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Search results

1000 results found for “dead box protein”

Name

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  • View Data Sheet

    Name :

    BNP Protein

    Description:

    B-type Natriuretic Peptide Human Recombinant

    NPPB, Natriuretic Peptide Precursor B, BNP, B-type Natriuretic Peptide.

    Product # :

    CYT-327

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    Description

    B-type Natriuretic Peptide Recombinant Human produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 32 amino acids and having a molecular mass of 3,500 Dalton. NPPB is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Natriuretic Peptide Precursor B was lyophilized from a 0.2 µm filtered concentrated solution in PBS, pH 7.4.

    Purity

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

    More Info

    • Introduction

      Natriuretic Peptide Precursor B acts as a cardiac hormone with a variety of biological actions including natriuresis, diuresis, vasorelaxation, and inhibition of renin and aldosterone secretion. It is thought to play a key role in cardiovascular homeostasis. Helps restore the body's salt and water balance. Improves heart function.

    • Synonyms

      NPPB, Natriuretic Peptide Precursor B, BNP, B-type Natriuretic Peptide.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Amino Acid Sequence

      SPKMVQGSGCFGRKMDRISSSSGLGCKVLRRH.

    • Background

      What is the molecular weight / Mw of BNP Protein?
      BNP Protein has a total Mw of 3.5kDa.

      What is the source or expression system of BNP Protein?

      Escherichia Coli.

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

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

      What is the amino acid sequence of BNP Protein?

      SPKMVQGSGCFGRKMDRISSSSGLGCKVLRRH.

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

      What is the endotoxin level for BNP Protein?

      The endotoxin level is minimal, BNP 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.

    Nppb Human Recombinant
  • View Data Sheet

    Name :

    C1QTNF3 Human

    Description:

    Complement C1q Tumor Necrosis Factor-Related Protein 3 Human Recombinant

    Complement C1q tumor necrosis factor-related protein 3, Secretory protein CORS26, C1QTNF3, CTRP3, Cors, Corcs, CORS26, FLJ37576, Cartducin.

    Product # :

    PRO-653

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    Description

    C1QTNF3 Human Recombinant produced in E.Coli is a single, non-glycosylated, Polypeptide chain containing 234 amino acids and having a molecular mass of 25.4 kDa. The protein contains an extra 10 aa His tag at N-terminus. The C1QTNF3 amino acid sequence is identical to UniProtKB/Swiss-Prot entry Q9BXJ4 amino acids 23–246. The C1QTNF3 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Human C1QTNF3 was filtered (0.4µm) and lyophilized in 0.5 mg/ml in 0.05M Acetate buffer pH4.

    Purity

    The purity of C1QTNF3 is greater than 95% as determined by SDS PAGE.

    More Info

    • Introduction

      C1QTNF3 also called Cartducin is a novel angiogenic factor in the formation of neointima following angioplasty. C1QTNF3 a paralog of Acrp30 (adiponectin). C1QTNF3 is a secretory protein produced by chondrogenic precursors & proliferating chondrocytes, and belongs to a novel C1q family of proteins. Cartducin promotes the growth of mesenchymal chondroprogenitor cells & chondrosarcoma-derived chondrocytic cells in vitro. Cartducin stimulates mesenchymal chondroprogenitor cell proliferation through extracellular signal-regulated kinase and phosphatidylinositol 3-kinase/Akt pathways. C1QTNF3 promotes proliferation & the migration of endothelial cells.

    • Synonyms

      Complement C1q tumor necrosis factor-related protein 3, Secretory protein CORS26, C1QTNF3, CTRP3, Cors, Corcs, CORS26, FLJ37576, Cartducin.

    • Stability

      Store lyophilized C1QTNF3 at -20°C. Aliquot the product after reconstitution to avoid repeated freezing/thawing cycles. Reconstituted C1QTNF3 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 0.1M Acetate buffer pH4 to prepare a working stock solution of approximately 0.5 mg/ml and let the lyophilized pellet dissolve completely. For conversion into higher pH value, we recommend intensive dilution by relevant buffer to a concentration of 10µg/ml. In higher concentrations the solubility of the protein is limited. Product is not sterile! Please filter the product by an appropriate sterile filter before using it in the cell culture.

    • Amino Acid Sequence

      MKHHHHHHAS QDEYMESPQT GGLPPDCSKC CHGDYSFRGY QGPPGPPGPP GIPGNHGNNG NNGATGHEGA KGEKGDKGDL GPRGERGQHG PKGEKGYPGI PPELQIAFMA SLATHFSNQN SGIIFSSVET NIGNFFDVMT GRFGAPVSGV YFFTFSMMKH EDVEEVYVYL MHNGNTVFSM YSYEMKGKSD TSSNHAVLKL AKGDEVWLRM GNGALHGDHQ RFSTFAGFLLFETK.

    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.

    C1Qtnf3 Human
  • View Data Sheet

    Name :

    C5a Protein

    Description:

    Complement C5a Human

    Complement Component 5, C3 and PZP-Like Alpha-2-Macroglobulin Domain-Containing Protein 4, C5a Anaphylatoxin, Prepro-C5, CPAMD4, Anaphylatoxin C5a Analog, ECLZB, C5A, C5D, C5b, C5.

    Product # :

    PRO-2692

    Price :

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    • More Info

    Description

    Human Complement C5a produced in Human plasma having a molecular mass of 10.4 kDa.

    Source

    Human Plasma.

    Formulation

    C5a protein solution contains 120 mM NaCl and 10mM HEPES, pH 7.2.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Complement Component C5a (C5a) is involved in the complement system and it is encoded by the C5 gene in human. Complement C5 is cleaved into C5a and C5b. C5a has an imperative role in chemotaxis and C5b forms the 1st part of the complement membrane attack complex. Complement C5 is the 5th component of complement, which plays a central role in inflammatory and cell killing processes. C5a protein is composed of alpha and beta polypeptide chains, which are linked by a disulfide bridge. An activation peptide, C5a, which is an anaphylatoxin, which has potent spasmogenic and chemotactic activity, is derivative from the alpha polypeptide via cleavage with a convertase. The C5b macromolecular cleavage product forms a complex with the C6 complement component, and this complex is the basis for creation of the membrane attack complex, which includes supplementary complement components.

    • Synonyms

      Complement Component 5, C3 and PZP-Like Alpha-2-Macroglobulin Domain-Containing Protein 4, C5a Anaphylatoxin, Prepro-C5, CPAMD4, Anaphylatoxin C5a Analog, ECLZB, C5A, C5D, C5b, C5.

    • Physical Appearance

      Sterile filtered solution.

    • Stability

      C5a Human is stable at 4°C if entire vial will be used within 2-4 weeks.Store, frozen below -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.

    • Human Virus Test

      Plasma from each donor has been tested and found negative for antibody to HIV-1, HIV-2, HCV, HTLV-I &II, STS and HBSAG.

