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Search results

1000 results found for “trefoil factor”

Name

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  • View Data Sheet

    Name :

    EGFL6 Human

    Description:

    EGF Like Domain Multiple 6 Human Recombinant

    EGF Like Domain Multiple 6, MAM and EGF Domains-Containing Gene Protein, MAM and EGF Domain Containing, EGF-Like Protein 6, MAEG, EGF Repeat-Containing Protein 6, W80, EGFL6.

    Product # :

    CYT-974

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    Quantity :

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    Shipped at Room temp

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    • source
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    • purity
    • biological activity
    • More Info
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    Description

    EGF Like Domain Multiple 6 Human Recombinant produced in HEK cells is a polypeptide chain starting at amino acid Asn at position 22 to amino acid Arg at position 363, fused to an FC, 6 x His-tag at C-terminus, containing a total of 348 amino acids and having a predicted molecular mass of 40-55kDa. The EGFL6 is purified by proprietary chromatographic techniques.

    Source

    HEK (Human embryonic kidney cells).

    Formulation

    The EGFL6 protein was lyophilized from a 0.2µm filtered solution in 20mM MES and 500mM NaCl, pH 6.0 with 5% Trehalose.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Biological Activity

    EGFL6 activity is determined by its ability of the immobilized protein to support the adhesion of NIH-3T3 mouse embryonic fibroblast cells. The expected ED50 for this effect is 1-5 μg/ml.

    Citations

    More Info

    • Introduction

      Epidermal Growth Factor­like Domain Multiple 6 (EGFL6) belongs to the EGF repeat superfamily of proteins, whose members are involved in the regulation of cell cycle, proliferation, and developmental processes. EGFL6 gene product contains a signal peptide, suggesting that EGFL6 is secreted; an EGF repeat region consisting of four complete EGF-like repeats and 1 partial EGF-like repeat, 3 of which have a calcium-binding consensus sequence; an arg-gly-asp integrin association motif; and a MAM domain, which is assumed to have an adhesive function. Within shared regions, human EGFL6 shares 75% and 78% amino acid sequence identity with the mouse and rat orthologs, respectively. EGFL6 is expressed in various fetal tissues during early development such as the lung, heart, liver, spleen, cochlea and the placenta, as well as meningioma tumors.

    • Synonyms

      EGF Like Domain Multiple 6, MAM and EGF Domains-Containing Gene Protein, MAM and EGF Domain Containing, EGF-Like Protein 6, MAEG, EGF Repeat-Containing Protein 6, W80, EGFL6.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized EGFL6 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution EGFL6 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 EGFL6 in sterile PBS at 500µg/ml, which can then be further diluted to other aqueous solutions.

    • Background

      Illuminating Epidermal Growth Factor Rat Recombinant: Deciphering Cellular Signaling and Therapeutic Potential

      Abstract:

      This research paper delves into the enigmatic realm of Epidermal Growth Factor Rat Recombinant (EGF-RR), unraveling its intricate molecular attributes, signaling cascades, and therapeutic prospects. By employing cutting-edge methodologies encompassing protein expression, receptor binding assays, and bioinformatics analyses, this study sheds light on the multifaceted interplay between EGF-RR and cellular responses, offering novel avenues for therapeutic interventions.

      Introduction:

      Epidermal Growth Factor (EGF) is pivotal in cellular regulation. This paper navigates the complexities of Epidermal Growth Factor Rat Recombinant (EGF-RR), focusing on its unique molecular properties and potential therapeutic applications.

      Protein Expression and Purification:

      The study embarks on precise gene optimization to enhance EGF-RR expression. Purification techniques like affinity chromatography yield purified EGF-RR, primed for subsequent analyses.

      Receptor Binding Assays and Ligand Interaction:

      Employing advanced receptor binding assays, the paper deciphers EGF-RR's engagement with its cognate receptor. Quantitative assessments uncover binding kinetics, shedding light on the intricacies of EGF-RR's molecular interaction.

      Cellular Signaling Pathways and Responses:

      In vitro cellular assays unveil the signaling cascades ignited by EGF-RR. Through quantitative phosphoproteomic profiling, the study unravels phosphorylation events triggered by EGF-RR, delineating its role in cellular proliferation, migration, and differentiation.

      Bioinformatics Insights and Structural Modeling:

      Bioinformatics tools facilitate molecular dynamics simulations, offering insights into EGF-RR's receptor interactions and downstream signaling pathways. Structural modeling captures EGF-RR's conformational changes during signaling cascades.

