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Search results

1000 results found for “Ferritin”

Name

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  • View Data Sheet

    Name :

    RBP1 Human

    Description:

    Retinol Binding Protein-1 Human Recombinant

    Retinol binding protein 1 cellular, CRBP, CRBP1, CRABP-I, RBPC.

    Product # :

    CYT-122

    Price :

    Quantity :

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    • source
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    • More Info

    Description

    RBP1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 220 amino acids (1-197 a.a.) and having a molecular mass of 24.7kDa.RBP1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    RBP1 protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH8.0), 200mM NaCl, 2mM DTT and 20% glycerol.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    More Info

    • Introduction

      RBP1 is a member of the calycin superfamily and fatty-acid binding protein (FABP) family. RBP1 is the carrier protein which takes part in the transport of retinol (vitamin A alcohol) from the liver storage site to peripheral tissue. Additionally, RBP1 performs as a bridging molecule to recruit histone deacetylases (HDACs) which is a forceful regulator of gene expression. RBP1 is found in almost all the tissues with higher expression in pancreas, adrenal gland and pituitary gland, fetal liver and adult ovary.

    • Synonyms

      Retinol binding protein 1 cellular, CRBP, CRBP1, CRABP-I, RBPC.

    • 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 MGSMDPPAGF VRAGNPAVAA PQSPLSPEGA HFRAAHHPRS TGSRCPGSLQ PSRPLVANWL QSLPEMPVDF TGYWKMLVNE NFEEYLRALD VNVALRKIAN LLKPDKEIVQ DGDHMIIRTL STFRNYIMDF QVGKEFEEDL TGIDDRKCMT TVSWDGDKLQ CVQKGEKEGR GWTQWIEGDE LHLEMRVEGV VCKQVFKKVQ

    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.

    Rbp1 Human
  • View Data Sheet

    Name :

    MIF Rat

    Description:

    Macrophage Migration Inhibitory Factor Rat Recombinant

    Macrophage migration inhibitory factor, MIF, Glutathione-binding 13 kDa protein, L-dopachrome isomerase, L-dopachrome tautomerase, Phenylpyruvate tautomerase.

    Product # :

    CYT-193

    Price :

    Quantity :

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    Shipped at Room temp

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    • description
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    • More Info

    Description

    MIF Rat Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 115 amino acids and having a molecular mass of 12.5kDa. The MIF is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Lyophilized from a 0.2µm filtered concentrated solution in 1×PBS, pH 7.4 and 5% trehalose.

    Purity

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

    More Info

    • Introduction

      The cytokine Macrophage migration inhibitory factor (MIF) has been identified to be secreted by the pituitary gland and the monocyte/macrophage and to play an important role in endotoxic shock. MIF has the unique property of being released from macrophages and T cells in response to physiological concentrations of glucocorticoids. The secretion of MIF is tightly regulated and decreases at high, anti-inflammatory steroid concentration.

    • Synonyms

      Macrophage migration inhibitory factor, MIF, Glutathione-binding 13 kDa protein, L-dopachrome isomerase, L-dopachrome tautomerase, Phenylpyruvate tautomerase.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Amino Acid Sequence

      MPMFIVNTNV PRASVPEGFL SELTQQLAQA TGKPAQYIAV HVVPDQLMTF SGTSDPCALC SLHSIGKIGG AQNRNYSKLL CGLLSDRLHI SPDRVYINYY DMNAANVGWN GSTFA.

    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.

    Mif Rat
  • View Data Sheet

    Name :

    IFNA14 Human

    Description:

    Interferon-alpha 14 Human Recombinant

    Interferon alpha-14, IFN-alpha-14, Interferon alpha-H, LeIF H, Interferon lambda-2-H, IFNA14, LEIF2H, IFN-alphaH.

    Product # :

    CYT-135

    Price :

    Quantity :

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    • description
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    • SDS-PAGE

    Description

    IFNA14 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 191 amino acids (24-189 a.a.) and having a molecular mass of 22.4kDa.IFNA14 is fused to a 25 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    IFNA14 protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH8.0), 50% glycerol, 0.2M NaCl and 2mM DTT.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    SDS-PAGE

    IFNA14 Human - Product image 1

    More Info

    • Introduction

      Interferon alpha-14 (IFNA14) is a member of the alpha/beta interferon family. IFNA14 is produced by macrophages (IFN-alpha have antiviral activities). The interferon stimulates the production of 2 enzymes: a protein kinase and an oligoadenylate synthetase.

    • Synonyms

      Interferon alpha-14, IFN-alpha-14, Interferon alpha-H, LeIF H, Interferon lambda-2-H, IFNA14, LEIF2H, IFN-alphaH.

    • 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 MGSHMCNLSQ THSLNNRRTL MLMAQMRRIS PFSCLKDRHD FEFPQEEFDG NQFQKAQAIS VLHEMMQQTF NLFSTKNSSA AWDETLLEKF YIELFQQMND LEACVIQEVG VEETPLMNED SILAVKKYFQ RITLYLMEKK YSPCAWEVVR AEIMRSLSFS TNLQKRLRRK D.

    • Background

      What is the molecular weight/Mw of IFNA14 HUMAN Protein?
      IFNA14 HUMAN Protein has a total Mw of 22.4kDa.

      What is the source or expression system of IFNA14 HUMAN Protein?
      Escherichia Coli.

      What is the Purity of IFNA14 HUMAN Protein?
      IFNA14 HUMAN Protein is >90% pure as determined by SDS-PAGE.

      What is the Biological Activity of IFNA14 HUMAN Protein?
      The biological functionality of IFNA14 HUMAN Protein will be determined in the future.

      What is the amino acid sequence of IFNA14 HUMAN Protein?
      MGSSHHHHHH SSGLVPRGSH MGSHMCNLSQ THSLNNRRTL MLMAQMRRIS PFSCLKDRHD FEFPQEEFDG NQFQKAQAIS VLHEMMQQTF NLFSTKNSSA AWDETLLEKF YIELFQQMND LEACVIQEVG VEETPLMNED SILAVKKYFQ RITLYLMEKK YSPCAWEVVR AEIMRSLSFS TNLQKRLRRK D.