    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.

    Complement C5A
  • View Data Sheet

    Name :

    RBP4 Protein

    Description:

    Retinol Binding Protein-4 Human

    Retinol Binding Protein 4, RBP-4, RBP4, Plasma retinol-binding protein, PRBP, RBP.

    Product # :

    CYT-1218

    Price :

    Quantity :

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    • description
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    • More Info

    Description

    RBP4 Human produced in Pooled human plasma can be used as a calibrator in immunoassays. Immunoreactivity was checked using monoclonal antibodies specific to RBP4.

    Source

    Human Plasma.

    Formulation

    RBP4 was lyophilized from PBS, 150mM NaCl, and 10mM K-phosphate, pH 7.4.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Synonyms

      Retinol Binding Protein 4, RBP-4, RBP4, Plasma retinol-binding protein, PRBP, RBP.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized Retinol Binding Protein-4 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution RBP4 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 RBP4 in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Background

      Retinol Binding Protein 4 (RBP4) is a multifunctional protein that plays a crucial role in the transport of retinol (vitamin A) in the bloodstream. Beyond its traditional role in vitamin A metabolism, RBP4 has emerged as a key player in various physiological processes and pathological conditions. This research endeavors to explore the diverse facets of RBP4 in human biology, shedding light on its physiological functions, regulatory mechanisms, and implications in health and disease.

      Physiological Functions:

      At its core, RBP4 acts as a carrier protein, shuttling retinol from the liver, where it is stored, to peripheral tissues where it is utilized. Retinol is vital for vision, immune function, growth, and development, making RBP4 an essential component in these processes. By regulating the availability of retinol, RBP4 contributes significantly to maintaining normal vision, immune responses, and cellular differentiation, particularly in epithelial tissues.

      Metabolic Significance:

      Research has unveiled RBP4’s role in metabolic regulation. It has been associated with insulin resistance, a hallmark of type 2 diabetes mellitus. Elevated RBP4 levels are observed in individuals with obesity and insulin resistance, implicating its involvement in metabolic disorders. Understanding the interplay between RBP4, insulin signaling, and glucose metabolism is crucial for deciphering the complexities of diabetes and metabolic syndrome.

      Immunological Implications:

      Beyond its metabolic functions, RBP4 has been implicated in immune responses. Studies have suggested its involvement in modulating inflammatory processes and immune cell functions. By influencing immune cell differentiation and cytokine production, RBP4 may play a role in both immune defense and autoimmune disorders. Investigating these immunological implications provides insights into the crosstalk between metabolic and immune pathways.

      Genetic and Environmental Influences:

      Genetic variations and environmental factors, such as diet and lifestyle, can impact RBP4 levels and functions. Research into these influences is essential for understanding individual susceptibility to metabolic disorders and inflammatory conditions. Genetic studies shed light on the hereditary aspects of RBP4 regulation, providing valuable information for personalized medicine approaches.

      Clinical Relevance:

      RBP4’s involvement in various diseases, including diabetes, cardiovascular diseases, and certain cancers, underscores its clinical relevance. It serves as a potential biomarker for metabolic dysregulation and a target for therapeutic interventions. Moreover, RBP4-targeted therapies are being explored for their potential in managing metabolic disorders and related complications.

      Conclusion:

      RBP4, once primarily recognized for its role in vitamin A transport, has evolved into a multifaceted protein with intricate roles in metabolism, immunity, and disease. Its functions extend far beyond being a mere carrier of retinol, influencing diverse physiological processes and serving as a nexus between metabolic health and immunological responses. Unraveling the complexities of RBP4 opens avenues for understanding diseases like diabetes and offers promising prospects for innovative therapies, emphasizing its significance in human biology and medicine.

    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.

    Rbp4 Protein
  • View Data Sheet

    Name :

    Leptin qA Ovine, PEG

    Description:

    Leptin Quadruple Antagonist Pegylated Ovine Recombinant

    Product # :

    CYT-1246

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    Description

    Leptin Antagonist Quadruple Mutant Ovine Recombinant is a single non-glycosilated polypeptide chain containing 146 amino acids and additional Ala at N-terminus. The Ovine Leptin antagonist was mutated, resulting in D23L/L39A/D40A/F41A mutant. The Ovine Leptin antagonist is bound to 20 kDa mono-PEG at N-terminus, resulting in 35.6 kDa. The Ovine Leptin Quadruple anatagonist Pegylated runs as a 48 kDa due to enlarged hydrodymanic volume. Leptin Antagonist Quadruple Mutant Ovine Recombinant was purified by proprietary chromatographic techniques.

    Source

    Escherichia coli.

    Formulation

    The Ovine Leptin Quadruple anatagonist was lyophilized from a concentrated (0.65mg/ml) solution with 0.003mM NaHCO3.

    Purity

    Greater than 95.0% as determined by:

    (a) Gel filtration analysis.

    (b) Analysis by SDS-PAGE.

    Biological Activity

    Pegylated Ovine Leptin Quadruple Antagonist inhibits leptin-induced proliferation of BAF/3 cells stably transfected with the long form of human leptin receptor. Pegylated recombinant Ovine leptin antagonist in vitro activity is 6-8 fold lower than the non-pegylated recombinant super Ovine leptin antagonist but is 15 fold higher as compared to pegylated recombinant super active ovine leptin antagonist.

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    • Physical Appearance

      White lyophilized (freeze-dried) powder.

    • Stability

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

    • Solubility

      It is recommended to reconstitute the lyophilized Leptin Antagonist Quadruple Mutant Ovine Recombinant in sterile water or sterile 0.4% NaHCO3adjusted to pH 8-9, not less than 100µg/ml, which can then be further diluted with other aqueous solutions.

    • Background

      Leptin is mainly produced by adipocytes. Leptin’s main part is to regulate long-term energy balance. Leptin is encoded by the LEP gene. Leptin effects mostly on leptin receptors in the cell mambrane of various cells in the human body. The leptin receptor can be found on a various cell types. The leptin receptor is a single-transmembrane-domain type 1 cytokine receptor. leptin levels influence satiety, appetite and triggers behaviours which save energy. High leptin levels are interpreted by the brain that energy reserves are high, whereas low leptin levels means that energy reserves are low, in the process adapting the organism to starvation through a variety of metabolic, neurobiochemical, endocrine and behavioral change.

    • Protein content

      Protein quantization was carried out by UV spectroscopy at 280 nm using the absorbency value of 0.2 as the extinction coefficient for a 0.1% (1mg/ml) solution at pH 8.0. This value is calculated by the PC GENE computer analysis program of protein sequences (IntelliGenetics).

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    Leptin Antagonist Peg Ovine
  • View Data Sheet

    Name :

    PF 4 Protein

    Description:

    Platelet Factor-4 Human (CXCL4)

    CXCL4, PF-4, PF4, Iroplact, Oncostatin-A, SCYB4, MGC138298.

