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Search results

1000 results found for “Osteoprotegerin”

Name

Description

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  • View Data Sheet

    Name :

    CXCL16 Human

    Description:

    CXCL16 Human Recombinant

    Chemokine (C-X-C Motif) Ligand 16, Scavenger Receptor For Phosphatidylserine And Oxidized Low Density Lipoprotein, Transmembrane Chemokine CXCL16, Small-Inducible Cytokine B16, CXC Chemokine Ligand 16, SR-PSOX, SRPSOX, C-X-C Motif Chemokine 16, CXCLG16, SCYB16, CXCL16.

    Product # :

    CHM-029

    Price :

    Quantity :

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    • source
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    • More Info

    Description

    CXCL16 Human Recombinant (30-118 a.a.) produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 89 amino acids and having a molecular mass of 10kDa.The CXCL16 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    CXCL16 protein was lyophilized from a 0.2µm filtered solution in PBS.

    Purity

    Greater than 97.0% as determined by SDS-PAGE.

    Biological Activity

    The ED50, as measured by its ability to chemoattract mouse CXCR6-transfected mouse BaF3 cells, is less than 12ng/ml.

    More Info

    • Introduction

      CXC chemokine ligand 16 (CXCL16) is a type I membrane protein, which contains a non-ELR motif-containing CXC chemokine domain in its extracellular region. Human and Mouse CXCL16 share a 70% a.a. sequence similarity within their chemokine domains and 49% overall a.a. sequence identity. Functional CXCL16 can be dropped from the cell surface as an approximately 35kDa soluble protein. CXCR6 is the functional receptor for CXCL16. CXCL16 functions as a scavenger receptor on macrophages, which specifically binds to OxLDL (oxidized low density lipoprotein), proposing that CXCL16 may be involved in pathophysiology such as atherogenesis. In addition, CXCL16 induces a strong chemotactic response and calcium mobilization. CXCL16 binds to CXCR6/Bonzo.

    • Synonyms

      Chemokine (C-X-C Motif) Ligand 16, Scavenger Receptor For Phosphatidylserine And Oxidized Low Density Lipoprotein, Transmembrane Chemokine CXCL16, Small-Inducible Cytokine B16, CXC Chemokine Ligand 16, SR-PSOX, SRPSOX, C-X-C Motif Chemokine 16, CXCLG16, SCYB16, CXCL16.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized CXCL16 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution CXCL16 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 CXCL16 in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      NEGSVTGSCY CGKRISSDSP PSVQFMNRLR KHLRAYHRCL YYTRFQLLSW SVCGGNKDPW VQELMSCLDL KECGHAYSGI VAHQKHLLP.

    • Background

      What is the molecular weight/Mw of CXCL16 HUMAN Protein?
      CXCL16 HUMAN Protein has a total Mw of 10kDa.

      What is the source or expression system of CXCL16 HUMAN Protein?
      Escherichia Coli.

      What is the Purity of CXCL16 HUMAN Protein?
      CXCL16 HUMAN Protein is >97% pure as determined by SDS-PAGE.

      What is the Biological Activity of CXCL16 HUMAN Protein?
      The ED50, as measured by its ability to chemoattract mouse CXCR6-transfected mouse BaF3 cells, is less than 12ng/ml.

      What is the amino acid sequence of CXCL16 HUMAN Protein?
      NEGSVTGSCY CGKRISSDSP PSVQFMNRLR KHLRAYHRCL YYTRFQLLSW SVCGGNKDPW VQELMSCLDL KECGHAYSGI VAHQKHLLP.

      What applications can CXCL16 HUMAN Protein be used in?
      CXCL16 HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for CXCL16 HUMAN Protein?
      The endotoxin level is minimal, CXCL16 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.

    Cxcl16 Human
  • View Data Sheet

    Name :

    MUSTN1 Human

    Description:

    Musculoskeletal, Embryonic Nuclear Protein 1 Human Recombinant

    Musculoskeletal, Embryonic Nuclear Protein 1, MUSTANG, Musculoskeletal Embryonic Nuclear Protein 1, Musculoskeletal Temporally Activated Novel, MUSTN1.

    Product # :

    PRO-2061

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    • description
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    Description

    MUSTN1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 105 amino acids (1-82 a.a) and having a molecular mass of 11.3kDa. MUSTN1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    MUSTN1 protein solution (0.25 mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 10% glycerol and 1mM DTT.

    Purity

    Greater than 80.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Musculoskeletal, Embryonic Nuclear Protein 1, also known as MUSTN1 is a member of the MUSTANG family. MUSTN1 is implicated in the development andregeneration of the musculoskeletal system.

    • Synonyms

      Musculoskeletal, Embryonic Nuclear Protein 1, MUSTANG, Musculoskeletal Embryonic Nuclear Protein 1, Musculoskeletal Temporally Activated Novel, MUSTN1.

    • 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 MGSMSQAGAQ EAPIKKKRPP VKEEDLKGAR GNLTKNQEIK SKTYQVMREC EQAGSAAPSV FSRTRTGTET VFEKPKAGPT KSVFG.

    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.

    Mustn1 Human
  • View Data Sheet

    Name :

    S100A6 Murine

    Description:

    S100 Calcium Binding Protein A6 Mouse

    Protein S100-A6, S100 calcium-binding protein A6, Calcyclin, Prolactin receptor-associated protein, 5B10, S100a6, Cacy, 2A9, PRA.

    Product # :

    PRO-409

    Price :

    Quantity :

    Shipping Method :

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    • description
    • formulation
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    • More Info

    Description

    S100A6 also called Calcyclin has been purified by HPLC (see Kuznicki et al. (1989) Biochem. J. 263: 951-956).

    Formulation

    The protein was lyophilized from a concentrated solution (1mg/ml) containing no additives.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    More Info

    • Introduction

      S100A6 is a member of the S100 family of proteins containing 2 EF-hand calcium-binding motifs. S100 proteins are localized either in the cytoplasm or the nucleus of a wide range of cells. S100 proteins are involved in the regulation of a number of cellular processes such as cell cycle progression and differentiation. There are at least 13 members in the S100 gene family, which are located as a cluster on chromosome 1q21.
      S100A6 may function in stimulation of Ca2+-dependent insulin release, stimulation of prolactin secretion, and exocytosis. Chromosomal rearrangements and altered expression of the S100A6 gene are implicated in melanoma.

    • Synonyms

      Protein S100-A6, S100 calcium-binding protein A6, Calcyclin, Prolactin receptor-associated protein, 5B10, S100a6, Cacy, 2A9, PRA.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized Mouse S100A6 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Mouse S100A6 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 Mouse S100A6 in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

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

    S100A6
  • View Data Sheet

    Name :

    ANXA3 Human

    Description:

    Annexin A3 Human Recombinant

    ANX3, ANXA3, Annexin-III, Lipocortin-3, Lipocortin-III, Annexin-3, Annexin A3, Placental anticoagulant protein III, PAP-III, 35-alpha calcimedin, Inositol 1,2-cyclic phosphate 2-phosphohydrolase.

