHIAGTSGSSLSFHSTVINHYRMRGHSPFANLKSCCVPTKLRPMSMLYYDDGQNIIKKDIQNMIVEECGCS

      What applications can ACTIVIN-A Protein be used in?

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

       

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    Activin A Active
  • View Data Sheet

    Name :

    LZTFL1 Human

    Description:

    Leucine Zipper Transcription Factor-Like 1 Human Recombinant

    Leucine Zipper Transcription Factor-Like 1, BBS17, Leucine Zipper Transcription Factor-Like Protein 1, Leucine zipper transcription factor-like protein 1.

    Product # :

    PRO-2157

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    Description

    LZTFL1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 322 amino acids (1-299 a.a) and having a molecular mass of 37.0kDa. LZTFL1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    LZTFL1 protein solution (1mg/ml) containing PBS buffer (pH 7.4), 10% glycerol and 1mM DTT.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    More Info

    • Introduction

      Leucine Zipper Transcription Factor-Like 1, also known as LZTFL1 is a ubiquitously expressed protein which localizes to the cytoplasm. LZTFL1 interacts with Bardet-Biedl Syndrome proteins (BBS) and during its interaction with BBS protein complexes, regulates protein trafficking to the ciliary membrane. Nonsense mutations in LZTFL1 cause a form of Bardet-Biedl Syndrome; a ciliopathy characterized partly by polydactyly, obesity, cognitive impairment, hypogonadism, and kidney failure. LZTFL1 also acts as a tumor suppressor; possibly by interacting with E-cadherin as well as the actin cytoskeleton and in this manner regulating the transition of epithelial cells to mesenchymal cells.

    • Synonyms

      Leucine Zipper Transcription Factor-Like 1, BBS17, Leucine Zipper Transcription Factor-Like Protein 1, Leucine zipper transcription factor-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 MGSMAELGLN EHHQNEVINY MRFARSKRGL RLKTVDSCFQ DLKESRLVED TFTIDEVSEV LNGLQAVVHS EVESELINTA YTNVLLLRQL FAQAEKWYLK LQTDISELEN RELLEQVAEF EKAEITSSNK KPILDVTKPK LAPLNEGGTA ELLNKEILRL QEENEKLKSR LKTIEIQATN ALDEKSKLEK ALQDLQLDQG NQKDFIKAQD LSNLENTVAA LKSEFQKTLN DKTENQKSLE ENLATAKHDL LRVQEQLHMA EKELEKKFQQ TAAYRNMKEI LTKKNDQIKD LRKRLAQYEP ED.

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    Lztfl1 Human
  • View Data Sheet

    Name :

    LGALS3 Human, His

    Description:

    Galectin-3 Human Recombinant, His Tag

    Galectin-3, GAL3, MAC2, CBP35, GALB, GALIG, LGALS2, LGALS3, Galactose-specific lectin 3, Mac-2 antigen, IgE-binding protein, 35 kDa lectin, Carbohydrate-binding protein 35, CBP 35, Laminin-binding protein, Lectin L-29, L-31, Galactoside-binding protein, GALBP.

    Product # :

    CYT-693

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    • sds-page

    Description

    LGALS3 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 270 amino acids (1-250 a.a.) and having a molecular mass of 28.3 kDa. The LGALS3 is fused to a 20 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The Galectin-3 protein solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH8.0), 0.1M NaCl, 1mM DTT and 10% Glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Biological Activity

    The ED50 for this effect is < 15ug/ml as measured by its ability to agglutinate human red blood cells.

    sds-page

    LGALS3 Human, His-sds-page - Product image 1

    More Info

    • Introduction

      Galectin-3 mediates with the alpha-3, beta-1 integrin the stimulation by cspg4 of endothelial cells migration. Galectin-3 plays an necessary part during the acquisition of vasculogenic mimicry and angiogenic properties associated with melanoma progression. LGALS3 overexpression is highly expressed in early stages of papillary carcinoma, and its expression intensity declines during tumor progression. Serum levels of LGALS3 are high in patients with thyroid malignancy but there is considerable overlap in serum LGALS3 concentrations between those with benign and malignant nodular thyroid disease. LGLAS3 takes part as an immune regulator to inhibit T-cell immune responses and promote tumor growth, as a result providing a new mechanism for tumor immune tolerance.

    • Synonyms

      Galectin-3, GAL3, MAC2, CBP35, GALB, GALIG, LGALS2, LGALS3, Galactose-specific lectin 3, Mac-2 antigen, IgE-binding protein, 35 kDa lectin, Carbohydrate-binding protein 35, CBP 35, Laminin-binding protein, Lectin L-29, L-31, Galactoside-binding protein, GALBP.

    • 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 MADNFSLHDA LSGSGNPNPQ GWPGAWGNQP AGAGGYPGAS YPGAYPGQAP PGAYPGQAPP GAYPGAPGAY PGAPAPGVYP GPPSGPGAYP SSGQPSATGA YPATGPYGAP AGPLIVPYNL PLPGGVVPRM LITILGTVKP NANRIALDFQ RGNDVAFHFN PRFNENNRRV IVCNTKLDNN WGREERQSVF PFESGKPFKI QVLVEPDHFK VAVNDAHLLQ YNHRVKKLNE ISKLGISGDI DLTSASYTMI.

    • Background

      What is the molecular weight/Mw of LGALS3 HUMAN, HIS Protein?
      LGALS3 HUMAN, HIS Protein has a total Mw of 28.3kDa.

      What is the source or expression system of LGALS3 HUMAN, HIS Protein?
      Escherichia Coli.

      What is the Purity of LGALS3 HUMAN, HIS Protein?
      LGALS3 HUMAN, HIS Protein is >95% pure as determined by SDS-PAGE.

      What is the Biological Activity of LGALS3 HUMAN, HIS Protein?
      The ED50 for this effect is < 2.5ug/ml as measured by its ability to agglutinate human red blood cells.

