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Search results

1000 results found for “Neuritin”

Name

Description

Product #

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  • View Data Sheet

    Name :

    NXPH1 Human

    Description:

    Neurexophilin 1 Human Recombinant

    Nbla00697, NPH1, Neurexophilin-1, NXPH1.

    Product # :

    PRO-1859

    Price :

    Quantity :

    Shipping Method :

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    • description
    • source
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    • purity
    • More Info

    Description

    NXPH1 Human Recombinant produced in E. coli is. a single polypeptide chain containing 273 amino acids (22-271) and having a molecular mass of 31kDa. NXPH1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The NXPH1 solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.4M UREA and 10% glycerol.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    More Info

    • Introduction

      Neurexophilin 1 (NXPH1) is a part of the neurexophilin family which encodes a secreted protein with a variable N terminal domain, an extremely conserved, N-glycosylated central domain, a short linker region, and a cysteine-rich Cterminal domain. NXPH1 shapes a very tight complex with alpha neurexins, a group of proteins which promote adhesion among dendrites and axons.

    • Synonyms

      Nbla00697, NPH1, Neurexophilin-1, NXPH1.

    • 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 MGSANLTNGG KSELLKSGSS KSTLKHIWTE SSKDLSISRL LSQTFRGKEN DTDLDLRYDT PEPYSEQDLW DWLRNSTDLQ EPRPRAKRRP IVKTGKFKKM FGWGDFHSNI KTVKLNLLIT GKIVDHGNGT FSVYFRHNST GQGNVSVSLV PPTKIVEFDL AQQTVIDAKD SKSFNCRIEY EKVDKATKNT LCNYDPSKTC YQEQTQSHVS WLCSKPFKVI CIYISFYSTD YKLVQKVCPD YNYHSDTPYF PSG.

    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.

    Nxph1 Human
  • View Data Sheet

    Name :

    NMB Human

    Description:

    Neuromedin B Human Recombinant

    Neuromedin-B, NMB, Neuromedin-B-32, Neuromedin B.

    Product # :

    PRO-1518

    Price :

    Quantity :

    Shipping Method :

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    Description

    NMB Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 120 amino acids (25-121) and having a molecular mass of 13.2 kDa.NMB is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The NMB solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.4M urea and 10% glycerol.

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Neuromedin B (NMB) which is a part of the bombesin/neuromedin-B/ranatensin family and stimulates smooth muscle contraction in a way similar to that of bombesin.

    • Synonyms

      Neuromedin-B, NMB, Neuromedin-B-32, Neuromedin B.

    • 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 MGSAPLSWDL PEPRSRASKI RVHSRGNLWA TGHFMGKKSL EPSSPSPLGT APHTSLRDQR LQLSHDLLGI LLLKKALGVS LSRPAPQIQY RRLLVQILQK.

    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.

    Nmb Human
  • View Data Sheet

    Name :

    NRG1 Human, SF9

    Description:

    Neuregulin-1 Human Recombinant, Sf9

    Neuregulin-1, NRG1, GGF, HGL, HRGA, NDF, SMDF, HRG, ARIA, GGF2, HRG1

    Product # :

    CYT-1186

    Price :

    Quantity :

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    • More Info

    Description

    NRG1 Human produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 231 amino acids (20-241 aa) and having a molecular mass of 25.1kDa.NRG1 is fused to a 6 amino acid His tag at C-terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    The NRG1 solution (0.5mg/ml) contains 10% Glycerol and Phosphate-Buffered Saline (pH 7.4).

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    Biological Activity

    Determined by cell proliferation assay MCF7 human breast cancer cell. ED50 range for this effect is ≤ 15 ng/ml/

    More Info

    • Introduction

      Neuregulin/Heregulin is a family of structurally related polypeptide growth factors which are stemmed from alternatively spliced genes (NRG1, NRG2, NRG3 and NRG4). There are more than 14 soluble and transmembrane proteins derived from the NRG1 gene. Proteolytic processing of the extracellular domain of the transmembrane NRG1 isoforms release soluble growth factors. These isoforms contain the heregulins (HRGs), glial growth factors (GGFs) and sensory and motor neuron-derived factor (SMDF). All these factors have the Ig and EGF-like domain, and are able to bind to ErbB3 and ErbB4 receptor tyrosin kinases. This binding stimulates erb3 and erb4 heterodimerization with erb2, promoting intrinsic kinase activity, which results in tyrosine phosphorylation. NRG1 isoforms induce the growth and differentiation of epithelial, neuronal, glial, and other types of cells.

    • Synonyms

      Neuregulin-1, NRG1, GGF, HGL, HRGA, NDF, SMDF, HRG, ARIA, GGF2, HRG1

    • 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

      ADPSGKKPES AAGSQSPALP PRLKEMKSQE SAAGSKLVLR CETSSEYSSL RFKWFKNGNE
      LNRKNKPQNI KIQKKPGKSE LRINKASLAD SGEYMCKVIS KLGNDSASAN ITIVESNEII TGMPASTEGA YVSSESPIRI SVSTEGANTS SSTSTSTTGT SHLVKCAEKE KTFCVNGGEC FMVKDLSNPS RYLCKCPNEF TGDRCQNYVM ASFYSTSTPF LSLPEHHHHH H

    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.

    Nrg1 Human
  • View Data Sheet

    Name :

    NRG4 Human

    Description:

    Neuregulin-4 Human Recombinant

    Neuregulin 4, HRG4, Pro-neuregulin-4, membrane-bound isoform, Pro-NRG4, NRG-4.

    Product # :

    CYT-808

    Price :

    Quantity :

    Shipping Method :

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    More Info

    • description
    • source
    • formulation
    • purity
    • More Info

    Description

    NRG4 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 84 amino acids (1-61 a.a.) and having a molecular mass of 9.1kDa. NRG4 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    NRG4 protein solution (0.25mg/ml) contains 20mM Tris-HCl(pH8.0), 30% glycerol, 0.15M NaCl and 1mM DTT.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    More Info

    • Introduction

      Neuregulin-4 (NRG4) is a part of the neuregulin family that owns 1 EGF-like domain and is a low affinity ligand for the ERBB4 tyrosine kinase receptor. NRG4 links ERBB1 and ERBB2 coreceptors, resulting in ligand-stimulated tyrosine phosphorylation and activation of the ERBB receptors.