      Therapeutic Implications and Future Prospects:

      EGF-RR's intricate signaling dynamics open avenues for therapeutic exploration. Harnessing its potential in wound healing, tissue regeneration, and cancer modulation emerges as a promising avenue for precision medicine.

      Challenges and Future Directions:

      Challenges, including context-specific responses, beckon further investigation. Future research should delve into cross-talk between signaling pathways and EGF-RR's contributions to diverse disease contexts.

      Conclusion:

      A fusion of advanced methodologies and visionary insights unveils Epidermal Growth Factor Rat Recombinant as an intriguing subject. Its molecular intricacies and complex cellular interplay ignite prospects for therapeutic breakthroughs, ushering in a new era of precision medicine.

      What is the molecular weight/Mw of EGFL6 HUMAN Protein?
      EGFL6 HUMAN Protein has a total Mw of 40-55kDa.

      What is the source or expression system of EGFL6 HUMAN Protein?
      HEK (Human embryonic kidney cells).

      What is the Purity of EGFL6 HUMAN Protein?
      EGFL6 HUMAN Protein is >95% pure as determined by SDS-PAGE.

      What is the Biological Activity of EGFL6 HUMAN Protein?
      EGFL6 activity is determined by its ability of the immobilized protein to support the adhesion of NIH-3T3 mouse embryonic fibroblast cells. The expected ED50 for this effect is 1-5 μg/ml.

      What is the amino acid sequence of EGFL6 HUMAN Protein?
      EGFL6 HUMAN Protein is composed from 348 amino acids.

      What applications can EGFL6 HUMAN Protein be used in?
      EGFL6 HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for EGFL6 HUMAN Protein?
      The endotoxin level is minimal, EGFL6 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.

    Egfl6 Human
  • View Data Sheet

    Name :

    Gliadin Alpha Wheat

    Description:

    Gliadin Alpha Wheat Recombinant

    Product # :

    PRO-2147

    Price :

    Quantity :

    Shipping Method :

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    Shipped with Ice Packs

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    • Citations

    Description

    Recombinant Wheat Gliadin Alpha protein produced in E.Coli and fused to a 6 His Tag at C-terminus, having a theoretical Mw of 34557.64 Dalton, pI 7.70. Purified by proprietary chromatographic technique.

    Source

    Escherichia Coli.

    Formulation

    Gliadin Alpha protein solution in 10mM Tris-HCl pH 7.2.

    Purity

    Protein is >90% pure.

    Citations

    More Info

    • Introduction

      Wheat Gliadin and related gluten components from barley, rye and possibly oats can cause an abnormal immune response called Celiac disease which is a chronic gastrointestinal disorder. Celiac disease characteristics are flattening of the jejunal mucosa and intestinal lesions of variable severity in hereditarily inclined individuals. Even though Celiac disease is not a classic autoimmune disease it is related to anti-tissue transglutaminase antibodies and gliadin antibodies tests are most recommended in screening populations at risk for CD and other gluten-sensitive enteropathies. In the past, serologic tests for gliadin antibodies usually were not very precise and were not enough for accurate diagnosis due to missing deamidated epitopes within the authentic gliadin fraction traditionally used in diagnostic test kits. ProSpec's deamidated Gliadin isoform matches to the deamidated neo-epitopes, which in the natural antigen are formed by transglutaminase-mediated glutamine side chain deamidation.

    • Physical Appearance

      Sterile Filtered clear solution.

    • Stability

      Gliadin Alpha although stable at 4°C for 1 week, should be stored below -18°C. Please prevent freeze thaw cycles.

    • Amino Acid Sequence

      MVRVPVPQLQPQNPSQQQPQEQVPLVQQQQFPGQQQPFPPQQPYPQPQPFPSQQPYLQ
      LQPFPQPQLPYPQPQLPYPQPQLPYPQPQPFRPQQPYPQSQPQYSQPQQPISQQQQQQQQ
      QQQQKQQQQQQQQILQQILQQQLIPCRDVVLQQHSIAYGSSQVLQQSTYQLVQQLCCQQL
      WQIPEQSRCQAIHNVVHAIILHQQQQQQQQQQQQPLSQVSFQQPQQQYPSGQGSFQPSQ
      QNPQAQGSVQPQQLPQFEEIRNLALETLPAMCNVYIPPYCTIAPVGIFGTNYRHHHHHH.

    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.