      What is the amino acid sequence of LGALS3 HUMAN, HIS Protein?
      MGSSHHHHHH SSGLVPRGSH MADNFSLHDA LSGSGNPNPQ GWPGAWGNQP AGAGGYPGAS YPGAYPGQAP PGAYPGQAPP GAYPGAPGAY PGAPAPGVYP GPPSGPGAYP SSGQPSATGA YPATGPYGAP AGPLIVPYNL PLPGGVVPRM LITILGTVKP NANRIALDFQ RGNDVAFHFN PRFNENNRRV IVCNTKLDNN WGREERQSVF PFESGKPFKI QVLVEPDHFK VAVNDAHLLQ YNHRVKKLNE ISKLGISGDI DLTSASYTMI.

      What applications can LGALS3 HUMAN, HIS Protein be used in?
      LGALS3 HUMAN, HIS Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for LGALS3 HUMAN, HIS Protein?
      The endotoxin level is minimal, LGALS3 HUMAN, HIS Protein was purified using conventional chromatography techniques.


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    Lgals3 Human His
  • View Data Sheet

    Name :

    TNFRSF25 Human

    Description:

    TNF Ligand Receptor Superfamily Member 25 Recombinant Human

    Tumor necrosis factor receptor superfamily member 25, TNFRSF25, TNF Ligand Receptor Superfamily Member 25, APO-3, DDR3, DR3, LARD, TNFRSF12, TR3, TRAMP, WSL-1, WSL-LR, Apo-3, Apoptosis-inducing receptor AIR, Protein WSL, Apoptosis-mediating receptor DR3, Apoptosis-mediating receptor TRAMP, Death receptor 3, Lymphocyte-associated receptor of death.

    Product # :

    CYT-980

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    Description

    TNFRSF25 Human Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 417 amino acids (25-199) and having a molecular mass of 46.1kDa (Molecular size on SDS-PAGE will appear at approximately 40-57kDa). TNFRSF25 is fused to a 242 amino acid IgG His-Tag at C-terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    TNFRSF25 protein solution (0.25mg/ml) containing Phosphate Buffered Saline (pH 7.4) and 10% glycerol.

    Purity

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

    Biological Activity

    Determined by the binding ability in a functional ELISA with Human VEGI (CAT# cyt-589). The ED50 range ≤ 5ug/ml.

    More Info

    • Introduction

      TNF Ligand Receptor Superfamily Member 25 (TNFRSF25) belongs to the TNF receptor superfamily that binds to the TNF-like protein TL1A. TNFRSF25 interacts directly with the adapter TRADD and regulates lymphocyte homeostasis. TNFRSF25 is also mediates activation of NF-kappa-B and induces apoptosis. TNFRSF25 signals are vital to exert T helper cell 2 effector activity in Th2-polarized CD4 cells and co-stimulate interleukin-13 production by glycosphingolipid-activated NKT cells.

    • Synonyms

      Tumor necrosis factor receptor superfamily member 25, TNFRSF25, TNF Ligand Receptor Superfamily Member 25, APO-3, DDR3, DR3, LARD, TNFRSF12, TR3, TRAMP, WSL-1, WSL-LR, Apo-3, Apoptosis-inducing receptor AIR, Protein WSL, Apoptosis-mediating receptor DR3, Apoptosis-mediating receptor TRAMP, Death receptor 3, Lymphocyte-associated receptor of death.

    • 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

      ADPQGGTRSP RCDCAGDFHK KIGLFCCRGC PAGHYLKAPC TEPCGNSTCL VCPQDTFLAW ENHHNSECAR CQACDEQASQ VALENCSAVA DTRCGCKPGW FVECQVSQCV SSSPFYCQPC LDCGALHRHT RLLCSRRDTD CGTCLPGFYE HGDGCVSCPT STLGSCPERC AAVCGWRQLE PKSCDKTHTC PPCPAPELLG GPSVFLFPPK PKDTLMISRT PEVTCVVVDV SHEDPEVKFN WYVDGVEVHN AKTKPREEQY NSTYRVVSVL TVLHQDWLNG KEYKCKVSNK ALPAPIEKTI SKAKGQPREP QVYTLPPSRD ELTKNQVSLT CLVKGFYPSD IAVEWESNGQ PENNYKTTPP VLDSDGSFFL YSKLTVDKSR WQQGNVFSCS VMHEALHNHY TQKSLSLSPG KHHHHHH.

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    Tnfrsf25 Human
  • View Data Sheet

    Name :

    Placental Lactogen Human

    Description:

    Placental Lactogen Human Recombinant

    Chorionic Somatomammotropin Hormone 1, CSH1, Choriomammotropin, Lactogen, CSH2, PL, CSA, CSMT, FLJ75407.

    Product # :

    CYT-656

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    Description

    Placental Lactogen Human Recombinant, is a single polypeptide chain containing 199 amino acids and an additional Ala at the N-terminus having a molecular mass of approximately 22.4 kDa. Placental Lactogen Recombinant is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

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

    Purity

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

    Biological Activity

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

    More Info

    • Introduction

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

    • Synonyms

      Chorionic Somatomammotropin Hormone 1, CSH1, Choriomammotropin, Lactogen, CSH2, PL, CSA, CSMT, FLJ75407.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized Placental Lactogen Human Recombinant although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Placental Lactogen 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 Placental Lactogen in sterile water or 0.4% NaHCO3 adjusted to pH 8-9, not less than 100µg/ml, which can then be further diluted to other aqueous solutions, preferably in presence of carrier protein.

    • Amino Acid Sequence

      The sequence of the first 6 N-terminal amino acids was determined and was found to be Ala-Val-Gln-Thr-Val-Pro.

    • Protein content

      UV spectroscopy at 280 nm using the absorbency value of 0.73 as the extinction coefficient for a 0.1% (1mg/ml) solution. This value is calculated by the DNAman computer analysis program of protein sequences.

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    Placental Lactogen Human
  • View Data Sheet

    Name :

    TCEAL7 Human

    Description:

    Transcription Elongation Factor A (SII)-Like 7 Human Recombinant

    Transcription elongation factor A (SII)-like 7, TCEA-like protein 7, transcription elongation factor A protein-like 7, MGC23947, MPMGp800C04260Q003.

