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Search results

1000 results found for “RASSF”

Name

Description

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  • View Data Sheet

    Name :

    NSDHL Human

    Description:

    NAD (P) Dependent Steroid Dehydrogenase-Like Human Recombinant

    H105E3, SDR31E1, XAP104, Sterol-4-alpha-carboxylate 3-dehydrogenase, decarboxylating, Protein H105e3, NSDHL.

    Product # :

    PRO-1800

    Price :

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    Description

    NSDHL Human Recombinant produced in E. coli is a single polypeptide chain containing 320 amino acids (1-297) and having a molecular mass of 35.5kDa. NSDHL is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The NSDHL solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH8.0), 10% glycerol and 0.1M NaCl.

    Purity

    Greater than 80% as determined by SDS-PAGE.

    More Info

    • Introduction

      NAD (P) Dependent Steroid Dehydrogenase-Like (NSDHL) takes part in synthesis of cholesterol. NSDHL is involved in one of a few steps which convert lanosterol to cholesterol by removing a carbon atom and three hydrogen atoms (a methyl group). NSDHL is also a vital element of cell membranes and myelin, the fatty covering that insulates nerve cells.

    • Synonyms

      H105E3, SDR31E1, XAP104, Sterol-4-alpha-carboxylate 3-dehydrogenase, decarboxylating, Protein H105e3, NSDHL.

    • 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 MGSMEPAVSE PMRDQVARTH LTEDTPKVNA DIEKVNQNQA KRCTVIGGSG FLGQHMVEQL LARGYAVNVF DIQQGFDNPQ VRFFLGDLCS RQDLYPALKG VNTVFHCASP PPSSNNKELF YRVNYIGTKN VIETCKEAGV QKLILTSSAS VIFEGVDIKN GTEDLPYAMK PIDYYTETKI LQERAVLGAN DPEKNFLTTA IRPHGIFGPR DPQLVPILIE AARNGKMKFV IGNGKNLVDF TFVENVVHGH ILAAEQLSRD STLGGKAFHI TNDEPIPFWT FLSRILTGLN YEAPKYHIPY.

    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.

    Nsdhl Human
  • View Data Sheet

    Name :

    GDF6 Human

    Description:

    Bone Morphogenetic protein-13 Human Recombinant

    Growth Differentiation Factor 6, Growth/Differentiation Factor 16, Bone Morphogenetic Protein 13, BMP-13, BMP13, GDF-6, Klippel-Feil Malformation, Segmentation Syndrome 1, Klip-Feil Malformation, Klippel-Feil Syndrome, MCOPCB6, SCDO4, CDMP2, LCA17, MCOP4, GDF16, KFS1, KFSL, SGM1, KFM, KFS, GDF6.

    Product # :

    CYT-938

    Price :

    Quantity :

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    Description

    BMP13 Human Recombinant produced in E.coli is a non-glycosylated disulfide linked homodimer containing 2 chains of 120 amino acids and having a molecular mass of 27.1kDa.The BMP-13 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    BMP-13 protein was lyophilized from a 0.2µm filtered concentrated solution in 30% Acetonitrile and 0.1% TFA.

    Purity

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

    Biological Activity

    The ED50 as determined by inducing alkaline phosphatase production of murine ATDC5 cells is less than 2.0µg/ml, corresponding to a specific activity of > 500IU/mg.

    More Info

    • Introduction

      Growth/differentiation factors (GDF1-GDF15) belong to the BMP family of TGF-beta superfamily proteins. These factors are produced as inactive preproproteins which are subsequently cleaved and assembled into active secreted homodimers. BMP13 is a growth factor which controls proliferation and cellular differentiation in the retina and bone formation. BMP13 has a central role in regulating apoptosis during retinal development. GDF proteins are vital during embryonic development, particularly in the skeletal, nervous, and muscular systems. BMP13 gene mutations result in colobomata, which are congenital abnormalities in ocular development, and in Klippel-Feil syndrome (KFS), which is a congenital disorder of spinal segmentation.

    • Synonyms

      Growth Differentiation Factor 6, Growth/Differentiation Factor 16, Bone Morphogenetic Protein 13, BMP-13, BMP13, GDF-6, Klippel-Feil Malformation, Segmentation Syndrome 1, Klip-Feil Malformation, Klippel-Feil Syndrome, MCOPCB6, SCDO4, CDMP2, LCA17, MCOP4, GDF16, KFS1, KFSL, SGM1, KFM, KFS, GDF6.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized BMP13 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution BMP-13 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 BMP13 in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      TAFASRHGKR HGKKSRLRCS KKPLHVNFKE LGWDDWIIAP LEYEAYHCEG VCDFPLRSHL EPTNHAIIQT LMNSMDPGST PPSCCVPTKL TPISILYIDA GNNVVYKQYE DMVVESCGCR.

    • Background

      Bone Morphogenetic Protein-13 Human Recombinant: Unraveling its Potential in Tissue Engineering and Regenerative Medicine

      Abstract:

      Bone Morphogenetic Protein-13 (BMP-13) human recombinant is a pivotal member of the bone morphogenetic protein family, known for its crucial role in tissue development, regeneration, and repair. This research paper aims to provide a comprehensive analysis of BMP-13, including its characteristics, signaling pathways, and potential therapeutic applications. Furthermore, innovative methodologies for the production and optimization of BMP-13 human recombinant are proposed, shedding light on its future implications in the field of tissue engineering and regenerative medicine.

      Introduction:

      Tissue engineering and regenerative medicine hold great promise in addressing tissue repair and regeneration challenges. BMP-13, a prominent member of the BMP family, plays a vital role in orchestrating cellular responses during tissue development and healing. This paper explores the distinctive features of BMP-13 and presents novel approaches for the production and optimization of BMP-13 human recombinant, aiming to unlock its therapeutic potential in various regenerative contexts.

      Characteristics and Signaling Pathways:

      BMP-13 is a secreted growth factor belonging to the transforming growth factor-beta (TGF-β) superfamily. It exerts its biological effects by binding to specific cell surface receptors, initiating intricate intracellular signaling cascades. BMP-13 signaling pathways, including Smad-dependent and Smad-independent pathways, regulate critical processes such as cell differentiation, proliferation, and extracellular matrix synthesis, influencing tissue development and repair.

      Production of BMP-13 Human Recombinant:

      Efficient production methodologies are crucial for harnessing the therapeutic potential of BMP-13 human recombinant. Various recombinant protein expression systems, such as mammalian cells or baculovirus-insect cell systems, have been utilized for the production of functional BMP-13. Optimization strategies, including codon optimization, signal peptide engineering, and protein folding enhancement, have been employed to improve the yield and bioactivity of BMP-13 recombinant protein.

      Potential Therapeutic Applications:

      BMP-13 human recombinant holds immense promise in the field of tissue engineering and regenerative medicine. Its involvement in cartilage formation, osteogenesis, and tissue repair makes it a potential candidate for the treatment of musculoskeletal disorders, joint injuries, and cartilage defects. Furthermore, the ability of BMP-13 to modulate cell behavior and tissue remodeling indicates its wider therapeutic applications in diverse regenerative processes.

      Conclusion:

      BMP-13 human recombinant emerges as a crucial regulator in tissue engineering and regenerative medicine, offering significant potential for tissue repair and regeneration. Optimizing production methodologies and further unraveling its signaling mechanisms will undoubtedly enhance its therapeutic applications. Given its involvement in cartilage and bone formation, as well as tissue repair, BMP-13 human recombinant represents a valuable tool for promoting tissue regeneration and addressing the unmet clinical needs in regenerative medicine.

      What is the molecular weight/Mw of GDF6 Protein?
      GDF6 Protein has a total Mw of 27.1kDa.

      What is the source or expression system of GDF6 Protein?
      Escherichia Coli.

      What is the Purity of GDF6 Protein?
      GDF6 Protein is >95% pure as determined by SDS-PAGE.

      What is the Biological Activity of GDF6 Protein?
      The ED50 as determined by inducing alkaline phosphatase production of murine ATDC5 cells is less than 2.0µg/ml, corresponding to a specific activity of > 500IU/mg.

      What is the amino acid sequence of GDF6 Protein?
      TAFASRHGKR HGKKSRLRCS KKPLHVNFKE LGWDDWIIAP LEYEAYHCEG VCDFPLRSHL EPTNHAIIQT LMNSMDPGST PPSCCVPTKL TPISILYIDA GNNVVYKQYE DMVVESCGCR.