    Product # :

    CHM-234

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    Description

    Human PF-4 a 7.8 kDa protein consisting of 70 amino acid residues.

    Source

    Human Platelets.

    Formulation

    The CXCL4 protein was lyophilized in PBS buffer pH-7.4.

    Purity

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

    More Info

    • Introduction

      Platelet factor-4 is a 70-amino acid protein that is released from the alpha-granules of activated platelets and binds with high affinity to heparin. Its major physiologic role appears to be neutralization of heparin-like molecules on the endothelial surface of blood vessels, thereby inhibiting local antithrombin III activity and promoting coagulation. As a strong chemoattractant for neutrophils and fibroblasts, PF4 probably has a role in inflammation and wound repair. Oncostatin-A is a member of the CXC chemokine family. Human PF4 is used for the proof of heparin-induced thrombocytopenia. Furthermore it is used as an inhibitor in the angiogenesis during tumor therapy.

    • Synonyms

      CXCL4, PF-4, PF4, Iroplact, Oncostatin-A, SCYB4, MGC138298.

    • Physical Appearance

      Sterile Filtered white lyophilized powder.

    • Stability

      Human CXCL4 although stable at 25°C 1 week, should be stored desiccated below -18°C. Please prevent freeze-thaw cycles.

    • Solubility

      It is recommended to reconstitute the lyophilized CXCL4 in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      The sequence of the first four N-terminal amino acids was determined and was found to be Glu-Ala-Glu-Glu.

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    Pf 4 Human
  • View Data Sheet

    Name :

    STEAP4 Human

    Description:

    STEAP Family Member 4 Human Recombinant

    DKFZp666D049, FLJ23153, STAMP2, TIARP, TNFAIP9, Six-transmembrane epithelial antigen of prostate 4, SixTransMembrane protein of prostate 2, Tumor necrosis factor, alpha-induced protein 9.

    Product # :

    PRO-1893

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    Description

    STEAP4 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 188 amino acids (1-152 a.a) and having a molecular mass of 20.6kDa.STEAP4 is fused to a 36 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    STEAP4 protein solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.4M UREA and 10% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      STEAP Family Member 4 (STEAP4) is a member of the STEAP (six transmembrane epithelial antigen of prostate) family, resides in the golgi apparatus. STEAP4 act as a metalloreductase which has the ability to reduce both Fe(3+) to Fe(2+) and Cu(2+) to Cu(1+),using NAD(+) as acceptor. According to studies in mice and human it is possible that STEAP4 may involve in adipocyte development and metabolism, and also contribute to the normal biology of the prostate cell.

    • Synonyms

      DKFZp666D049, FLJ23153, STAMP2, TIARP, TNFAIP9, Six-transmembrane epithelial antigen of prostate 4, SixTransMembrane protein of prostate 2, Tumor necrosis factor, alpha-induced protein 9.

    • 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

      MRGSHHHHHH GMASMTGGQQ MGRDLYDDDD KDRWGSMEKT CIDALPLTMN SSEKQETVCI FGTGDFGRSL GLKMLQCGYS VVFGSRNPQK TTLLPSGAEV LSYSEAAKKS GIIIIAIHRE HYDFLTELTE VLNGKILVDI SNNLKINQYP ESNAEYLAHL VPGAHVVKAF NTISAWALQS GALDASRQ.

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    Steap4 Human
  • View Data Sheet

    Name :

    HNRNPK Human

    Description:

    Heterogeneous Nuclear Ribonucleoprotein K Human Recombinant

    CSBP, HNRPK, TUNP, Heterogeneous nuclear ribonucleoprotein K, hnRNP K, Transformation up-regulated nuclear protein, HNRNPK.

    Product # :

    PRO-1539

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    Description

    HNRNPK Human Recombinant produced in E. coli is a single polypeptide chain containing 299 amino acids (1-276) and having a molecular mass of 33kDa. HNRNPK is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

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

    Purity

    Greater than 95% as determined by SDS-PAGE.

    More Info

    • Introduction

      Heterogeneous Nuclear Ribonucleoprotein K, also known as HNRNPK, is a part of the subfamily of ubiquitously expressed heterogeneous nuclear ribonucleoproteins (hnRNPs). HNRNPK takes part in p53/TP53 reaction to DNA damage, acting at the level of both transcription activation and repression. HNRNPK is located in the nucleoplasm and has 3 repeats of KH domains which bind to RNAs.

    • Synonyms

      CSBP, HNRPK, TUNP, Heterogeneous nuclear ribonucleoprotein K, hnRNP K, Transformation up-regulated nuclear protein, HNRNPK.

    • 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 MGSMETEQPE ETFPNTETNG EFGKRPAEDM EEEQAFKRSR NTDEMVELRI LLQSKNAGAV IGKGGKNIKA LRTDYNASVS VPDSSGPERI LSISADIETI GEILKKIIPT LEEGLQLPSP TATSQLPLES DAVECLNYQH YKGSDFDCEL RLLIHQSLAG GIIGVKGAKI KELRENTQTT IKLFQECCPH STDRVVLIGG KPDRVVECIK IILDLISESP IKGRAQPYDP NFYDETYDYG GFTMMFDDRR GRPVGFPMRG RGGFDRMPPG RGGRPMPPS.

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    Hnrnpk Human
  • View Data Sheet

    Name :

    HAUS1 Human

    Description:

    HAUS Augmin-Like Complex, Subunit 1 Human Recombinant

    HAUS augmin-like complex subunit 1, Coiled-coil domain-containing protein 5, Enhancer of invasion-cluster, HEI-C, HAUS1, CCDC5, HEIC, HsT1461.

    Product # :

    PRO-1077

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    Description

    HAUS1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 302 amino acids (1-278 a.a) and having a molecular mass of 34.4kDa.HAUS1 is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    HAUS1 protein solution (0.25mg/ml) containing 20mM Tris-HCl buffer (pH8.0), 50% glycerol, 0.2M NaCl and 2mM DTT.

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      HAUS augmin-like complex subunit 1 (HAUS1) is 1 of 8 subunits of the 390kDa human augmin complex/ HAUS complex. The augmin complex is a microtubule-binding complex required in microtubule generation within the mitotic spindle and is imperative to mitotic spindle compilation. HAUS1 contributes to mitotic spindle assembly, maintenance of centrosome integrity and completion of cytokinesis as part of the HAUS augmin-like complex. HAUS1 is broadly expressed, especially in the pancreas, kidney, skeletal muscle, liver and heart. However it is weakly expressed in the lung, brain and placenta. HAUS1-depleted cells hold functional cell cycle checkpoints, but the depletion reduces the G2/M cell cycle compartment and stimulates apoptosis. The HAUS1 protein level remains constant through the cell cycle.