    Gliadin Alpha Wheat
  • View Data Sheet

    Name :

    MIF Mouse, His

    Description:

    Macrophage Migration Inhibitor Factor Mouse Recombinant, His Tag

    Macrophage migration inhibitory factor, MIF, Delayed early response protein 6, DER6, Glycosylation-inhibiting factor, GIF, L-dopachrome isomerase, L-dopachrome tautomerase, Phenylpyruvate tautomerase.

    Product # :

    CYT-896

    Price :

    Quantity :

    Shipping Method :

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    Shipped with Ice Packs

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    • description
    • source
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    Description

    MIF Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 138 amino acids (1-115 a.a) and having a molecular mass of 14.9kDa. MIF is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    MIF protein solution (0.5mg/ml) containing Phosphate buffered saline , 10% glycerol and 1mM DTT.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    Citations

    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, Delayed early response protein 6, DER6, Glycosylation-inhibiting factor, GIF, L-dopachrome isomerase, L-dopachrome tautomerase, Phenylpyruvate tautomerase.

    • 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 MGSMPMFIVN TNVPRASVPE GFLSELTQQL AQATGKPAQY IAVHVVPDQL MTFSGTNDPC ALCSLHSIGK IGGAQNRNYS KLLCGLLSDR LHISPDRVYI NYYDMNAANV GWNGSTFA.

    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 Mouse His
  • View Data Sheet

    Name :

    IRF2 Human

    Description:

    IFN Regulatory Factor-2 Human Recombinant

    IRF-2, IRF2, MAR, DKFZp686F0244, IFN regulatory factor 2.

    Product # :

    CYT-534

    Price :

    Quantity :

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    Shipped with Ice Packs

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    • SDS-PAGE
    • Citations

    Description

    IFN Regulatory Factor-2 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 133 amino acids (1-113) with a His Tag of 20 aa, and having a molecular mass of 15 kDa.The IRF2 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    1 mg/ml in 20mM Tris pH-8, 1mM DTT and 10% Glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    SDS-PAGE

    IRF2 Human - Product image 1

    Citations

    More Info

    • Introduction

      IFN regulatory factor 2 is a member of the IFN regulatory transcription factor (IRF) family. IRF2 competitively inhibits the IRF1-mediated transcriptional activation of IFNs alpha and beta, and presumably other genes that employ IRF1 for transcription activation. However, IRF2 also functions as a transcriptional activator of histone H4. IRF2 binds to the upstream regulatory region of type-1 IFN and IFN-inducible MHC class-1 genes (the IFN consensus sequence (ics) and represses those genes.

    • Synonyms

      IRF-2, IRF2, MAR, DKFZp686F0244, IFN regulatory factor 2.

    • 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 MPVERMRMRP WLEEQINSNT IPGLKWLNKE KKIFQIPWMHAARHGWDVEK DAPLFRNWAI HTGKHQPGVD KPDPKTWKAN FRCAMNSLPD IEEVKDKSIKKGNNAFRVYR MLP.

    • Background

      What is the molecular weight/Mw of IRF2 HUMAN Protein?
      IRF2 HUMAN Protein has a total Mw of 15kDa.

      What is the source or expression system of IRF2 HUMAN Protein?
      Escherichia Coli.

      What is the Purity of IRF2 HUMAN Protein?
      IRF2 HUMAN Protein is >95% pure as determined by SDS-PAGE.

      What is the Biological Activity of IRF2 HUMAN Protein?
      The biological functionality of IRF2 HUMAN Protein will be determined in the future.

      What is the amino acid sequence of IRF2 HUMAN Protein?
      MGSSHHHHHH SSGLVPRGSH MPVERMRMRP WLEEQINSNT IPGLKWLNKE KKIFQIPWMHAARHGWDVEK DAPLFRNWAI HTGKHQPGVD KPDPKTWKAN FRCAMNSLPD IEEVKDKSIKKGNNAFRVYR MLP.

      What applications can IRF2 HUMAN Protein be used in?
      IRF2 HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for IRF2 HUMAN Protein?
      The endotoxin level is minimal, IRF2 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.