      What applications can GDF6 Protein be used in?
      GDF6 Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for GDF6 Protein?

      The endotoxin level is minimal, GDF6 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.

    Bmp13 Human
  • View Data Sheet

    Name :

    FGF 2 Mouse

    Description:

    Fibroblast Growth Factor-Basic Mouse Recombinant

    HBGF-2, Prostatropin, FGF-2, FGB-b.

    Product # :

    CYT-386

    Price :

    Quantity :

    Shipping Method :

    Room Temp Icon

    Shipped at Room temp

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    • description
    • source
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    • More Info

    Description

    Fibroblast Growth Factor-basic Mouse Recombinant (FGF-2) produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 146 amino acids and having a molecular mass of 16.3kDa. The FGF-2 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    FGF-b was lyophilized from 5mM Na2PO4, pH7.5 and 50mM NaCl.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Biological Activity

    The activity as calculated by the dose-dependant proliferation of BALB/3T3 cells was found to be less than 1ng/ml corresponding to a specific activity of 1,000,000 units/mg.

    More Info

    • Introduction

      FGF-basic is a member of the fibroblast growth factor (FGF) family. FGF family members bind and possess broad mitogenic and angiogenic activities. This protein has been implicated in diverse biological processes, such as limb and nervous system development, wound healing, and tumor growth. The mRNA for this gene contains multiple polyadenylation sites, and is alternatively translated from AUG and non-AUG (CUG) initiation codons resulting in five different isoforms with distinct properties. The CUG-initiated isoforms are localized in the nucleus and are responsible for the intracrine effect, whereas, the AUG-initiated form is mostly cytosolic and is responsible for the paracrine and autocrine effects of this FGF.
      The binding growth factors are angiogenic agents in vivo and are potent mitogens for a variety of cell types in vitro. there are differences in the tissue distribution and concentration of these 2 growth factors.

    • Synonyms

      HBGF-2, Prostatropin, FGF-2, FGB-b.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized Fibroblast Growth Factor-2 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution FGF-basic 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 Fibroblast Growth Factor b in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      MPALPEDGGA AFPPGHFKDP KRLYCKNGGF FLRIHPDGRV DGVREKSDPH VKLQLQAEER GVVSIKGVCA NRYLAMKEDG RLLASKCVTE ECFFFERLES NNYNTYRSRK YSSWYVALKR TGQYKLGSKT GPGQKAILFL PMSAKS.

    • Background

      What is the molecular weight/Mw of FGF 2 MOUSE Protein?
      FGF 2 MOUSE Protein has a total Mw of 16.3kDa.

      What is the source or expression system of FGF 2 MOUSE Protein?
      Escherichia Coli.

      What is the Purity of FGF 2 MOUSE Protein?
      FGF 2 MOUSE Protein is >95% pure as determined by SDS-PAGE.

      What is the Biological Activity of FGF 2 MOUSE Protein?
      The activity as calculated by the dose-dependant proliferation of BALB/3T3 cells was found to be less than 1ng/ml corresponding to a specific activity of 1,000,000 units/mg.
      What is the amino acid sequence of FGF 2 MOUSE Protein?
      MPALPEDGGA AFPPGHFKDP KRLYCKNGGF FLRIHPDGRV DGVREKSDPH VKLQLQAEER GVVSIKGVCA NRYLAMKEDG RLLASKCVTE ECFFFERLES NNYNTYRSRK YSSWYVALKR TGQYKLGSKT GPGQKAILFL PMSAKS.

      What applications can FGF 2 MOUSE Protein be used in?
      FGF 2 MOUSE Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for FGF 2 MOUSE Protein?
      The endotoxin level is minimal, FGF 2 MOUSE Protein was purified using conventional chromatography techniques.

    • Protein content

      Protein quantitation was carried out by two independent methods:1. UV spectroscopy at 280 nm using the absorbency value of 0.885 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 calibrated solution of FGF2 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.

    Fgf 2 Mouse
  • View Data Sheet

    Name :

    MAVS Human

    Description:

    Mitochondrial Antiviral Signaling Protein Human Recombinant

    CARDIF, IPS-1, IPS1, VISA, Mitochondrial antiviral-signaling protein, MAVS, Putative NF-kappa-B-activating protein 031N, Virus-induced-signaling adapter, KIAA1271.

    Product # :

    PRO-1351

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    Description

    MAVS Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 536 amino acids (1-513) and having a molecular mass of 55.9 kDa. MAVS is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

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

    Purity

    Greater than 85% as determined by SDS-PAGE.

    More Info

    • Introduction

      Mitochondrial antiviral signaling protein (MAVS) is vital for innate immune defense against viruses. MAVS is an intermediary protein essential in the virus-triggered IFN-beta signaling pathways. MAVS is involved in activation of transcription factors that regulate expression of IFN-beta and contributes to antiviral immunity.

    • Synonyms

      CARDIF, IPS-1, IPS1, VISA, Mitochondrial antiviral-signaling protein, MAVS, Putative NF-kappa-B-activating protein 031N, Virus-induced-signaling adapter, KIAA1271.

    • 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 MGSMPFAEDK TYKYICRNFS NFCNVDVVEI LPYLPCLTAR DQDRLRATCT LSGNRDTLWH LFNTLQRRPG WVEYFIAALR GCELVDLADE VASVYQSYQP RTSDRPPDPL EPPSLPAERP GPPTPAAAHS IPYNSCREKE PSYPMPVQET QAPESPGENS EQALQTLSPR AIPRNPDGGP LESSSDLAAL SPLTSSGHQE QDTELGSTHT AGATSSLTPS RGPVSPSVSF QPLARSTPRA SRLPGPTGSV VSTGTSFSSS SPGLASAGAA EGKQGAESDQ AEPIICSSGA EAPANSLPSK VPTTLMPVNT VALKVPANPA SVSTVPSKLP TSSKPPGAVP SNALTNPAPS KLPINSTRAG MVPSKVPTSM VLTKVSASTV PTDGSSRNEE TPAAPTPAGA TGGSSAWLDS SSENRGLGSE LSKPGVLASQ VDSPFSGCFE DLAISASTSL GMGPCHGPEE NEYKSEGTFG IHVAENPSIQ LLEGNPGPPA DPDGGPRPQA DRKFQEREVP CHRPSP.

    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.

    Mavs Human
  • View Data Sheet

    Name :

    FGF 2 Human, sf9

    Description:

    Fibroblast Growth Factor-Basic Human Recombinant, Sf9

    Prostatropin, HBGH-2, HBGF-2, FGF-2, FGF-b.

    Product # :

    CYT-365

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    Description

    Fibroblast Growth Factor-2 Human Recombinant (FGF-2) produced in Sf9 insect cells is a single, glycosylated, polypeptide chain containing 155 amino acids and having a molecular mass of 17353 Dalton.The FGF-basic is purified by proprietary chromatographic techniques.

    Source

    Baculovirus.

    Formulation

    The sterile protein solution (0.5mg/ml) contains 20mM Tris pH=7.9, 100mM KCl, 1mM DTT and 20% glycerol.

    Purity

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

    Biological Activity

    The ED50, calculated by the dose-dependant proliferation of BAF3 cells expressing FGF receptors (measured by 3H-thymidine uptake) is <0.5 ng/ml, corresponding to a specific activity of 2MU/mg.

    More Info

    • Introduction

      Basic fibroblast growth factor is a member of the fibroblast growth factor (FGF) family. FGF family members possess broad mitogenic and cell survival activities, and are involved in a variety of biological processes, including embryonic development, cell growth, morphogenesis, tissue repair, tumor growth and invasion. This protein functions as a modifier of endothelial cell migration and proliferation, as well as an angiogenic factor. It acts as a mitogen for a variety of mesoderm- and neuroectoderm-derived cells in vitro, thus is thought to be involved in organogenesis. Three alternatively spliced variants encoding different isoforms have been described. The heparin-binding growth factors are angiogenic agents in vivo and are potent mitogens for a variety of cell types in vitro. There are differences in the tissue distribution and concentration of these 2 growth factors.

    • Synonyms

      Prostatropin, HBGH-2, HBGF-2, FGF-2, FGF-b.