      What applications can IFNA14 HUMAN Protein be used in?
      IFNA14 HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for IFNA14 HUMAN Protein?
      The endotoxin level is minimal, IFNA14 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.

    Ifna14 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

    Price :

    Quantity :

    Shipping Method :

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    Shipped at Room temp

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    More Info

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

    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 :

    TACI Human, His

    Description:

    Tumor Necrosis Factor Receptor 13B Human Recombinant, His Tag

    CD267, CVID, CVID2, TACI, TNFRSF14B, Tumor necrosis factor receptor superfamily, member 13B, Tumor necrosis factor receptor superfamily, member 13B, isoform CRA_a, TNFRSF13B.

    Product # :

    CYT-032

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    Description

    TACI Human Recombinant fused with a 23 amino acid His tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 188 amino acids (1- 165a.a.) and having a molecular mass of 20.9kDa. The TACI is purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    The TACI solution (1mg/1ml) contains 20mM Tris-HCl buffer (pH8.0), 10% glycerol and 0.4M Urea.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    More Info

    • Introduction

      TNFRSF13B (TACI) is a transmembrane receptor protein found predominantly on the surface of B cells (a significant part of the immune system). TACI was at first discovered owing to its ability to interact with calcium-modulator and cyclophilin ligand (CAML). Later on, it was found that TACI plays a key role in humoral immunity by interacting with two members of the TNF family. Also, TACI controls T cell-independent B cell antibody responses, isotype switching, and B cell homeostasis.

    • Synonyms

      CD267, CVID, CVID2, TACI, TNFRSF14B, Tumor necrosis factor receptor superfamily, member 13B, Tumor necrosis factor receptor superfamily, member 13B, isoform CRA_a, TNFRSF13B.

    • 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 MGSMSGLGRS RRGGRSRVDQ EERFPQGLWT GVAMRSCPEE QYWDPLLGTC MSCKTICNHQ SQRTCAAFCR SLSCRKEQGK FYDHLLRDCI SCASICGQHP KQCAYFCENK LRSPVNLPPE LRRQRSGEVE NNSDNSGRYQ GLEHRGSEAS PALPGLKLSA DQVALVYS.

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    Taci Human
  • View Data Sheet

    Name :

    FGF 19 Human, His

    Description:

    Fibroblast Growth Factor-19 Human Recombinant, His Tag

    Fibroblast growth factor 19, FGF-19.

    Product # :

    CYT-279

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    Description

    Fibroblast Growth Factor-19 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 206 amino acids and having a molecular mass of 23 kDa. The amino acid sequence of the recombinant human FGF19 is 100% homologous to the amino acid sequence of the human FGF19 without signal sequence and contains his tag at N-terminal. The FGF-19 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Filtered (0.4µm) and lyophilized from 0.5mg/ml in 20mM TRIS, 20mM NaCl, pH 7.5.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      The FGFs are a family of more than 20 small (~17–26 kDa) secreted peptides. The initial characterization of these proteins focused on their ability to stimulate fibroblast proliferation. This mitogenic activity was mediated through FGF receptors (FGFRs) 1, 2, or 3. A fourth closely related tyrosine kinase receptor (FGFR4) was able to bind the FGFs but did not lead to a mitogenic response.
      FGFs modulate cellular activity via at least 5 distinct subfamilies of high-affinity FGF receptors (FGFRs): FGFR-1, -2, -3, and -4, all with intrinsic tyrosine kinase activity and, except for FGFR-4, multiple splice isoforms, and FGFR-5, which lacks an intracellular kinase domain. There is growing evidence that FGFRs can be important for regulation of glucose and lipid homeostasis. The overexpression of a dominant negative form of FGFR-1 in ? cells leads to diabetes in mice, which thus implies that proper FGF signaling is required for normal ? cell function and glycemia maintenance. FGFR-2 appears to be a key molecule during pancreatic development. Moreover, FGFR-4 has been implicated in cholesterol metabolism and bile acid synthesis.
      FGF-19, has been shown to cause resistance to diet-induced obesity and insulin desensitization and to improve insulin, glucose, and lipid profiles in diabetic rodents. Since these effects, at least in part, are mediated through the observed changes in metabolic rates, FGF-19 can be considered as a regulator of energy expenditure.
      FGF-21 is preferentially expressed in liver, but an exact knowledge of FGF-21 bioactivity and its mode of action have been lacking to date. FGF-21 is a potent activator of glucose uptake on adipocytes, protects animals from diet-induced obesity when overexpressed in transgenic mice, and lowers blood glucose and triglyceride levels when therapeutically administered to diabetic rodents.

    • Synonyms

      Fibroblast growth factor 19, FGF-19.

    • Physical Appearance

      Filtered white lyophilized powder.

    • Stability

      Lyophilized FGF-19 Human Recombinant although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Fibroblast Growth Factor-19 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

      Add deionized water to a working concentration approximately 0.5mg/ml and let the lyophilized pellet dissolve completely. Product is not sterile! Please filter the product by appropriate sterile filter before using it in the cell culture.

    • Amino Acid Sequence

      MRGSHHHHHH GMASLAFSDA GPHVHYGWGD PIRLRHLYTS GPHGLSSCFL RIRADGVVDC ARGQSAHSLLEIKAVALRTV AIKGVHSVRY LCMGADGKMQ GLLQYSEEDC AFEEEIRPDG YNVYRSEKHR LPVSLSSAKQ RQLYKNRGFL PLSHFLPMLP MVPEEPEDLR GHLESDMFSS PLETDSMDPF GLVTGLEAVR SPSFEK.

    • Background

      What is the molecular weight/Mw of FGF19 HUMAN,HIS Protein?
      FGF19 HUMAN,HIS Protein has a total Mw of 23kDa.

      What is the source or expression system of FGF19 HUMAN,HIS Protein?
      Escherichia Coli.

      What is the Purity of FGF19 HUMAN,HIS Protein?
      FGF19 HUMAN,HIS Protein is >95% pure as determined by SDS-PAGE.

      What is the Biological Activity of FGF19 HUMAN,HIS Protein?
      The biological functionality of FGF19 HUMAN,HIS Protein will be determined in the future.