    Irf 2 Human
  • View Data Sheet

    Name :

    SDF2 Human, sf9

    Description:

    Stromal Cell-Derived Factor 2, Sf9 Human Recombinant

    Stromal Cell Derived Factor 2, Stromal Cell-Derived Factor 2, SDF-2 

    Product # :

    CHM-034

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    Description

    SDF2 produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 202 amino acids (19-211a.a.) and having a molecular mass of 22.3kDa. (Molecular size on SDS-PAGE will appear at approximately 18-28kDa). SDF2 is expressed with an 9 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    SDF2 protein solution (0.25mg/ml) contains 50mM Tris-HCl (pH 8.0), 10% glycerol, 0.1M NaCl 0.1mM PMSF and 0.5mM EDTA.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      Stromal Cell-Derived Factor 2 (SDF2) is a secretory protein which is partly similar to the hydrophilic segments of yeast mannosyltransferases. SDF2 protein’s expression is ubiquitous and the gene is rather conserved among mammals. SDF2 is a protein-coding gene whose alternative splicing results in coding and non-coding variants.

    • Synonyms

      Stromal Cell Derived Factor 2, Stromal Cell-Derived Factor 2, SDF-2

    • 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

      ADPSSLGVVT CGSVVKLLNT RHNVRLHSHD VRYGSGSGQQ SVTGVTSVDD SNSYWRIRGK SATVCERGTP IKCGQPIRLT HVNTGRNLHS HHFTSPLSGN QEVSAFGEEG EGDYLDDWTV LCNGPYWVRD GEVRFKHSST EVLLSVTGEQ YGRPISGQKE VHGMAQPSQN NYWKAMEGIF MKPSELLKAE AHHAELHHHH HH

    • Background

      What is the molecular weight/Mw of SDF2 HUMAN, SF9 Protein?
      SDF2 HUMAN, SF9 Protein has a total Mw of 22.3kDa.

      What is the source or expression system of SDF2 HUMAN, SF9 Protein?
      Sf9, Baculovirus cells.

      What is the Purity of SDF2 HUMAN, SF9 Protein?
      SDF2 HUMAN, SF9 Protein is > 95% pure as determined by SDS-PAGE.

      What is the Biological Activity of SDF2 HUMAN, SF9 Protein?
      The biological functionality of SDF2 HUMAN, SF9 Protein will be determined in the future.

      What is the amino acid sequence of SDF2 HUMAN, SF9 Protein?
      ADPSSLGVVT CGSVVKLLNT RHNVRLHSHD VRYGSGSGQQ SVTGVTSVDD SNSYWRIRGK SATVCERGTP IKCGQPIRLT HVNTGRNLHS HHFTSPLSGN QEVSAFGEEG EGDYLDDWTV LCNGPYWVRD GEVRFKHSST EVLLSVTGEQ YGRPISGQKE VHGMAQPSQN NYWKAMEGIF MKPSELLKAE AHHAELHHHH HH

      What applications can SDF2 HUMAN, SF9 Protein be used in?
      SDF2 HUMAN, SF9 Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for SDF2 HUMAN, SF9 Protein?
      The endotoxin level is minimal, SDF2 HUMAN, SF9 Protein was purified using conventional chromatography techniques.

      Who supplies SDF2 HUMAN, SF9 that is in stock and available to order?
      ProSpec has the protein in stock and available for immediate delivery.

      Where can I order bulk mg quantities of SDF2 HUMAN, SF9?
      ProSpec supplies bulk mg quantities at affordable prices that meets research and academic budgets.

    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.

    Sdf 2 Human
  • View Data Sheet

    Name :

    CDNF Human

    Description:

    Cerebral Neurotrophic Factor Human Recombinant

    Cerebral neurotrophic factor, arginine-rich, mutated in early stage tumors-like 1, Conserved neurotrophic factor, ARMET-like protein 1, ARMETL1.

    Product # :

    CYT-167

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    Description

    CDNF Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 161 amino acids and having a molecular mass of 18.5kDa.The CDNF is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    CDNF protein was lyophilized from a 0.2µm filtered concentrated solution in 1xPBS, pH 7.4.

    Purity

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

    Biological Activity

    The ED50 as determined by its ability to stimulate the proliferation of rat C6 cells is 15-25µg/ml, corresponding to a specific activity of 40-67units/mg.

    Citations

    More Info

    • Introduction

      CDNF is a member of the ARMET family and acts as a trophic factor for neurons. CDNF inhibits the (6-OHDA)-induced degeneration of neurons. When CDNF controlled after 6-OHDA-lesioning, it reestablishes the function and inhibits the degeneration of neurons in substantia nigra. CDNF is universally expressed in neuronal and non-neuronal tissues. The highest levels in the brain are found in the optic nerve and corpus callosum.