    • Synonyms

      Neuregulin 4, HRG4, Pro-neuregulin-4, membrane-bound isoform, Pro-NRG4, NRG-4.

    • 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 MGSMPTDHEE PCGPSHKSFC LNGGLCYVIP TIPSPFCRCV ENYTGARCEE VFLPGSSIQT KSNL.

    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.

    Nrg4 Human
  • View Data Sheet

    Name :

    NEFH Bovine

    Description:

    Neurofilament Heavy Chain Bovine

    Neurofilament light polypeptide, NF-L, NEFL, NF68, NFL, 68 kDa neurofilament protein.

    Product # :

    PRO-2787

    Price :

    Quantity :

    Shipping Method :

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    Shipped at Room temp

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    More Info

    • description
    • source
    • formulation
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    • More Info

    Description

    NEFH Bovine having a calculated molecular mass of 200 kDa, pI-5.5.

    Source

    Bovine spinal cord.

    Formulation

    NEFH was lyophilized from a 1mg/ml solution containing 10mM sodium phosphate buffer pH 7.5, 6M urea, 1mM EDTA, 2mM DTT and 10mM methylammonium chloride.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Synonyms

      Neurofilament light polypeptide, NF-L, NEFL, NF68, NFL, 68 kDa neurofilament protein.

    • Physical Appearance

      Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Store the lyophilized NEFH between 2-8°C, do not freeze. Upon reconstitution NEFH should be stored at -20°C.Please prevent freeze-thaw cycles.

    • Solubility

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

    • Background

      Neurofilament heavy chain (NEFH) is a vital structural protein in neurons, predominantly found in the central and peripheral nervous systems. Although extensive research has been conducted on NEFH in humans and rodents, the investigation of NEFH in bovine nervous tissues presents an emerging area with substantial potential for advancing our understanding of neuronal biology in larger mammals and its applications in veterinary medicine and neurobiology.

      Bovine nervous tissues, including the brain and spinal cord, are of particular interest due to their relevance in cattle health, neuroscience, and the food industry. This research aims to provide a comprehensive exploration of NEFH in bovine nervous tissues, elucidating its functions, structural significance, and potential applications.

      The primary objective of this research is to elucidate the role of NEFH in bovine nervous tissues, particularly in maintaining neuronal structural integrity and axonal function. In vitro and ex vivo experiments, utilizing bovine neuronal cell cultures and tissue specimens, will be conducted to investigate how NEFH contributes to neuronal morphology, axonal transport, and overall neuronal resilience. Understanding these mechanisms is fundamental for deciphering the complexities of neuronal biology in bovine species.

      The second objective is to assess the relevance of bovine NEFH in veterinary medicine. Studies involving bovine models will be conducted to evaluate the impact of NEFH mutations or variations on neuronal health, disease susceptibility, and neurodegenerative conditions. These investigations may provide valuable insights into potential applications in cattle health, the development of diagnostic tools for neurological disorders, and strategies for enhancing animal welfare.

      The third objective is to explore the potential applications of bovine NEFH in neurobiology and biotechnology. Research will investigate the use of bovine NEFH-expressing cells as models for studying neuronal-related diseases and for developing tissue engineering approaches in veterinary medicine and biotechnology.

      By delving into the functions and roles of NEFH in bovine nervous tissues, this research aims to expand our knowledge of neuronal biology, its implications for veterinary medicine, and its potential applications in neurobiology, cattle health, and biotechnology.

    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.

    Nefh Bovine
  • View Data Sheet

    Name :

    NUCB2 Human

    Description:

    Nucleobindin-2 Human Recombinant

    Nucleobindin-2, DNA-binding protein NEFA, Gastric cancer antigen Zg4, NUCB2, NEFA, Nesfatin.

    Product # :

    PRO-492

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    Description

    The Recombinant Human NUCB2 (Nesfatin) produced in E.coli has a molecular mass of 9.7kDa containing 82 amino acid residues of the human NUCB2.

    Source

    Escherichia Coli.

    Formulation

    The NUCB2 protein was lyophilized from a 0.2µm filtered concentrated solution in 1×PBS, pH 7.4.

    Purity

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

    More Info

    • Introduction

      Nucleobindin-2 (also known as NUCB2 or Nesfatin) is a EF-hand calcium-binding protein. Nucleobindin-2 takes part in calcium homeostasis and is a multifunctional protein that interacts with Ca(2+) nucleic acids & various regulatory proteins in different signaling pathways. NUCB2 (Nesfatin) is localized in neuronal perikarya and dendrites of mouse brain.

    • Synonyms

      Nucleobindin-2, DNA-binding protein NEFA, Gastric cancer antigen Zg4, NUCB2, NEFA, Nesfatin.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized NUCB2 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution NUCB2 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 NUCB2 in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      VPIDIDKTKV QNIHPVESAK IEPPDTGLYY DEYLKQVIDV LETDKHFREK LQKADIEEIK SGRLSKELDL VSHHVRTKLD EL.

    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.

    Nucb2 Human
  • View Data Sheet

    Name :

    NT 3 Human

    Description:

    Neurotrophin-3 Human Recombinant

    Neurotrophic factor, Nerve growth factor-2, NGF-2, HDNF, NT-3.

    Product # :

    CYT-257

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    Description

    Neurotrophin-3 Human Recombinant produced in E.Coli is a non-glycosylated and non-covalently linked homodimer, containing 2x120 amino acid chains, having a total Mw of 27.5 kDa. The NT-3 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Lyophilized from 0.1% TFA.

    Purity

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

    Biological Activity

    The ED50 as determined by the dose-dependent proliferation of neuroblastoma cell line expressing BR6 is 3.49 ng/ml.

    More Info

    • Introduction

      NT3 a member of the neurotrophin family, that controls survival and differentiation of mammalian neurons. This protein is closely related to both nerve growth factor and brain-derived neurotrophic factor. It may be involved in the maintenance of the adult nervous system, and may affect development of neurons in the embryo when it is expressed in human placenta. NTF3-deficient mice generated by gene targeting display severe movement defects of the limbs. The mature peptide of this protein is identical in all mammals examined including human, pig, rat and mouse.