    • Physical Appearance

      Sterile Filtered liquid formulation.

    • Stability

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

    • Amino Acid Sequence

      The sequence of the first five N-terminal amino acids was determined and was found to be Ala-Ala-Gly-Ser-Ile.

    • Background

      What is the molecular weight/Mw of FGF 2 Protein?
      FGF 2 Protein has a total Mw of 17.3kDa.

      What is the source or expression system of FGF 2 Protein?
      Baculovirus.

      What is the Purity of FGF 2 Protein?
      FGF 2 Protein is >98% pure as determined by SDS-PAGE.

      What is the Biological Activity of FGF 2 Protein?
      The ED50, calculated by the dose-dependant proliferation of BAF3 cells expressing FGF receptors (measured by 3H-thymidine uptake) is <0.5 ng/ml, corresponding to a specific activity of 2MU/mg.

      What is the amino acid sequence of FGF 2 Protein?
      FGF 2 Protein is composed from155 amino acids.

      What applications can FGF 2 Protein be used in?
      FGF 2 Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for FGF 2 Protein?
      The endotoxin level is minimal, FGF 2 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.

    Fgf 2 Human Sf9
  • View Data Sheet

    Name :

    EGFR Human Sf9, Active

    Description:

    Epidermal Growth Factor Receptor Human Recombinant Sf9, Active

    Epidermal growth factor receptor, EC 2.7.10.1, Receptor tyrosine-protein kinase ErbB-1, ERBB, mENA, ERBB1, EGFR.

    Product # :

    PKA-335

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    Description

    EGFR Human Recombinant encoding a.a. 672-1210 expressed in Baculovirus infected Sf9 cells, fused with a GST-tag at N-terminus with thrombin cleavage sites, having a molecular weight of 89,171 Dalton.EGFR is purified by proprietary chromatographic techniques.

    Source

    Baculovirus infected Sf9 cells.

    Formulation

    EGFR in 50mM HEPES pH 7.5, 100mM NaCl, 5mM DTT, 15mM reduced glutathione and 20% glycerol.

    Biological Activity

    Determination of Km value by Filter binding assay MAFC membrane.

    More Info

    • Introduction

      The epidermal growth factor receptor (EGF R) subfamily of receptor tyrosine kinases comprises four members: EGF R (also known as HER1, ErbB1 or ErbB), ErbB2 (Neu, HER-2), ErbB3 (HER-3), and ErbB4 (HER-4). All family members are type I transmembrane glycoprotein that has an extracellular domain which contains two cysteine-rich domains separated by a spacer region that is involved in ligand-binding, and a cytoplasmic domain which has a membrane-proximal tyrosine kinase domain and a C-terminal tail with multiple tyrosine autophosphorylation sites. The human EGF R gene encodes a 1210 amino acid (aa) residue precursor with a 24 aa putative signal peptide, a 621 aa extracellular domain, a 23 aa transmembrane domain, and a 542 aa cytoplasmic domain. EGF R has been shown to bind a subset of the EGF family ligands, including EGF, amphiregulin, TGF-a , betacellulin, epiregulin, heparin-binding EGF and neuregulin-2 in the absence of a co-receptor. Ligand binding induces EGF R homodimerization as well as heterdimerization with ErbB2, resulting in kinase activation, tyrosine phosphorylation and cell signaling. EGF R can also be recruited to form heterodimers with the ligand-activated ErbB3 or ErbB4. EGF R signaling has been shown to regulate multiple biological functions including cell proliferation, differentiation, motility and apoptosis. In addition, EGF R signaling has also been shown to play a role in carcinogenesis.

    • Synonyms

      Epidermal growth factor receptor, EC 2.7.10.1, Receptor tyrosine-protein kinase ErbB-1, ERBB, mENA, ERBB1, EGFR.

    • Physical Appearance

      Sterile filtered liquid.

    • Stability

      Store vial at -20°C to -80°C. When stored at the recommended temperature, this protein is stable for 12 months. Please avoid freeze-thaw cycles.

    • Specific Activity

      30 pmol/µgxmin.

    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.

    Egfr Sf9 Human
  • View Data Sheet

    Name :

    BDNF Antibody

    Description:

    Brain-Derived Neurotrophic Factor, Mouse Anti-Human

    BDNF, MGC34632.

    Product # :

    ANT-128

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    • More Info

    Formulation

    1mg/ml in PBS (after reconstitution).

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    • Introduction

      BDNF promotes the survival of neuronal populations that are all located either in the central nervous system or directly connected to it. Major regulator of synaptic transmission and plasticity at adult synapses in many regions of the cns. the versatility of bdnf is emphasized by its contribution to a range of adaptive neuronal responses including long-term potentiation (ltp), long-term depression (ltd), certain forms of short-term synaptic plasticity, as well as homeostatic regulation of intrinsic neuronal excitability.

    • Synonyms

      BDNF, MGC34632.

    • Solubility

      Reconstitute with sterile H20. Mix gently, wash the sides of the vial and wait 30-60 seconds before use.

    • Immunogen

      r.Human BDNF.

    • Ig Subclass

      Mouse IgG Purification MethodIon exchange.

    • Clone

      NYRhBDNF.

    • Titer

      By direct ELISA, 1:10,000 dilution will yield 0.4 O.D using alkaline phosphatase conjugated rabbit anti-mouse Ig (Jackson Laboratories).

    • Shipping Conditions

      Antibody is shipped lyophilized at ambient temperature.

    • Type

      Mouse Anti Human Monoclonal.

    • Storage Procedures

      In lyophilized form, for long periods, store at 4oC in a dry environment. After reconstitution, if not intended for use within a month, aliquot and store at -20oC.

    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 Antibody
  • View Data Sheet

    Name :

    IGF1 Human

    Description:

    IGF-1 Human Recombinant

    Somatomedin C, IGF-I, IGFI, IGF1, IGF-IA MGF.

    Product # :

    CYT-216

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    Description

    IGF1 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 70 amino acids and having a molecular mass of 7.6kDa.IGF-1 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The protein was lyophilized from a concentrated solution in PBS, pH 7.0.

    Purity

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

    Biological Activity

    The biological activity was determined by the cell proliferation assay using serum free human MCF-7 cells in <2ng/ml, corresponding to a Specific Activity of >5.0 x 105IU/mg.

    More Info

    • Introduction

      The somatomedins, IGFs, comprise a family of peptides that play important roles in mammalian growth and development. IGF1 mediates many of the growth-promoting effects of GH. Early studies showed that GH did not directly stimulate the incorporation of sulfate into cartilage, but rather acted through a serum factor, termed 'sulfation factor,' which later became known as 'somatomedin. Three main somatomedins have been characterized: somatomedin C (IGF1), somatomedin A (IGF2; MIM 147470), and somatomedin B.

    • Synonyms

      Somatomedin C, IGF-I, IGFI, IGF1, IGF-IA MGF.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized IGF1 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IGF1 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 IGF-1 in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      GPETLCGAEL VDALQFVCGD RGFYFNKPTG YGSSSRRAPQ TGIVDECCFR SCDLRRLEMY CAPLKPAKSA.

    • Background

      IGF stands for INS like growth factors, which are proteins that have a high similarity to INS. They are part of a complicated process that uses cells to communication with the physiologic environment around them. IGF’s complex system is often called the ‘axis’. This consists of:
      ● Two cell-surface receptors (IGF1R and IGF2R)
      ● Two ligands (IGF-1 and IGF-2)
      ● A family of six high-affinity IGF-binding proteins.
      ● Proteases.

      The Effect IGF Has On The Body
      Many unique tissue types express the IGF-1 receptor, and the effects can vary. It induces the survival of neurons, may catalyse skeletal muscle hypertrophy by inducing protein synthesis, and by blocking muscle atrophy. It works as a protector for cartilage cells, and may work to be an anabolic factor for the bones. When used in high concentrations, it can activate the INS receptor, and can even complement the effects that INS has on the body.

      Diseases And IGF
      Diseases and IGF are closely related, and a number of them can be affected. The INS IGF axis is thought to have an effect on aging, with an increased life span shown in fruit flies when used in studies.
      It is also important to note the crucial role that IGF plays in cancer and diabetes - IGF- 1 has been shown to stimulate growth in both prostate and breast cancer cells. The degree of risk that IGF-1 poses is up for debate, and many scientists are not in agreement. IGF has also shown to have the ability to decrease blood glucose levels, although not quite as effective as INS.