    • Synonyms

      HAUS augmin-like complex subunit 1, Coiled-coil domain-containing protein 5, Enhancer of invasion-cluster, HEI-C, HAUS1, CCDC5, HEIC, HsT1461.

    • 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 MGSHMEPQEE RETQVAAWLK KIFGDHPIPQ YEVNPRTTEI LHHLSERNRV RDRDVYLVIE DLKQKASEYE SEAKYLQDLL MESVNFSPAN LSSTGSRYLN ALVDSAVALE TKDTSLASFI PAVNDLTSDL FRTKSKSEEI KIELEKLEKN LTATLVLEKC
      LQEDVKKAEL HLSTERAKVD NRRQNMDFLK AKSEEFRFGI KAAEEQLSAR GMDASLSHQS LVALSEKLAR LKQQTIPLKK KLESYLDLMP NPSLAQVKIE EAKRELDSIE AELTRRVDMM EL.

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    Haus1 Human
  • View Data Sheet

    Name :

    Protein Cys-A/G

    Description:

    Protein Cys-A/G Recombinant

    Product # :

    PRO-1929

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    Description

    Protein-A/G Recombinant produced in E.Coli is a single non-glycosylated polypeptide chain fused with a Cys at N-terminus. Protein-A/G is comprised of 5 IgG-binding regions of protein A (E-D-A-B-C) and 2 of protein G (C1-C3) containing 430 amino acids in total and having a molecular mass of 47.8kDa. Cell wall binding region, cell membrane binding region and albumin binding region have been eliminated from the recombinant Protein A/G to guarantee the maximum specific IgG binding.

    Source

    Escherichia Coli.

    Formulation

    Protein-A/G was lyophilized without any additives.

    Purity

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

    More Info

    • Introduction

      The recombinant Protein A/G is a genetically engineered protein comprised of 7 IgG-binding domains EDABC-C1C3, corresponding to the Protein A and G domains which are included in the recombinant sequence. The Protein A part is from Staphylococcus aureus segments E, D, A, B and C. The Protein G part is from Streptococcus segments C1 and C3. The recombinant Protein A/G has a broader binding capacity than either Protein A or Protein G alone. The recombinant Protein A/G is ideal for purification of monoclonal or polyclonal IgG antibodies. Protein A/G binds to various human, mouse and rat IgG subclasses such as the human IgG1, IgG2, IgG3, IgG4; mouse IgG2a, IgG2b, IgG3 and rat IgG2a, IgG2c. In addition, Protein A/G binds to total IgG from cow, goat, sheep, horse, rabbit, guinea pig, pig, dog and cat.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized Protein-A/G although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Protein-A/G 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 Protein-A/G in sterile 18M-cm H2O not less than 0.1mg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      CNAAQHDEAQ QNAFYQVLNM PNLNADQRNG FIQSLKDDPS QSANVLGEAQ KLNDSQAPKA DAQQNNFNKD QQSAFYEILN MPNLNEAQRN GFIQSLKDDP SQSTNVLGEA KKLNESQAPK ADNNFNKEQQ NAFYEILNMP NLNEEQRNGF IQSLKDDPSQ SANLLSEAKK LNESQAPKAD NKFNKEQQNA FYEILHLPNL NEEQRNGFIQ SLKDDPSQSA NLLAEAKKLN DAQAPKADNK FNKEQQNAFY EILHLPNLTE EQRNGFIQSL KDDPSVSKEI LAEAKKLNDA QAPKEEDSLE GSGSGTYKLI LNGKTLKGET TTEAVDAATA EKVFKQYAND NGVDGEWTYD DATKTFTVTE KPEVIDASEL TPAVTTYKLV INGKTLKGET TTKAVDAETA EKAFKQYAND NGVDGVWTYD DATKTFTVTE.

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    Protein Cys A G
  • View Data Sheet

    Name :

    FAM107B Human

    Description:

    Family with Sequence Similarity 107, Member B Human Recombinant

    FAM107B protein, FLJ45505, MGC11034, Protein FAM107B, Family with Sequence Similarity 107, Member B, FAM107B, C10orf45.

    Product # :

    PRO-1691

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    Description

    FAM107B Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 154 amino acids (1-131) and having a molecular mass of 17.9kDa.FAM107B is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The FAM107B solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 20% glycerol and 1mM DTT.

    Purity

    Greater than 95% as determined by SDS-PAGE.

    More Info

    • Introduction

      Family with Sequence Similarity 107, Member B (FAM107B) which is a part of the FAM107 family, is expressed in most tissues in the human body. FAM107B exists in all stages of human development.

    • Synonyms

      FAM107B protein, FLJ45505, MGC11034, Protein FAM107B, Family with Sequence Similarity 107, Member B, FAM107B, C10orf45.

    • 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 MGSMAEPDYI EDDNPELIRP QKLINPVKTS RNHQDLHREL LMNQKRGLAP QNKPELQKVM EKRKRDQVIK QKEEEAQKKK SDLEIELLKR QQKLEQLELE KQKLQEEQEN APEFVKVKGN LRRTGQEVAQ AQES.

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    Fam107B Human
  • View Data Sheet

    Name :

    C3 Rat

    Description:

    Complement C3 Rat

    Complement C3, C3 and PZP-like alpha-2-macroglobulin domain-containing protein 1, C3, CPAMD1.

    Product # :

    PRO-2706

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    Description

    Rat Complement C3 produced in Rat plasma having a molecular weight of 187kDa.

    Source

    Rat Plasma.

    Formulation

    C3 solution contains phosphate buffer saline.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      C3 is central to the activation of all 3 pathways of complement activation. Initiation of each pathway generates proteolytic enzyme complexes which binds the target surface. These enzymes cleave a peptide bond in C3 releasing the anaphylatoxin C3a and activating C3b. Most of the C3 activated during complement activation never attaches to the surface due to its thioester reaction with water forming fluid phase C3b which is rapidly inactivated by factors H and I forming iC3b. Surface-bound C3b is necessary in all 3 pathways for efficient activation of C5 and formation of C5b-9 complexes that lyse the target cell membrane.

    • Synonyms

      Complement C3, C3 and PZP-like alpha-2-macroglobulin domain-containing protein 1, C3, CPAMD1.

    • Physical Appearance

      Sterile filtered solution.

    • Stability

      C3 Mouse is stable at 4°C if entire vial will be used within 2-4 weeks.Store, frozen below -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.

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    C3 Rat
  • View Data Sheet

    Name :

    SMAC/DIABLO Human

    Description:

    SMAC/DIABLO Human Recombinant

    Diablo homolog mitochondrial, Second mitochondria-derived activator of caspase, Smac protein, Direct IAP-binding protein with low pI, DIABLO, SMAC, SMAC3, DIABLO-S, FLJ10537, FLJ25049.