    Product # :

    PRO-765

    Price :

    Quantity :

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    • description
    • source
    • formulation
    • purity
    • More Info

    Description

    ANXA3 produced in E.Coli is a single, non-glycosylated polypeptide chain containing 323 amino acids (1-323 a.a.) and having a molecular mass of 36.3 kDa. ANXA3 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The ANXA3 protein solution contains 20mM Tris-HCl, pH-7.5, 1mM DTT and 10% glycerol.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    More Info

    • Introduction

      ANXA3 is an inhibitor of phospholipase A2. ANXA3 possesses anti-coagulant properties. ANXA3 cleaves the cyclic bond of inositol 1,2-cyclic phosphate to form inositol 1-phosphate. ANXA3 is part of the annexin family which are members of the calcium-dependent phospholipid-binding protein family that are involved in the regulation of cellular growth and in signal transduction pathways. ANXA3 takes part as an anti-coagulation factor.

    • Synonyms

      ANX3, ANXA3, Annexin-III, Lipocortin-3, Lipocortin-III, Annexin-3, Annexin A3, Placental anticoagulant protein III, PAP-III, 35-alpha calcimedin, Inositol 1,2-cyclic phosphate 2-phosphohydrolase.

    • 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

      MASIWVGHRG TVRDYPDFSP SVDAEAIQKA IRGIGTDEKM LISILTERSN AQRQLIVKEY QAAYGKELKD DLKGDLSGHF EHLMVALVTP PAVFDAKQLK KSMKGAGTNE DALIEILTTR TSRQMKDISQ AYYTVYKKSL GDDISSETSG DFRKALLTLA DGRRDESLKV DEHLAKQDAQ ILYKAGENRW GTDEDKFTEI LCLRSFPQLK LTFDEYRNIS QKDIVDSIKG ELSGHFEDLL LAIVNCVRNT PAFLAERLHR ALKGIGTDEF TLNRIMVSRS EIDLLDIRTE FKKHYGYSLY SAIKSDTSGD YEITLLKICG GDD.

    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.

    Anxa3 Human
  • View Data Sheet

    Name :

    Elamipretide

    Description:

    Elamipretide

    SS-31, MTP-131, Bendavia.

    Product # :

    HOR-040

    Price :

    Quantity :

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    • description
    • source
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    • More Info
    • HPLC, MS

    Description

    Elamipretide Synthetic is a single, non-glycosylated polypeptide chain containing 4 amino acids, having a molecular mass of 639.79 Dalton and a Molecular formula of C32H49N9O5
    .

    Source

    Synthetic Peptide

    Formulation

    The protein was lyophilized with no additives.

    Purity

    Greater than 97.0% as determined by analysis by RP-HPLC.

    HPLC, MS

    Elamipretide hplc - Product image 1
    elamipretide mass spec - Product image 2

    More Info

    • Synonyms

      SS-31, MTP-131, Bendavia.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Amino Acid Sequence

      H-D-Arg-(2',6'-dimethyl-Tyr)-Lys-Phe-NH2

    • Background

      What is the molecular weight/Mw of Elamipretide Protein?
      Elamipretide Protein has a total Mw of 639Da.
      What is the source or expression system of Elamipretide Protein?
      Synthetic peptide

      What is the Purity of Elamipretide Protein?

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

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

      What is the amino acid sequence of Elamipretide Protein?
      H-D-Arg-(2',6'-dimethyl-Tyr)-Lys-Phe-NH2

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

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

      Elamipretide (also known as SS-31) is a novel mitochondrial-targeted peptide with immense promise as a therapeutic agent in mitochondrial dysfunction-related disorders. This research paper aims to provide a comprehensive analysis of Elamipretide, delving into its biochemical properties, mechanisms of action, and potential applications in various disease conditions.

      Elamipretide, a mitochondria-targeting tetrapeptide, has garnered attention for its unique ability to protect mitochondria from oxidative stress and attenuate mitochondrial dysfunction (Siegel et al., 2013). This paper endeavors to explore Elamipretide's biochemical basis and its potential as a therapeutic agent in various diseases linked to mitochondrial impairment.

      Elamipretide selectively accumulates within the inner mitochondrial membrane, where it exerts its cytoprotective effects. By reducing reactive oxygen species (ROS) production and enhancing electron transport chain efficiency, Elamipretide plays a crucial role in mitochondrial homeostasis (Kloner et al., 2015).

      The mitochondrial protective actions of Elamipretide arise from its interaction with cardiolipin, a phospholipid predominantly localized in the inner mitochondrial membrane. By binding to cardiolipin, Elamipretide stabilizes mitochondrial cristae, improves membrane integrity, and enhances oxidative phosphorylation (Minkler et al., 2015).

      Elamipretide's potential applications extend to a myriad of disease conditions characterized by mitochondrial dysfunction. In preclinical studies, Elamipretide has shown promise in mitigating tissue damage following ischemia-reperfusion injury, preserving cardiac function after myocardial infarction, and ameliorating neurodegenerative processes (Birk et al., 2017; Cho et al., 2015).

      As the research on Elamipretide progresses, further investigation is warranted to better understand its pharmacokinetics, long-term safety, and potential off-target effects. Clinical trials exploring its therapeutic efficacy in human diseases offer exciting prospects for the future.

      Elamipretide, a mitochondria-targeting peptide, emerges as a promising candidate in combating mitochondrial dysfunction-related disorders. Its unique ability to stabilize mitochondrial membranes and enhance cellular bioenergetics positions Elamipretide as a novel therapeutic option for a diverse range of diseases.

    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.

    Elamipretide
  • View Data Sheet

    Name :

    Ferritin Human

    Description:

    Human Liver Ferritin

    Product # :

    PRO-564

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    Description

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

    Source

    Human Liver.

    Formulation

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

    Purity

    Greater than 96.0%.

    More Info

    • Introduction

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

    • Physical Appearance

      Sterile Filtered brownish solution.

    • Stability

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

    • Human Virus Test

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

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

    Ferritin Human
  • View Data Sheet

    Name :

    FGF12 Human

    Description:

    Fibroblast Growth Factor 12 Human Recombinant

    FGF-12, FGF12, FGF12B, FHF1, Fibroblast growth factor 12, Fibroblast growth factor homologous factor 1, FHF-1, Myocyte-activating factor.

    Product # :

    CYT-1113

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    Description

    Fibroblast Growth Factor 12 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 181 amino acids and having a molecular mass of 20.5kDa. The FGF12 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Lyophilized from a 0.2μm filtered concentrated solution in PBS, pH7.4 and 1mM DTT.

    Purity

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

    Biological Activity

    Determined by FGF12 binding ability in a functional ELISA. Immobilized FGFR4/Fc Chimera at 5 µg/mL (100 µL/well) can bind FGF12 with a linear range of 1.6100 ng/mL.