    Product # :

    PRO-1147

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    Description

    TCEAL7 Human Recombinant produced in E. coli is a single polypeptide chain containing 124 amino acids (1-100) and having a molecular mass of 14.8 kDa.TCEAL7 is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    The TCEAL7 solution (0.5mg/1ml) contains 20mM Tris-HCl buffer (pH 8.0), 200mM NaCl, 2mM DTT and 50% glycerol.

    Purity

    Greater than 80% as determined by SDS-PAGE.

    More Info

    • Introduction

      Transcription Elongation Factor A (SII)-Like 7 (TCEAL7) has a role in the negative regulation of NF-kappa-B signaling at the basal level by controlling transcriptional activity of NF-kappa-B on its target gene promoters. TCEAL7 links with cyclin D1 promoter containing Myc E-box sequence and transcriptionally inhibits cyclin D1 expression. TCEAL7 regulates telomerase reverse transcriptase expression and telomerase activity in both alternative lengthening of telomeres (ALT) and telomerase-positive cell lines. TCEAL7 is highly expressed in normal and fetal brain tissues, and weakly expressed in the uterus and ovary. TCEAL7 is down-regulated in epithelial ovarian, cervical, prostate, breast, brain and lung cancer cell lines and in the brain and ovarian tumors.

    • Synonyms

      Transcription elongation factor A (SII)-like 7, TCEA-like protein 7, transcription elongation factor A protein-like 7, MGC23947, MPMGp800C04260Q003.

    • 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 MGSHMQKPCK ENEGKPKCSV PKREEKRPYG EFERQQTEGN FRQRLLQSLE EFKEDIDYRH FKDEEMTREG DEMERCLEEI RGLRKKFRAL HSNHRHSRDR PYPI

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    Tceal7 Human
  • View Data Sheet

    Name :

    Leptin N82K Human, PEG

    Description:

    Leptin N82K Human Recombinant, Pegylated

    OB Protein, Obesity Protein, OBS, Obesity factor.

    Product # :

    CYT-1107

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    Description

    Pegylated Leptin N82K Human Recombinant produced in E.Coli is a single non-glycosilated polypeptide chain containing 146 amino acids, an additional Ala at N-terminus and one molecule of PEG 20 kDa at its N-terminus acids and having a molecular weight of 35.6kDa. However due to enlarged hydrodymanic volume it runs on the SDS-PAGE as 48 kDa protein and in gel-filtration on Superdex 200 as over 200 kDa protein. Pegylated Leptin N82K Human Recombinant was purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Lyophilized from a concentrated (0.65mg/ml) solution with 0.003mM NaHCO3 Having 35-40% protein.

    Purity

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

    Biological Activity

    Pegylated Leptin Human is capable of stimulatng proliferation of BAF/3 cells stably transfected with the long form of human leptin receptor. Pegylated Leptin in vitro activity is 5-7 fold lower than the non-pegylated recombinant human leptin but in vivo Pegylated Leptin has profound weight reducing effect (as compared to the non-pegylated recombinant human leptin), resulting mainly from reduced food intake.

    More Info

    • Introduction

      Leptin takes an important part in the regulation of energy balance and body weight control.After entering the circulation, Leptin binds LEPRwhich results in the activation of several major signalling pathways. In the hypothalamus Leptin acts as an appetite-regulating factor that induces a decrease in food intake and an increase in energy consumption and also regulates bone mass and secretion of hypothalamo-pituitary-adrenal hormones. In the periphery, increases basal metabolism, regulates pancreatic beta-cell function and insulin secretion and affects innate and adaptive immunity.

    • Synonyms

      OB Protein, Obesity Protein, OBS, Obesity factor.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized Pegylated Leptin although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Pegylated Leptin N82K 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 Pegylated Leptin in sterile water or 0.4% NaHCO3 adjusted to pH 8-9, not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

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

    Leptin Mutant Protein
  • View Data Sheet

    Name :

    TNFR2 Human, His

    Description:

    Tumor Necrosis Factor Receptor Type 2 Human Recombinant, His Tag

    Tumor necrosis factor receptor superfamily member 1B, Tumor necrosis factor receptor 2, Tumor necrosis factor receptor type II, p75, p80 TNF-alpha receptor, CD120b, Etanercept, TNF-R2, TNF-RII, TNFR-II, TNFRSF1B, TNFBR, TNFR2, TBPII, TNFR2, TNFR1B, TNFR80, TNF-R75, p75TNFR, TNF-R-II.

    Product # :

    CYT-674

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    Description

    TNFR2 Human Recombinant produced in E.Coli is a single, non-glycosylated, Polypeptide chain containing 184 amino acids fragment (23-206) having a molecular weight of 24.45kDa and fused with a 4.5kDa amino-terminal hexahistidine tag. The TNFR2 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    TNFR2 protein is supplied in 20mM Tris HCl pH-8, 5mM EDTA and 50% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      TNFR2 belongs to the TNF-receptor superfamily. TNFR2 is receptor with high affinity for TNFSF2/TNF-alpha and approximately 5-fold lower affinity for homotrimeric TNFSF1/lymphotoxin-alpha. TNFR2 mediates the majority of the metabolic effects of TNF-alpha. In addition, knockout studies in mice propose a role for TNFR2 in protecting neurons from apoptosis by stimulating antioxidative pathways. TNFR2 expression might have a significant role in the angiogenesis, tumor cell proliferation and metastasis of Invasive micropapillary carcinoma of the breast.
      There are 2 types of soluble TNF receptors: sTNFR-I and sTNFR-II, which act to neutralize the biological activities of TNF alpha and TNF beta. The levels of these soluble receptors seem to increase as a result of shedding of the extracellular domains of the membrane bound receptors. High levels of soluble TNF receptors are found in the amniotic fluid of pregnant women. TNFR2 and TNFR1 form a heterocomplex which mediates the recruitment of 2 anti-apoptotic proteins, c-IAP1 and c-IAP2, which possess E3 ubiquitin ligase activity. IAPs’ function in TNF-receptor signaling is unknown; nevertheless, c-IAP1 is believed to potentiate TNF-induced apoptosis by the ubiquitination and degradation of TNF-receptor-associated factor 2, which mediates anti-apoptotic signals. Oxidative stress promotes TNFR1 and TNFR2 self-interaction, ligand-independent and enhanced ligand-dependent TNF signaling. TNF-a, TNFR1 and TNFR2 have roles in cellular differentiation. TNFR1 and TNFR2 function in cell type-specific renal injury.