    Product # :

    PRO-614

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    Description

    Smac/Diablo Human Recombinant fused to N-terminal T7-Tag produced in E.Coli is a single, non-glycosylated polypeptide chain containing 199 amino acids and having a molecular mass of 22 kDa.

    Source

    Escherichia Coli.

    Formulation

    The Smac/Diablo solution contains 20mM Tris pH-7.5.

    Purity

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

    More Info

    • Introduction

      Smac/Diablo is a proapoptotic protein that increases caspase activation in the cytochrome c/Apaf-1/caspase-9 pathway by its binding to the inhibitor of apoptosis proteins (IAPs) and removing their inhibitory activity. Smac/Diablo is a mitochondrial protein which enters the cytosol when cells go through apoptosis, and it moderates the caspase inhibition of IAPs.
      Smac/DIABLO expression is associated with the result of renal cell carcinoma.
      Dimeric form of Smac/DIABLO implies that once expressed in the cell the protein has a little probability of dissociation and, thus, loss of function.
      Survivin, Smac/DIABLO, & PKC-? play an important part in the inhibition of apoptosis by FGF-2 in human small cell lung cancer cells. Mitochondrial survivin associates with Smac/DIABLO, delaying its release. Decreased expression of Smac protein takes part in ovarian carcinogenesis and chemotherapeutic resistance. Smac/DIABLO plays a role in tumor cells during the pathway of apoptosis induction. SMAC protein is regulated by XIAP and degraded by proteasome. SMAC protein takes part inleukemic cell apoptosis.
      Smac is released during stress-induced apoptosis in multiple myeloma cells.

    • Synonyms

      Diablo homolog mitochondrial, Second mitochondria-derived activator of caspase, Smac protein, Direct IAP-binding protein with low pI, DIABLO, SMAC, SMAC3, DIABLO-S, FLJ10537, FLJ25049.

    • 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

      MASMTGGQQM GRGSMAVPIA QKSEPHSLSS EALMRRAVSL VTDSTSTFLS QTTYALIEAI TEYTKAVYTL TSLYRQYTSL LGKMNSEEED EVWQVIIGAR AEMTSKHQEY LKLETTWMTA VGLSEMAAEA AYQTGADQAS ITARNHIQLV KLQVEEVHQL SRKAETKLAE AQIEELRQKT QEEGEERAES EQEAYLRED.

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    Smac Diablo Human
  • View Data Sheet

    Name :

    C1QTNF1 Human

    Description:

    Complement C1q Tumor Necrosis Factor-Related Protein 1 Human Recombinant

    GIP, CTRP1, ZSIG37, FLJ90694, C1QTNF1, Complement C1q Tumor Necrosis Factor-Related Protein 1, G protein-coupled receptor-interacting protein.

    Product # :

    PRO-654

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    Description

    C1QTNF1 Human Recombinant produced in E.Coli is a single, non-glycosylated, Polypeptide chain containing 266 amino acids and having a molecular mass of 30.45 kDa. The protein contains an extra His tag at N-terminus. The C1QTNF1 amino acid sequence is identical to UniProtKB/Swiss-Prot entry Q9BXJ1 amino acids 26–281.The C1QTNF1 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Human C1QTNF1 was lyophilized from 50mM Acetate Buffer pH-4.

    Purity

    Greater than 95% as determined by SDS PAGE.

    More Info

    • Introduction

      C1QTNF1 is a novel adipokine, providing a significant framework to further address the physiological functions and mechanisms of the action of this family of secreted glycoproteins in normal and disease states. C1QTNF1 increases the production of aldosterone. C1QTNF1 is vastly expressed in obese subjects as well as up-regulated in hypertensive patients, C1QTNF1 is identified molecular link between obesity and hypertension. C1QTNF1 expression may be associated with a low-grade chronic inflammation status in adipose tissues.

    • Synonyms

      GIP, CTRP1, ZSIG37, FLJ90694, C1QTNF1, Complement C1q Tumor Necrosis Factor-Related Protein 1, G protein-coupled receptor-interacting protein.

    • 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 0.1M Acetate buffer pH4 to prepare a working stock solution of approximately 0.5mg/mL and let the lyophilized pellet dissolve completely. For conversion into higher pH value, we recommend intensive dilution by relevant buffer to a concentration of 10μg/ml. In higher concentrations the solubility of this antigen is limited. Product is not sterile! Please filter the product by an appropriate sterile filter before using it in the cell culture.

    • Amino Acid Sequence

      MKHHHHHHAS RVPHVQGEQQ EWEGTEELPS PPDHAERAEE QHEKYRPSQD QGLPASRCLR CCDPGTSMYP ATAVPQINIT ILKGEKGDRG DRGLQGKYGK TGSAGARGHT GPKGQKGSMG APGERCKSHY AAFSVGRKKP MHSNHYYQTV IFDTEFVNLY DHFNMFTGKF YCYVPGLYFF SLNVHTWNQK ETYLHIMKNE EEVVILFAQV GDRSIMQSQS LMLELREQDQ VWVRLYKGER ENAIFSEELD TYITFSGYLVKHATEP.

    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.

    C1Qtnf1 Human
  • View Data Sheet

    Name :

    DHH Human

    Description:

    Desert Hedgehog Human Recombinant

    HHG-3, Desert Hedgehog homolog, MGC35145, Desert hedgehog protein, DHH.

    Product # :

    CYT-467

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    Description

    DHH Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 197 amino acids (23-198) and having a molecular mass of 22 kDa. DHH is fused to His-tag (20 a.a.) at N-terminus and is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    DHH solution containing 20mM MES pH-5.5, 0.5mM DTT and 20% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      DHH is part of the Hedgehog family which encodes signaling molecules that are involved in regulating morphogenesis. DHH protein is a precursor that is autocatalytically cleaved, the N-terminal portion is soluble and contains the signalling activity while the C-terminal portion is involved in precursor processing. Additionally, the C-terminal product covalently attaches a cholesterol moiety to the N-terminal product, restricting the N-terminal product to the cell surface and preventing it from freely diffusing throughout the organism. Defects in DHH protein have been associated with partial gonadal dysgenesis (PGD) accompanied by minifascicular polyneuropathy. DHH plays a role both male gonadal differentiation and perineurial development.
      DHH plays a role in intercellular signaling which is essential for a variety of patterning events during development. DHH functions as a spermatocyte survival factor in the testes & is essential for testes development.

    • Synonyms

      HHG-3, Desert Hedgehog homolog, MGC35145, Desert hedgehog protein, DHH.

    • 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 MCGPGRGPVG RRRYARKQLV PLLYKQFVPG VPERTLGASG PAEGRVARGS ERFRDLVPNY NPDIIFKDEE NSGADRLMTE RCKERVNALA IAVMNMWPGV RLRVTEGWDE DGHHAQDSLH YEGRALDITT SDRDRNKYGL LARLAVEAGF DWVYYESRNH VHVSVKADNS LAVRAGG.