    • Synonyms

      Neurotrophic factor, Nerve growth factor-2, NGF-2, HDNF, NT-3.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized NGF2 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution NGF-2 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 Neurotrophin-3 in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      MYAEHKSHRGE YSVCDSESLW VTDKSSAIDI RGHQVTVLGE IKTGNSPVKQ YFYETRCKEA RPVKNGCRGI DDKHWNSQCK TSQTYVRALT SENNKLVGWR WIRIDTSCVC ALSRKIGRT.

    • Protein content

      Protein quantitation was carried out by two independent methods:1. UV spectroscopy at 280 nm using the absorbency value of 2.165 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 NT-3 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.

    Neurotrophin 3 Human
  • View Data Sheet

    Name :

    NT 3 Mouse

    Description:

    Neurotrophin-3 Mouse Recombinant

    Neurotrophic factor, Nerve growth factor-2, NGF-2, HDNF, NT-3, Neurotrophin-3, Ntf3, Ntf-3, AI316846, AI835689, Nt3.

    Product # :

    CYT-688

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    Description

    Neurotrophin-3 Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 119 amino acids and having a molecular mass of 13.6kDa. The NT-3 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Lyophilized from 0.02% TFA.

    Purity

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

    Biological Activity

    The activity, as determined by the dose-dependent proliferation of BaF3 cells transfected with the TrkB receptor, is typically in the range of 1-10 ng/ml, corresponding to a specific activity of 100,000-1,000,000 units/mg.

    More Info

    • Introduction

      NT3 a member of the neurotrophin family, that controls survival and differentiation of mammalian neurons. This protein is closely related to both nerve growth factor and brain-derived neurotrophic factor. It may be involved in the maintenance of the adult nervous system, and may affect development of neurons in the embryo when it is expressed in human placenta. NTF3-deficient mice generated by gene targeting display severe movement defects of the limbs. The mature peptide of this protein is identical in all mammals examined including human, pig, rat and mouse.

    • Synonyms

      Neurotrophic factor, Nerve growth factor-2, NGF-2, HDNF, NT-3, Neurotrophin-3, Ntf3, Ntf-3, AI316846, AI835689, Nt3.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized NGF2 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution NGF-2 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 Neurotrophin-3 in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      YAEHKSHRGE YSVCDSESLW VTDKSSAIDI RGHQVTVLGE IKTGNSPVKQ YFYETRCKEA RPVKNGCRGI DDKHWNSQCK TSQTYVRALT SENNKLVGWR WIRIDTSCVC ALSRKIGRT.

    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.

    Neurotrophin 3 Mouse
  • View Data Sheet

    Name :

    bNGF Human, CHO

    Description:

    Beta-Nerve Growth Factor Human Recombinant, CHO

    Beta Polypeptide, NGF, NGFB, HSAN5, Beta-NGF, MGC161426, MGC161428.

    Product # :

    CYT-246

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    Description

    Nerve Growth Factor-beta Human Recombinant produced in CHO is a noncovalently disulfide linked homodimer, glycosylated, polypeptide chain (Ser122-Arg239) containing 2 identical 118 amino acids and having a molecular mass of 26.5 kDa.The NGF-b is purified by proprietary chromatographic techniques.

    Source

    Chinese Hamster Ovary Cells.

    Formulation

    The protein was lyophilized from a 0.2µm filtered solution in 20mM PB and 250mM NaCl, pH 7.0.

    Purity

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

    Biological Activity

    The ED50, calculated by its ability to stimulate chick E9 DRG neurite outgrowth was found to be < 1.0 ng/ml, corresponding to a specific activity of > 1 x 106 units/mg.

    More Info

    • Introduction

      NGF-beta has nerve growth stimulating activity and the complex is involved in the regulation of growth and the differentiation of sympathetic and certain sensory neurons. Mutations in this gene have been associated with hereditary sensory and autonomic neuropathy, type 5 (HSAN5), and dysregulation of this gene's expression is associated with allergic rhinitis.

    • Synonyms

      Beta Polypeptide, NGF, NGFB, HSAN5, Beta-NGF, MGC161426, MGC161428.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Amino Acid Sequence

      Was analyzed by Mass spectrometry.

    • Background

      What is the molecular weight/Mw of B NGF Protein?
      B NGF Protein has a total Mw of 26.5kDa.

      What is the source or expression system of B NGF Protein?
      Chinese Hamster Ovary Cells.

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

      What is the Biological Activity of B NGF Protein?
      The ED50, calculated by its ability to stimulate chick E9 DRG neurite outgrowth was found to be < 1.0 ng/ml, corresponding to a specific activity of > 1 x 106 units/mg.

      What is the amino acid sequence of B NGF Protein?
      B NGF Protein is composed from 118 amino acids.

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

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

    Beta Ngf Human Cho
  • View Data Sheet

    Name :

    GDNF Human

    Description:

    Glial-Derived Neurotrophic Factor Human Recombinant

    ATF1, ATF2, HFB1-GDNF, GDNF.

    Product # :

    CYT-305

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    • sds-page

    Description

    Glial derived Neurotrophic Factor Human Recombinant produced in E.Coli is a non-glycosylated disulfide-linked homodimer containing 2 x 135 amino acids and having a total molecular mass of approximately 30kDa. GDNF is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    GDNF was lyophilized from a 0.2µm filtered concentrated solution in 1×PBS, pH 7.4 and 5% Trehalose.

    Purity

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

    Biological Activity

    The ED50 was determined by the proliferation of rat C6 cells is < 0.1 ng/ml, corresponding to a specific activity of > 1.0x107 units/mg.

    sds-page

    GDNF sds-page - Product image 1

    More Info

    • Introduction

      GDNF promotes the survival and differentiation of minergic neurons in culture, and is able to prevent apoptosis of motor neurons induced by axotomy. The encoded protein is processed to a mature secreted form that exists as a homodimer. The mature form of the protein is a ligand for the product of the RET (rearranged during transfection) protooncogene. In addition to the transcript encoding GDNF, two additional alternative transcripts encoding distinct proteins, referred to as astrocyte-derived trophic factors, have also been described. Mutations in this gene may be associated with Hirschsprung disease.
      GDNF enhances survival and morphological differentiation of minergic neurons and increases their high-affinity uptake.