    More Info

    • Introduction

      FGF12 is part of the Fibroblast Growth Factor (FGF) family which has a vast mitogenic and cell survival functions, and play a role in a range of biological activities, among them are embryonic development, cell growth, morphogenesis, tissue repair, tumor growth, and invasion. FGF-12 doesn’t obtain the N-terminal signal sequence present in the majority of the FGF family members, but it contains clusters of basic residues that act as a nuclear localization signal. When transfected into mammalian cells, FGF12 accumulated in the nucleus, but was not secreted. FGF12 is involved in nervous system development and function. FGF12 binds to IB2 (islet brain-2), a cellular kinase scaffold, and voltage gated sodium channels and is also involved in intracellular signalling and ion exchange.

    • Synonyms

      FGF-12, FGF12, FGF12B, FHF1, Fibroblast growth factor 12, Fibroblast growth factor homologous factor 1, FHF-1, Myocyte-activating factor.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized FGF12 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Fibroblast Growth Factor 12 should be stored at 4°C between 2-7 days and for future use below -18°C. Please prevent freeze-thaw cycles.

    • Solubility

      It is recommended to reconstitute the lyophilized Fibroblast Growth Factor 12 in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      MESKEPQLKG IVTRLFSQQG YFLQMHPDGT IDGTKDENSD YTLFNLIPVG LRVVAIQGVK ASLYVAMNGE GYLYSSDVFT PECKFKESVF ENYYVIYSST LYRQQESGRA WFLGLNKEGQ IMKGNRVKKT KPSSHFVPKP IEVCMYREQS LHEIGEKQGR SRKSSGTPTM NGGKVVNQDS T.

    • Background

      What is the molecular weight/Mw of FGF12 Protein?
      FGF12 Protein has a total Mw of 20.5kDa.

      What is the source or expression system of FGF12 Protein?
      Escherichia Coli.

      What is the Purity of FGF12 Protein?
      FGF12 Protein is >98% pure as determined by SDS-PAGE.

      What is the Biological Activity of FGF12 Protein?
      Determined by FGF12 binding ability in a functional ELISA. Immobilized FGFR4/Fc Chimera at 5 µg/mL (100 µL/well) can bind FGF12 with a linear range of 1.6100 ng/mL.

      What is the amino acid sequence of FGF12 Protein?
      MESKEPQLKG IVTRLFSQQG YFLQMHPDGT IDGTKDENSD YTLFNLIPVG LRVVAIQGVK ASLYVAMNGE GYLYSSDVFT PECKFKESVF ENYYVIYSST LYRQQESGRA WFLGLNKEGQ IMKGNRVKKT KPSSHFVPKP IEVCMYREQS LHEIGEKQGR SRKSSGTPTM NGGKVVNQDS T.

      What applications can FGF12 Protein be used in?
      FGF12 Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for FGF12 Protein?
      The endotoxin level is minimal, FGF12 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 12 Protein
  • View Data Sheet

    Name :

    SCG3 Human

    Description:

    Secretogranin III Human Recombinant

    Secretogranin III, secretogranin-3, SGIII.

    Product # :

    PRO-1556

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    Description

    SCG3 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 472 amino acids (20-468) and having a molecular mass of 53.0kDa.SCG3 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The SCG3 solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 1mM DTT and 20% glycerol.

    Purity

    Greater than 85% as determined by SDS-PAGE.

    More Info

    • Introduction

      SCG3 belongs to the chromogranin/secretogranin family of neuroendocrine secretory proteins. Though, the function of SCG3 is unknown, Granins operate as precursors for biologically active peptides. Several granins are known to serve as helper proteins in sorting and proteolytic processing of prohormones.

    • Synonyms

      Secretogranin III, secretogranin-3, SGIII.

    • 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 MGSFPKPGGS QDKSLHNREL SAERPLNEQI AEAEEDKIKK TYPPENKPGQ SNYSFVDNLN LLKAITEKEK IEKERQSIRS SPLDNKLNVE DVDSTKNRKL IDDYDSTKSG LDHKFQDDPD GLHQLDGTPL TAEDIVHKIA ARIYEENDRA VFDKIVSKLL NLGLITESQA HTLEDEVAEV LQKLISKEAN NYEEDPNKPT SWTENQAGKI PEKVTPMAAI QDGLAKGEND ETVSNTLTLT NGLERRTKTY SEDNFEELQY FPNFYALLKS IDSEKEAKEK ETLITIMKTL IDFVKMMVKY GTISPEEGVS YLENLDEMIA LQTKNKLEKN ATDNISKLFP APSEKSHEET DSTKEEAAKM EKEYGSLKDS TKDDNSNPGG KTDEPKGKTE AYLEAIRKNI EWLKKHDKKG NKEDYDLSKM RDFINKQADA YVEKGILDKE EAEAIKRIYS SL.

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    Scg3 Human
  • View Data Sheet

    Name :

    CHGB Human

    Description:

    Chromogranin B Human Recombinant

    SCG1, Secretogranin 1, secretogranin B, CHGB, Sgl, CgB.

    Product # :

    PRO-824

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    Description

    CHGB Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 677 amino acids (21-677 a.a.) and having a molecular mass of 78.4kDa. CHGB protein is fused to a 20 amino acid His-Tag at N-terminus and purified by standard chromatography.

    Source

    Escherichia Coli.

    Formulation

    The CHGB protein 0.25mg/ml solution containing 20mM Tris-HCl pH-8, 0.15M NaCl & 10% glycerol.

    Purity

    Greater than 80% as determined by SDS-PAGE.

    More Info

    • Introduction

      CHGB is a neuroendocrine secretory granule protein, that is the precursor for other biologically active peptides. CHGB is part of the chromogranin/secretogranin protein family and is expressed in the adrenal medulla, and in pheochromocytoma.

    • Synonyms

      SCG1, Secretogranin 1, secretogranin B, CHGB, Sgl, CgB.

    • 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 MPVDNRNHNE GMVTRCIIEV LSNALSKSSA PPITPECRQV LKTSRKDVKD KETTENENTK FEVRLLRDPA DASEAHESSS RGEAGAPGEE DIQGPTKADT EKWAEGGGHS RERADEPQWS LYPSDSQVSE EVKTRHSEKS QREDEEEEEG ENYQKGERGE DSSEEKHLEE PGETQNAFLN ERKQASAIKK EELVARSETH AAGHSQEKTH SREKSSQESG EEAGSQENHP QESKGQPRSQ EESEEGEEDA TSEVDKRRTR PRHHHGRSRP DRSSQGGSLP SEEKGHPQEE SEESNVSMAS LGEKRDHHST HYRASEEEPE YGEEIKGYPG VQAPEDLEWE RYRGRGSEEY RAPRPQSEES WDEEDKRNYP SLELDKMAHG YGEESEEERG LEPGKGRHHR GRGGEPRAYF MSDTREEKRF LGEGHHRVQE NQMDKARRHP QGAWKELDRN YLNYGEEGAP GKWQQQGDLQ DTKENREEAR FQDKQYSSHH TAEKRKRLGE LFNPYYDPLQ WKSSHFERRD NMNDNFLEGE EENELTLNEK NFFPEYNYDW WEKKPFSEDV NWGYEKRNLA RVPKLDLKRQ YDRVAQLDQL LHYRKKSAEF PDFYDSEEPV STHQEAENEK DRADQTVLTE DEKKELENLA AMDLELQKIA EKFSQRG.