    • Synonyms

      Cerebral neurotrophic factor, arginine-rich, mutated in early stage tumors-like 1, Conserved neurotrophic factor, ARMET-like protein 1, ARMETL1.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Amino Acid Sequence

      QEAGGRPGAD CEVCKEFLNR FYKSLIDRGV NFSLDTIEKE LISFCLDTKG KENRLCYYLG ATKDAATKIL SEVTRPMSVH MPAMKICEKL KKLDSQICEL KYEKTLDLAS VDLRKMRVAE LKQILHSWGE ECRACAEKTD YVNLIQELAP KYAATHPKTE L

    • Background

      Cerebral Neurotrophic Factor Human Recombinant: A Leap Forward in Neurobiology

      The field of neurobiology is replete with wonder, particularly due to the influential role of neurotrophic factors. These essential proteins, responsible for the survival and growth of neurons, have become a focal point in modern research. Among these, the Cerebral Neurotrophic Factor (CNF) stands out, offering novel insights and potential breakthroughs in our understanding of neurological health.

      Enter the world of bioengineering, a scientific arena where we have successfully replicated CNF, leading to the birth of Cerebral Neurotrophic Factor Human Recombinant (CNF-HR). This is a massive step towards conquering neurodegenerative disorders such as Alzheimer's and Parkinson's diseases, conditions that have perplexed scientists and clinicians for decades.

      The extraordinary capacity of CNF-HR lies in its dual functionality - it acts as a defender and a promoter. It defends neurons from harmful degenerative processes while promoting their growth and development. Picture a devoted gardener who tirelessly protects his garden from pests and nurtures the growth of each plant. In this context, the brain is the vibrant garden, and the neurons, the delicate plants we must care for.

      Although this scientific breakthrough sparks enthusiasm, it's crucial to remember the challenges that lie ahead. The path to determining the most effective method of delivering CNF-HR to the brain, identifying the optimal dosage, and monitoring potential side effects is a winding one. Nevertheless, with continuous research and relentless scientific curiosity, we are optimistic about overcoming these challenges.

      In conclusion, the development of CNF-HR is a significant milestone in the fascinating journey of neurobiology. Its potential to change the trajectory of treating neurodegenerative diseases and enhancing our understanding of neuronal function is tremendous. While the journey is strewn with complexities, the potential rewards we stand to reap promise a future where neurodegenerative diseases could be effectively managed or even cured.

      What is the molecular weight/Mw of CDNF Protein?
      CDNF Protein has a total Mw of 18.5kDa.

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

      What is the Purity of CDNF Protein?
      CDNF Protein is >96% pure as determined by SDS-PAGE.

      What is the Biological Activity of CDNF Protein?
      The ED50 as determined by its ability to stimulate the proliferation of rat C6 cells is 15-25µg/ml, corresponding to a specific activity of 40-67units/mg.

      What is the amino acid sequence of CDNF Protein?
      QEAGGRPGAD CEVCKEFLNR FYKSLIDRGV NFSLDTIEKE LISFCLDTKG KENRLCYYLG ATKDAATKIL SEVTRPMSVH MPAMKICEKL KKLDSQICEL KYEKTLDLAS VDLRKMRVAE LKQILHSWGE ECRACAEKTD YVNLIQELAP KYAATHPKTE L

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

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

    Cdnf Human
  • View Data Sheet

    Name :

    NEFL Human

    Description:

    Neurofilament Light Human Recombinant

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

    Product # :

    PRO-2584

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    Description

    NEFL Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain (2-543 a.a) containing 551 amino acids including a 9 a.a N-terminal His tag. The total molecular mass is 62.5kDa (calculated).

    Source

    Escherichia Coli.

    Formulation

    NEFL filtered (0.4 µm) and lyophilized from 0.5mg/ml solution in 15mM Tris and 85mM Glycine, pH 8.5.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      NEFL or Neurofilament light polypeptide is a protein that is encoded through the NEFL gene. NEFL is correlated to a disease called Charcot–Marie–Tooth. The protein’s light subunit is determined by immunoassays in the plasma and cerebrospinal fluid, if present, it can indicate on axonal damage in neurological diseases. By doing so, NEFL can act as a marker for Huntington's disease, Amyotrophic Lateral Sclerosis and multiple sclerosis.