    • Synonyms

      ATF1, ATF2, HFB1-GDNF, GDNF.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Amino Acid Sequence

      SPDKQMAVLP RRERNRQAAA ANPENSRGKG RRGQRGKNRG CVLTAIHLNV TDLGLGYETK EELIFRYCSG SCDAAETTYD KILKNLSRNR RLVSDKVGQA CCRPIAFDDD LSFLDDNLVY HILRKHSAKR CGCI.

    • Background

      What is the molecular weight/Mw of GDNF HUMAN Protein?
      GDNF HUMAN Protein has a total Mw of 30kDa.

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

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

      What is the Biological Activity of GDNF HUMAN Protein?
      The ED50 was determined by the proliferation of rat C6 cells is < 0.1 ng/ml, corresponding to a specific activity of > 1.0x107 units/mg.

      What is the amino acid sequence of GDNF HUMAN Protein?
      SPDKQMAVLP RRERNRQAAA ANPENSRGKG RRGQRGKNRG CVLTAIHLNV TDLGLGYETK EELIFRYCSG SCDAAETTYD KILKNLSRNR RLVSDKVGQA CCRPIAFDDD LSFLDDNLVY HILRKHSAKR CGCI.
      What applications can GDNF HUMAN Protein be used in?
      GDNF HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.

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

    Gdnf Human
  • View Data Sheet

    Name :

    b NGF Human

    Description:

    Beta Nerve Growth Factor Human Recombinant

    Beta Polypeptide, NGF, NGFB, HSAN5, Beta-NGF, MGC161426, MGC161428.

    Product # :

    CYT-579

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    Description

    Nerve Growth Factor-beta Human Recombinant produced in E.Coli is a non-covalently disulfide-linked homodimer, non-glycosylated, polypeptide chain containing 2 identical 121 amino acids with a molecular weight of two 13.6 kDa polypeptide monomers.The NGF-b is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The beta-NGF protein was lyophilized from a 0.2µm filtered solution containing 0.1% Trifluoroacetic Acid (TFA).

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Biological Activity

    The ED50, calculated by its ability to stimulate proliferation of TF-1 cells and is typically 1.31 ng/ml, corresponding to a specific activity of 7.6x105units/mg.

    More Info

    • Introduction

      NGF-beta has nerve growth stimulating activity and the complex is involved in the regulation of growth and the differentiation of sympathetic and certain sensory neurons. Mutations in this gene have been associated with hereditary sensory and autonomic neuropathy, type 5 (HSAN5), and dysregulation of this gene's expression is associated with allergic rhinitis.

    • Synonyms

      Beta Polypeptide, NGF, NGFB, HSAN5, Beta-NGF, MGC161426, MGC161428.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Amino Acid Sequence

      MSSSHPIFHRG EFSVCDSVSV WVGDKTTATD IKGKEVMVLG EVNINNSVFK QYFFETKCRD PNPVDSGCRG IDSKHWNSYC TTTHTFVKAL TMDGKQAAWR FIRIDTACVC VLSRKAVRRA.

    • Background

      What is the molecular weight/Mw of B NGF Protein?
      B NGF Protein has a total Mw of 13.6kDa.

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

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

      What is the Biological Activity of B NGF Protein?
      The ED50, calculated by its ability to stimulate proliferation of TF-1 cells and is typically 1.31 ng/ml, corresponding to a specific activity of 7.6x105units/mg.

      What is the amino acid sequence of B NGF Protein?
      MSSSHPIFHRG EFSVCDSVSV WVGDKTTATD IKGKEVMVLG EVNINNSVFK QYFFETKCRD PNPVDSGCRG IDSKHWNSYC TTTHTFVKAL TMDGKQAAWR FIRIDTACVC VLSRKAVRRA.

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

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

    Beta Ngf Human
  • View Data Sheet

    Name :

    NGB Human

    Description:

    Neuroglobin Human Recombinant

    NGB.

    Product # :

    CYT-450

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    • More Info

    Description

    17kDa protein containing 151 amino acid residues of the Neuroglobin human.

    Source

    Escherichia Coli.

    Formulation

    Filtered and lyophilized from 0.5mg/ml in 0.05M phosphate buffer, 0.1M NaCl, pH 7.2.

    Purity

    Greater than 95% as determined by SDS-PAGE.

    More Info

    • Introduction

      Neuroglobin, 151 amino acid residue protein, mainly expressed in vertebrate brain and retina, is a recently identified member of the globin superfamily. Augmenting O (2) supply, neuroglobin promotes survival of neurons upon hypoxic injury, potentially limiting brain damage. Moreover, neuroglobin may be a novel oxidative stress-responsive sensor for signal transduction in the brain. Neuroglobin expression is increased by neuronal hypoxia in vitro and focal cerebral ischemia in vivo, and neuronal survival after hypoxia is reduced by inhibiting neuroglobin expression with an antisense oligodeoxynucleotide and enhanced by neuroglobin overexpression.

    • Synonyms

      NGB.

    • 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

      Add H2O and let the lyophilized pellet dissolve completely.

    • Amino Acid Sequence

      MERPEPELIR QSWRAVSRSP LEHGTVLFAR LFALEPDLLP LFQYNCRQFS SPEDCLSSPE FLDHIRKVML VIDAAVTNVE DLSSLEEYLA SLGRKHRAVG VKLSSFSTVG ESLLYMLEKC LGPAFTPATR AAWSQLYGAV VQAMSRGWDG E.

    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.

    Neuroglobin Human
  • View Data Sheet

    Name :

    MTPN Human

    Description:

    Myotrophin Human Recombinant

    Protein V-1, GCDP, Myotrophin, FLJ31098, FLJ99857.