    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.

    Dhh Human
  • View Data Sheet

    Name :

    IMPACT Human

    Description:

    Impact RWD Domain Protein Human Recombinant

    RWDD5, Protein IMPACT, Imprinted and ancient gene protein homolog, IMPACT.

    Product # :

    PRO-1653

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    Description

    IMPACT Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 343 amino acids (1-320 a.a.) and having a molecular mass of 38.9kDa.IMPACT is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

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

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Impact RWD Domain Protein (IMPACT) is a member of the IMPACT family which is comprised of 1 RWD domain. IMPACT is a translational regulator which certifies constant high levels of translation under amino acid starvation. IMPACT interacts with GCN1/GCN1L1, thus preventing activation of GCN2 protein kinases (EIF2AK1 to 4) and subsequent down-regulation of protein synthesis. IMPACT is highly expressed especially in brain.

    • Synonyms

      RWDD5, Protein IMPACT, Imprinted and ancient gene protein homolog, IMPACT.

    • 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 MGSMAEGDAG SDQRQNEEIE AMAAIYGEEW CVIDDCAKIF CIRISDDIDD PKWTLCLQVM LPNEYPGTAP PIYQLNAPWL KGQERADLSN SLEEIYIQNI GESILYLWVE KIRDVLIQKS QMTEPGPDVK KKTEEEDVEC EDDLILACQP ESSVKALDFD ISETRTEVEV EELPPIDHGI PITDRRSTFQ AHLAPVVCPK QVKMVLSKLY ENKKIASATH NIYAYRIYCE DKQTFLQDCE DDGETAAGGR LLHLMEILNV KNVMVVVSRW YGGILLGPDR FKHINNCARN ILVEKNYTNS PEESSKALGK NKKVRKDKKR NEH.

    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.

    Impact Human
  • View Data Sheet

    Name :

    HHEX Human

    Description:

    Hematopoietically Expressed Homeobox Human Recombinant

    Hematopoietically Expressed Homeobox, Hematopoietically-Expressed Homeobox Protein HHEX, Homeobox Hematopoietically Expressed, Proline-Rich Homeodomain-Containing Transcription Factor, Homeobox Protein PRH, Homeobox Protein HEX, HOX11L-PEN, PRHX, HMPH, PRH, HEX.

    Product # :

    PRO-1624

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    Description

    HHEX Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 293 amino acids (1-270) and having a molecular mass of 32.4kDa. HHEX is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The HHEX solution contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 1mM DTT and 40% glycerol.

    Purity

    Greater than 85% as determined by SDS-PAGE.

    More Info

    • Introduction

      The homeobox protein family of transcription factors has many members that take part in developmental processes such as HHEX. HHEX is known to interact with Promyelocytic leukemia protein and expression in specific hematopoietic lines indicates that this protein is involved in hematopoietic differentiation.

    • Synonyms

      Hematopoietically Expressed Homeobox, Hematopoietically-Expressed Homeobox Protein HHEX, Homeobox Hematopoietically Expressed, Proline-Rich Homeodomain-Containing Transcription Factor, Homeobox Protein PRH, Homeobox Protein HEX, HOX11L-PEN, PRHX, HMPH, PRH, HEX.

    • 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 MGSMQYPHPG PAAGAVGVPL YAPTPLLQPA HPTPFYIEDI LGRGPAAPTP APTLPSPNSS FTSLVSPYRT PVYEPTPIHP AFSHHSAAAL AAAYGPGGFG GPLYPFPRTV NDYTHALLRH DPLGKPLLWS PFLQRPLHKR KGGQVRFSND QTIELEKKFE TQKYLSPPER KRLAKMLQLS ERQVKTWFQN RRAKWRRLKQ ENPQSNKKEE LESLDSSCDQ RQDLPSEQNK GASLDSSQCS PSPASQEDLE SEISEDSDQE VDIEGDKSYF NAG

    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.

    Hhex Human
  • View Data Sheet

    Name :

    SKP1 Alpha Human

    Description:

    S-phase Kinase-Associated Protein 1 Isoform A Human Recombinant

    SKP-1, EMC19, MGC34403, OCP-II, OCP2, p19A, SKP1A, TCEB1L, S-phase kinase-associated protein 1, Cyclin-A/CDK2-associated protein p19, p19skp1, RNA polymerase II elongation factor-like protein, Organ of Corti protein 2, OCP-2, Organ of Corti protein II, Transcription elongation factor B, SIII, SKP1.

    Product # :

    PKA-356

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    Description

    Recombinant Human SKP1 produced in E.Coli is a single, non-glycosylated polypeptide chain containing 160 amino acids (1-160 a.a.) and having a molecular mass of 18kDa.SKP1 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The SKP1 protein solution contains 20mM Tris-HCl, pH-8, 10% glycerol and 50mM NaCl.

    Purity

    Greater than 90.0% as determined by(a) Analysis by RP-HPLC.
    (b) Analysis by SDS-PAGE.

    More Info

    • Introduction

      SKP1 is a F-box enzyme which functions as a substrate recognition component of the SCF ubiquitin ligase complex which controls the ubiquitination of proteins involved in cell cycle progression, signal transduction and transcription. SKP1 binds to proteins containing an F-box motif, such as cyclin F, S-phase kinase-associated protein 2, and other regulatory proteins involved in ubiquitin dependent proteolysis. SKP1 takes part in the control of beta-catenin levels and the activity of beta-catenin dependent TCF transcription factors. SKP1 serves as an adapter that links the F-box protein to CUL1 in the SCF complex.

    • Synonyms

      SKP-1, EMC19, MGC34403, OCP-II, OCP2, p19A, SKP1A, TCEB1L, S-phase kinase-associated protein 1, Cyclin-A/CDK2-associated protein p19, p19skp1, RNA polymerase II elongation factor-like protein, Organ of Corti protein 2, OCP-2, Organ of Corti protein II, Transcription elongation factor B, SIII, SKP1.

    • 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

      MPSIKLQSSD GEIFEVDVEI AKQSVTIKTM LEDLGMDDEG DDDPVPLPNV NAAILKKVIQ WCTHHKDDPP PPEDDENKEK RTDDIPVWDQ EFLKVDQGTL FELILAANYL DIKGLLDVTC KTVANMIKGK TPEEIRKTFN IKNDFTEEEE AQVGSTQFCL.

    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.

    Skp1 Human
  • View Data Sheet

    Name :

    POU5F1 Human

    Description:

    POU Class 5 Homeobox 1 Human Recombinant

    POU domain class 5 transcription factor 1, Octamer-binding protein 3, Oct-3, Octamer-binding protein 4, Oct-4, Octamer-binding transcription factor 3, OTF-3, POU5F1, OCT3, OCT4, OTF3, OTF4, MGC22487.