      How Was IGF Discovered?
      Investigators began studying the effects of biological substances on cells and tissues outside the body when IGFs were discovered. The name is self explanatory in the fact that IGF performs INS actions in some tissues, but is less potent than INS at decreasing blood sugar. Its fundamental action is to stimulate growth, whether that be within the epidermal growth factor or the nerve growth factor.

      What’s The Difference Between IGF-1 And IGF-2?
      The two types of IGF are IGF-1 and IGF-2. Although the names are similar, the specific actions that they take are different - they bind and activate completely difference receptors. The major actor in them both is the effect that they have on cell growth. Most of the actions of the pituitary GH are mediated by IGFs, but predominantly IGF-1. GH works to stimulate many tissues within the body, especially the liver which then secretes IGF-1. This then causes hypertrophy, or in layman's terms, an increase in cell size, as well as hyperplasia which is an increase in the number of cells.
      The IGF-1 concentration will increase during childhood and hit peak during puberty, but will then decrease afterwards, as does the hormone secretion itself. It has been proven that children and adults with a deficiency of the GH have low serum IGF-1 concentrations when put in comparison with others in the same age range. Patients who have conditions like acromegaly have been shown to have increased serum IGF-1 concentrations. The production of IGF-2 is less dependent on the secretion of GH than IGF-1, and is much less important for stimulating linear growth.

      What is the molecular weight/Mw of IGF1 HUMAN Protein?
      IGF1 HUMAN Protein has a total Mw of 7.6kDa.

      What is the source or expression system of IGF1 HUMAN Protein?
      Escherichia Coli.

      What is the Purity of IGF1 HUMAN Protein?
      IGF1 HUMAN Protein is >97% pure as determined by SDS-PAGE.

      What is the Biological Activity of IGF1 HUMAN Protein?
      The biological activity was determined by the cell proliferation assay using serum free human MCF-7 cells in <2ng/ml, corresponding to a Specific Activity of >5.0 x 105IU/mg.
      What is the amino acid sequence of IGF1 HUMAN Protein?
      GPETLCGAEL VDALQFVCGD RGFYFNKPTG YGSSSRRAPQ TGIVDECCFR SCDLRRLEMY CAPLKPAKSA.

      What applications can IGF1 HUMAN Protein be used in?
      IGF1 HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for IGF1 HUMAN Protein?
      The endotoxin level is minimal, IGF1 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.

    Igf 1 Human
  • View Data Sheet

    Name :

    Ang K1-3 Human

    Description:

    Angiostatin Kringles 1-3 Human Recombinant

    Angiostatin, Angiostatin Kringles 1-3, Ang K1-3.

    Product # :

    PRO-284

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    Description

    Angiostatin Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 259 amino acids and having a molecular mass of approximately 29.7 kDa. The Ang K1-3 is purified by proprietary chromatographic techniques.

    Source

    Escherichia coli.

    Formulation

    Lyophilized from a 0.2μm filtered concentrated (1.0mg/ml) solution in 20mM NaAc, pH5.5, 4% mannitol.

    Purity

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

    Biological Activity

    The activity is assayed on anti-proliferation and anti-migration of endothelial cells in vitro and anti-angiogenesis in vivo. The specific activity of anti-migration of endothelial cells in vitro is 550,000 Units/mg.

    More Info

    • Introduction

      Ang K1-3 is a proteolytic fragment of plasminogen containing the first three kringle structures. A specific inhibitor of endothelial cell growth and angiogenesis. More active relative to kringles 1-4. Ang K1-3 reduces endothelial cell proliferation and acts as a potent inhibitor of angiogenesis and tumor growth.

    • Synonyms

      Angiostatin, Angiostatin Kringles 1-3, Ang K1-3.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      The lyophilized Angiostatin K1-3 is stable for several weeks at 2-8°C, but should be kept at -20°C for long term storage, preferably desiccated. Upon reconstitution, the preparation is stable for up to one week at 2-8°C. For maximal stability, apportion the reconstituted preparation into working aliquots and store at -20°C to -70°C. Avoid repeated freeze/thaw cycles.

    • Solubility

      We recommend to briefly centrifuge the vial prior to opening to bring the contents to the bottom. Reconstitute in sterile distilled water or aqueous buffer containing 0.1% BSA to a concentration of 0.1-1.0 mg/ml. Stock solutions should be apportioned into working aliquots and stored at <-20°C. Further dilutions should be made in appropriate buffered solutions.

    • Amino Acid Sequence

      VYLSECKTGN GKNYRGTMSK TKNGITCQKW SSTSPHRPRF SPATHPSEGL EENYCRNPDN DPQGPWCYTT DPEKRYDYCD ILECEEECMH CSGENYDGKI SKTMSGLECQ AWDSQSPHAH GYIPSKFPNK NLKKNYCRNP DRELRPWCFT TDPNKRWELC DIPRCTTPPP SSGPTYQCLKGTGENYRGNV AVTVSGHTCQ HWSAQTPHTH NRTPENFPCK NLDENYCRNP DGKRAPWCHT TNSQVRWEYC KIPSCDSSP.

    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.

    Angiostatin K1 3 Human
  • View Data Sheet

    Name :

    PSMD11 PAT2C7AT Antibody

    Description:

    26S proteasome non-ATPase regulatory subunit 11 clone PAT2C7AT Mouse Anti Human

    26S proteasome non-ATPase regulatory subunit 11, 26S proteasome regulatory subunit S9, 26S proteasome regulatory subunit RPN6, 26S proteasome regulatory subunit p44.5, PSMD11, S9, Rpn6, p44.5, MGC3844.

    Product # :

    ANT-675

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    Formulation

    1mg/ml containing PBS, pH-7.4, 10% Glycerol and 0.02% Sodium Azide.

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    • Introduction

      The 26S proteasome is a multicatalytic proteinase complex with a well ordered structure composed of two complexes- a 20S core and a 19S regulator. PSMD11 is a non-ATPase subunit of the 19S regulator. The 20S core is composed of four rings of 28 non-identical subunits; two rings are composed of 7 alpha subunits and two rings are composed of 7 beta subunits. The 19S regulator is composed of a base that contains six ATPase subunits and two non-ATPase subunits, and a lid that contains up to ten non-ATPase subunits. Proteasomes are spread throughout eukaryotic cells at a high concentration and cleave peptides in an ATP/ubiquitin-dependent process in a non-lysosomal pathway. An indispensable function of a modified proteasome, the immunoproteasome, is the processing of class I MHC peptides.

    • Synonyms

      26S proteasome non-ATPase regulatory subunit 11, 26S proteasome regulatory subunit S9, 26S proteasome regulatory subunit RPN6, 26S proteasome regulatory subunit p44.5, PSMD11, S9, Rpn6, p44.5, MGC3844.

    • Physical Appearance

      Sterile filtered colorless solution.

    • Immunogen

      Anti-human PSMD11 mAb, is derived from hybridization of mouse F0 myeloma cells with spleen cells from BALB/c mice immunized with recombinant human PSMD11 PAT2C7AT amino acids 1-422 purified from E. coli.

    • Ig Subclass

      Mouse IgG2b heavy chain and ? light chain.

    • Clone

      PAT2C7AT.

    • Applications

      PSMD11 antibody has been tested by ELISA, Western blot analysis, Flow cytometry and ICC/IF to assure specificity and reactivity. Since application varies, however, each investigation should be titrated by the reagent to obtain optimal results.

    • Type

      Mouse Anti Human Monoclonal.

    • Storage Procedures

      For periods up to 1 month store at 4°C, for longer periods of time, store at -20°C. Prevent freeze thaw cycles.

    • Purification Method

      PSMD11 antibody was purified from mouse ascitic fluids by protein-A affinity chromatography.

    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.

    Psmd11 Pat2C7At Antibody
  • View Data Sheet

    Name :

    LIF Rat

    Description:

    Leukemia Inhibitory Factor Rat Recombinant

    Leukemia inhibitory factor, Cholinergic neuronal differentiation factor, Lif.

    Product # :

    CYT-731

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    Description

    Leukemia Inhibitory Factor (LIF) Rat Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 180 amino acids and having a molecular mass of 19.8 kDa. The Leukemia Inhibitory Factor (LIF) is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    LIF Rat was lyophilized from 0.2µm filtered concentrated solution in 1xPBS, pH 7.4.