    • Synonyms

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

    • 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

      MKHHHHHHAS SFSYEPYYST SYKRRYVETP RVHISSVRSG YSTARSAYSS YSAPVSSSLS VRRSYSSSSG SLMPSLENLD LSQVAAISND LKSIRTQEKA QLQDLNDRFA SFIERVHELE QQNKVLEAEL LVLRQKHSEP SRFRALYEQE IRDLRLAAED ATNEKQALQG EREGLEETLR NLQARYEEEV LSREDAEGRL MEARKGADEA ALARAELEKR IDSLMDEISF LKKVHEEEIA ELQAQIQYAQ ISVEMDVTKP DLSAALKDIR AQYEKLAAKN MQNAEEWFKS RFTVLTESAA KNTDAVRAAK DEVSESRRLL KAKTLEIEAC RGMNEALEKQ LQELEDKQNA DISAMQDTIN KLENELRTTK SEMARYLKEY QDLLNVKMAL DIEIAAYRKL LEGEETRLSF TSVGSITSGY SQSSQVFGRS AYGGLQTSSY LMSTRSFPSY YTSHVQEEQI EVEETIEAAK AEEAKDEPPS EGEAEEEEKD KEEAEEEEAA EEEEAAKEES EEAKEEEEGG EGEEGEETKE AEEEEKKVEG AGEEQAAKKK D.

    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.

    Hepsin Human
  • View Data Sheet

    Name :

    ENHO Human

    Description:

    Energy Homeostasis Associated Human Recombinant

    Adropin, Energy homeostasis-associated protein, ENHO, C9orf165, UNQ470.

    Product # :

    PRO-1569

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    Description

    ENHO Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain (a.a 34-76) containing 121 amino acids including extra 78 N-terminal amino acids. The total molecular mass is 13.05kDa (calculated).

    Source

    Escherichia Coli.

    Formulation

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

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      Energy Homeostasis Associated (ENHO) participates in glucose homeostasis maintenance and lipid metabolism. ENHO is expressed in the liver and the brain. The role of ENHO in obesity or diabetes is studied.

    • Synonyms

      Adropin, Energy homeostasis-associated protein, ENHO, C9orf165, UNQ470.

    • 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. ENHO is not sterile! Please filter the product by an appropriate sterile filter before using it in the cell culture.

    • Amino Acid Sequence

      MGGKSNGEKK YIVGFKQGFK SCAKKEDVIS EKGGKLQKCF KYVDAASATL NEKAVEELKK DPSVAYVEED KLFKALTSCHSRSADVDSLS ESSPNSSPGP CPEKAPPPQK PSHEGSYLLQ P.

    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.

    Enho Human
  • View Data Sheet

    Name :

    FTSJ2 Human

    Description:

    FtsJ RNA Methyltransferase Homolog 2 Human Recombinant

    FtsJ RNA methyltransferase homolog 2 (E. coli), putative ribosomal RNA methyltransferase 2, MRM2 RNA methyltransferase homolog, rRNA (uridine-2'-O-)-methyltransferase, cell division protein FtsJ, Protein ftsJ homolog 2, MRM2, FJH1, EC 2.1.1.-.

    Product # :

    PRO-1207

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    Description

    FTSJ2 Human Recombinant produced in E. coli is a single polypeptide chain containing 219 amino acids (51-246) and having a molecular mass of 24.1 kDa.FTSJ2 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    The FTSJ2 solution (1mg/1ml) 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.

    Citations

    More Info

    • Introduction

      FtsJ RNA Methyltransferase Homolog 2 (FTSJ2) belongs to the S-adenosylmethionine-binding protein family. FTSJ2 is a nucleolar protein and which is involved in cell cycle control and DNA repair and the processing and modification of rRNA. FTSJ2 is extensively expressed, with the highest expression in the muscle, placenta, and heart.

    • Synonyms

      FtsJ RNA methyltransferase homolog 2 (E. coli), putative ribosomal RNA methyltransferase 2, MRM2 RNA methyltransferase homolog, rRNA (uridine-2'-O-)-methyltransferase, cell division protein FtsJ, Protein ftsJ homolog 2, MRM2, FJH1, EC 2.1.1.-.

    • 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 MGSSYRCRSA FKLLEVNERH QILRPGLRVL DCGAAPGAWS QVAVQKVNAA GTDPSSPVGF VLGVDLLHIF PLEGATFLCP ADVTDPRTSQ RILEVLPGRR ADVILSDMAP NATGFRDLDH DRLISLCLTL LSVTPDILQP GGTFLCKTWA GSQSRRLQRR LTEEFQNVRI IKPEASRKES SEVYFLATQY HGRKGTVKQ

    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.