    • Synonyms

      Tumor necrosis factor receptor superfamily member 1B, Tumor necrosis factor receptor 2, Tumor necrosis factor receptor type II, p75, p80 TNF-alpha receptor, CD120b, Etanercept, TNF-R2, TNF-RII, TNFR-II, TNFRSF1B, TNFBR, TNFR2, TBPII, TNFR2, TNFR1B, TNFR80, TNF-R75, p75TNFR, TNF-R-II.

    • Physical Appearance

      Sterile Filtered clear solution.

    • Stability

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

    • Amino Acid Sequence

      LPAQVAFTPYAPEPGSTCRLREYYDQTAQMCCSKCSPGQHAKVFCTKTSDTVCDSCEDSTYTQLWNWV
      PECLSCGSRCSSDQVETQACTREQNRICTCRPGWYCALSKQEGCRLCAPLRKCRPGFGVARPGTETSD
      VVCKPCAPGTFSNTTSSTDICRPHQICNVVAIPGNASMDAVCTSTSPT.

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    Tnfr2 Human
  • View Data Sheet

    Name :

    NXT2 Human

    Description:

    NTF2-like Export Factor 2 Human Recombinant

    NTF2-related export protein 2, Protein p15-2, NXT2, BM-025, DC9, P15-2.

    Product # :

    PRO-1051

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    Description

    NXT2 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 221 amino acids (1-197 a.a) and having a molecular mass of 25.3kDa.NXT2 is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    NXT2 protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 2mM DTT, 40% glycerol and 200mM NaCl.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

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    • Introduction

      Nuclear transport factor 2-like export factor 2 (NXT2) belongs to the NXT family proteins which are commonly involved in exporting nuclear RNA in eukaryotic cells. The NXT2 protein is a regulator of protein export for NES-containing proteins. In addition, NXT2 associates with NXF1, NXF2, NXF3 and NXF5 and has a role in mRNA nuclear export. NXT2 has a critical role in upholding morphogenetic integrity of embryonic heart in vertebrate species. The NXT2 protein contains a nuclear transport factor 2 (NTF2) domain, which has a vital role in the trafficking of macromolecules, ions, and small molecules between the cytoplasm and nucleus, it may also have a role in mRNA nuclear export.

    • Synonyms

      NTF2-related export protein 2, Protein p15-2, NXT2, BM-025, DC9, P15-2.

    • Physical Appearance

      Sterile Filtered clear solution.

    • Stability

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

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MGSHMRKYRS HWSQGDREGY QRRSNYYEGP HTSHSSPADR TREEVVTPTL PEHTATRSQM ATSLDFKTYV DQACRAAEEF VNIYYETMDK RRRALTRLYL DKATLIWNGN AVSGLDALNN FFDTLPSSEF QVNMLDCQPV HEQATQSQTT VLVVTSGTVK
      FDGNKQHFFN QNFLLTAQST PNNTVWKIAS DCFRFQDWSS S.

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    Nxt2 Human
  • View Data Sheet

    Name :

    PRLR Human, Antagonist S.Active

    Description:

    Prolactin Receptor Antagonist, S. Active Human Recombinant

    Mammotropin, Luteotropic hormone, Luteotropin, PRL.

    Product # :

    CYT-1253

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    Description

    Prolactin Human Receptor Antagonist del 1-9, G129R mutant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 190 amino acids + an additional Ala at n-terminal and having a molecular mass of ~ 22 kDa was modified by additional 12 mutations. The Human Prolactin Receptor Antagonist is purified by proprietary chromatographic techniques.

    Source

    Escherichia coli.

    Formulation

    The protein was lyophilized from a concentrated (1-2mg/ml) solution with 0.02% -0.03% NaHCO3.

    Purity

    Greater than 97.0% as determined by:

    (a) Analysis by Gel Filtration.

    (b) Analysis by SDS-PAGE.

    Biological Activity

    fully biologically active as evidenced by inhibiting PRLR-induced proliferation of Nb2 cells or Baf3 cells stably transfected with hPRL receptors. It also interacts at 1:1 molar ratio with human prolactin receptor extracellular domain as documented by SEC and SPR (Biacore analysis). It is ~ 100 fold more potent than 1-9 G129R hPRL in Ba/F3 cells and > 1000-fold potent in Nb2 cells.

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    • Synonyms

      Mammotropin, Luteotropic hormone, Luteotropin, PRL.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized PRLR although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution at > 0.1 mg/ml and up to 3 mg/ml and filter sterilization PRLR can be stored at 4C for several weeks. Please prevent freeze-thaw cycles.

    • Solubility

      It is recommended to reconstitute the lyophilized PRLR in sterile 0.4% NaHCO3 adjusted to pH 8-9 not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      The sequence of the first six N-terminal amino acids was determined and was found to be Ala-Arg-Ser-Gln-Val-Thr

    • Background

      Prolactin is a pituitary hormone which takes part in the stimulation of milk production, salt and water regulation, development, growth and reproduction. The primary step in its action is binding a specific membrane receptor (prolactin receptor) which belongs to the superfamily of class 1 cytokine receptors. PRLR varies in size (short and long forms) with tissue source and species, from ~40 kDa to 100 kDa. The PRL-R consists of at least 3 separate domains: an extracellular region with 5 cysteines which contains the prolactin binding site, a single transmembrane domain and a cytoplasmic region, the length of which appears to influence ligand binding and regulate cellular function.

    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.