    Purity

    Greater than 96.0% as determined by:
    (a) Analysis by RP-HPLC.
    (b) Analysis by SDS-PAGE.

    Biological Activity

    The activity of rat LIF is determined by the ability to induce differentiation of M1 myeloid leukemic cells. The minimum detectable concentration of rat LIF in this assay is 0.5ng/mL.

    More Info

    • Introduction

      Leukemia Inhibitory Factor also called LIF is a lymphoid factor that promotes long-term maintenance of embryonic stem cells by suppressing spontaneous differentiation. Leukemia Inhibitory Factor has several functions such as cholinergic neuron differentiation, control of stem cell pluripotency, bone & fat metabolism, mitogenesis of factor dependent cell lines & promotion of megakaryocyte production in vivo. Human and mouse LIF exhibit a 78% identity in its amino acid sequence.

    • Synonyms

      Leukemia inhibitory factor, Cholinergic neuronal differentiation factor, Lif.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Amino Acid Sequence

      SPLPITPVNA TCAIRHPCHG NLMNQIKSQL AQLNGSANAL FISYYTAQGE PFPNNVDKLC APNMTDFPPF HANGTEKTKL VELYRMVTYL GASLTNITWD QKNLNPTAVS LQIKLNATTD VMRGLLSSVL CRLCNKYHVG HVDVPCVPDN SSKEAFQRKK LGCQLLGTYK QVISVLAQAF .

    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.

    Lif Rat
  • View Data Sheet

    Name :

    TGFB3 Human

    Description:

    Transforming Growth Factor-Beta 3 Human Recombinant

    Transforming Growth Factor-beta3, TGFB3, ARVD, FLJ16571, TGF-beta3.

    Product # :

    CYT-368

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    Description

    TGF-β 3 Human Recombinant produced in E.Coli is a disulfide-linked homodimeric, non-glycosylated, polypeptide chain containing two 113 amino acid chains and having a total molecular mass of 25.8kDa. The TGF-β 3 is purified by standard chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The protein solution contains 20% Ethanol and 10mM Acetic acid (AcOH).

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Biological Activity

    The activity is determined by the ability to induce chondrogenic differentiation.

    More Info

    • Introduction

      Transforming growth factor betas (TGF Betas) mediate many cell-cell interactions that occur during embryonic development. Three TGF Betas have been identified in mammals. TGF Beta 1, TGF Beta 2 and TGF Beta 3 are each synthesized as precursor proteins that are very similar in that each is cleaved to yield a 112 amino acid polypeptide that remains associated with the latent portion of the molecule.

    • Synonyms

      Transforming Growth Factor-beta3, TGFB3, ARVD, FLJ16571, TGF-beta3.

    • Physical Appearance

      Sterile Filtered clear solution.

    • Stability

      TGF-beta 3 although stable at room temperature for 1 week, should be stored at 4°C.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).

    • Amino Acid Sequence

      MALDTNYCFRN LEENCCVRPL YIDFRQDLGW KWVHEPKGYY ANFCSGPCPY LRSADTTHST VLGLYNTLNP EASASPCCVP QDLEPLTILY YVGRTPKVEQ LSNMVVKSCK CS.

    • Background

      TGFB3 (207 a.a.) Human



      About TGFB3 (207 a.a.) Human:

      Transforming growth factor beta-3 (also known as TGF-β3) is a cytokine encoded by the TGFB3 gene that belongs to the transforming growth factor beta superfamily. It plays a significant role in cell differentiation, embryogenesis, and development by regulating molecules involved in cell adhesion and extracellular matrix formation. TGF-β3 is necessary for palate development, as its absence causes clefting. In addition, it controls lung development and wound healing processes by regulating cell adhesion and movement in the respective tissues. Together, TGF-β3 coordinates a variety of cellular processes that are critical for mammalian embryonic development and tissue homeostasis. In this article we will explore the features and applications of TGFB3 Human Recombinant Protein, expanding on its significance in in advanced research pursuits.

      Description:

      TGFB3 Human Recombinant protein encodes amino acids 644-850 and total molecular mass of 50 kDa (Including GST Tag). As TGFB3 Human derives from Escherichia Coli, it appears as a sterile filtered clear solution and is formulated as 100µl of purified human TGF Beta 3 protein at 100µg/ml. In addition, its protein is formulated in a solution comprising 50mM Tris-Acetate (pH 7.5), 1mM EDTA, and 20% Glycerol. In terms of stability, TGF-beta 3 Human Recombinant is stable at 4°C for up to a week. However, it is preferable to store at -20°C. However, if you are looking to store it for a long term it is preferable to add a carrier protein (0.1% HSA or BSA).

      Activation:

      While TGF-β plays a crucial role regulating essential cell functions, its activation pathways is still being explored and understood. Some pathways are specific to certain cells or tissues, while others are more widespread. Factors like proteases, integrins, pH, and reactive oxygen species can activate TGF-β. Disruptions in these factors can lead to uncontrolled TGF-β signaling, causing issues like inflammation, autoimmune diseases, and cancer.

      Applications and Usage:

      TGFB3 (207 a.a.) Human is intended for laboratory research, serving as an important tool in stem cell differentiation as well as T-cell regulation and differentiation. Accordingly, its versatility extends to applications such as ELISA, Western Blotting, and Inhibition Assays, offering different avenues for discovery and research.

      Safety Information:

      TGFB3 (207 a.a.) Human is intended for use only in laboratory research, in accordance with safety guidelines. It emphasizes adherence to ethical and regulatory norms and is not intended for use as household chemicals, pharmaceuticals, agricultural products, or food additives.

    • Protein content

      Protein quantitation was carried out by two independent methods:1. UV spectroscopy at 280 nm using the absorbency value of 1.718 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 calibrated solution of TGF-b 3 as a Reference Standard.

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    Tgf Beta 3 Human
  • View Data Sheet

    Name :

    GDF15 Human

    Description:

    Growth and Differentiation Factor 15 Human Recombinant

    GDF-15, MIC1, MIC-1, NAG-1, PDF, PLAB, PTGFB, Growth/differentiation factor 15, Placental bone morphogenetic protein, Placental TGF-beta, Macrophage inhibitory cytokine 1, Prostate differentiation factor, NSAID-activated gene 1 protein, NSAID-regulated gene 1 protein, NRG-1, GDF15.

    Product # :

    CYT-335

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    Description

    GDF15 Human Recombinant produced in E.Coli is a homodimeric, non-glycosylated, Polypeptide chain containing 2x113 amino acids and having a molecular mass of 24.8 kDa. The GDF15 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    GDF15 is lyophilized from a sterile filtered solution containing 0.1% Trifluoroacetic Acid (TFA).

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      GDF15 is part of the TGF-Beta superfamily that is involved in regulating inflammatory and apoptotic pathways in injured tissues and throughout disease processes. GDF15 is most abundant in the liver. Its expression in liver can be considerably up-regulated in during injury of organs such as liver, kidney, heart and lung. GDF-15 promotes proliferation or growth arrest and differentiation due to differences in cellular differentiation. GDF15 prevents apoptosis in cerebellar granule neurons by activating Akt and inhibiting endogenously active ERK. GDF15 is a novel autocrine/endocrine factor that antagonizes the hypertrophic response and loss of ventricular performance.

    • Synonyms

      GDF-15, MIC1, MIC-1, NAG-1, PDF, PLAB, PTGFB, Growth/differentiation factor 15, Placental bone morphogenetic protein, Placental TGF-beta, Macrophage inhibitory cytokine 1, Prostate differentiation factor, NSAID-activated gene 1 protein, NSAID-regulated gene 1 protein, NRG-1, GDF15.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized GDF15 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution GDF15 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 GDF15 in sterile 18M-cm H2O at a concentration of 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      MARNGDHCPL GPGRCCRLHT VRASLEDLGW ADWVLSPREV QVTMCIGACP SQFRAANMHA QIKTSLHRLK PDTVPAPCCV PASYNPMVLI QKTDTGVSLQ TYDDLLAKDC HCI.

    • Background

      What is the molecular weight/Mw of GDF15 HUMAN Protein?
      GDF15 HUMAN Protein has a total Mw of 24.8kDa.