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    Chgb Human
  • View Data Sheet

    Name :

    PF4 Bovine

    Description:

    Platelet Factor-4 (CXCL4) Bovine Recombinant

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

    Product # :

    CHM-039

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    Description

    Platelet Factor-4 (CXCL4) Bovine Recombinant produced in E.Coli is a non-glycosylated polypeptide chain containing 88 amino acid and having a molecular mass of approximately 9.5kDa.PF4 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Lyophilized from a 0.2μm filtered concentrated solution in 20 mM PB and 500mM NaCl, pH 7.0.

    Purity

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

    Biological Activity

    The biological activity determined by a chemotaxis bioassay using human neutrophils is 10-100ng/ml.

    More Info

    • Introduction

      Platelet factor-4 is a 70-amino acid protein that is released from the alpha-granules of activated platelets.PF4’s major physiologic role appears to be neutralization of 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. 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 (freeze-dried) powder.

    • Stability

      Lyophilized CXCL4 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Platelet Factor-4 should be stored at 4°C between 2-7 days and for future use below -18°C. Please prevent freeze-thaw cycles.

    • Solubility

      It is recommended to reconstitute the lyophilized Platelet Factor-4 in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      ESSFPATFVP LPADSEGGED EDLQCVCLKT TSGINPRHIS SLEVIGAGTH CPSPQLLATK KTGRKICLDQ QRPLYKKILK KLLDGDES.

    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.

    Cxcl4 Bovine
  • 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

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    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.

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    Rbp4 Protein
  • View Data Sheet

    Name :

    HSA Protein

    Description:

    HSA Human Protein

    HSA, ALB, PRO0883, PRO0903, PRO1341, DKFZp779N1935, GIG20, GIG42, PRO1708, PRO2044, PRO2619, PRO2675, UNQ696, SA, HSA.

    Product # :

    PRO-354

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    Description

    HSA contains 584 amino acid residues derived from the prototypicalHSA sequence.

    Source

    Human Serum.

    Formulation

    0.2gr/ml solution containing no additives.

    Purity

    Greater than 97.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      HSA is synthesized in the liver as preproalbumin which has an N-terminal peptide that is removed before the nascent protein is released from the rough endoplasmic reticulum. The product, proalbumin, is in turn cleaved in the Golgi vesicles to produce the secreted HSA. HSA is a soluble, monomeric protein which comprises about one-half of the blood serum protein. HSA functions primarily as a carrier protein for steroids, fatty acids, and thyroid hormones and plays a role in stabilizing extracellular fluid volume. Mutations in this gene on chromosome 4 result in various anomalous proteins. HSA is a globular unglycosylated serum protein of molecular weight 65,000. The human HSA gene is 16,961 nucleotides long from the putative 'cap' site to the first poly (A) addition site. It is split into 15 exons which are symmetrically placed within the 3 domains that are thought to have arisen by triplication of a single primordial domain.
      HSA is widely used to stabilize blood volume generally from donors but the fear of contamination such as HIV & Hepatitis has enticed great interest in the recombinant form which is identical to the natural blood.
      Suitable for use in biochemical, excipient (an inert substance used as a diluent or vehicle for a drug), culture media and chromatographic applications.

    • Synonyms

      HSA, ALB, PRO0883, PRO0903, PRO1341, DKFZp779N1935, GIG20, GIG42, PRO1708, PRO2044, PRO2619, PRO2675, UNQ696, SA, HSA.

    • Physical Appearance

      Sterile Filtered clear yellowish solution.

    • Stability

      HSA although stable at room temperature for 2 weeks should be stored at 4°C.

    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.

    Human Serum Albumin
  • View Data Sheet

    Name :

    AHSG Human

    Description:

    Alpha-2-HS-Glycoprotein Human Recombinant

    PRO2743, A2HS, AHS, FETUA, HSGA, Alpha-2-HS-glycoprotein, Alpha-2-Z-globulin, Ba-alpha-2-glycoprotein, Fetuin-A.

    Product # :

    PRO-1450

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    Description

    AHSG Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 372 amino acids (19-367 a.a) and having a molecular mass of 39.7kDa (Molecular size on SDS-PAGE will appear higher).AHSG is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    AHSG protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH8.0), 10% glycerol 0.1M NaCl and 1mM DTT.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      AHSG (fetuin-A) which is a glycoprotein present in the serum, is synthesized by hepatocytes. AHSG is one of the fetuin class of plasma binding proteins. It is involved in a number of functions, such as endocytosis, brain development and the formation of bone tissue. It is usually present in the cortical plate of the immature cerebral cortex and bone marrow hemopoietic matrix, hence it has been postulated that it participates in the development of the tissues. Yet, its exact significance is still vague. AHSG promotes endocytosis, hold opsonic properties and influences the mineral phase of the bone. Affinity for calcium and barium ions has been shown.

    • Synonyms

      PRO2743, A2HS, AHS, FETUA, HSGA, Alpha-2-HS-glycoprotein, Alpha-2-Z-globulin, Ba-alpha-2-glycoprotein, Fetuin-A.

    • 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 MGSAPHGPGL IYRQPNCDDP ETEEAALVAI DYINQNLPWG YKHTLNQIDE VKVWPQQPSG ELFEIEIDTL ETTCHVLDPT PVARCSVRQL KEHAVEGDCD FQLLKLDGKF SVVYAKCDSS PDSAEDVRKV CQDCPLLAPL NDTRVVHAAK AALAAFNAQN NGSNFQLEEI SRAQLVPLPP STYVEFTVSG TDCVAKEATE AAKCNLLAEK QYGFCKATLS EKLGGAEVAV TCTVFQTQPV TSQPQPEGAN EAVPTPVVDP DAPPSPPLGA PGLPPAGSPP DSHVLLAAPP GHQLHRAHYD LRHTFMGVVS LGSPSGEVSH PRKTRTVVQP SVGAAAGPVV PPCPGRIRHF KV.

    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.

    Ahsg Human
  • View Data Sheet

    Name :

    AMH Human, HEK

    Description:

    Anti-Mullerian Hormone Human Recombinant, HEK

    Anti-Muellerian hormone, AMH, Muellerian-inhibiting substance, MIS, MIF. 

    Product # :

    PRO-2665

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    Description

    AMH Human Recombinant is a single, glycosylated polypeptide chain containing 439 amino acids (19-451a.a) and having a molecular mass of 46.5kDa (calculated). AMH is fused to a 6 a.a His tag at C-terminal.

    Source

    HEK293

    Formulation

    AMH filtered (0.4 µm) and lyophilized in PBS and 5% (w/v) trehalose.