    Prlr Antagonist Human
  • View Data Sheet

    Name :

    TNFRSF10A Human

    Description:

    TRAIL Receptor-1 Human Recombinant

    TNFRSF10A, TNF Receptor Superfamily Member 10a, Tumor Necrosis Factor Receptor Superfamily, Member 10a, TNF-Related Apoptosis-Inducing Ligand Receptor 1, Death Receptor 4, TRAIL Receptor 1, TRAIL-R1, TRAILR1, APO2, DR4, Tumor Necrosis Factor Receptor Superfamily Member 10a Variant 2, Tumor Necrosis Factor Receptor Superfamily Member 10A, Cytotoxic TRAIL Receptor, CD261 Antigen, TRAILR-1, CD261.          

    Product # :

    CYT-1043

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    Description

    TNFRSF10A produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 224 amino acids (24-239a.a.) and having a molecular mass of 23.9kDa. TNFRSF10A is expressed with an 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    TNFRSF10A 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.

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    • Introduction

      Human TNFRSF10A is a type 1 transmembrane protein in the TNF R superfamily. TNFRSF10A is not expressed in rodents. The trimeric ligand Trail binds TNFRSF10A and induces apoptosis, and recombinant, soluble forms of the receptor inhibit Trail-induced apoptosis. TNFRSF10A is expressed generally in damaged, infected, and malignant cells. TNFRSF10A functions in immune surveillance, inducing apoptosis in cancer cells but not normal cells.

    • Synonyms

      TNFRSF10A, TNF Receptor Superfamily Member 10a, Tumor Necrosis Factor Receptor Superfamily, Member 10a, TNF-Related Apoptosis-Inducing Ligand Receptor 1, Death Receptor 4, TRAIL Receptor 1, TRAIL-R1, TRAILR1, APO2, DR4, Tumor Necrosis Factor Receptor Superfamily Member 10a Variant 2, Tumor Necrosis Factor Receptor Superfamily Member 10A, Cytotoxic TRAIL Receptor, CD261 Antigen, TRAILR-1, CD261.

    • 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

      ASGTEAAAAT PSKVWGSSAG RIEPRGGGRG ALPTSMGQHG PSARARAGRA PGPRPAREAS PRLRVHKTFK FVVVGVLLQV VPSSAATIKL HDQSIGTQQW EHSPLGELCP PGSHRSEHPG ACNRCTEGVG YTNASNNLFA CLPCTACKSD EEERSPCTTT RNTACQCKPG TFRNDNSAEM CRKCSRGCPR GMVKVKDCTP WSDIECVHKE SGNGHNLEHH HHHH

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    TNFRSF10A Human
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    Name :

    TNFAIP8 Human

    Description:

    Tumor Necrosis Factor, Alpha-Induced Protein 8 Human Recombinant

    GG2-1; MDC-3.13, SCC-S2, SCCS2, Tumor necrosis factor alpha-induced protein 8, TNF alpha-induced protein 8, Head and neck tumor and metastasis-related protein, NF-kappa-B-inducible DED-containing protein, NDED, TNF-induced protein GG2-1, TNFAIP8.

    Product # :

    CYT-759

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    Description

    TNFAIP8 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 221 amino acids (1-198a.a.) and having a molecular mass of 25kDa. TNFAIP8 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    TNFAIP8 protein solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 10% glycerol and 1mM DTT.

    Purity

    Greater than 90% as determined by SDS-PAGE.

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    • Introduction

      TNFAIP8 which is a part of the TNFAIP8 family acts as a negative mediator of apoptosis and takes part in tumor progression. TNFAIP8 suppresses the TNF-mediated apoptosis by inhibiting caspase-8 activity but not the processing of procaspase-8, resulting in inhibition of BID cleavage and activation of caspase-3.

    • Synonyms

      GG2-1; MDC-3.13, SCC-S2, SCCS2, Tumor necrosis factor alpha-induced protein 8, TNF alpha-induced protein 8, Head and neck tumor and metastasis-related protein, NF-kappa-B-inducible DED-containing protein, NDED, TNF-induced protein GG2-1, TNFAIP8.

    • 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 MGSMHSEAEE SKEVATDVFN SKNLAVQAQK KILGKMVSKS IATTLIDDTS SEVLDELYRV TREYTQNKKE AEKIIKNLIK TVIKLAILYR NNQFNQDELA LMEKFKKKVH QLAMTVVSFH QVDYTFDRNV LSRLLNECRE MLHQIIQRHL TAKSHGRVNN VFDHFSDCEF LAALYNPFGN FKPHLQKLCD GINKMLDEEN I.

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    Tnfaip8 Human
  • View Data Sheet

    Name :

    EIF1AX Human

    Description:

    Eukaryotic Translation Initiation Factor 1 X-linked Human Recombinant

    eukaryotic translation initiation factor 1A, X-linked, eIF-4C, EIF1A, EIF4C, eIF-1A, EIF1AP1.

    Product # :

    PRO-253

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    Description

    EIF1AX Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 150 amino acids (1-144a.a.) and having a molecular wieght of 18.6kDa. EIF1AX is fused to 20a.a. His-Tag at N-terminus and purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The EIF1AX protein solution (1mg/1ml) contains 20mM Tris-HCl buffer (pH8.0) containing 5mM DTT, 200mM NaCl and 40% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

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    • Introduction

      EIF1AX is an important eukaryotic translation initiation factor. EIF1AX is essential for the binding of the 43S complex (a 40S subunit, eIF2/GTP/Met-tRNAi and eIF3) to the 5'' end of capped RNA. EIF1AP1 is needed for maximal rate of protein biosynthesis. EIF1AX increases ribosome dissociation into subunits and stabilizes the binding of the initiator Met-tRNA (I) to 40 S ribosomal subunits.

    • Synonyms

      eukaryotic translation initiation factor 1A, X-linked, eIF-4C, EIF1A, EIF4C, eIF-1A, EIF1AP1.

    • 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 MPKNKGKGGK NRRRGKNENE SEKRELVFKE DGQEYAQVIK MLGNGRLEAM CFDGVKRLCH IRGKLRKKVW INTSDIILVG LRDYQDNKAD VILKYNADEA RSLKAYGELP EHAKINETDT FGPGDDDEIQ FDDIGDDDED IDDI

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    Eif1Ax Human
  • View Data Sheet

    Name :

    proBDNF Human

    Description:

    Precursor Brain-Derived Neurotrophic Factor Human Recombinant

    proBDNF, Precursor Form Brain-derived Neurotrophic Factor.