    Product # :

    CYT-723

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    Description

    MTPN Recombinant Human produced in E.Coli is a single, non-glycosylated polypeptide chain containing 138 amino acids (1-118 a.a.) and having a molecular mass of 15 kDa. The MTPN is fused to 20 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    MTPN Human solution containing 20mM Tris-HCl pH-8 and 10% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      MTPN is an ankyrin repeat protein, that stimulates protein synthesis and cardiomyocyte growth to commence cardiac hypertrophy by activating the NF-kappaB signaling cascade. Myotrophin participates in cerebellar morphogenesis and takes part in differentiation of cerebellar neurons, particularly of granule cells. High levels of MTPN are expressed in human dilated cardiomyopathic and ischemic hearts.

    • Synonyms

      Protein V-1, GCDP, Myotrophin, FLJ31098, FLJ99857.

    • 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 MCDKEFMWAL KNGDLDEVKD YVAKGEDVNR TLEGGRKPLH YAADCGQLEI LEFLLLKGAD INAPDKHHIT PLLSAVYEGH VSCVKLLLSK GADKTVKGPD GLTAFEATDN QAIKALLQ.

    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.

    Mtpn Human
  • View Data Sheet

    Name :

    NTRK2 Mouse

    Description:

    Neurotrophic Receptor Tyrosine Kinase 2 Mouse Recombinant

    TrkB, NTRK2, NTRK-2, Tyrosine Kinase Receptor B, BDNF/NT-3 Growth Factors Receptor

    Product # :

    CYT-919

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    Description

    NTRK2 Mouse produced in Sf9 Insect cells is a single, glycosylated polypeptide chain containing 409 amino acids (32-429a.a.) and having a molecular mass of 45.7kDa (Molecular size on SDS-PAGE will appear at approximately 57-70kDa under reducing conditions).NTRK2 Mouse is expressed with an 11 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Insect cells.

    Formulation

    NTRK2 Mouse protein solution (0.5mg/ml) contains PBS pH 7.4 and 10% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      NTRK2 plays a role in the growth and the development of the central and the peripheral nervous systems using the regulation of neuron proliferation, migration, survival, differentiation, and synapse production. NTRK2 is a receptor for B-DNF and NT4. NTRK2 binds to neurotrophin-3 which regulates neuron survival through NTRK2. NTRK-2 activates numerous effectors such as SHC-1, SH2B-1, PLCG-1 and SH2B-2 that control overlapping signaling cascades.

    • Synonyms

      TrkB, NTRK2, NTRK-2, Tyrosine Kinase Receptor B, BDNF/NT-3 Growth Factors Receptor

    • 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

      CPTSCKCSSA RIWCTEPSPG IVAFPRLEPN SVDPENITEI LIANQKRLEI INEDDVEAYV GLRNLTIVDS GLKFVAYKAF LKNSNLRHIN FTRNKLTSLS RRHFRHLDLS DLILTGNPFT CSCDIMWLKT LQETKSSPDT QDLYCLNESS KNMPLANLQI PNCGLPSARL AAPNLTVEEG KSVTLSCSVG GDPLPTLYWD VGNLVSKHMN ETSHTQGSLR ITNISSDDSG KQISCVAENL VGEDQDSVNL TVHFAPTITF LESPTSDHHW CIPFTVRGNP KPALQWFYNG AILNESKYIC TKIHVTNHTE YHGCLQLDNP THMNNGDYTL MAKNEYGKDE RQISAHFMGR PGVDYETNPN YPEVLYEDWT TPTDIGDTTN KSNEIPSTDV ADQSNREHAA ALEHHHHHH.

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

    Bdnf Mouse
  • View Data Sheet

    Name :

    NXPH1 Human, Sf9

    Description:

    Neurexophilin 1 Human Recombinant, Sf9

    NXPH1, Nbla00697, NPH1 , Neurexophilin-1, Neurexophilin 1.

    Product # :

    PRO-2418

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    Description

    NXPH1 Human Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 259 amino acids (22-271) and having a molecular mass of 29.7kDa (Molecular size on SDS-PAGE will appear at approximately 28-40kDa).NXPH1 is fused to 9 amino acid His-Tag at C-terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    NXPH1 protein solution (0.5mg/ml) containing Phosphate Buffered Saline (pH 7.4) and 10% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Neurexophilin 1 (NXPH1) is a part of the neurexophilin family which encodes a secreted protein with a variable N terminal domain, an extremely conserved, N-glycosylated central domain, a short linker region, and a cysteine-rich Cterminal domain. NXPH1 shapes a very tight complex with alpha neurexins, a group of proteins which promote adhesion among dendrites and axons.

    • Synonyms

      NXPH1, Nbla00697, NPH1 , Neurexophilin-1, Neurexophilin 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

      ADPANLTNGG KSELLKSGSS KSTLKHIWTE SSKDLSISRL LSQTFRGKEN DTDLDLRYDT PEPYSEQDLW DWLRNSTDLQ EPRPRAKRRP IVKTGKFKKM FGWGDFHSNI KTVKLNLLIT GKIVDHGNGT FSVYFRHNST GQGNVSVSLV PPTKIVEFDL AQQTVIDAKD SKSFNCRIEY EKVDKATKNT LCNYDPSKTC YQEQTQSHVS WLCSKPFKVI CIYISFYSTD YKLVQKVCPD YNYHSDTPYF PSGHHHHHH.

    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.

    Nxph1 Human Sf9
  • View Data Sheet

    Name :

    Beta NGF Mouse

    Description:

    Beta Nerve Growth Factor Mouse Recombinant

    Beta Polypeptide, NGF, NGFB, HSAN5, Beta-NGF, MGC161426, MGC161428.

    Product # :

    CYT-581

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    Description

    Recombinant Mouse b-NGF produced in E.Coli is a noncovalently disulfide-linked homodimer, non-glycosylated, polypeptide chain containing 2 identical chains of 120 amino acids each and having a molecular mass of 13,471 Dalton each.The Recombinant Mouse-beta-NGF is purified by advanced biology purification technology.

    Source

    Escherichia Coli.

    Formulation

    The Recombinant Mouse b-NGF was lyophilized without additives.

    Purity

    Greater than 98% as determined by:
    (a) Analysis by RP-HPLC.
    (b) Analysis by SDS-PAGE .

    Biological Activity

    The Mouse b-NGF activity was measured in a cell proliferation assay using a factor-dependent human erythroleukemic cell line, TF-1, the ED50 for this effect is 0.2 ng/ml, corresponding to a Specific Activity of 5,000,000 units/mg.