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Anti-Mullerian Hormone also known as AMH is a member of the TGF-beta family. AMH is a glycoprotein which is produced by the Sertoli cells of the testis, causes regression of the Muellerian duct. AMH inhibits the growth of tumors derived from tissues of Muellerian duct origin. Moreover, AMH participates in Leydig cell differentiation and function in addition to follicular development in adult females.

    • Synonyms

      Anti-Muellerian hormone, AMH, Muellerian-inhibiting substance, MIS, MIF.

    • 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.

    • Amino Acid Sequence

      LLGTEALRAE EPAVGTSGLI FREDLDWPPG SPQEPLCLVA LGGDSNGSSS PLRVVGALSA YEQAFLGAVQ RARWGPRDLA TFGVCNTGDR QAALPSLRRL GAWLRDPGGQ RLVVLHLEEV TWEPTPSLRF QEPPPGGAGP PELALLVLYP GPGPEVTVTR AGLPGAQSLC PSRDTRYLVL AVDRPAGAWR GSGLALTLQP RGEDSRLSTA RLQALLFGDD HRCFTRMTPA LLLLPRSEPA PLPAHGQLDT VPFPPPRPSA ELEESPPSAD PFLETLTRLV RALRVPPARA SAPRLALDPD ALAGFPQGLV NLSDPAALER LLDGEEPLLL LLRPTAATTG DPAPLHDPTS APWATALARR VAAELQAAAA ELRSLPGLPP ATAPLLARLL ALCPGGPGGL GDPLRALLLL KALQGLRVEW RGRDPRGPGR AQRHHHHHH

    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.

    Anti Mullerian Hormone Human
  • View Data Sheet

    Name :

    Latexin Human

    Description:

    Latexin Human Recombinant

    LXN, TCI, ECI, Latexin, Endogenous carboxypeptidase inhibitor, Tissue carboxypeptidase inhibitor, MUM.

    Product # :

    ENZ-407

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    Description

    Recombinant Human Latexin produced in E.Coli is a single, non-glycosylated polypeptide chain containing 222 amino acids and having a molecular mass of 25.7kDa. Latexin is purified by conventional chromatography techniques.

    Source

    Escherichia Coli.

    Formulation

    The Latexin protein solution contains 20mM Tris-HCl, pH-7.5, 50mM NaCl and 10% Glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Latexin enzyme is a carboxypeptidase A inhibitor that is highly expressed in the heart, prostate, ovary, kidney, pancrease, brain and colon. Latexin has no noticeable sequence resemblance with plant and parasite inhibitors, however it is related to a human putative tumor suppressor protein, TIG1. Latexin is down-regulated in the presenilin-1-deficient mouse brain, thus putatively playing a role in Alzheimer's disease.

    • Synonyms

      LXN, TCI, ECI, Latexin, Endogenous carboxypeptidase inhibitor, Tissue carboxypeptidase inhibitor, MUM.

    • 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

      MEIPPTNYPA SRAALVAQNY INYQQGTPHR VFEVQKVKQA SMEDIPGRGH KYRLKFAVEE IIQKQVKVNC TAEVLYPSTG QETAPEVNFTFEGETGKNPD EEDNTFYQRL KSMKEPLEAQ NIPDNFGNVS PEMTLVLHLA WVACGYIIWQ NSTEDTWYKM VKIQTVKQVQ RNDDFIELDYTILLHNIASQ EIIPWQMQVL WHPQYGTKVK HNSRLPKEVQ LE.

    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.

    Latexin Human
  • View Data Sheet

    Name :

    DIRAS1 Human

    Description:

    DIRAS family, GTP-binding RAS-like 1 Human Recombinant

    GTP-binding protein Di-Ras1, Distinct subgroup of the Ras family member 1, Ras-related inhibitor of cell growth, Rig, Small GTP-binding tumor suppressor 1, DIRAS1, GBTS1, Di-Ras1, FLJ42681.

    Product # :

    PRO-256

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    Description

    DIRAS1 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 215 amino acids (1-195a.a.) and having a molecular mass of 24.1 kDa. DIRAS1 protein is fused to a 20 amino acid His tag at N-terminus and is purified by standard chromatography.

    Source

    Escherichia Coli.

    Formulation

    DIRAS1 Human solution (1mg/ml) containing 20mM Tris-HCl buffer(pH 8.0) containing 20% glycerol, 1mM DTT, 0.1M NaCl and 1mM EDTA.

    Purity

    Greater than 95% as determined by SDS-PAGE.

    More Info

    • Introduction

      DIRAS1 is a member of a distinct branch of the functionally diverse Ras superfamily of monomeric GTPases. DIRAS1 demonstrates low GTPase activity and exists mainly in the GTP-bound form. Ras proteins operate as binary molecular switches that control intracellular signaling networks. Ras-regulated signal pathways regulate such processes as actin cytoskeletal integrity, proliferation, differentiation, cell adhesion, apoptosis, and cell migration. Ras and ras-related proteins are frequently deregulated in cancers, leading to increased invasion and metastasis, and decreased apoptosis.

    • Synonyms

      GTP-binding protein Di-Ras1, Distinct subgroup of the Ras family member 1, Ras-related inhibitor of cell growth, Rig, Small GTP-binding tumor suppressor 1, DIRAS1, GBTS1, Di-Ras1, FLJ42681.

    • 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 MPEQSNDYRV VVFGAGGVGK SSLVLRFVKG TFRDTYIPTI EDTYRQVISC DKSVCTLQIT DTTGSHQFPA MQRLSISKGH AFILVFSVTS KQSLEELGPI YKLIVQIKGS VEDIPVMLVG KCDETQREV DTREAQAVAQ EWKCAFMETS AKMNYNVKEL FQELLTLETR RNMSLNIDGK RSGKQKRTDR KGKC.

    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.

    Diras1 Human
  • View Data Sheet

    Name :

    FGFBP Human

    Description:

    Fibroblast Growth Factor Binding Protein 1 Human Recombinant

    Fibroblast Growth Factor Binding Protein 1, FGFBP, HBP17, 17 KDa Heparin-Binding Growth Factor-Binding Protein, 17 KDa HBGF-Binding Protein, FGF-Binding Protein 1, FGF-BP1, FGFBP-1, FGF-BP, Heparin-Binding Growth Factor Binding Protein, Fibroblast Growth Factor-Binding Protein 1, Fibroblast growth factor-binding protein 1.

    Product # :

    CYT-860

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    • sds-page

    Description

    FGFBP Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 234 amino acids (24-234 a.a) and having a molecular mass of 26.2kDa. FGFBP is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    FGFBP protein solution (0.25mg/ml) containing Phosphate buffered saline (pH7.4), 10% glycerol and 1mM DTT.