    Product # :

    CYT-014

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    Description

    proBDNF Human Recombinant produced in E.Coli is a single, non-glycosylated, non-covalently linked homodimer with each polypeptide chain containing 229 amino acids and having a molecular mass of 52kDa. The proBDNF is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    proBDNF was lyophilized from a concentrated (0.5mg/ml) solution in 20mM PB, pH 8.0 and 500mM NaCl.

    Purity

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

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    • Introduction

      proBDNF (the precursor form of Brain-derived neurotrophic factor) interacts preferentially with p75NTR (the pan-neurotrophin receptor p75) and vps10p domain-containing receptor sortilin and induces neuronal apoptosis, while the mature BDNF selectively binds with great affinity to the TrkB kinase receptor and promotes the survival, growth and differentiation of neurons. Since proneurotrophins and mature neurotrophins bring forth opposite biological effects, proBDNF cleavage in the neuronal system is regulated in a specific and cell-context dependent manner. proBDNF has an important role in negative regulation of neurotrophic actions in the brain.

    • Synonyms

      proBDNF, Precursor Form Brain-derived Neurotrophic Factor.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized proBDNF although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution proBDNF 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 proBDNF in sterile 18M-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-Pro-Met-Lys.

    • Background

      Precursor Brain-Derived Neurotrophic Factor Human Recombinant: Unveiling the Potential of a Key Neurotrophic Factor

      Abstract:

      Precursor Brain-Derived Neurotrophic Factor (proBDNF) human recombinant is a pivotal neurotrophic factor that plays a critical role in neuronal development, survival, and synaptic plasticity. This research paper provides a comprehensive overview of proBDNF, including its characteristics, processing mechanisms, and potential therapeutic applications. Furthermore, innovative methodologies for the production and optimization of proBDNF human recombinant are proposed, highlighting its future implications in the field of neuroregenerative medicine.

      Introduction:

      Understanding the intricate processes underlying neuronal development and function is crucial for advancing neuroregenerative strategies. Neurotrophic factors, such as proBDNF, have garnered significant attention due to their pivotal roles in supporting neuronal growth and survival. This paper delves into the unique features of proBDNF and presents novel approaches for its production and optimization.

      Characteristics and Processing Mechanisms:

      proBDNF is a precursor protein consisting of 247 amino acids and is processed into mature brain-derived neurotrophic factor (mBDNF) through proteolytic cleavage. The ratio between proBDNF and mBDNF is tightly regulated and determines the balance between neuronal survival and apoptosis. Additionally, proBDNF exerts distinct biological functions through its receptor interactions, modulating synaptic plasticity and neuronal activity.

      Production of proBDNF Human Recombinant:

      Efficient production methodologies are essential to harness the therapeutic potential of proBDNF human recombinant. Various expression systems, including bacterial, yeast, and mammalian cell-based platforms, have been explored. Each system presents unique advantages and challenges, necessitating careful selection to achieve high yields and protein quality. Optimization strategies, such as codon optimization, fusion protein tags, and growth conditions, have been employed to enhance production efficiency. Purification techniques, such as affinity chromatography and size exclusion chromatography, have been optimized to isolate high-quality proBDNF recombinant.

      Potential Therapeutic Applications:

      proBDNF human recombinant holds immense promise for neuroregenerative medicine. Its role in promoting neuronal survival, axonal growth, and synaptic plasticity positions it as a valuable therapeutic agent for neurodegenerative disorders, spinal cord injuries, and stroke. Additionally, the balance between proBDNF and mBDNF presents a potential therapeutic target for fine-tuning neuronal processes and restoring proper brain function.

      Conclusion:

      proBDNF human recombinant represents a crucial neurotrophic factor with diverse therapeutic applications in neuroregenerative medicine. Optimizing production methodologies and further understanding its processing mechanisms will enhance its clinical utility. With its potential implications in neurodegenerative disorders and neuronal repair, proBDNF human recombinant holds immense promise as a transformative tool for promoting neural health and regeneration.

      What is the molecular weight/Mw of BDNF Protein?
      BDNF Protein has a total Mw of 52kDa.

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

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

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

      What is the amino acid sequence of BDNF Protein?
      The sequence of the first five N-terminal amino acids was determined and was found to be Met-Ala-Pro-Met-Lys.

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

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

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

    Probdnf Human
  • View Data Sheet

    Name :

    SDF2 Human

    Description:

    Stromal Cell-Derived Factor 2 Human Recombinant

    Stromal cell-derived factor 2, SDF-2.

    Product # :

    CHM-028

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    Description

    SDF2 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 216 amino acids (19-211 a.a) and having a molecular mass of 23.7kDa. SDF2 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    SDF2 protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 10% glycerol and 0.4M Urea.

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

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    • Introduction

      Stromal Cell-Derived Factor 2 (SDF2) is a secretory protein which is partly similar to the hydrophilic segments of yeast mannosyltransferases. SDF2 protein’s expression is ubiquitous and the gene is rather conserved among mammals. SDF2is a protein-coding gene whose alternative splicing results in coding and non-coding variants.

    • Synonyms

      Stromal cell-derived factor 2, SDF-2.

    • Physical Appearance

      Sterile Filtered colorless solution.

    • Stability

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

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MGSSSLGVVT CGSVVKLLNT RHNVRLHSHD VRYGSGSGQQ SVTGVTSVDD SNSYWRIRGK SATVCERGTP IKCGQPIRLT HVNTGRNLHS HHFTSPLSGN QEVSAFGEEG EGDYLDDWTV LCNGPYWVRD GEVRFKHSST EVLLSVTGEQ YGRPISGQKE VHGMAQPSQN NYWKAMEGIF MKPSELLKAE AHHAEL.