    Product # :

    PRO-088

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    Description

    POU5F1 Human Recombinant produced in E. coli is a single polypeptide chain containing 285 amino acids (1-265) and having a molecular mass of 32.2 kDa.POU5F1 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The POU5F1 solution contains 20mM Tris-HCl buffer (pH 8.0), 0.4M Urea and 10% glycerol.

    Purity

    Greater than 85% as determined by SDS-PAGE.

    More Info

    • Introduction

      POU5F1 is a homeodomain transcription factor of the POU family, expressed in embryonic stem (ES) cells and embryonic carcinoma (EC) cells.POU5F1 is significantly involved in the signaling pathway for maintaining self-renewal and pluripotency of ES cells. POU5F1 has 2 distinct DNA binding domains which independently bind half-sites of the canonical octamer motif. This flexibility allows POU5F1 to bind with distinct DNA motifs by forming heterodimers with other transcription factors or by forming homodimers in several conformations. Human POU5F1 contains a 75aa POU specific (POUS) domain and a 60aa POU-Homeo-(POUH) domain connected by a linker region. The Human POU5F1 specifically interacts with Octamer motif ATGCAAAT. In addition, 2 proline-rich domains in the N-terminal and C-terminal regions are vital for POU5F1 transactivation. POU5F1 regulates a number of target genes and has been shown to work jointly with other transcription factors including Sox2 as well as Nanog to sustain stem cell potency and self-renewal.

    • Synonyms

      POU domain class 5 transcription factor 1, Octamer-binding protein 3, Oct-3, Octamer-binding protein 4, Oct-4, Octamer-binding transcription factor 3, OTF-3, POU5F1, OCT3, OCT4, OTF3, OTF4, MGC22487.

    • 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 MHFYRLFLGA TRRFLNPEWK GEIDNWCVYV LTSLLPFKIQ SQDIKALQKE LEQFAKLLKQ KRITLGYTQA DVGLTLGVLF GKVFSQTTIC RFEALQLSFK NMCKLRPLLQ KWVEEADNNE NLQEICKAET LVQARKRKRT SIENRVRGNL ENLFLQCPKP TLQQISHIAQ QLGLEKDVVR VWFCNRRQKG KRSSSDYAQR EDFEAAGSPF SGGPVSFPLA PGPHFGTPGY GSPHFTALYS SVPFPEGEAF PPVSVTTLGS PMHSN.

    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.

    Pou5F1 Human
  • View Data Sheet

    Name :

    GHRL Protein

    Description:

    Ghrelin Human

    Appetite-regulating hormone precursor, Growth hormone secretagogue, Growth hormone-releasing peptide, GHRP, Motilin-related peptide, M46 protein, Ghrelin, Obestatin, MTLRP.

    Product # :

    HOR-297

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    Description

    Ghrelin Human contains 28 amino acids and a total molecular mass of 3370.9 Dalton and a molecular formula of C149H249N47O42.The GHRL is purified by proprietary chromatographic techniques.

    Formulation

    GHRL was lyophilized without additives.

    Purity

    Greater than 97% as determined by:
    (a) Analysis by RP-HPLC.
    (b) Analysis by SDS-PAGE.

    More Info

    • Introduction

      Obestatin is a hormone that is produced in the cells lining the stomach and small intestine of several mammals including humans; it drastically reduces appetite in mice and is expected to do the same in humans. Obestatin is a peptide hormone - a relatively small protein. It is encoded by the same gene that also encodes ghrelin, a peptide hormone that increases appetite. The protein produced by that gene breaks into two smaller peptides, ghrelin and obestatin. Ghrelin is an endogenous ligand for the growth hormone secretagogue receptor and is involved in regulating growth hormone release. Ghrelin is derived from a preprohormone called preproghrelin, which also generates a second peptide called obestatin. Ghrelin is an endogenous ligand for the orphan G protein-coupled receptor GPR39 and is involved in satiety and decreased food intake.

    • Synonyms

      Appetite-regulating hormone precursor, Growth hormone secretagogue, Growth hormone-releasing peptide, GHRP, Motilin-related peptide, M46 protein, Ghrelin, Obestatin, MTLRP.

    • Physical Appearance

      Sterile Filtered Yellowish lyophilized (freeze-dried) powder that may appear as a gel form.

    • Stability

      Store the lyophilized Ghrelin at -20°C. Aliquot the product after reconstitution to avoid repeated freezing/thawing cycles. Reconstituted GHRL 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 deionized water to a working concentration approximately 0.5mg/1ml and let the lyophilized pellet dissolve completely.

    • Amino Acid Sequence

      Gly-Ser-Ser(n-octanoyl)-Phe-Leu-Ser-Pro-Glu-His-Gln-Arg-Val-Gln-Gln-Arg-Lys-Glu-Ser-Lys-Lys-Pro-Pro-Ala-Lys-Leu-Gln-Pro-Arg-OH.

    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.

    Ghrelin Human
  • View Data Sheet

    Name :

    SPA17 Human

    Description:

    Sperm Autoantigenic Protein 17 Human Recombinant

    CT22, SP17, SP17-1, Sperm surface protein Sp17, Cancer/testis antigen 22, Sperm autoantigenic protein 17, Sperm protein 17, SPA17.

    Product # :

    PRO-1425

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    Description

    SPA17 Human Recombinant produced in E. coli is a single polypeptide chain containing 174 amino acids (1-151) and having a molecular mass of 19.8kDa. SPA17 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    The SPA17 solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 10% glycerol and 1mM DTT.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    More Info

    • Introduction

      SPA17 is a protein present at the cell surface. SPA17 was characterized by its participation in the binding of sperm to the zona pellucida of the oocyte. The central portion of SPA17 has carbohydrate binding motifs and likely takes part in cell-cell adhesion functions such as immune cell migration and metastasis.

    • Synonyms

      CT22, SP17, SP17-1, Sperm surface protein Sp17, Cancer/testis antigen 22, Sperm autoantigenic protein 17, Sperm protein 17, SPA17.

    • 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 MGSMSIPFSN THYRIPQGFG NLLEGLTREI LREQPDNIPA FAAAYFESLL EKREKTNFDP AEWGSKVEDR FYNNHAFEEQ EPPEKSDPKQ EESQISGKEE ETSVTILDSS EEDKEKEEVA AVKIQAAFRG HIAREEAKKM KTNSLQNEEK EENK.

    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.

    Spa17 Human
  • View Data Sheet

    Name :

    SPOP Human

    Description:

    Speckle-Type POZ Protein Human Recombinant

    Speckle-type POZ protein, HIB homolog 1, Roadkill homolog 1, SPOP, TEF2.