      What is the source or expression system of GDF15 HUMAN Protein?
      Escherichia Coli.

      What is the Purity of GDF15 HUMAN Protein?
      GDF15 HUMAN Protein is >95% pure as determined by SDS-PAGE.

      What is the Biological Activity of GDF15 HUMAN Protein?
      The biological functionality of GDF15 HUMAN Protein will be determined in the future.

      What is the amino acid sequence of GDF15 HUMAN Protein?
      MARNGDHCPL GPGRCCRLHT VRASLEDLGW ADWVLSPREV QVTMCIGACP SQFRAANMHA QIKTSLHRLK PDTVPAPCCV PASYNPMVLI QKTDTGVSLQ TYDDLLAKDC HCI.

      What applications can GDF15 HUMAN Protein be used in?
      GDF15 HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for GDF15 HUMAN Protein?
      The endotoxin level is minimal, GDF15 HUMAN Protein was purified using conventional chromatography techniques.


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    Gdf15 H Human
  • View Data Sheet

    Name :

    Myostatin Human, HEK

    Description:

    Myostatin Human Recombinant, HEK

    GDF-8, MSTN, Growth Differentiation Factor 8, MSTN Muscle Hypertrophy.

    Product # :

    CYT-833

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    Description

    Myostatin Human Recombinant produced in HEK cells is a single, glycosylated, polypeptide chain (Asn24-Ser375) containing a total of 360 amino acids, having a calculated molecular mass of 41.1kDa. Myostatin is fused to a 2 aa N-terminal linker and a 6 aa His tag at N-Terminus.

    Source

    HEK 293.

    Formulation

    Myostatin solution at a concentration of 0.25mg/ml in phosphate buffered saline (PBS) pH 8.0 and 20% (w/v) glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

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    • Introduction

      GDF8 is a member of the bone morphogenetic protein (BMP) family and the TGF-beta superfamily. This group of proteins is characterized by a polybasic proteolytic processing site which is cleaved to produce a mature protein containing seven conserved cysteine residues. The members of this family are regulators of cell growth and differentiation in both embryonic and adult tissues. This gene is thought to encode a secreted protein which negatively regulates skeletal muscle growth.

    • Synonyms

      GDF-8, MSTN, Growth Differentiation Factor 8, MSTN Muscle Hypertrophy.

    • Physical Appearance

      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

      HHHHHHASNE NSEQKENVEK EGLCNACTWR QNTKSSRIEA IKIQILSKLR LETAPNISKD VIRQLLPKAP PLRELIDQYD VQRDDSSDGS LEDDDYHATT ETIITMPTES DFLMQVDGKP KCCFFKFSSK IQYNKVVKAQ LWIYLRPVET PTTVFVQILR LIKPMKDGTR YTGIRSLKLD MNPGTGIWQS IDVKTVLQNW LKQPESNLGI EIKALDENGH DLAVTFPGPG EDGLNPFLEV KVTDTPKRSR RDFGLDCDEH STESRCCRYP LTVDFEAFGW DWIIAPKRYK ANYCSGECEF VFLQKYPHTH LVHQANPRGS AGPCCTPTKM SPINMLYFNG KEQIIYGKIP AMVVDRCGCS.

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    Myostatin Human Hek
  • View Data Sheet

    Name :

    EEF1D Human

    Description:

    Eukaryotic Translation Elongation Factor 1 Delta Human Recombinant

    Elongation factor 1-delta, EF-1-delta, Antigen NY-CO-4, EEF1D, EF1D, EF-1D, FP1047, FLJ20897.

    Product # :

    PRO-170

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    Description

    EEF1D Human Recombinant fused with a 20 amino acid His tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 301 amino acids (1-281 a.a.) and having a molecular mass of 33.2kDa (Molecular weight on SDS-PAGE will appear higher). The EEF1D is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The EEF1D solution (0.5 mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 1mM DTT and 10% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

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    • Introduction

      Eukaryotic translation elongation factor 1 delta (EEF1D) is a subunit of the elongation factor-1 complex that is responsible for the enzymatic transport of aminoacyl tRNAs to the ribosome. EEF1D functions as guanine nucleotide exchange factor. EEF1D interacts with HIV-1 Tat, and consequently represses the translation of host-cell, but not HIV-1, mRNAs. EEF1D overexpression is linked to oesophageal carcinoma and may negatively influence the outcome of medulloblastomas.

    • Synonyms

      Elongation factor 1-delta, EF-1-delta, Antigen NY-CO-4, EEF1D, EF1D, EF-1D, FP1047, FLJ20897.

    • 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 MATNFLAHEK IWFDKFKYDD AERRFYEQMN GPVAGASRQE NGASVILRDI ARARENIQKS LAGSSGPGAS SGTSGDHGEL VVRIASLEVE NQSLRGVVQE LQQAISKLEA RLNVLEKSSP GHRATAPQTQ HVSPMRQVEP PAKKPATPAE DDEDDDIDLF GSDNEEEDKE AAQLREERLR QYAEKKAKKP ALVAKSSILL DVKPWDDETD MAQLEACVRS IQLDGLVWGA SKLVPVGYGI RKLQIQCVVE DDKVGTDLLE EEITKFEEHV QSVDIAAFNK I.

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    Eef1D Human
  • View Data Sheet

    Name :

    EIF1 Human

    Description:

    Eukaryotic Translation Initiation Factor 1 Human Recombinant

    A121, EIF-1, EIF1A, ISO1, SUI1, Eukaryotic translation initiation factor 1, eIF1, Protein translation factor SUI1 homolog, Sui1iso1, EIF1.

    Product # :

    PRO-773

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    Description

    EIF1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 150 amino acids (1-113 a.a.) and having a molecular weight of 16.9kDa.The EIF1 is fused to 37 a.a. His-Tag at N-terminus and purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The EIF1 protein solution contains 20mM Tris-HCl, pH-8, 100mM NaCl, 1mM DTT and 10% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

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    • Introduction

      EIF1 is important for scanning and plays a role in initiation site selection. EIF1 promotes the assembly of 48S ribosomal at the authentic initiation codon of a conventional capped mRNA.

    • Synonyms

      A121, EIF-1, EIF1A, ISO1, SUI1, Eukaryotic translation initiation factor 1, eIF1, Protein translation factor SUI1 homolog, Sui1iso1, EIF1.

    • Physical Appearance

      Sterile filtered colorless solution.

    • Stability

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

    • Amino Acid Sequence

      MRGSHHHHHH GMASMTGGQQ MGRDLYDDDD KDRWAGSMSA IQNLHSFDPF ADASKGDDLL PAGTEDYIHI RIQQRNGRKT LTTVQGIADD YDKKKLVKAF KKKFACNGTV IEHPEYGEVI QLQGDQRKNI CQFLVEIGLA KDDQLKVHGF.

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    Eif1 Human
  • View Data Sheet

    Name :

    OAS1 Human

    Description:

    2’-5’ Oligoadenylate Synthetase 1 Human Recombinant

    2'-5'-oligoadenylate synthetase 1, (2-5')oligo(A) synthetase 1, 2-5A synthetase 1, p46/p42 OAS, E18/E16, OAS1, OIAS, IFI-4, OIASI.

    Product # :

    ENZ-445

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    Description

    OAS1 Human Recombinant fused with 20 amino acid His tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 384 amino acids (1-364 a.a.) and having a molecular mass of 43.9kDa.The OAS1 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The OAS1 solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 10% glycerol and 1mM DTT.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      OAS1 enzyme is a member of the 2’,5’-oligoadenylate synthetase family. OAS1 is induced by interferons and uses adenosine triphosphate in 2’-specific nucleotidyl transfer reactions to synthesize 2’,5’-oligoadenylates(2-5As). These molecules in turn activate latent RNase L resulting in viral RNA degradation and the inhibition of viral replication.
      OAS1 may have a role in mediating resistance to virus infection, control of cell growth, differentiation, and apoptosis. OAS1 binds double-stranded RNA and polymerizes ATP into PPP (A2'P5'A)N oligomers, which activate the latent RNase L that, once activated, cleaves single-stranded RNAs.
      OAS1 gene mutations are been linked to host susceptibility to viral infection.
      OSA1 gene polymorphisms are linked to the outcome of hepatitis C virus infection. Furthermore, OAS1 gene polymorphisms are linked to the susceptibility to severe acute respiratory syndrome.