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    Sdf2 Human
  • View Data Sheet

    Name :

    TRIM33 Human

    Description:

    Tripartite Motif Containing 33 Human Recombinant

    E3 ubiquitin-protein ligase TRIM33, Ectodermin homolog, RET-fused gene 7 protein, Protein Rfg7, Transcription intermediary factor 1-gamma, TIF1-gamma, Tripartite motif-containing protein 33, TRIM33, KIAA1113, RFG7, TIF1G, ECTO, PTC7, TF1G, TIFGAMMA, TIF1GAMMA.

    Product # :

    PRO-1506

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    Description

    TRIM33 Human Recombinant produced in SF9 is a glycosylated, polypeptide chain having a calculated molecular mass of 124,041 Dalton. TRIM33 is expressed with a -10xHis tag at N-terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9 Insect Cells.

    Formulation

    TRIM33 is supplied in 20mM HEPES buffer pH-7.9, 550mM NaCl and 6M Urea.

    Purity

    Greater than 80.0% as determined by SDS-PAGE.

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    • Introduction

      Tripartite Motif Containing 33 (TRIM33) belongs to the tripartite motif family. This motif includes 3 zinc-binding domains, a RING, a B-box type 1 and a B-box type 2, and a coiled-coil region. TRIM33 is assumed to be a transcriptional corepressor. TRIM33 functions as an E3 ubiquitin-protein ligase. TRIM33 also promotes SMAD4 ubiquitination, nuclear exclusion and degradation via the ubiquitin proteasome pathway. In addition, TRIM33 inhibits the transcriptional response to TGF-beta/BMP signaling cascade. Furthermore, TRIM33 has a role in the control of cell proliferation.

    • Synonyms

      E3 ubiquitin-protein ligase TRIM33, Ectodermin homolog, RET-fused gene 7 protein, Protein Rfg7, Transcription intermediary factor 1-gamma, TIF1-gamma, Tripartite motif-containing protein 33, TRIM33, KIAA1113, RFG7, TIF1G, ECTO, PTC7, TF1G, TIFGAMMA, TIF1GAMMA.

    • Physical Appearance

      Sterile Filtered clear solution.

    • Stability

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

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    Trim33 Human
  • View Data Sheet

    Name :

    Prolactin Mouse, His

    Description:

    Prolactin Mouse Recombinant, His Tag

    AV290867, Gha1, Prl1a1, Growth hormone a1, Mammotropin, Luterotropic hormone, Lutetropin, PRL.

    Product # :

    CYT-1060

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    Description

    Prolactin Mouse produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 222 amino acids (30-228a.a.) and having a molecular mass of 25 kDa. Prolactin Mouse protein is fused to a 23 amino acid His tag at N-terminus and is purified by standard chromatography.

    Source

    Escherichia Coli.

    Formulation

    The Prolactin Mouse solution (0.25mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 20% glycerol.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    More Info

    • Introduction

      Prolactin is a neuroendocrine hormone synthesized primarily by the pituitary gland but also a variety of other cell types including the placenta, brain and uterus. Its primary function is to promote and maintain lactation but has also been shown to have a role in breast cancer development, regulation of reproductive function and immunoregulation.

    • Synonyms

      AV290867, Gha1, Prl1a1, Growth hormone a1, Mammotropin, Luterotropic hormone, Lutetropin, PRL.

    • 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 MGSQPLPICS AGDCQTSLRE LFDRVVILSH YIHTLYTDMF IEFDKQYVQD REFMVKVIND CPTSSLATPE DKEQALKVPP EVLLNLILSL VQSSSDPLFQ LITGVGGIQE APEYILSRAK EIEEQNKQLL EGVEKIISQA YPEAKGNGIY VWSQLPSLQ GVDEESKILS LRNTIRCLRR DSHKVDNFLK VLRCQIAHQN NC.

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    Mouse Prolactin
  • View Data Sheet

    Name :

    Leptin Rat, PEG

    Description:

    Pegylated Rat Leptin Recombinant

    OB Protein, Obesity Protein, OBS, Obesity factor.

    Product # :

    CYT-592

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    Description

    Mono-Pegylated Leptin Rat Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 146 amino acids and an additional Ala at N-terminus having a molecular mass of 35.6 kDa (with 20 kDa PEG) as determined by mass spectometry. However due to enlarged hydrodymanic volume it runs on the SDS-PAGE as 48 kDa protein and in gel-filtration on Superdex 200 as over 100 kDa protein. Its half-life in circulation after SC injection was over 20 hours. Rat Leptin was purified by proprietary chromatographic techniques according to Salomon et al (2006) Protein Expression and Purification 47, 128–136 and then pegylated.

    Source

    Escherichia Coli.

    Formulation

    The protein was lyophilized from a concentrated (0.65mg/ml) solution with 0.003mM NaHCO3.

    Purity

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

    Biological Activity

    Pegylated Rat Leptin is capable of stimulatng proliferation of BAF/3 cells stably transfected with the long form of human leptin receptor. Its in vitro activity is only slightly lower than the non-pegylated antagonist but in vivo it has profound weight reducing effect (as compared to the non-pegylated leptin), resulting mainly from reduced food intake.

    More Info

    • Introduction

      A 16-kDa peptide hormone secreted from white adipocytes and implicated in the regulation of food intake and energy balance. Leptin provides the key afferent signal from fat cells in the feedback system that controls body fat stores.

    • Synonyms

      OB Protein, Obesity Protein, OBS, Obesity factor.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized pegylated Rat Leptin Antagonist although stable at room temperature for several weeks, should be stored desiccated below -18°C. Upon reconstitution of pegylated Rat Leptin at > 0.1 mg/ml and up to 2 mg/ml and filter sterilization Rat leptin can be stored at 4C or even room temperature for several weeks making it suitable for long term infusion studies using osmotic pumps. At lower concentration addition of a carrier protein (0.1% HSA or BSA) is suggested. Please prevent freeze-thaw cycles.