    More Info

    • Introduction

      NGF-beta has nerve growth stimulating activity and the complex is involved in the regulation of growth and the differentiation of sympathetic and certain sensory neurons. Mutations in this gene have been associated with hereditary sensory and autonomic neuropathy, type 5 (HSAN5), and dysregulation of this gene's expression is associated with allergic rhinitis. Nerve Growth Factor was the 1st protein found from the family of neurotrophic factors that influence the growth and differentiation of sympathetic and sensory neurons. NGF consists of 3 different subunits: alpha, beta, and gamma. The beta subunit is accountable for its growth stimulating activity. The synthesis of NGF in astrocytes is enhanced by a range of cytokines such as IL1, TNF-a, PDGF & TGF-b.

    • Synonyms

      Beta Polypeptide, NGF, NGFB, HSAN5, Beta-NGF, MGC161426, MGC161428.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Amino Acid Sequence

      MSSTHPVFHM GEFSVCDSVS VWVGDKTTAT DIKGKEVTVL AEVNINNSVF RQYFFETKCR ASNPVESGCR GIDSKHWNSY CTTTHTFVKA LTTDEKQAAW RFIRIDTACV CVLSRKATRR G.

    • Background

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

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

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

      What is the Biological Activity of B NGF Protein?
      The Mouse b-NGF activity was measured in a cell proliferation assay using a factor-dependent human erythroleukemic cell line, TF-1, the ED50 for this effect is 0.2 ng/ml, corresponding to a Specific Activity of 5,000,000 units/mg.


      What is the amino acid sequence of B NGF Protein?
      MSSTHPVFHM GEFSVCDSVS VWVGDKTTAT DIKGKEVTVL AEVNINNSVF RQYFFETKCR ASNPVESGCR GIDSKHWNSY CTTTHTFVKA LTTDEKQAAW RFIRIDTACV CVLSRKATRR G.

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

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

    Beta Ngf Mouse Recombinant
  • View Data Sheet

    Name :

    b NGF Human, HEK

    Description:

    beta Nerve Growth Factor Human Recombinant, HEK

    Beta Polypeptide, NGF, NGFB, HSAN5, Beta-NGF, MGC161426, MGC161428.

    Product # :

    CYT-079

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    Description

    BNGF Human Recombinant produced in HEK293 is a noncovalently disulfide linked homodimer, glycosylated, polypeptide chain (Ser122-Arg239) containing 2 identical 118 amino acids and having a molecular mass of 26.5 kDa.

    Source

    HEK293 cells.

    Formulation

    The b-NGF was lyophilized from 1mg/ml in 20mM PB and 0.25M NaCl pH-7.5.

    Purity

    Greater than 97% as obsereved by SDS-PAGE.

    Biological Activity

    The specific activity was determined by the dose-dependent stimulation of the proliferation of human TF-1 cells (human erythroleukemic indicator cell line), the ED50 is <0.04-0.4ng/ml.

    More Info

    • Introduction

      NGF-beta has nerve growth stimulating activity and the complex is involved in the regulation of growth and the differentiation of sympathetic and certain sensory neurons. Mutations in this gene have been associated with hereditary sensory and autonomic neuropathy, type 5 (HSAN5), and dysregulation of this gene's expression is associated with allergic rhinitis.

    • Synonyms

      Beta Polypeptide, NGF, NGFB, HSAN5, Beta-NGF, MGC161426, MGC161428.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized b-NGF although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution b-NGF 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 b-NGF in sterile distilled pyrogen free water at a concentration of 0.25mg/ml.

    • Background

      What is the molecular weight/Mw of B NGF Protein?
      B NGF Protein has a total Mw of 26.5kDa.

      What is the source or expression system of B NGF Protein?
      HEK293 cells.

      What is the Purity of B NGF Protein?

      B NGF Protein is >97% pure as determined by SDS-PAGE.

      What is the Biological Activity of B NGF Protein?
      The specific activity was determined by the dose-dependent stimulation of the proliferation of human TF-1 cells (human erythroleukemic indicator cell line), the ED50 is <0.04-0.4ng/ml.

      What is the amino acid sequence of B NGF Protein?
      B NGF Protein is composed from 118 amino acids.

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

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

    B Ngf Human Hek
  • View Data Sheet

    Name :

    GDNF Mouse

    Description:

    Glial-Derived Neurotrophic Factor Mouse Recombinant

    ATF1, ATF2, HFB1-GDNF, GDNF.

    Product # :

    CYT-243

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    Description

    Glial derived Neurotrophic Factor Mouse Recombinant produced in E.Coli is a non-glycosylated homodimer containing 2 x 135 amino acids and having a total molecular mass of 30.2kDa. GDNF is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    GDNF was lyophilized with no additives.

    Purity

    Greater than 98.0% as determined by analysis by SDS-PAGE.

    Biological Activity

    The ED50 as determined by the dose-dependent proliferation of C6 cells, is 0.8-0.12µg/ml.

    More Info

    • Introduction

      GDNF promotes the survival and differentiation of neurons in culture, and is able to prevent apoptosis of motor neurons induced by axotomy. The encoded protein is processed to a mature secreted form that exists as a homodimer. The mature form of the protein is a ligand for the product of the RET (rearranged during transfection) protooncogene. In addition to the transcript encoding GDNF, two additional alternative transcripts encoding distinct proteins, referred to as astrocyte-derived trophic factors, have also been described. Mutations in this gene may be associated with Hirschsprung disease.
      GDNF enhances survival and morphological differentiation of neurons and increases their high-affinity uptake.

    • Synonyms

      ATF1, ATF2, HFB1-GDNF, GDNF.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Amino Acid Sequence

      MSPDKQAAL PRRENRNRQAA AASPENSRGK GRRGQRGKNR GCVLTAIHLN VTDLGLGYET KEELIFRYCS GSCESAETMY DKILKNLSRS RRLTSDKVGQ ACCRPVAFDD DLSFLDDNLV YHILRKHSAK RCGCI.

    • Background

      What is the molecular weight/Mw of GDNF MOUSE Protein?
      GDNF MOUSE Protein has a total Mw of 30.2kDa.