      What is the amino acid sequence of FGF19 HUMAN,HIS Protein?
      MRGSHHHHHH GMASLAFSDA GPHVHYGWGD PIRLRHLYTS GPHGLSSCFL RIRADGVVDC ARGQSAHSLLEIKAVALRTV AIKGVHSVRY LCMGADGKMQ GLLQYSEEDC AFEEEIRPDG YNVYRSEKHR LPVSLSSAKQ RQLYKNRGFL PLSHFLPMLP MVPEEPEDLR GHLESDMFSS PLETDSMDPF GLVTGLEAVR SPSFEK.

      What applications can FGF19 HUMAN,HIS Protein be used in?
      FGF19 HUMAN,HIS Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for FGF19 HUMAN,HIS Protein?
      The endotoxin level is minimal, FGF19 HUMAN,HIS 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.

    Fgf19 Human His
  • View Data Sheet

    Name :

    ING2 Human

    Description:

    Inhibitor of Growth Family, Member 2 Human Recombinant

    Inhibitor Of Growth Family Member 2, ING1L, Inhibitor Of Growth 1-Like Protein, P33ING2, ING1Lp, P32, Inhibitor Of Growth Family Member 1-Like, Inhibitor Of Growth Protein 2, ING2.

    Product # :

    PRO-1739

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    Description

    ING2 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 303 amino acids (1-280 a.a) and having a molecular mass of 35.2kDa.ING2 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    ING2 protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.4M UREA and 10% glycerol.

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Inhibitor of Growth Family, Member 2 (ING2) belongs to the inhibitor of growth (ING) family. ING family members associate with and modulate the activity of histone acetyltransferase (HAT) and histone deacetylase (HDAC) complexes and serve in DNA repair and apoptosis. ING2 appears to be involved in p53/TP53 activation and p53/TP53-dependent apoptotic pathways, most likely by enhancing acetylation of p53/TP53. ING2 is a component of an mSin3A-like corepressor complex, which is probably involved in deacetylation of nucleosomal histones. ING2 activity is modulated by binding to phosphoinositides (PtdInsPs).

    • Synonyms

      Inhibitor Of Growth Family Member 2, ING1L, Inhibitor Of Growth 1-Like Protein, P33ING2, ING1Lp, P32, Inhibitor Of Growth Family Member 1-Like, Inhibitor Of Growth Protein 2, ING2.

    • 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 MGSMLGQQQQ QLYSSAALLT GERSRLLTCY VQDYLECVES LPHDMQRNVS VLRELDNKYQ ETLKEIDDVY EKYKKEDDLN QKKRLQQLLQ RALINSQELG DEKIQIVTQM LELVENRARQ MELHSQCFQD PAESERASDK AKMDSSQPER SSRRPRRQRT SESRDLCHMA NGIEDCDDQP PKEKKSKSAK KKKRSKAKQE REASPVEFAI DPNEPTYCLC NQVSYGEMIG CDNEQCPIEW FHFSCVSLTY KPKGKWYCPK CRGDNEKTMD KSTEKTKKDR RSR.

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    Ing2 Human
  • View Data Sheet

    Name :

    GM-CSF Human, Pichia

    Description:

    Granulocyte Macrophage-Colony Stimulating Factor Human Recombinant, Pichia

    CSF-2, MGI-1GM, GM-CSF, Pluripoietin-alpha, Molgramostin, Sargramostim, MGC131935, MGC138897.

    Product # :

    CYT-324

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    Description

    Granulocyte Macrophage Colony Stimulating Factor Human Recombinant produced in Yeast is a single, glycosylated, polypeptide chain containing 127 amino acids and having a molecular mass of 26-32 kDa. rhGMCSF differs from the natural human GM-CSF by a substitution of leucine at position 23 (R to L), and the carbohydrate moiety may be different from the native protein. GM-CSF is purified by proprietary chromatographic techniques.

    Source

    Pichia Pastoris.

    Formulation

    The protein was lyophilized from a concentrated (1mg/ml) solution containing 10mM phosphate buffer pH 7.0, 40 mg mannitol and 10 mg sucrose.

    Purity

    Greater than 97.0% as determined by1. Analysis by RP-HPLC.
    2. Analysis by SDS-PAGE.

    Biological Activity

    The ED50 as determined by the dose-dependant stimulation of the proliferation of human TF-1 cells (human erythroleukemic indicator cell line) is < 0.183 ng/ml, corresponding to a Specific Activity of 5,500,000IU/mg.

    More Info

    • Introduction

      GMCSF is a cytokine that controls the production, differentiation, and function of granulocytes and macrophages. The active form of the protein is found extracellularly as a homodimer. This gene has been localized to a cluster of related genes at chromosome region 5q31, which is known to be associated with interstitial deletions in the 5q- syndrome and acute myelogenous leukemia. Other genes in the cluster include those encoding interleukins 4, 5, and 13.
      GM-CSF stimulates the growth and differentiation of hematopoietic precursor cells from various lineages, including granulocytes, macrophages, eosinophils and erythrocytes.

    • Synonyms

      CSF-2, MGI-1GM, GM-CSF, Pluripoietin-alpha, Molgramostin, Sargramostim, MGC131935, MGC138897.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized Granulocyte Macrophage Colony Stimulating Factor although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution GMCSF 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 Granulocyte Macrophage Colony Stimulating Factor 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 five N-terminal amino acids was determined and was found to be Ala-Pro-Ala-Arg-Ser.

    • Background

      What is the molecular weight/Mw of GM-CSF HUMAN, PICHIA Protein?
      GM-CSF HUMAN, PICHIA Protein has a total Mw of 29kDa.

      What is the source or expression system of GM-CSF HUMAN, PICHIA Protein?
      Pichia Pastoris.
      What is the Purity of GM-CSF HUMAN, PICHIA Protein?
      GM-CSF HUMAN, PICHIA Protein is >97% pure as determined by SDS-PAGE.

      What is the Biological Activity of GM-CSF HUMAN, PICHIA Protein?
      The ED50 as determined by the dose-dependant stimulation of the proliferation of human TF-1 cells (human erythroleukemic indicator cell line) is < 0.183 ng/ml, corresponding to a Specific Activity of 5,500,000IU/mg.