    • Solubility

      It is recommended to reconstitute the lyophilized pegylated Rat Leptin in sterile water or in sterile 0.4% NaHCO3 adjusted to pH-8.5, not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

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

    Leptin Rat Pegylated
  • View Data Sheet

    Name :

    EEF1A1 Human

    Description:

    Eukaryotic Translation Elongation Factor 1 Alpha 1 Human Recombinant

    Eukaryotic Translation Elongation Factor 1 Alpha 1, EF1A, EEF1A, LENG7, Leukocyte Receptor Cluster (LRC) Member 7, Elongation Factor Tu, Eukaryotic Elongation Factor 1 A-1, Leukocyte Receptor Cluster Member 7, EF-1-alpha-1, EF-Tu, eEF1A-1, CCS-3, CCS3, EE1A1, EEF-1, GRAF-1EF, HNGC:16303, PTI1, Cervical Cancer Suppressor 3, CTCL Tumor Antigen, EF1a-Like Protein, Elongation Factor 1 Alpha Subunit, Elongation Factor 1-Alpha 1, Eukaryotic Translation Elongation Factor 1 Alpha 1-Like 14, Glucocorticoid Receptor AF-1 Specific Elongation Factor, Prostate Tumor-Inducing Protein 1, Translation Elongation Factor 1 Alpha 1-Like 14.

    Product # :

    PRO-1910

    Price :

    Quantity :

    Shipping Method :

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    Shipped with Ice Packs

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    More Info

    • description
    • source
    • formulation
    • purity
    • More Info

    Description

    EEF1A1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 462 amino acids (1-462 a.a) and having a molecular mass of 50kDa.

    Source

    Escherichia Coli.

    Formulation

    EEF1A1 protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.4M Urea and 10% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      EEF1A1 is an isoform of the alpha subunit of the elongation factor-1 complex, which is responsible forthe enzymatic release of aminoacyl tRNAs to the ribosome. EEF1A1 is expressed in brain, placenta, lung, liver, kidney, and pancreas, and the other isoform (alpha 2) is expressed in brain, heart and skeletal muscle. EEF1A1 is recognized as an autoantigen in 66% of patients with Felty syndrome. EEF1A1 has multiple copies on numerous chromosomes, part of them, if not all, symbolize different pseudogenes. Among the diseases associated with EEF1A1 are tinea nigra and andcervical cancer.

    • Synonyms

      Eukaryotic Translation Elongation Factor 1 Alpha 1, EF1A, EEF1A, LENG7, Leukocyte Receptor Cluster (LRC) Member 7, Elongation Factor Tu, Eukaryotic Elongation Factor 1 A-1, Leukocyte Receptor Cluster Member 7, EF-1-alpha-1, EF-Tu, eEF1A-1, CCS-3, CCS3, EE1A1, EEF-1, GRAF-1EF, HNGC:16303, PTI1, Cervical Cancer Suppressor 3, CTCL Tumor Antigen, EF1a-Like Protein, Elongation Factor 1 Alpha Subunit, Elongation Factor 1-Alpha 1, Eukaryotic Translation Elongation Factor 1 Alpha 1-Like 14, Glucocorticoid Receptor AF-1 Specific Elongation Factor, Prostate Tumor-Inducing Protein 1, Translation Elongation Factor 1 Alpha 1-Like 14.

    • 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

      MGKEKTHINI VVIGHVDSGK STTTGHLIYK CGGIDKRTIE KFEKEAAEMG KGSFKYAWVL DKLKAERERG ITIDISLWKF ETSKYYVTII DAPGHRDFIK NMITGTSQAD CAVLIVAAGV GEFEAGISKN GQTREHALLA YTLGVKQLIV GVNKMDSTEP PYSQKRYEEI VKEVSTYIKK IGYNPDTVAF VPISGWNGDN MLEPSANMPW FKGWKVTRKD GNASGTTLLE ALDCILPPTR PTDKPLRLPL QDVYKIGGIG TVPVGRVETG VLKPGMVVTF APVNVTTEVK SVEMHHEALS EALPGDNVGF NVKNVSVKDV RRGNVAGDSK NDPPMEAAGF TAQVIILNHP GQISAGYAPV LDCHTAHIAC KFAELKEKID RRSGKKLEDG PKFLKSGDAA IVDMVPGKPM CVESFSDYPP LGRFAVRDMR QTVAVGVIKA VDKKAAGAGK ITKSAQKAQK AK

    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.

    Eef1A1 Human
  • View Data Sheet

    Name :

    TCEB1 Human

    Description:

    Transcription Elongation Factor B Polypeptide 1 Human Recombinant

    Transcription elongation factor B polypeptide 1, Elongin 15 kDa subunit, Elongin-C, EloC, RNA polymerase II transcription factor SIII subunit C, SIII p15, TCEB1, SIII.

    Product # :

    PRO-1017

    Price :

    Quantity :

    Shipping Method :

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    More Info

    • description
    • source
    • formulation
    • purity
    • More Info

    Description

    TCEB1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 132 amino acids (1-112 a.a.) and having a molecular mass of 14.6kDa. TCEB1 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    TCEB1 protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 10% glycerol, 1mM DTT and 0.15M NaCl.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      TCEB1 (elongin C) is a subunit of elongin, which is a common transcription elongation factor that increases the RNA polymerase II transcription elongation past template encoded arresting sites. The SIII complex is comprised of elongins A/A2, B and C. The SIII complex activates elongation by RNA polymerase II by curbing transient pausing of the polymerase at numerous sites within transcription units. Elongin A acts as the transcriptionally active component of the SIII complex, while elongins B and C are regulatory subunits. Elongin A2 is specifically expressed in the testis, and able to forming a stable complex with elongins B and C. The VHL (von Hippel-Lindau) tumor suppressor protein binds to elongins B and C, and thus inhibits transcription elongation.

    • Synonyms

      Transcription elongation factor B polypeptide 1, Elongin 15 kDa subunit, Elongin-C, EloC, RNA polymerase II transcription factor SIII subunit C, SIII p15, TCEB1, SIII.

    • 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 MDGEEKTYGG CEGPDAMYVK LISSDGHEFI VKREHALTSG TIKAMLSGPG QFAENETNEV NFREIPSHVL SKVCMYFTYK VRYTNSSTEI PEFPIAPEIA LELLMAANFL DC.

    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.

    Tceb1 Human
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