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

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

      What is the Biological Activity of GDNF MOUSE Protein?
      The ED50 as determined by the dose-dependent proliferation of C6 cells, is 0.8-0.12µg/ml.

      What is the amino acid sequence of GDNF MOUSE Protein?
      MSPDKQAAL PRRENRNRQAA AASPENSRGK GRRGQRGKNR GCVLTAIHLN VTDLGLGYET KEELIFRYCS GSCESAETMY DKILKNLSRS RRLTSDKVGQ ACCRPVAFDD DLSFLDDNLV YHILRKHSAK RCGCI.
      What applications can GDNF MOUSE Protein be used in?
      GDNF MOUSE Protein can probably be used in western blot, ELISA and Lateral Flow.

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

    Gdnf Mouse
  • View Data Sheet

    Name :

    VAMP8 Human

    Description:

    Endobrevin Human Recombinant

    VAMP8, VAMP-8, Endobrevin, Vesicle-Associated Membrane Protein 8, EDB.

    Product # :

    PRO-660

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    Description

    VAMP8 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 96 amino acids (1-76 a.a.) and having a molecular mass of 10.9 kDa. The VAMP8 is fused to a 20 amino acid His Tag at N-terminus and purified by proprietary chromatography techniques.

    Source

    Escherichia Coli.

    Formulation

    The VAMP8 protein solution (0.25mg/ml) contains 20mM Tris pH-8, 0.1mM PMSF, 0.2M NaCl and 50% glycerol.

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      VAMP8 also called endobrevin, is the main component of a SNARE complex involved in the docking and fusion of synaptic vesicles with the presynaptic membrane. VAMP8 protein is involved in the regulatation of enzyme secretion in pancreatic acinar cells and plays a part in the abscission of the midbody during cell division, which leads to completely separate daughter cells. VAMP8 is essential for dense-granule secretion in platelets. VAMP8 is related with the perinuclear vesicular structures of the early endocytic compartment. VAMP8 interacts particularly with the soluble NSF-attachment protein (alpha-SNAP), through an VAMP8-containing SNARE complex.

    • Synonyms

      VAMP8, VAMP-8, Endobrevin, Vesicle-Associated Membrane Protein 8, EDB.

    • Physical Appearance

      Sterile Filtered colorless solution.

    • Stability

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

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MEEASEGGGN DRVRNLQSEV EGVKNIMTQN VERILARGEN LEHLRNKTED LEATSEHFKT TSQKVARKFW WKNVKM.

    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.

    Vamp8 Human
  • View Data Sheet

    Name :

    Ferritin Human

    Description:

    Human Liver Ferritin

    Product # :

    PRO-564

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    Description

    Ferritin is a glycoprotein produced in Human Liver having a molecular mass of 440- 450kDa and pI of 5.5, which stores iron atoms in the ferric state. It is predominantly intracellular, where it forms an exchangeable pool of iron acting as an iron store. Ferritin level in serum is directly proportional to body iron stores and serum levels are an excellent indicator in monitoring iron status in anemia. It can be used as a marker for inflammation and also used for monitoring and prediction of future events in coronary artery disease.

    Source

    Human Liver.

    Formulation

    The protein solution is in 0.05M TRIS buffer pH 7.5 containing 1.0M NaCl and 0.09% NaN3.

    Purity

    Greater than 96.0%.

    More Info

    • Introduction

      Ferritin is the main intracellular iron storage protein in prokaryotes and eukaryotes. Ferritin’s major functions are the storage of iron in a soluble and nontoxic state and its release in a controlled fashion. An iron-containing protein complex is found mostly in the intestinal mucosa, spleen, and liver. Ferritin is composed of 24 subunits of the heavy and light chains. Variation in ferritin subunit composition may influence the rates of iron uptake and release in different tissues. Defects in the light chain ferritin gene are linked to a number of neurodegenerative diseases and hyperferritinemia-cataract syndrome. The genes that encode the light and heavy chains are on located different chromosomes. The light chain genes are in chromosome region 19q13.3-q13.4 whilst those for the heavy chain are in chromosome region 11q12-q13. Ferritin is shaped like a hollow sphere, inside which the iron is stored in the Fe(III) oxidation state. The iron is integrated in the mineral ferrihydrite, [FeO(OH)]8[FeO(H2PO4)], which is attached to the inner wall of the sphere. To release iron once the body needs it, the iron must be altered from the Fe(III) to the Fe(II) oxidation state. Subsequently, the iron leaves through channels in the spherical structure. Therefore, the structure of ferritin is tremendously important for the protein's ability to store and release iron in a controlled mode.
      The amount of ferritin in the blood (serum ferritin level) is directly related to the amount of iron stored in the body. The body has a "buffer" against iron deficiency (if the blood has too little iron, ferritin can release more) and, to a lesser extent, iron overload (if the blood and tissues of the body have too much iron, ferritin can help store the excess iron).

    • Physical Appearance

      Sterile Filtered brownish solution.

    • Stability

      Human Ferritin should be stored at 2-8°C.

    • Human Virus Test

      Tissue sample tested and found negative for HIV-1 & 2 antibodies, Hepatatis B surface antigen, Syphilis RPR and Hepatatis C antibodies.

    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.

    Ferritin Human
  • View Data Sheet

    Name :

    MANF Human, His

    Description:

    Mesencephalic Astrocyte-Derived Neurotrophic Factor Human Recombinant, His Tag

    Mesencephalic astrocyte-derived neurotrophic factor, Protein ARMET, ARP, arginine-rich mutated in early stage tumors, Arginine-rich protein.

    Product # :

    CYT-133

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    Description

    MANF Human Recombinant produced in E. coli is a single polypeptide chain containing 183 amino acids (25-182) and having a molecular mass of 20.8kDa.MANF is fused to a 25 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    The MANF solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 100mM NaCl, 1mM DTT and 10% glycerol.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    More Info

    • Introduction

      MANF is a 20kDa protein which belongs to the ARMET family. MANF was originally known as an arginine-rich region protein which was extremely mutated in a large number of tumors. MANF Expression is induced during ER stress, signifying that MANF takes part in protein quality control during ER stress.