      What is the amino acid sequence of GM-CSF HUMAN, PICHIA Protein?
      The sequence of the first five N-terminal amino acids was determined and was found to be Ala-Pro-Ala-Arg-Ser.

      What applications can GM-CSF HUMAN, PICHIA Protein be used in?
      GM-CSF HUMAN, PICHIA Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for GM-CSF HUMAN, PICHIA Protein?
      The endotoxin level is minimal, GM-CSF HUMAN, PICHIA 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.

    Gm Csf Human Pichia
  • View Data Sheet

    Name :

    CRABP1 Human

    Description:

    Cellular Retinoic Acid binding Protein 1 Human Recombinant

    Cellular retinoic acid-binding protein 1, Cellular retinoic acid-binding protein I, CRABP-I, CRABP1, RBP5, CRABP, CRABPI.

    Product # :

    PRO-710

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    Description

    CRABP1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 137 amino acids and having a molecular mass of 15.5kDa. The CRABP1 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The CRABP1 (1mg/ml) protein solution contains 20mM Tris-HCl buffer (pH8.0) and 10% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      CRABP1 is a member of special carrier proteins for members of the vitamin A family. It is believed that CRABP1 has an essential role in retinoic acid-mediated differentiation and proliferation processes. Though, CRABP1 is structurally similar to the cellular retinol-binding proteins, it binds only retinoic acid at specific sites within the nucleus, which may contribute to vitamin A-directed differentiation in epithelial tissue. CRABP1 is constitutively expressed and is thought to have different functions in the cell than the related CRABP2. CRABP1 forms a beta-barrel structure which accommodates hydrophobic ligands in its interior.
      Loss of CRABP1 function as a result of hypermethylation of its promoter leads to pathogenesis of papillary thyroid carcinoma. Furthermore, frequent methylation-associated silencing of CRABP1 is linked to esophageal squamous-cell carcinoma.

    • Synonyms

      Cellular retinoic acid-binding protein 1, Cellular retinoic acid-binding protein I, CRABP-I, CRABP1, RBP5, CRABP, CRABPI.

    • 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

      MPNFAGTWKM RSSENFDELL KALGVNAMLR KVAVAAASKP HVEIRQDGDQ FYIKTSTTVR TTEINFKVGE GFEEETVDGR KCRSLATWEN ENKIHCTQTL LEGDGPKTYW TRELANDELI LTFGADDVVC TRIYVRE.

    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.

    Crabp1 Human
  • View Data Sheet

    Name :

    Secretin Human

    Description:

    Secretin Human

    Product # :

    HOR-273

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    Description

    Secretin has a molecular formula of C130H220N44O41, a.a. sequence of H-His-Ser-Asp-Gly-Thr-Phe-Thr-Ser-Glu-Leu-Ser-Arg-Leu-Arg- Asp-Ser-Ala-Arg-Leu-Gln-Arg-Leu-Leu-Gln-Gly-Leu-Val-NH2 and having an Mw of 3055.4 Dalton.

    Formulation

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

    Purity

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

    More Info

    • Introduction

      Human Secretin stimulates the secretion of bicarbonate by the pancreas and inhibits the production of gastrin and acid production in the stomach. It also potentiates the release of digestive enzymes from the pancreas triggered by cholecystokinin.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized Secretin although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Secretin 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 Secretin in sterile 18MΩ-cm H2O not less than 100 µg/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.

    Secretin Human
  • View Data Sheet

    Name :

    MRRF Human

    Description:

    Mitochondrial Ribosome Recycling Factor Human Recombinant

    MRFF, MTRRF, RRF, Ribosome-recycling factor, mitochondrial, Ribosome-releasing factor, mitochondrial.

    Product # :

    PRO-1299

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    Description

    MRRF Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 228 amino acids (56-262 a.a.) and having a molecular mass of 25.1kDa.MRRF is fused to a 21 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    MRRF protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer, (pH 8.0), 0.2M NaCl, 30% glycerol and 2mM DTT.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Mitochondrial Ribosome Recycling Factor (MRRF) is a member of the RRF family. MRRF attaches to the large ribosomal subunit in the cleft which has a peptidyl transferase center. MRRF controls the release of ribosome from messenger RNA at the termination of protein biosynthesis. Also, it may intensify the efficacy of translation by recycling ribosome from one round of translation to another.

    • Synonyms

      MRFF, MTRRF, RRF, Ribosome-recycling factor, mitochondrial, Ribosome-releasing factor, mitochondrial.

    • 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 MATKKAKAKG KGQSQTRVNI NAALVEDIIN LEEVNEEMKS VIEALKDNFN KTLNIRTSPG SLDKIAVVTA DGKLALNQIS QISMKSPQLI LVNMASFPEC TAAAIKAIRE SGMNLNPEVE GTLIRVPIPQ VTREHREMLV KLAKQNTNKA KDSLRKVRTN SMNKLKKSKD TVSEDTIRLI EKQISQMADD TVAELDRHLA VKTKELLG.

    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.

    Mrrf Human
  • View Data Sheet

    Name :

    SFRP2 Human

    Description:

    Secreted Frizzled-Related Protein 2 Human Recombinant

    FRP-2, SARP1, SDF-5, Secreted frizzled-related protein 2, UNQ361/PRO697, FKSG12, FKSG12.

    Product # :

    PRO-1905

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    Description

    SFRP2 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 297 amino acids (20-295 a.a) and having a molecular mass of 33.8kDa.SFRP2 is fused to a 21 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    SFRP2 protein solution (1mg/ml) contains 20mM Tris-HCl buffer (pH8.0), 10% glycerol and 0.4M Urea.

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Secreted frizzled-related protein 2 (SFRP2) belongs to the SFRP family which contains a cysteine-rich domain homologous to the putative Wnt-binding site of Frizzled proteins. SFRP2 function as soluble modulators of Wnt signaling. Methylation of SFRP2 is a possible marker for the existence of colorectal cancer.

    • Synonyms

      FRP-2, SARP1, SDF-5, Secreted frizzled-related protein 2, UNQ361/PRO697, FKSG12, FKSG12.