    Ftsj2 Human
  • View Data Sheet

    Name :

    FUT3 Human

    Description:

    Fucosyltransferase 3 Human Recombinant

    Galactoside 3(4)-L-fucosyltransferase, Blood group Lewis alpha-4-fucosyltransferase, Lewis FT, Fucosyltransferase 3, Fucosyltransferase III, FucT-III, FUT3, FT3B, LE, CD174, Les.

    Product # :

    ENZ-745

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    Description

    FUT3 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 350 amino acids (35-361 a.a) and having a molecular mass of 40.6kDa.FUT3 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The FUT3 solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.4M urea and 10% glycerol.

    Purity

    Greater than 80% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      Fucosyltransferase 3 (FUT3) catalyzes alpha-1, 3 and alpha-1, 4 glycosidic linkages which take part in the expression of Vim-2, Lewis A, Lewis B, sialyl Lewis X and Lewis X/SSEA-1 antigens. FUT3 takes part in blood group Lewis determination; Lewis-positive (Le+) individuals have an active enzyme while Lewis-negative (Le-) individuals have an inactive enzyme. FUT3 also operates on the corresponding 1, 4-galactosyl derivative, creating1, 3-L-fucosyl links.

    • Synonyms

      Galactoside 3(4)-L-fucosyltransferase, Blood group Lewis alpha-4-fucosyltransferase, Lewis FT, Fucosyltransferase 3, Fucosyltransferase III, FucT-III, FUT3, FT3B, LE, CD174, Les.

    • 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 MGSRVSRDDA TGSPRAPSGS SRQDTTPTRP TLLILLWTWP FHIPVALSRC SEMVPGTADC HITADRKVYP QADTVIVHHW DIMSNPKSRL PPSPRPQGQR WIWFNLEPPP NCQHLEALDR YFNLTMSYRS DSDIFTPYGW LEPWSGQPAH PPLNLSAKTE LVAWAVSNWK PDSARVRYYQ SLQAHLKVDV YGRSHKPLPK GTMMETLSRY KFYLAFENSL HPDYITEKLW RNALEAWAVP VVLGPSRSNY ERFLPPDAFI HVDDFQSPKD LARYLQELDK DHARYLSYFR WRETLRPRSF SWALDFCKAC WKLQQESRYQ TVRSIAAWFT.

    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.

    Fut3 Human
  • View Data Sheet

    Name :

    Leptin Rat

    Description:

    Leptin Rat Recombinant

    OB Protein, Obesity Protein, OBS, Obesity factor.

    Product # :

    CYT-227

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    Description

    Leptin Rat Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 147 amino acids and having a molecular mass of 16 kDa.The Leptin is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The protein was lyophilized from a concentrated (1mg/ml) solution with 0.0045mM NaHCO3.

    Purity

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

    Biological Activity

    Biological activity of Leptin Rat is evidenced by inducing proliferation of BAF/3 cells stably transfected with the long form of human leptin receptor.

    Citations

    More Info

    • Introduction

      A 16-kDa peptide hormone secreted from white adipocytes and implicated in the regulation of food intake and energy balance. Leptin provides the key afferent signal from fat cells in the feedback system that controls body fat stores.

    • Synonyms

      OB Protein, Obesity Protein, OBS, Obesity factor.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized Leptin although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Leptin 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 Leptin 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-Val-Pro-Ile-His.

    • Protein content

      Protein quantitation was carried out by two independent methods:1. UV spectroscopy at 280 nm using the absorbency value of 0.201 as the extinction coefficient for a 0.1% (1mg/ml) solution. This value is calculated by the PC GENE computer analysis program of protein sequences (IntelliGenetics).2. Analysis by RP-HPLC, using a calibrated solution of Leptin rat as a Reference Standard.

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

    Leptin Rat
  • View Data Sheet

    Name :

    glpE E.Coli

    Description:

    Thiosulfate sulfurtransferase E.Coli Recombinant

    ECK3411, JW3388, b3425, Thiosulfate sulfurtransferase GlpE.

    Product # :

    ENZ-714

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    Description

    glpE Recombinant produced in E. coli is a single polypeptide chain containing 131 amino acids (1-108) and having a molecular mass of 14.5kDa. glpE is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

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

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      Thiosulfate sulfurtransferase (glpE) is a mitochondrial matrix enzyme which is encoded by the nucleus. Escherichia coli glpE is a prototype for the single-domain rhodanese superfamily. glpE catalyzes the sulfur-transfer reaction in which a sulfur atom is transferred from thiosulfate to cyanide by a double-displacement mechanism.