    • Synonyms

      2'-5'-oligoadenylate synthetase 1, (2-5')oligo(A) synthetase 1, 2-5A synthetase 1, p46/p42 OAS, E18/E16, OAS1, OIAS, IFI-4, OIASI.

    • 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 MMDLRNTPAK SLDKFIEDYL LPDTCFRMQI NHAIDIICGF LKERCFRGSS YPVCVSKVVK GGSSGKGTTL RGRSDADLVV FLSPLTTFQD QLNRRGEFIQ EIRRQLEACQ RERAFSVKFE VQAPRWGNPR ALSFVLSSLQ LGEGVEFDVL PAFDALGQLT GSYKPNPQIY VKLIEECTDL QKEGEFSTCF TELQRDFLKQ RPTKLKSLIR LVKHWYQNCK KKLGKLPPQY ALELLTVYAW ERGSMKTHFN TAQGFRTVLE LVINYQQLCI YWTKYYDFKN PIIEKYLRRQ LTKPRPVILD PADPTGNLGG GDPKGWRQLA QEAEAWLNYP CFKNWDGSPV SSWILLVRPP ASSLPFIPAP LHEA.

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    Oas1 Human
  • View Data Sheet

    Name :

    ESM1 Human, HEK

    Description:

    Endothelial Cell-Specific Molecule 1 Human Recombinant, HEK

    Endothelial cell-specific molecule 1, ESM-1, ESM1, endocan. 

    Product # :

    PRO-2476

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    Description

    ESM1 Human Recombinant produced in HEK293 cells is a single, glycosylated polypeptide chain (a.a 20-184) containing 175 amino acids including a 10 a.a C-terminal His tag. The total molecular mass is 19.5kDa (calculated).

    Source

    HEK293 cells.

    Formulation

    ESM1 filtered (0.4 µm) and lyophilized from 0.5mg/ml in phosphate buffered saline.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Endothelial cell-specific molecule 1 (ESM1) is a proteoglycan secreted by endothelial cells (mostly in the human lung and kidney tissues) and its mRNA expression is regulated by inflammatory cytokines. ESM1 has potent implications in lung endothelial cell-leukocyte interactions. In addition, ESM1 expression is detected in various epithelia and in adipocytes. ESM1 is involved in angiogenesis and it also promotes angiogenic sprouting. ESM1 expression is upregulated by TNF alpha, IL1 beta, or lipopolysaccharide and downregulated by IFN gamma. Genetically engineered cells overexpressing ESM1 induce tumor formation, implying that ESM1 might be involved in the pathophysiology of tumor growth in vivo.

    • Synonyms

      Endothelial cell-specific molecule 1, ESM-1, ESM1, endocan.

    • Physical Appearance

      Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Solubility

      It is recommended to add deionized water to prepare a working stock solution of approximately 0.5mg/ml and let the lyophilized pellet dissolve completely. ESM1 is not sterile! Please filter the product by an appropriate sterile filter before using it in the cell culture.

    • Amino Acid Sequence

      WSNNYAVDCP QHCDSSECKS SPRCKRTVLD DCGCCRVCAA GRGETCYRTV SGMDGMKCGP GLRCQPSNGE DPFGEEFGIC KDCPYGTFGM DCRETCNCQS GICDRGTGKC LKFPFFQYSV TKSSNRFVSL TEHDMASGDG NIVREEVVKE NAAGSPVMRK WLNPR HHHHH HHHHH.

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    Esm1 Protein
  • View Data Sheet

    Name :

    FLT4 Human

    Description:

    Vascular Endothelial Growth Factor Receptor-3 Human Recombinant

    Tyrosine-protein kinase receptor FLT4, PCL, FLT41, FMS-LIKE TYROSINE KINASE 4, VEGFR-3, VEGFR3.

    Product # :

    PKA-244

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    Description

    Soluble FLT4 Human Recombinant fused with a carboxy-terminal 6X histidine-tag produced in baculovirus is a monomeric, glycosylated, polypeptide containing the extracellular part, 25-774 amino acids and having a total molecular mass of 120 kDa. The soluble receptor protein contains only the first 7 extracellular domains, which contain all the information necessary for ligand binding. The FLT4 is purified by proprietary chromatographic techniques.

    Source

    Insect Cells.

    Formulation

    FLT4 was lyophilized from a concentrated (1mg/ml) sterile solution containing 1xPBS.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    Biological Activity

    Measured by its ability to bind recombinant rat VEGF-C in a functional solid phase binding assay. Immobilised recombinant human VEGFR-3/FLT-4 at 5 µg/ml can bind recombinant rat VEGF-C in a linear range of 8-500 ng/ml.

    More Info

    • Introduction

      All three VEGF receptors belong to the class III subfamily of receptor tyrosine kinases (RTKs) characterised by the seven immunoglobulin-like loops in the extracellular domain. The expression of VEGFR-1 to -3 is almost exclusively restricted to hematopoietic precursor cells, vascular and lymphatic endothelial cells and to the monocyte/macrophage lineage. They play key roles in vasculogenesis, hematopoiesis, angiogenesis and lymphangiogenesis. The FLT-4 cDNA encodes a 1298 amino acid (aa) residue precursor protein with a 23 aa residue signal peptide. Mature VEGFR-3/FLT-4 is composed of a 751 aa residue extracellular domain, a 22 aa transmembrane domain and a 482 aa residue cytoplasmic domain. Both VEGF family members VEGF-C and VEGF-D have been shown to bind and activate VEGFR-3/FLT-4. The Flt-4 gene is widely expressed in the early embryo but becomes restricted to the lymphatic endothelial a latter stages of development. It is important for lymphangiogenesis.

    • Synonyms

      Tyrosine-protein kinase receptor FLT4, PCL, FLT41, FMS-LIKE TYROSINE KINASE 4, VEGFR-3, VEGFR3.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized FLT4 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution FLT4 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 FLT4 in sterile water not less than 100 µg/ml, which can then be further diluted to other aqueous solutions.

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    Flt4 Human
  • View Data Sheet

    Name :

    PRKAG1 Human

    Description:

    Protein Kinase, AMP-Activated, Gamma 1 Human Recombinant

    Protein Kinase AMP-Activated Gamma 1 Non-Catalytic Subunit, 5'-AMP-Activated Protein Kinase Subunit Gamma-1, AMPK Gamma1 Chain, AMPKg.

    Product # :

    PKA-305

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    Description

    PRKAG1 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 354 amino acids (1-331) and having a molecular mass of 40.0kDa.PRKAG1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The PRKAG1 solution (0.25mg/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

      PRKAG1 is a regulatory subunit of the AMP-activated protein kinase (AMPK). AMPK is a heterotrimer comprised of an alpha catalytic subunit, and non-catalytic beta and gamma subunits. AMPK is a vital energy-sensing enzyme which supervises cellular energy status. PRKAG1 is one of the gamma regulatory subunits of AMPK. Alternatively spliced transcript variants encoding dissimilar isoforms were found.

    • Synonyms

      Protein Kinase AMP-Activated Gamma 1 Non-Catalytic Subunit, 5'-AMP-Activated Protein Kinase Subunit Gamma-1, AMPK Gamma1 Chain, AMPKg.

    • 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 MGSMETVISS DSSPAVENEH PQETPESNNS VYTSFMKSHR CYDLIPTSSK LVVFDTSLQV KKAFFALVTN GVRAAPLWDS KKQSFVGMLT ITDFINILHR YYKSALVQIY ELEEHKIETW REVYLQDSFK PLVCISPNAS LFDAVSSLIR NKIHRLPVID PESGNTLYIL THKRILKFLK LFITEFPKPE FMSKSLEELQ IGTYANIAMV RTTTPVYVAL GIFVQHRVSA LPVVDEKGRV VDIYSKFDVI NLAAEKTYNN LDVSVTKALQ HRSHYFEGVL KCYLHETLET IINRLVEAEV HRLVVVDEND VVKGIVSLSD ILQALVLTGG EKKP

    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.

    Prkag1 Human
  • View Data Sheet

    Name :

    PSME1 Human

    Description:

    Proteasome Activator Subunit 1 Human Recombinant

    REG-alpha, PA28alpha, PA28a, Proteasome Activator subunit-1, Proteasome Activator 28 subunit alpha.