    • Synonyms

      Mesencephalic astrocyte-derived neurotrophic factor, Protein ARMET, ARP, arginine-rich mutated in early stage tumors, Arginine-rich 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 MGSHMLRPGD CEVCISYLGR FYQDLKDRDV TFSPATIENE LIKFCREARG KENRLCYYIG ATDDAATKII NEVSKPLAHH IPVEKICEKL KKKDSQICEL KYDKQIDLST VDLKKLRVKE LKKILDDWGE TCKGCAEKSD YIRKINELMP KYAPKAASAR TDL

    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.

    Manf Human
  • View Data Sheet

    Name :

    NT 4 Human

    Description:

    Neurotrophin-4 Human Recombinant

    NT4, NT5, NTF5, NT-4/5, NTF4, Neurotrophin-4, Neutrophic factor 4, Neurotrophin-5, NT-5.

    Product # :

    CYT-626

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    Description

    Neurotrophin-4 Human Recombinant produced in E.Coli is a noncovalently linked homodimer, non-glycosylated polypeptide chain containing 2 x 130 amino acids (81-210 amino acids) and having a total molecular mass of 28 kDa. The NT-4 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Lyophilized from a concentrated (1mg/ml) solution in water containing 20mM phosphate buffer pH-7.4 and 150mM NaCl.

    Purity

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

    Biological Activity

    Determined by the dose-dependent induction of choline acetyl transferase activity in rat basal forebrain primary septal cell cultures was found to be in the range of 20-50 ng/ml.

    More Info

    • Introduction

      NT-4 is part of the family of neurotrophic factors, neurotrophins, that are in charge for the survival and differentiation of mammalian neurons. NT-4 expression is dominant and less influenced by environmental signals. NT-4 deficient mice shows slight cellular deficits and develop normally to adulthood. NT-4 is a target-derived survival factor for peripheral sensory sympathetic neurons.NT-4 is involved in the proliferation and differentiation of periodontal ligament cells.

    • Synonyms

      NT4, NT5, NTF5, NT-4/5, NTF4, Neurotrophin-4, Neutrophic factor 4, Neurotrophin-5, NT-5.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Amino Acid Sequence

      GVSETAPASR RGELAVCDAV SGWVTDRRTA VDLRGREVEV LGEVPAAGGS PLRQYFFETR CKADNAEEGG PGAGGGGCRG VDRRHWVSEC KAKQSYVRAL TADAQGRVGW RWIRIDTACV CTLLSRTGRA.

    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.

    Nt 4 Human
  • View Data Sheet

    Name :

    NREP Human

    Description:

    Neuronal Regeneration Related Protein Human Recombinant

    Neuronal regeneration-related protein, Neuronal protein 3.1, Protein p311, NREP, C5orf13, P311, PTZ17, Chromosome 5 Open Reading Frame 13, Neuronal Regeneration Related Protein Homolog (Rat), D4S114, PRO1873, SEZ17, Neuronal Regeneration Related Protein Homolog, Neuronal Regeneration-Related Protein.

    Product # :

    PRO-1780

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    Description

    NREP Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 91 amino acids (1-68) and having a molecular mass of 10.3kDa.NREP is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The NREP solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH8.0), 10% glycerol and 0.1M NaCl.

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Neuronal Regeneration Related Protein (NREP) has roles in neural function. NREP promotes axonal regeneration. In addition, NREP has functions in cellular differentiation. NREP protein induces differentiation of fibroblast into myofibroblast and increases retinoic-acid regulation of lipid-droplet biogenesis. NREP down-regulates the expression of TGFB1 and TGFB2 but not of TGFB3. NREP has a role in the regulation of alveolar generation.

    • Synonyms

      Neuronal regeneration-related protein, Neuronal protein 3.1, Protein p311, NREP, C5orf13, P311, PTZ17, Chromosome 5 Open Reading Frame 13, Neuronal Regeneration Related Protein Homolog (Rat), D4S114, PRO1873, SEZ17, Neuronal Regeneration Related Protein Homolog, Neuronal Regeneration-Related 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 MGSMVYYPEL FVWVSQEPFP NKDMEGRLPK GRLPVPKEVN RKKNDETNAA SLTPLGSSEL RSPRISYLHF F.

    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.

    Nrep Human
  • View Data Sheet

    Name :

    CNTF Rat

    Description:

    Ciliary Neurotrophic Factor Rat Recombinant

    HCNTF, CNTF, Ciliary Neurotrophic Factor.

    Product # :

    CYT-654

    Price :

    Quantity :

    Shipping Method :

    Room Temp Icon

    Shipped at Room temp

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    More Info

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

    Description

    CNTF Recombinant Rat produced in E.Coli is a single, non-glycosylated polypeptide chain containing 200 amino acids and having a molecular mass of 22834 Dalton. The CNTF is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Lyophilized from a concentrated (1mg/ml) solution in water containing 0.025% NaHCO3.

    Purity

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

    Biological Activity

    Fully biologically active by its ability to phosphorylate STAT3 in several cells lines.

    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 CNTF 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 CNTF 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

      AFAEQTPLTL HRRDLSSRSIWLARKIRSDLTALMESYVKHQGLNKNI
      NLDSVDGVPVASTDRWSEMTEAERLQENLQAYRTFQGMLTKLLEDQRV
      HFTPTEGDFHQAIHTLMLQVSAFAYQLEELMVLLEQKIPENEADGMPA
      TVGDGGLFEKKLWGLKVLQELSQWTVRSIHDLRVISSHQMGISALESH
      YGAKDKQM.

    • Background

      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 >99% pure as determined by SDS-PAGE.

      What is the Biological Activity of CNTF Protein?
      Fully biologically active by its ability to phosphorylate STAT3 in several cells lines.
      What is the amino acid sequence of CNTF Protein?
      AFAEQTPLTL HRRDLSSRSIWLARKIRSDLTALMESYVKHQGLNKNI
      NLDSVDGVPVASTDRWSEMTEAERLQENLQAYRTFQGMLTKLLEDQRV
      HFTPTEGDFHQAIHTLMLQVSAFAYQLEELMVLLEQKIPENEADGMPA
      TVGDGGLFEKKLWGLKVLQELSQWTVRSIHDLRVISSHQMGISALESH YGAKDKQM.


      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.

    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 Rat
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