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

    sds-page

    FGFBP Human - Product image 1

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    • Introduction

      Fibroblast Growth Factor Binding Protein 1, also known as FGFBP1 is a secreted fibroblast growth factor carrier protein. FGFBP1 plays a vital part in cell proliferation, differentiation and migration by binding to fibroblast growth factors and potentiating their biological effects on target cells. In addition, FGFBP1 also takes part in tumor growth as an angiogenic switch molecule, furthermore an expression of FGFBP1 has been associated with more than a few types of cancer as well as pancreatic and colorectal adenocarcinoma.

    • Synonyms

      Fibroblast Growth Factor Binding Protein 1, FGFBP, HBP17, 17 KDa Heparin-Binding Growth Factor-Binding Protein, 17 KDa HBGF-Binding Protein, FGF-Binding Protein 1, FGF-BP1, FGFBP-1, FGF-BP, Heparin-Binding Growth Factor Binding Protein, Fibroblast Growth Factor-Binding Protein 1, Fibroblast growth factor-binding protein 1.

    • Physical Appearance

      Sterile Filtered colorless clear solution.

    • Stability

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

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MGSKKKVKNG LHSKVVSEQK DTLGNTQIKQ KSRPGNKGKF VTKDQANCRW AATEQEEGIS LKVECTQLDH EFSCVFAGNP TSCLKLKDER VYWKQVARNL RSQKDICRYS KTAVKTRVCR KDFPESSLKL VSSTLFGNTK PRKEKTEMSP REHIKGKETT PSSLAVTQTM ATKAPECVED PDMANQRKTA LEFCGETWSS LCTFFLSIVQ DTSC.

    • Background

      What is the molecular weight/Mw of CYT-860 Protein?
      CYT-860 Protein has a total Mw of 26.2kDa.

      What is the source or expression system of CYT-860 Protein?
      Escherichia Coli.

      What is the Purity of CYT-860 Protein?
      CYT-860 Protein is >85% pure as determined by SDS-PAGE.

      What is the Biological Activity of CYT-860 Protein?
      The biological functionality of CYT-860 Protein will be determined in the future.

      What is the amino acid sequence of CYT-860 Protein?
      MGSSHHHHHH SSGLVPRGSH MGSKKKVKNG LHSKVVSEQK DTLGNTQIKQ KSRPGNKGKF VTKDQANCRW AATEQEEGIS LKVECTQLDH EFSCVFAGNP TSCLKLKDER VYWKQVARNL RSQKDICRYS KTAVKTRVCR KDFPESSLKL VSSTLFGNTK PRKEKTEMSP REHIKGKETT PSSLAVTQTM ATKAPECVED PDMANQRKTA LEFCGETWSS LCTFFLSIVQ DTSC.

      What applications can CYT-860 Protein be used in?
      CYT-860 Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for CYT-860 Protein?
      The endotoxin level is minimal, CYT-860 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.

    Fgfbp Human
  • View Data Sheet

    Name :

    GH Antagonist Ovine

    Description:

    Growth Hormone Antagonist Ovine Recombinant

    GH1, GH, GHN, GH-N, hGH-N, Pituitary growth hormone, Growth hormone 1, Somatotropin.

    Product # :

    CYT-215

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    Description

    Somatotropin Ovine Antagonist Recombinant G119R produced in E.Coli is a single, non-glycosylated polypeptide chain containing 191 amino acids and having a molecular mass of 22 kDa. The Somatotropin Ovine Antagonist Recombinant is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The protein was lyophilized from a concentrated (1mg/ml) solution with 0.0045M NaHCO3, pH 9.

    Purity

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

    Biological Activity

    GH G119R acts as antagonist using an in vitro bioassay in PDF-P1 3B9 cells stably transfected with rabbit GH receptors. It is capable of forming a 1:1 complex with the recombinant ovine growth hormone receptor extracellular domain (ECD) and binds to this ECD with affinity similar the the wild type oGH.

    More Info

    • Introduction

      GH is a member of the somatotropin/prolactin family of hormones which play an important role in growth control. The gene, along with four other related genes, is located at the growth hormone locus on chromosome 17 where they are interspersed in the same transcriptional orientation; an arrangement which is thought to have evolved by a series of gene duplications. The five genes share a remarkably high degree of sequence identity. Alternative splicing generates additional isoforms of each of the five growth hormones, leading to further diversity and potential for specialization. This particular family member is expressed in the pituitary but not in placental tissue as is the case for the other four genes in the growth hormone locus. Mutations in or deletions of the gene lead to growth hormone deficiency and short stature.

    • Synonyms

      GH1, GH, GHN, GH-N, hGH-N, Pituitary growth hormone, Growth hormone 1, Somatotropin.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized GH G119R although stable at room temperature for at least two weeks, should be stored desiccated below -18°C. Upon reconstitution and filter sterilization GH can be stored at 4°C, pH 9 for up to 4 weeks. For long term storage and more diluted solutions 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 GH G119R in 0.4% NaHCO3 or water adjusted to pH 9, not less than 100µg/ml, which can then be further diluted to other aqueous solutions, preferably in a presence of a carrier protein such as BSA or similar.

    • Amino Acid Sequence

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

    • Protein content

      Protein quantitation was carried out by UV spectroscopy at 280 nm using the absorbency value of 0.63 as the extinction coefficient for a 0.1% (1mg/ml) solution. This value is calculated by the DNAman computer analysis program of protein sequences.

    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.

    Gh Antagonist Ovine
  • View Data Sheet

    Name :

    LIN28 Human

    Description:

    LIN28 Human Recombinant

    CSDD1, FLJ12457, LIN-28, LIN28A, Protein lin-28 homolog A, ZCCHC1, Zinc finger CCHC domain-containing protein 1, Lin-28A, LIN28.

    Product # :

    PRO-743

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    Description

    Recombinant Human LIN28 produced in E.Coli is a single, non-glycosylated polypeptide chain containing 191 amino acids (42-209) and having a molecular mass of 21.1 kDa.LIN28 is expressed with a 23 amino acid His tag fused at N-Terminus and purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The LIN28 protein solution (0.5mg/ml) contains 20mM Tris-HCl, pH-8, 10% glycerol, 0.1mM PMSF and 0.1M NaCl.

    Purity

    Greater than 85.0% as determined by SDS-PAGE

    More Info

    • Introduction

      LIN28 plays an important role as a 'translational enhancer', leading specific mRNAs to polysomes and therefore increasing the competence of protein synthesis. LIN28 is a marker of undifferentiated human embryonic stem cells and it enhances the efficiency of the formation of induced pluripotent stem (iPS) cells from human fibroblasts. LIN28 binds to the let-7 pre-miRNA and blocks production of the mature let-7 microRNA in mouse embryonic stem cells. Overexpression of LIN28 is associated with human germ-cell tumors.

    • Synonyms

      CSDD1, FLJ12457, LIN-28, LIN28A, Protein lin-28 homolog A, ZCCHC1, Zinc finger CCHC domain-containing protein 1, Lin-28A, LIN28.