    • 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 MGSARGLFLF GQPDFSYKRS NCKPIPVNLQ LCHGIEYQNM RLPNLLGHET MKEVLEQAGA WIPLVMKQCH PDTKKFLCSL FAPVCLDDLD ETIQPCHSLC VQVKDRCAPV MSAFGFPWPD MLECDRFPQD NDLCIPLASS DHLLPATEEA PKVCEACKNK NDDDNDIMET LCKNDFALKI KVKEITYINR DTKIILETKS KTIYKLNGVS ERDLKKSVLW LKDSLQCTCE EMNDINAPYL VMGQKQGGEL VITSVKRWQK GQREFKRISR SIRKLQC.

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    Sfrp2 Human
  • View Data Sheet

    Name :

    IFN a 2a Human, Plant

    Description:

    Interferon Alpha 2a Human Recombinant, Tobacco

    Leukocyte interferon, B cell interferon, Type I interferon, IFNA2, IFN-a 2a.

    Product # :

    CYT-543

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    Description

    Interferon Alpha Human 2a Recombinant produced in Plant is a single, glycosylated, polypeptide chain containing 165 amino acids and having a molecular mass of 19 kDa.The Interferon-a 2a contains affinity 6xHis tag on C-terminus.The IFN-A 2a is purified by proprietary chromatographic techniques.

    Source

    Nicotiana Sp.Plant.

    Formulation

    Lyophilized, containing 50% SDS.

    Purity

    Greater than 99.0% as determined by both:
    (a) Analysis by RP-HPLC.
    (b) Analysis by SDS-PAGE.

    Biological Activity

    The specific activity was determined by a quantitative gene report bioassay using human Type I interferon-sensitive cells. Compared with bacterial derived recombinant IFN-a 2a, assayed in the same conditions, plant derived IFN-alpha 2a showed 6.1 × 108 Units/mg in reference to a viral resistance assay using bovine kidney MDBK cells.

    More Info

    • Introduction

      IFN-alpha is produced by macrophages and has antiviral activities. Interferon stimulates the production of two enzymes: protein kinase and an oligoadenylate synthetase.

    • Synonyms

      Leukocyte interferon, B cell interferon, Type I interferon, IFNA2, IFN-a 2a.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized Interferon alpha 2a although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IFN-alpha 2a 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 Interferon-alpha 2a 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 twelve N-terminal amino acids was determined and was found to be Cys-Asp-Leu-Pro-Gln-Thr-His-Ser-Leu-Gly-Ser-Arg.

    • Background

      What is the molecular weight/Mw of IFN A 2A HUMAN, PLANT Protein?
      IFN A 2A HUMAN, PLANT Protein has a total Mw of 19kDa.

      What is the source or expression system of IFN A 2A HUMAN, PLANT Protein?
      Nicotiana Sp.Plant.
      What is the Purity of IFN A 2A HUMAN, PLANT Protein?
      IFN A 2A HUMAN, PLANT Protein is >99% pure as determined by SDS-PAGE.

      What is the Biological Activity of IFN A 2A HUMAN, PLANT Protein?
      The specific activity was determined by a quantitative gene report bioassay using human Type I interferon-sensitive cells. Compared with bacterial derived recombinant IFN-a 2a, assayed in the same conditions, plant derived IFN-alpha 2a showed 6.1 × 108 Units/mg in reference to a viral resistance assay using bovine kidney MDBK cells.

      What is the amino acid sequence of IFN A 2A HUMAN, PLANT Protein?
      The sequence of the first twelve N-terminal amino acids was determined and was found to be Cys-Asp-Leu-Pro-Gln-Thr-His-Ser-Leu-Gly-Ser-Arg.

      What applications can IFN A 2A HUMAN, PLANT Protein be used in?
      IFN A 2A HUMAN, PLANT Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for IFN A 2A HUMAN, PLANT Protein?
      The endotoxin level is minimal, IFN A 2A HUMAN, PLANT 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.

    Interferon Alpha 2A Plant
  • View Data Sheet

    Name :

    IFT20 Human

    Description:

    Intraflagellar Transport 20 Homolog Human Recombinant

    Intraflagellar Transport 20 Homolog (Chlamydomonas), Intraflagellar Transport Protein IFT20, HIFT20.

    Product # :

    PRO-1222

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    Description

    IFT20 Human Recombinant produced in E. coli is a single polypeptide chain containing 152 amino acids (1-132) and having a molecular mass of 17.0 kDa.IFT20 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    The IFT20 solution contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 1mM DTT and 30% glycerol.

    Purity

    Greater than 95% as determined by SDS-PAGE.

    More Info

    • Introduction

      IFT20 is a fragment of intraflagellar transport (IFT) elements which takes part in ciliary process assembly. IFT20 is involved in the transferring of ciliary membrane proteins from the Golgi complex to the cilium and is expressed in virtually all tissues.

    • Synonyms

      Intraflagellar Transport 20 Homolog (Chlamydomonas), Intraflagellar Transport Protein IFT20, HIFT20.

    • 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 MAKDILGEAG LHFDELNKLR VLDPEVTQQT IELKEECKDF VDKIGQFQKI VGGLIELVDQ LAKEAENEKM KAIGARNLLK SIAKQREAQQ QQLQALIAEK KMQLERYRVE YEALCKVEAE QNEFIDQFIF QK

    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.

    Ift20 Human
  • View Data Sheet

    Name :

    IgG1 Fc Human

    Description:

    Immunoglobulin Heavy Constant Gamma 1 Human Recombinant

    IGHG1, IGHG-1, IGG-1FC, IGG1FC, IGG1-FC

    Product # :

    PRO-2763

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    Description

    IgG1 Fc Human Recombinant produced in HEK is a single polypeptide chain containing 231 amino acids (100-330) and having a molecular mass of 25.9kDa. IgG1 Fc is purified by proprietary chromatographic techniques.

    Source

    HEK293 Cells

    Formulation

    The IgG1 Fc solution (1mg/ml) contains 1x PBS and 10% glycerol.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    Biological Activity

    Determined functional ELISA with Human Recombinant CD16a (cat# pro-2360). The ED50 range ≤ 1.5 ug/ml

    More Info

    • Introduction

      IgG1 Fcplays a role in antigen binding activity and immunoglobulin receptor binding activity. IgG1 Fc takes part in the activation of immune & defensive response. IgG1 Fc takes part in the upstream of immunoglobulin mediated immune response, positive regulation of hypersensitivity & regulation of phagocytosis.