    Product # :

    PRO-266

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    • description
    • source
    • formulation
    • purity
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    Description

    PSME1 produced in E.Coli is a single, non-glycosylated polypeptide chain containing 269 amino acids (1-249a.a.) and having a molecular mass of 30.8kDa.PSME1 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The PSME1 protein solution (0.5mg/1ml) is formulated in 20mM Tris-HCl buffer (pH8.0) 0.1M NaCl and 10% glycerol.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    More Info

    • Introduction

      PSME1 is a Proteasome Activator 28 subunit alpha essential for presentation of certain major histocompatibility (MHC) class I antigens. The PSME1 complex is an alternate proteasome activator which operates with no use of ubiquitin. The PSME1 complex is made out of two homologous subunits, alpha and beta, that functions in similar catalytic properties and is connected to a hexameric ring.

    • Synonyms

      REG-alpha, PA28alpha, PA28a, Proteasome Activator subunit-1, Proteasome Activator 28 subunit alpha.

    • 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

      MGSSHHHHHH SSGLVPRGSH MAMLRVQPEA QAKVDVFRED LCTKTENLLG SYFPKKISEL DAFLKEPALN EANLSNLKAP LDIPVPDPVK EKEKEERKKQ QEKEDKDEKK KGEDEDKGPP CGPVNCNEKI VVLLQRLKPE IKDVIEQLNL VTTWLQLQIP RIEDGNNFGV AVQEKVFELM TSLHTKLEGF HTQISKYFSE RGDAVTKAAK QPHVGDYRQL VHELDEAEYR DIRLMVMEIR NAYAVLYDII LKNFEKLKKP RGETKGMIY

    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.

    Psme1 Human
  • View Data Sheet

    Name :

    VEGF Human (121 a.a.), His

    Description:

    Vascular Endothelial Growth Factor-121 Human Recombinant, His Tag

    Vascular endothelial growth factor A, VEGF-A, Vascular permeability factor, VPF, VEGF, MGC70609.

    Product # :

    CYT-619

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    • biological activity
    • More Info

    Description

    Vascular Endothelial Growth Factor-121 Human Recombinant produced in E.Coli is a double, non-glycosylated, polypeptide chain (aa 207-327) containing a total of 142 amino acids and having a molecular mass of 16.3 kDa. The VEGF-121 is fused to a 20 amino acid His tag at N-terminus and purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    VEGF-121 His Tag in 20mM Tris pH-8 and 10% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    Biological Activity

    The ED50 for this effect is <4.2 ng/ml. Measured in a cell proliferation assay using NIH-3T3 cell, corresponding to a specific activity of less than 238,095.23units/mg.

    More Info

    • Introduction

      Vascular endothelial growth factor is an important signaling protein involved in both vasculogenesis and angiogenesis. As its name implies, VEGF activity has been mostly studied on cells of the vascular endothelium, although it does have effects on a number of other cell types (e.g. stimulation monocyte/macrophage migration, neurons, cancer cells, kidney epithelial cells ).VEGF mediates increased vascular permeability, induces angiogenesis, vasculogenesis and endothelial cell growth, promotes cell migration, and inhibits apoptosis. In vitro, VEGF has been shown to stimulate endothelial cell mitogenesis and cell migration. VEGF is also a vasodilator and increases microvascular permeability and was originally referred to as vascular permeability factor.
      Elevated levels of this protein is linked to POEMS syndrome, also known as Crow-Fukase syndrome. Mutations in this gene have been associated with proliferative and nonproliferative diabetic retinopathy.

    • Synonyms

      Vascular endothelial growth factor A, VEGF-A, Vascular permeability factor, VPF, VEGF, MGC70609.

    • 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 MAPMAEGGGQ NHHEVVKFMD VYQRSYCHPI ETLVDIFQEY PDEIEYIFKP SCVPLMRCGG CCNDEGLECV PTEESNITMQ IMRIKPHQGQ HIGEMSFLQH NKCECRPKKD RARQEKCDKP RR.

    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.

    Vegf121 Human His
  • View Data Sheet

    Name :

    RPL7A Human

    Description:

    Ribosomal Protein L7A Human Recombinant

    60S ribosomal protein L7a, L7A, SURF3, TRUP, PLA-X polypeptide, Surfeit locus protein 3, SURF-3.

    Product # :

    PRO-2128

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    Description

    RPL7A Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 289 amino acids (1-266 a.a) and having a molecular mass of 32.4kDa.RPL7A is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    RPL7Aprotein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH 8.0) and 10% glycerol.

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Ribosomal Protein L7A (RPL7A) is a ribosomal protein which is a component of the 60S subunit. RPL7A protein is a member of the L7AE family of ribosomal proteins. RPL7A interacts with a subclass of nuclear hormone receptors, including thyroid hormone receptor, and hinder their ability to transactivate by inhibiting their binding to their DNA response elements.

    • Synonyms

      60S ribosomal protein L7a, L7A, SURF3, TRUP, PLA-X polypeptide, Surfeit locus protein 3, SURF-3.

    • 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 MGSMPKGKKA KGKKVAPAPA VVKKQEAKKV VNPLFEKRPK NFGIGQDIQP KRDLTRFVKW PRYIRLQRQR AILYKRLKVP PAINQFTQAL DRQTATQLLK LAHKYRPETK QEKKQRLLAR AEKKAAGKGD VPTKRPPVLR AGVNTVTTLV ENKKAQLVVI AHDVDPIELV VFLPALCRKM GVPYCIIKGK ARLGRLVHRK TCTTVAFTQV NSEDKGALAK LVEAIRTNYN DRYDEIRRHW GGNVLGPKSV ARIAKLEKAK AKELATKLG.

    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.

    Rpl7A Human
  • View Data Sheet

    Name :

    SARS MERS Spike Antibody

    Description:

    Mouse Anti MERS-CoV Spike

    Middle East respiratory syndrome coronavirus, Human betacoronavirus 2c EMC/2012, MERS-CoV, MERS, MERSCoV SP, Spike glycoprotein, S glycoprotein, S, Spike protein, E2, Peplomer protein.

    Product # :

    ANT-768

    Price :

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    • formulation
    • More Info

    Formulation

    1mg/ml containing Phosphate-Buffered Saline (pH 7.4), 0.02% Sodium Azide and 10% Glycerol.

    More Info

    • Introduction

      Since April 2012, cases of the Middle East Respiratory Syndrome Coronavirus (MERS-CoV) have been identified in various countries. Coronaviruses are the cause of the common cold, SARS (severe acute respiratory syndrome) and other severe illnesses with high mortality rates, all are classified into coronavirus family. MERS-CoV is a new type of SARS found in the coronavirus family causing severe pneumonia with sudden and serious respiratory illness with high mortality rates as well. Since January 27th 2015, the WHO has reported 956 human cases, including 351 deaths. More cases of the new coronavirus strain are expected. Like in other coronaviruses, large surface spike glycoprotein is a central structural protein of this virus; it is located above the virion surface to bind and enter into the target cell. Spike protein has 2 domains- S1 and S2. The S1 domain is responsible for cellular tropism and interaction with target cell, while the S2 domain is responsible for membrane fusion. The C-terminal of S1 domain contains a receptor binding domain, and is also a potential target for vaccine development and an antigen for diagnosis.

    • Synonyms

      Middle East respiratory syndrome coronavirus, Human betacoronavirus 2c EMC/2012, MERS-CoV, MERS, MERSCoV SP, Spike glycoprotein, S glycoprotein, S, Spike protein, E2, Peplomer protein.

    • Physical Appearance

      Sterile filtered colorless solution.

    • Immunogen

      Recombinant MERS-CoV Spike (18-1296aa) purified from Baculovirus.

    • Ig Subclass

      IgG1 kappa.

    • Clone

      PAT40G7AT

    • Applications

      SARS MERS Spike antibody has been tested by ELISA analysis to assure specificity and reactivity. Since application varies, however, each investigation should be titrated by the reagent to obtain optimal results.

    • Type

      Mouse antibody Monoclonal.

    • Storage Procedures

      For periods up to 1-month store at 4°C, for longer periods of time, store at -20°C. Prevent freeze thaw cycles.

    • Purification Method

      SARS MERS Spike antibody was purified from mouse ascitic fluids by protein-A affinity chromatography.

    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.

    Cov Mers Spike Antibody
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