    • 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 SSGLVPRGSHRSMGICKWFN VRMGFGFLSM TARAGVALDP PVDVFVHQSK LHMEGFRSLK EGEAVEFTFK KSAKGLESIR VTGPGGVFCI GSERRPKGKS MQKRRSKGDR CYNCGGLDHH AKECKLPPQP KKCHFCQSIS HMVASCPLKA QQGPSAQGKP TYFREEEEEI HSPTLLPEAQ N.

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    Lin28 Human
  • View Data Sheet

    Name :

    BD 1 Human

    Description:

    Beta Defensin-1 Human Recombinant

    Beta-defensin 1, BD-1, Defensin beta 1, hBD-1, HBD1, HBP1, DEFB1, HBD-1, HBP-1, DEFB101, DEFB-1, MGC51822.

    Product # :

    CYT-564

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    Description

    Beta Defensin-1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 47 amino acids and having a molecular mass of 5 kDa.The BD-1 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The Human BD-1 was lyophilized from a concentrated (1mg/ml) solution containing 20mM PBS pH-7.4 and 130mM sodium chloride.

    Purity

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

    Biological Activity

    Determined by its ability to chemoattract CD34+ dendritic cells using a concentration range of 100-1000ng/ml corresponding to a specific activity of 1,000-10,000IU/mg.

    More Info

    • Synonyms

      Beta-defensin 1, BD-1, Defensin beta 1, hBD-1, HBD1, HBP1, DEFB1, HBD-1, HBP-1, DEFB101, DEFB-1, MGC51822.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized Beta Defensin-1 Recombinant although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution BD-1 should be stored at 4°C between 2-7 days and for future use below -18°C.Please prevent freeze-thaw cycles.

    • Solubility

      It is recommended to reconstitute the lyophilized Beta Defensin-1 in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      GNFLTGLGHR SDHYNCVSSG GQCLYSACPI FTKIQGTCYR GKAKCCK.

    • Background

      Beta Defensin-1 Human Recombinant: Unveiling its Potential in Innate Immunity and Therapeutic Applications

      Abstract:


      Beta Defensin-1 (BD-1), a member of the defensin family, plays a crucial role in innate immunity and host defense. This research paper provides an overview of BD-1 human recombinant, exploring its molecular characteristics, antimicrobial properties, and therapeutic applications. Understanding the multifaceted role of BD-1 offers new avenues for developing innovative immunotherapies. This article offers a concise analysis of BD-1, highlighting its impact on innate immunity and its therapeutic potential.

      Introduction:


      Innate immunity serves as the first line of defense against invading pathogens. BD-1, a key peptide within the defensin family, exhibits broad-spectrum antimicrobial activity and plays a pivotal role in host defense mechanisms. This paper provides an overview of BD-1, shedding light on its structure, function, and therapeutic potential.

      BD-1 Structure and Function:


      BD-1 is a cationic peptide with a conserved cysteine motif that confers its antimicrobial properties. It acts by disrupting the integrity of microbial cell membranes, leading to microbial death. Additionally, BD-1 exhibits immunomodulatory effects by stimulating immune cell recruitment and cytokine production.

      Antimicrobial Properties and Therapeutic Applications:


      BD-1 demonstrates antimicrobial activity against a wide range of pathogens, including bacteria, fungi, and viruses. Its ability to combat multidrug-resistant strains makes it an attractive candidate for the development of novel antimicrobial therapies. Furthermore, BD-1's immunomodulatory effects contribute to its potential in treating inflammatory and infectious diseases.

      Therapeutic Potential of BD-1 Human Recombinant:


      BD-1 human recombinant holds significant promise in the field of immunotherapy. Strategies aimed at enhancing BD-1 expression or delivering exogenous BD-1 may help boost innate immune responses in patients with compromised immune systems or chronic infections. Furthermore, BD-1-based therapeutics could be developed to combat antibiotic-resistant infections and prevent biofilm formation.

      Challenges and Future Directions:


      While BD-1 shows immense therapeutic potential, challenges must be addressed. Further research is necessary to optimize the delivery methods of BD-1 and evaluate its long-term safety and efficacy. Additionally, understanding the interplay between BD-1 and other immune factors will aid in developing combinatorial approaches for enhanced therapeutic outcomes.

      Conclusion:


      BD-1 human recombinant represents a promising avenue for developing novel immunotherapies and combating antimicrobial resistance. Understanding the molecular mechanisms and functional implications of BD-1 in innate immunity opens new horizons for innovative treatments. Continued research in this field has the potential to revolutionize the field of immunotherapy and improve patient outcomes.

      What is the molecular weight/Mw of BD1 Protein?
      BD1 Protein has a total Mw of 5kDa.

      What is the source or expression system of BD1 Protein?
      Escherichia Coli.

      What is the Purity of BD1 Protein?
      BD1 Protein is >98% pure as determined by SDS-PAGE.

      What is the Biological Activity of BD1 Protein?
      Determined by its ability to chemoattract CD34+ dendritic cells using a concentration range of 100-1000ng/ml corresponding to a specific activity of 1,000-10,000IU/mg.

      What is the amino acid sequence of BD1 Protein?
      GNFLTGLGHR SDHYNCVSSG GQCLYSACPI FTKIQGTCYR GKAKCCK.

      What applications can BD1 Protein be used in?
      BD1 Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for BD1 Protein?
      The endotoxin level is minimal, BD1 Protein was purified using conventional chromatography techniques.

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

    Beta Defensin 1 Human
  • View Data Sheet

    Name :

    VEGF E (Orf Virus)

    Description:

    Vascular Endothelial Growth Factor-E Recombinant (Orf Virus)

    Product # :

    CYT-263

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    • More Info

    Description

    A DNA sequence encoding the mature variant of ovVEGF-E isolate D1701 (Dehio et al., 1999; GenBank accession No. AF106020) was expressed in E. coli as a 132 amino acid residue fusion protein with an N-terminal His-tag sequence and a thrombin cleavage site. Recombinant VEGF-E homodimer was dimerized in vitro and has a predicted mass of approximately 35 kDa.

    Source

    Escherichia Coli.

    Formulation

    The protein was lyophilized from a concentrated (1mg/ml) solution containing PBS.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    Biological Activity

    The biological activity was determined (1) by the ability to induce VEGFR-2/KDR receptor phosphorylation in PAE/KDR cells and (2) in a cell proliferation assay using primary HUVECs. The ED50 for this effect is typically 1-5ng/ml.

    More Info

    • Introduction

      Based on sequence similarity to VEGF-A, a gene encoding a VEGF homologue has recently been discovered in the genome of Orf virus (OV) (Lyttle et al., 1994). Different isolates of Orf virus show significant amino acid sequence similarity to VEGF-A and described as a viral virulence factor that appears to be derived from captured host genes. All eight cysteine residues of the central cysteine knot motif characteristic of members of the VEGF family are conserved among other residues in the VEGF-E proteins (Dehio et al., 1999; Wise et al., 1999). Alignment of all mammalian VEGF sequences indicated that VEGF-E is distinct from the previously described VEGFs but most closely related to VEGF-A. Like VEGF-A, VEGF-E was found to bind with high affinity to VEGF receptor-2 (KDR) resulting in receptor autophosphorylation, whilst in contrast to VEGF-A, VEGF-E can not bind to VEGF receptor-1 (Flt-1). Furthermore VEGF-E can also not bind to VEGF receptor-3 (FLT-4). Therefore VEGF-E is a potent angiog

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized Vascular Endothelial Growth Factor-E Orf Virus although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution VEGF E -OV should be stored at 4°C between 2-7 days and for future use below -18°C.Please prevent freeze-thaw cycles.