    • Synonyms

      IGHG1, IGHG-1, IGG-1FC, IGG1FC, IGG1-FC

    • 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

      PKSCDKTHTC PPCPAPELLG GPSVFLFPPK PKDTLMISRT PEVTCVVVDV SHEDPEVKFN WYVDGVEVHN AKTKPREEQY NSTYRVVSVL TVLHQDWLNG KEYKCKVSNK ALPAPIEKTI SKAKGQPREP QVYTLPPSRD ELTKNQVSLT CLVKGFYPSD IAVEWESNGQ PENNYKTTPP VLDSDGSFFL YSKLTVDKSR WQQGNVFSCS VMHEALHNHY TQKSLSLSPG K

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    Igg1 Fc Human
  • View Data Sheet

    Name :

    CCL24 Human

    Description:

    Eotaxin-2 Human Recombinant (CCL24)

    C-C motif chemokine 24, Small-inducible cytokine A24, Myeloid progenitor inhibitory factor 2, CK-beta-6, Eosinophil chemotactic protein 2, Eotaxin-2, CCL24, Ckb-6, MPIF2, MPIF-2, SCYA24, Eotaxin2, CCL-24.

    Product # :

    CHM-238

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    Description

    CCL24 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 78 amino acids and having a molecular mass of 8.8 kDa. The CCL24 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The CCL24 protein was lyophilized from a concentrated (1mg/ml) sterile solution containing 20mM PBS pH-7.4 and 0.15M sodium chloride.

    Purity

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

    Biological Activity

    The activity is determined by the chemoattract of human PBE (peripheral blood eosinophils) at a concentration between 50-100 ng/ml corresponding to a Specific Activity of 10,000-20,000IU/mg.

    More Info

    • Introduction

      Eotaxin-2, also called MPIF2 & Ckb6, is a novel CC chemokine produced by activated monocytes and T lymphocytes. Eotaxin-2 selectively chemoattracts cells expressing CCR3 including eosinophils, basophils, Th2 T cells, mast cells, and certain subsets of dendritic cells. Furthermore, Eotaxin-2 inhibits the proliferation of multipotential hematopoietic progenitor cells. The mature protein, which includes C-terminal truncation, contains 78 amino acids (92 amino acids for the mouse homolog, without C-terminal truncation).
      CCL24 functions as a chemotactic chemokine for resting t-lymphocytes, and eosinophils. CCL24 has lower chemotactic activity for neutrophils but none for monocytes and activated lymphocytes. CCL24 is a strong suppressor of colony formation by a multipotential hematopoietic progenitor cell line and binds to CCR3.

    • Synonyms

      C-C motif chemokine 24, Small-inducible cytokine A24, Myeloid progenitor inhibitory factor 2, CK-beta-6, Eosinophil chemotactic protein 2, Eotaxin-2, CCL24, Ckb-6, MPIF2, MPIF-2, SCYA24, Eotaxin2, CCL-24.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized Eotaxin-2 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution CCL24 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 CCL24 Human Recombinant in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      VVIPSPCCMFFVSKRIPENRVVSYQLSSRSTCLKGGVIFTTKKGQQFCG
      DPKQEWV QRYMKNLDAKQKKASPRARAVA.

    • Background

      What is the molecular weight/Mw of CCL24 HUMAN Protein?
      CCL24 HUMAN Protein has a total Mw of 8.8kDa.

      What is the source or expression system of CCL24 HUMAN Protein?
      Escherichia Coli.

      What is the Purity of CCL24 HUMAN Protein?
      CCL24 HUMAN Protein is >97% pure as determined by SDS-PAGE.

      What is the Biological Activity of CCL24 HUMAN Protein?
      The activity is determined by the chemoattract of human PBE (peripheral blood eosinophils) at a concentration between 50-100 ng/ml corresponding to a Specific Activity of 10,000-20,000IU/mg.

      What is the amino acid sequence of CCL24 HUMAN Protein?
      VVIPSPCCMFFVSKRIPENRVVSYQLSSRSTCLKGGVIFTTKKGQQFCG
      DPKQEWV QRYMKNLDAKQKKASPRARAVA.

      What applications can CCL24 HUMAN Protein be used in?
      CCL24 HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for CCL24 HUMAN Protein?
      The endotoxin level is minimal, CCL24 HUMAN Protein was purified using conventional chromatography techniques.


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    Ccl24 Human
  • View Data Sheet

    Name :

    STRADA Human

    Description:

    STE20-Related Kinase Adaptor Alpha Human Recombinant

    LYK5, NY-BR-96, PMSE, Stlk, STRAD, STE20-related kinase adapter protein alpha, STRAD alpha, STE20-related adapter protein, Serologically defined breast cancer antigen NY-BR-96, STRADA.

    Product # :

    PRO-1992

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    Description

    STRADA Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 337 amino acids (1-314a.a) and having a molecular mass of 37kDa. STRADA is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

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

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      STE20-Related Kinase Adaptor Alpha (STRADA) is a part of the STE- 20 like kinase family which stimulates MAPK pathways by activating MAPKKK. STRADA is an upstream activator of LKB1 and also leads the sub-cellular localization of LKB1 by fixing it in the cytoplasm. The interaction between STRADA-LKB1 leads to phosphorylation of STRADA and enhanced autophosphorylation of LKB1.

    • Synonyms

      LYK5, NY-BR-96, PMSE, Stlk, STRAD, STE20-related kinase adapter protein alpha, STRAD alpha, STE20-related adapter protein, Serologically defined breast cancer antigen NY-BR-96, STRADA.