    Product # :

    PRO-195

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    Description

    SPOP 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 394 amino acids (1-374 a.a.) and having a molecular mass of 44.3kDa. The SPOP is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The SPOP solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 5mM DTT, 50% glycerol, 0.2M NaCl and 2mM EDTA.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Speckle-type POZ protein (SPOP) belongs to the Tdpoz family containing one N-terminal MATH (Meprin and TRAF homology) domain and one C-terminal BTB/POZ domain. SPOP inhibits IPF1/PDX1 transactivation of established target promoters, may be by recruiting a repressor complex. SPOP is involved in ubiquitinylation and protein degradation as a result of an interaction with CUL-3.

    • Synonyms

      Speckle-type POZ protein, HIB homolog 1, Roadkill homolog 1, SPOP, TEF2.

    • Physical Appearance

      SPOP is supplied as a 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 MSRVPSPPPP AEMSSGPVAE SWCYTQIKVV KFSYMWTINN FSFCREEMGE VIKSSTFSSG ANDKLKWCLR VNPKGLDEES KDYLSLYLLL VSCPKSEVRA KFKFSILNAK GEETKAMESQ RAYRFVQGKD WGFKKFIRRD FLLDEANGLL PDDKLTLFCE
      VSVVQDSVNI SGQNTMNMVK VPECRLADEL GGLWENSRFT DCCLCVAGQE FQAHKAILAA RSPVFSAMFE HEMEESKKNR VEINDVEPEV FKEMMCFIYT GKAPNLDKMA DDLLAAADKY ALERLKVMCE DALCSNLSVE NAAEILILAD LHSADQLKTQ AVDFINYHAS DVLETSGWKS MVVSHPHLVA EAYRSLASAQ CPFLGPPRKR LKQS.

    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.

    Spop Human
  • View Data Sheet

    Name :

    DSTN Human

    Description:

    Destrin Human Recombinant

    Destrin (actin depolymerizing factor), ACTDP, ADF, bA462D18.2 (destrin (actin depolymerizing factor ADF) (ACTDP)), destrin, DSN.

    Product # :

    PRO-1137

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    Description

    DSTN Human Recombinant produced in E. coli is a single polypeptide chain containing 173 amino acids (1-165) and having a molecular mass of 19.5 kDa.DSTN is fused to an 8 amino acid His-tag at C-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    The DSTN solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.1M NaCl, 1mM DTT and 10% glycerol.

    Purity

    Greater than 95% as determined by SDS-PAGE.

    More Info

    • Introduction

      Actin depolymerizing factor (Destrin/DSTN) belongs to the ADF/Cofilin/destrin superfamily which has the ability to swiftly depolymerize F-Actin in a stoichiometric mode. The ADF family of proteins is responsible for enhancing the turnover rate of actin in vivo. Destrin is a small phosphoinositide-sensitive actin-binding protein capable of depolymerizing actin-filaments in vitro. DSTN functions in a pH-independent manner. DSTN is found in a variety of epithelial and endothelial cells, however it is virtually nonexistent in adult mouse heart and skeletal muscle cells. Destrin shares a 71% sequence homology with Cofilin, however the 2 proteins vary in their interaction with Actin.

    • Synonyms

      Destrin (actin depolymerizing factor), ACTDP, ADF, bA462D18.2 (destrin (actin depolymerizing factor ADF) (ACTDP)), destrin, DSN.

    • 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

      MASGVQVADE VCRIFYDMKV RKCSTPEEIK KRKKAVIFCL SADKKCIIVE EGKEILVGDV GVTITDPFKH FVGMLPEKDC RYALYDASFE TKESRKEELM FFLWAPELAP LKSKMIYASS KDAIKKKFQG IKHECQANGP EDLNRACIAE KLGGSLIVAF EGCPVLEHHH HHH

    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.

    Dstn Human
  • View Data Sheet

    Name :

    MBP Protein

    Description:

    Myelin Basic Protein Human

    Maltose-binding periplasmic protein, MBP, MMBP, Maltodextrin-binding protein, malE, b4034, JW3994.

    Product # :

    PRO-2798

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    Description

    MBP Human produced in Human brain is checked using poly and monoclonal antibodies against MBP.

    Source

    Human brain.

    Formulation

    MBP was lyophilized containing no additives.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Synonyms

      Maltose-binding periplasmic protein, MBP, MMBP, Maltodextrin-binding protein, malE, b4034, JW3994.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Background

      Myelin Basic Protein (MBP) stands as a cornerstone in the intricate architecture of the nervous system. As a vital component of the myelin sheath, MBP plays a pivotal role in ensuring the integrity and rapid transmission of nerve impulses. Over the years, scientific inquiry into MBP has revealed its multifaceted functions, not only as a structural element but also as a regulatory molecule involved in various cellular processes. This research seeks to unravel the complexities of MBP, exploring its structural characteristics, physiological significance, and its involvement in neurological disorders.

      Structural Marvel of MBP:

      MBP, an intrinsically disordered protein, boasts a unique structure allowing it to interact with lipid membranes, especially those found in the myelin sheath. Its high arginine and lysine content gives it a positive charge, enabling strong electrostatic interactions with the negatively charged lipids in myelin. This structural adaptation is crucial for the compact wrapping of myelin around axons, facilitating efficient electrical signal conduction.

      Physiological Significance in Myelination:

      In the central nervous system (CNS), oligodendrocytes produce myelin, a lipid-rich substance that insulates axons. MBP, as a major constituent of myelin, plays an indispensable role in this process. It stabilizes the myelin sheath’s structure, ensuring its tight adherence to the axon and promoting the fast, saltatory conduction of nerve impulses. Without functional MBP, myelin integrity is compromised, leading to reduced nerve conduction velocity and impaired neural communication.

      Beyond Structural Functions:

      Recent studies have revealed that MBP is not merely a structural protein but also possesses regulatory functions. It participates in signaling pathways crucial for oligodendrocyte development and myelination. Moreover, MBP’s interaction with cytoskeletal elements suggests its involvement in cellular processes such as axon guidance and neuronal plasticity. Understanding these regulatory roles provides insights into the broader impact of MBP on neural development and function.

      Implications in Neurological Disorders:

      Alterations in MBP have been linked to various neurological disorders, including multiple sclerosis (MS). In MS, the immune system erroneously targets MBP, leading to demyelination and subsequent neurological impairments. Research into MBP-related pathologies not only aids in understanding disease mechanisms but also offers potential therapeutic avenues. Targeting MBP-specific immune responses is a focus of research for developing MS treatments.

      Conclusion:

      MBP, as the guardian of neural transmission, stands as a testament to the marvels of biological architecture. Its intricate structure and multifaceted functions make it indispensable for the proper functioning of the nervous system. Beyond its role as a structural protein, MBP’s involvement in cellular signalling adds layers to its significance. In the realm of neurological disorders, MBP’s complexities provide both challenges and opportunities, guiding scientists toward innovative therapies. This research delves into the world of MBP, appreciating its contributions to neuroscience while aiming to decipher the mysteries that lie within its molecular intricacies.

    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.

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