    • Solubility

      The lyophilized oVEGF-E Orf Virus should be reconstituted in water or medium to a concentration not lower than 50µg/ml. For long term storage we would recommend to add at least 0.1% human or bovine serum albumin.

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH DSTKTWSEVF ENSGCKPRPM VFRVHDEHPE LTSQRFNPPC VTLMRCGGCC NDESLECVPT EEANVTMQLM GASVSGGNGM QHLSFVEHKK CDCKPPLTTT PPTTTRPPRR 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.

    Vegf E Orf Virus
  • View Data Sheet

    Name :

    Enfuvirtide

    Description:

    Enfuvirtide (T-20)

    Product # :

    PRO-376

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    Shipping Method :

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    Shipped at Room temp

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    • formulation
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    Description

    Enfuvirtide has an amino acid sequence Ac-Tyr-Thr-Ser-Leu-Ile-His-Ser-Leu-Ile-Glu-Glu-Ser-Gln-Asn-Gln-Gln-Glu-Lys-Asn-Glu-Gln-Glu-Leu-Leu-Glu-Leu-Asp-Lys-Trp-Ala-Ser-Leu-Trp-Asn-Trp-Phe-NH2, molecular formula of C204H301N51O64 and a molecular weight of 4488.9 Dalton.

    Formulation

    The protein (1mg/ml) was lyophilized with no additives.

    Purity

    Greater than 98.0% as determined by RP-HPLC.

    More Info

    • Introduction

      Enfuvirtide also called human immunodeficiency fusion inhibitor blocks HIV’s ability to infect healthy CD4 cells. It can reduce the amount of HIV in the blood and increase the number of CD4 cells. Enfuvirtide operates by disrupting the HIV-1 molecular machinery at the final phase of fusion with the target cell, preventing uninfected cells from becoming infected. Enfuvirtide mimics components of the HIV-1 fusion apparatus and displace them, preventing normal fusion. HIV attaches to the host CD4+ cell receptor using the viral protein GP120; upon binding, GP120 deforms allowing the viral protein GP41 to insert itself into the host cell's plasma membrane. Entry inhibitors bind to GP41 preventing the formation of an entry pore for the capsid of the virus, keeping it out of the cell.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized Enfuvirtide although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Enfuvirtide 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

      Enfuvirtide lyophilized powder is soluble in water at a concentration of 1mg/ml.

    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.

    Enfuvirtide
  • View Data Sheet

    Name :

    CHP Human

    Description:

    Calcium Binding Protein P22 Human Recombinant

    CHP, CHP Human, Calcium-binding protein p22, Calcium-binding protein CHP, Calcineurin homologous protein, Calcineurin B homolog, SLC9A1BP.

    Product # :

    PRO-847

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    Shipped with Ice Packs

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    Description

    CHP Recombinant E.coli produced in E.Coli is a single, non-glycosylated polypeptide chain containing 216 amino acids (1-195 a.a.) and having a molecular mass of 24.7 kDa. The CHP is fused to 21 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    CHP Human solution containing 20mM Tris-HCl pH-7.5 & 10% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Calcium-binding protein P22 is a phosphoprotein that binds to the sodium-hydrogen exchangers (NHEs). CHP is an essential cofactor which maintains the physiological activity of NHE family members. CHP has protein sequence resemblance to calcineurin B and it is also identified to be an endogenous inhibitor of calcineurin activity.CHP is necessary for constitutive membrane traffic. CHP Inhibits GTPase-stimulated Na(+)/H(+) exchange. CHP inhibits calcineurin phosphatase activity. Required for activity of SLC9A1/NHE1.

    • Synonyms

      CHP, CHP Human, Calcium-binding protein p22, Calcium-binding protein CHP, Calcineurin homologous protein, Calcineurin B homolog, SLC9A1BP.

    • 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 MMGSRASTLL RDEELEEIKK ETGFSHSQIT RLYSRFTSLD KGENGTLSRE DFQRIPELAI NPLGDRIINA FFPEGEDQVN FRGFMRTLAH FRPIEDNEKS KDVNGPEPLN SRSNKLHFAF RLYDLDKDEK ISRDELLQVL RMMVGVNISD EQLGSIADRT IQEADQDGDS AISFTEFVKV LEKVDVEQKM SIRFLH.

    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.

    Chp Human
  • View Data Sheet

    Name :

    ESAT6-CFP10

    Description:

    ESAT6-CFP10 Chimeric Recombinant

    Early Secretory Target Mycobacterium Tuberculosis, ESAT-6

    Product # :

    PRO-2737

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    Description

    Recombinant Chimeric ESAT6-CFP10 produced in E. coli is fused to a 6 amino acid his tag at its C-terminus and purified by proprietary chromatographic technique.

    Source

    Escherichia Coli.

    Formulation

    ESAT6-CFP10 solution contains 25mM K2CO3, 0.02% NaN3 and PBS.

    Purity

    Protein is >95% pure as determined by 12% PAGE (coomassie staining).

    More Info

    • Introduction

      Mycobacterium antigen ESAT6 has been isolated from low molecular weight fractions of the shot-term-culture filtrate (ST-CF) and it can easily be detected in tuberculosis patients. The export of ESAT-6 which is a potent T-cell antigen, and related proteins requires a dedicated secretory apparatus that is encoded by a group of genes, several of which also code for proteins that are recognized strongly by T cells. The ESAT-6 systems can consequently be considered as immunogenicity islands and there is mounting evidence that the equivalent genes are subject to selective pressure imposed by the immune system of the host. This antigen includes many epitopes detectable in the serum of most patients with tuberculosis (more than 90%). By the attempts to obtain the vaccine on the basis of ESAT-6 it was demonstrated that the optimization of adjuvant is very important when using the combination of dioctadecylammonium bromide and monophosphoryllipide. ESAT-6 is very potential as diagnostic for differentiation between the mycobacterial infection and BCG vaccination. The main topic in ESAT-6 using is in antibody production and in test-systems for tuberculosis elaboration. Early secretory antigen 6 (ESAT6) and cell filtrate protein 10 (CFP10) are 2 antigens secreted as a complex by the replicating Mycobacterium tuberculosis complex (MTC).

    • Synonyms

      Early Secretory Target Mycobacterium Tuberculosis, ESAT-6

    • 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.

    • Applications

      Immunoassay.

    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.

    Esat6 Cfp10
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