    • 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 MGSMSFLVSK PERIRTNDAS SESIASFSKQ EVMSSFLPEG GCYELLTVIG KGFEDLMTVN LARYKPTGEY VTVRRINLEA CSNEMVTFLQ GELHVSKLFN HPNIVPYRAT FIADNELWVV TSFMAYGSAK DLICTHFMDG MNELAIAYIL QGVLKALDYI HHMGYVHRSV KASHILISVD GKVYLSGLRS NLSMISHGQR QRVVHDFPKY SVKVLPWLSP EVLQQNLQGY DAKSDIYSVG ITACELANGH VPFKDMPATQ MLLEKLNGTV PCLLDTSTIP AEELTMSPSR SVANSGLSDS LTTSTPRPSN GPVPAPS.

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    Strada Human
  • View Data Sheet

    Name :

    C12ORF5 Human

    Description:

    Chromosome 12 Open Reading Frame 5 Human

    Fructose-2,6-bisphosphatase TIGAR, TP53-induced glycolysis and apoptosis regulator, TIGAR, C12orf5.

    Product # :

    PRO-1791

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    Description

    TIGAR Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 270 amino acids and having a molecular mass of 30.1kDa. The TIGAR is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    TIGAR was Lyophilized from a 0.2 µm filtered concentrated solution in 20mM Tris-HCl, pH8.5, 150mM NaCl.

    Purity

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

    More Info

    • Introduction

      TIGAR is a p53-inducible enzyme which catalyzes the hydrolysis of fructose-2-6 bisphosphate (F-2-6-BP) to fructose-6-phosphate and inorganic phosphate. F-2-6-BP is an influential activator of 6-phosphofructose-1 kinase (the rate limiting enzyme of glycolysis). By lowering the intracellular level of F-2-6-BP, TIGAR expression leads to increased glucose processing through the pentose phosphate pathway, the main cellular source for NADPH.

    • Synonyms

      Fructose-2,6-bisphosphatase TIGAR, TP53-induced glycolysis and apoptosis regulator, TIGAR, C12orf5.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized TIGAR stable at room temperature for 3 weeks, should be stored desiccated below -18C. Upon reconstitution TIGAR should be stored at 4C between 2-7 days and for future use below -18C. 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 TIGAR in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      MARFALTVVR HGETRFNKEK IIQGQGVDEP LSETGFKQAA AAGIFLNNVK FTHAFSSDLM RTKQTMHGIL ERSKFCKDMT VKYDSRLRER KYGVVEGKAL SELRAMAKAA REECPVFTPP GGETLDQVKM RGIDFFEFLC QLILKEADQK EQFSQGSPSN CLETSLAEIF PLGKNHSSKV NSDSGIPGLA ASVLVVSHGA YMRSLFDYFL TDLKCSLPAT LSRSELMSVT PNTGMSLFII NFEEGREVKP TVQCICMNLQ DHLNGLTETR

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    Tigar Human
  • View Data Sheet

    Name :

    PECR Human

    Description:

    Peroxisomal Trans-2-enoyl-CoA Reductase Human Recombinant

    Peroxisomal trans-2-enoyl-CoA reductase, TERP, HSA250303, SDR29C1, 2,4-dienoyl-CoA reductase-related protein, DCR-RP, pVI-ARL, EC 1.3.1.38, HPDHASE, putative short chain alcohol dehydrogenase, short chain dehydrogenase/reductase family 29C member 1.

    Product # :

    ENZ-177

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    Description

    PECR Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 327 amino acids (1-303) and having a molecular mass of 35.1 kDa.PECR is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    The PECR solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 2mM DTT and 10% glycerol.

    Purity

    Greater than 95% as determined by SDS-PAGE.

    More Info

    • Introduction

      PECR is the main enzyme for a projected peroxisomal chain elongation pathway and is primarily expressed in kidney and liver.

    • Synonyms

      Peroxisomal trans-2-enoyl-CoA reductase, TERP, HSA250303, SDR29C1, 2,4-dienoyl-CoA reductase-related protein, DCR-RP, pVI-ARL, EC 1.3.1.38, HPDHASE, putative short chain alcohol dehydrogenase, short chain dehydrogenase/reductase family 29C member 1.

    • Physical Appearance

      Sterile Filtered colorless solution.

    • Stability

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

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MGSHMASWAK GRSYLAPGLL QGQVAIVTGG ATGIGKAIVK ELLELGSNVV IASRKLERLK SAADELQANL PPTKQARVIP IQCNIRNEEE VNNLVKSTLD TFGKINFLVN NGGGQFLSPA EHISSKGWHA VLETNLTGTF YMCKAVYSSW MKEHGGSIVN IIVPTKAGFP LAVHSGAARA GVYNLTKSLA LEWACSGIRI NCVAPGVIYS QTAVENYGSW GQSFFEGSFQ KIPAKRIGVP EEVSSVVCFL LSPAASFITG QSVDVDGGRS LYTHSYEVPD HDNWPKGAGD LSVVKKMKET FKEKAKL

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    Pecr Human
  • View Data Sheet

    Name :

    FSCN1 Human

    Description:

    Recombinant Human Fascin

    Strongylocentrotus Purpuratus, actin-bundling protein, FAN1, HSN, SNL.

    Product # :

    PRO-527

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    Description

    FSCN1 Recombinant Human produced in E.Coli is a single, non-glycosylated polypeptide chain containing 513 amino acids (1-493 a.a.) and having a molecular mass of 56.7 kDa. The FSCN1 is fused to a 20 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    1mg/ml solution containing 20mM Tris pH-8, 2mM DTT, 0.1M NaCl & 20% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      FSCN1 is an actin-bundling protein that is responsible for rigidity to filopodial bundles to efficiently push the membrane forward during cytoskeleton remodeling and cell migration. FSCN1 takes part in the gathering of actin filament bundles present in microspikes, membrane ruffles, and stress fibers. FSCN1 is absent from most normal epithelia though is upregulated in multiple forms of human carcinoma, where its expression associates clinically with a poor prognosis. FSCN1 expression is abundantly found in neurons, glial cells, and endothelial cells.

    • Synonyms

      Strongylocentrotus Purpuratus, actin-bundling protein, FAN1, HSN, SNL.

    • 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 MTANGTAEAV QIQFGLINCG NKYLTAEAFG FKVNASASSL KKKQIWTLEQ PPDEAGSAAV CLRSHLGRYL
      AADKDGNVTC EREVPGPDCR FLIVAHDDGR WSLQSEAHRR YFGGTEDRLS CFAQTVSPAE KWSVHIAMHP QVNIYSVTRK RYAHLSARPA
      DEIAVDRDVP WGVDSLITLA FQDQRYSVQT ADHRFLRHDG RLVARPEPAT GYTLEFRSGK VAFRDCEGRY LAPSGPSGTL KAGKATKVGK
      DELFALEQSC AQVVLQAANE RNVSTRQGMD LSANQDEETD QETFQLEIDR DTKKCAFRTH TGKYWTLTAT GGVQSTASSK NASCYFDIEW
      RDRRITLRAS NGKFVTSKKN GQLAASVETA GDSELFLMKL INRPIIVFRG EHGFIGCRKV TGTLDANRSS YDVFQLEFND GAYNIKDSTG
      KYWTVGSDSA VTSSGDTPVD FFFEFCDYNK VAIKVGGRYL KGDHAGVLKA SAETVDPASL WEY.

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    Fscn1 Human
  • View Data Sheet

    Name :

    GCHFR Human

    Description:

    GTP Cyclohydrolase I Feedback Regulator Human Recombinant

    GFRP, HsT16933, P35,GTP cyclohydrolase 1 feedback regulatory protein, GTP cyclohydrolase I feedback regulatory protein, p35, GCHFR

    Product # :

    PRO-2006

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    Description

    GCHFR Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 107 amino acids (1-84a.a) and having a molecular mass of 12.1kDa. GCHFR is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    GCHFR protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 40% glycerol and 1mM DTT.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      GTP Cyclohydrolase I Feedback Regulator, also known as GCHFR, is a Protein coding gene which includes a homodimer. GCHFR binds and mediates tetrahydrobiopterin inhibition of GTP cyclohydrolase I. GCHFR also regulates phenylalanine metabolism in the liver and in the production of biogenic amine neurotransmitters and nitric oxide.

    • Synonyms

      GFRP, HsT16933, P35,GTP cyclohydrolase 1 feedback regulatory protein, GTP cyclohydrolase I feedback regulatory protein, p35, GCHFR

    • 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 MGSMPYLLIS TQIRMEVGPT MVGDEQSDPE LMQHLGASKR RALGNNFYEY YVDDPPRIVL DKLERRGFRV LSMTGVGQTL VWCLHKE.

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    Gchfr 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 :

    LECT1 (214-333) Human

    Description:

    Leukocyte Cell Derived Chemotaxin 1 (214-333 a.a.) Human Recombinant

    BRICD3, CHM-I, CHM1, MYETS1, Leukocyte cell-derived chemotaxin 1, Chondrosurfactant protein, CH-SP, Chondromodulin-1, ChM-I, LECT1.

    Product # :

    PRO-1857

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    Quantity :

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    • description
    • source
    • formulation
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    • More Info

    Description

    LECT1 Human Recombinant produced in E. coli is. a single polypeptide chain containing 143 amino acids (214-333) and having a molecular mass of 16.2kDa. LECT1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The LECT1 solution (1mg/ml) 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

      Leukocyte Cell Derived Chemotaxin 1 (214-333 a.a.), also known as LECT1, is a glycosylated transmembrane protein which is cleaved to form a mature, secreted protein. The mature protein encourages chondrocyte growth and inhibits angiogenesis. The mature protein takes part in endochondral bone development by permitting cartilaginous anlagen to be vascularized and replaced by bone. LECT1 is expressed in the avascular area of prehypertrophic cartilage and its expression reduces during vascular invasion and chondrocyte hypertrophy.

    • Synonyms

      BRICD3, CHM-I, CHM1, MYETS1, Leukocyte cell-derived chemotaxin 1, Chondrosurfactant protein, CH-SP, Chondromodulin-1, ChM-I, LECT1.

    • 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 MGSREVVRKI VPTTTKRPHS GPRSNPGAGR LNNETRPSVQ EDSQAFNPDN PYHQEGESMT FDPRLDHEGI CCIECRRSYT HCQKICEPLG GYYPWPYNYQ GCRSACRVIM PCSWWVARIL GMV.

    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.

    Lect1 214 333 Human
  • View Data Sheet

    Name :

    TXN1 Human

    Description:

    Thioredoxin Human Recombinant

    Thioredoxin, ATL-derived factor, ADF, Surface-associated sulphydryl protein, SASP, TXN, TRDX, TRX, TRX1, MGC61975, DKFZp686B1993.

    Product # :

    PRO-569

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    • description
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    • More Info

    Description

    Thioredoxin Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 105 amino acids and having a molecular mass of 11.7 kDa.

    Source

    Escherichia Coli.

    Formulation

    Thioredoxin solution containing 1mg/ml solution containing 1xPBS pH 7.4.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    Biological Activity

    Specific activity is>150 A650/min/mg, obtained by measuring the increase of insulin precipitation in absorbance at 650 nm resulting from the reduction of insulin.

    More Info

    • Introduction

      Thioredoxins are small disulphide-containing redox proteins (within the conserved Cys-Gly-Pro-Cys active site) that have been found in all the kingdoms of living organisms. Thioredoxin contains a single disulfide active site and serves as a general protein disulphide oxidoreductase. Thioredoxins are involved in the first unique step in DNA synthesis. It interacts with a broad range of proteins by a redox mechanism based on reversible oxidation of two cysteine thiol groups to a disulphide, accompanied by the transfer of two electrons and two protons. The net result is the covalent interconversion of a disulphide and a dithiol. It has been suggested that thioredoxin may catalyze the formation of correct disulfides during protein folding because of its ability to act as an efficient oxidoreductant. Trx also provides control over a number of transcription factors affecting cell proliferation and death through a mechanism referred to as redox regulation.

    • Synonyms

      Thioredoxin, ATL-derived factor, ADF, Surface-associated sulphydryl protein, SASP, TXN, TRDX, TRX, TRX1, MGC61975, DKFZp686B1993.

    • 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

      MVKQIESKTA FQEALDAAGD KLVVVDFSAT WCGPCKMIKP FFHSLSEKYS NVIFLEVDVD DCQDVASECE VKCMPTFQFFKKGQKVGEFS GANKEKLEAT INELV.

    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.

    Thioredoxin Human
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