    • Synonyms

      ECK3411, JW3388, b3425, Thiosulfate sulfurtransferase GlpE.

    • 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 MGSMDQFECI NVADAHQKLQ EKEAVLVDIR DPQSFAMGHA VQAFHLTNDT LGAFMRDNDF DTPVMVMCYH GNSSKGAAQY LLQQGYDVVY SIDGGFEAWQ RQFPAEVAYG A.

    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.

    Glpe Ecoli
  • View Data Sheet

    Name :

    Cyclophilin G Human

    Description:

    Cyclophilin-G Human Recombinant

    Peptidyl-prolyl cis-trans isomerase G, PPIase G, Rotamase G, PPIG, peptidylprolyl isomerase G, Cyclophilin G, Peptidyl-prolyl isomerase G, Rotamase G, Clk-associating RS-cyclophilin, CARS-cyclophilin, CARS-Cyp, SR-cyclophilin, SR-cyp, SRcyp, CASP10, CYP, MGC133241.

    Product # :

    ENZ-463

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    Description

    Cyclophilin-G Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 195 amino acids (1-175 a.a.) and having a molecular mass of 21.6 kDa. Cyclophilin-G is fused to a 20 amino acid His Tag at N-terminus and is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Cyclophilin-G solution containing 20mM Tris-HCl pH-8, 1mM DTT and 10% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Biological Activity

    Specific activity is > 200 nmoles/min/mg, and is defined as the amount of enzyme that cleaves 1umole of suc-AAFP-pNA per minute at 25C in Tris-Hcl pH8.0 using chymotrypsin.

    Citations

    More Info

    • Introduction

      Cyclophilin-G is a member of the peptidyl-prolyl cis-trans isomerase (PPIase) family. PPIases catalyze the cis-trans isomerization of proline imidic peptide bonds in oligopeptides and speeds up the protein folding. PPIG catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides and is involved in the folding, transport, and assembly of proteins. PPIG is localized to the nuclear speckles, a nuclear compartment rich in splicing factors, and cooperates with the splicing factors SC35 and pinin. Cyclophilin-G also takes part in the regulation of pre-mRNA splicing.

    • Synonyms

      Peptidyl-prolyl cis-trans isomerase G, PPIase G, Rotamase G, PPIG, peptidylprolyl isomerase G, Cyclophilin G, Peptidyl-prolyl isomerase G, Rotamase G, Clk-associating RS-cyclophilin, CARS-cyclophilin, CARS-Cyp, SR-cyclophilin, SR-cyp, SRcyp, CASP10, CYP, MGC133241.

    • 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 MGIKVQRPRC FFDIAINNQP AGRVVFELFS DVCPKTCENF RCLCTGEKGT GKSTQKPLHY KSCLFHRVVK DFMVQGGDFS EGNGRGGESI YGGFFEDESF AVKHNKEFLL SMANRGKDTN GSQFFITTKP TPHLDGHHVV FGQVISGQEV VREIENQKTD AASKPFAEVR ILSCG.

    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.

    Cyclophilin G Human
  • View Data Sheet

    Name :

    SNF8 Human

    Description:

    SNF8, ESCRT-II Complex Subunit Human Recombinant

    SNF8 ESCRT-II complex subunit homolog (S. cerevisiae), ESCRT-II complex subunit VPS22, ELL-associated protein of 30 kDa, EAP30 subunit of ELL complex, vacuolar-sorting protein SNF8, EAP30, VPS22, Dot3.

    Product # :

    PRO-1135

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    Description

    SNF8 Human Recombinant produced in E. coli is a single polypeptide chain containing 282 amino acids (1-258) and having a molecular mass of 31.4 kDa.SNF8 is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    The SNF8 solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.2M NaCl, 2mM DTT and 50% glycerol.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      SNF8 belongs to the SNF8 family of vacuolar sorting proteins and is restricts to both the nucleus and the cytoplasm. SNF8 is a subunit of the endosomal sorting complex essential for transport II (ESCRT-II), which is necessary for multivesicular body (MVB) formation and sorting of endosomal cargo proteins into MVBs. The MVB pathway facilitates transfer of transmembrane proteins into the lumen of the lysosome for degradation. Additionally, the ESCRT-II complex takes part in transcription regulation by contributing to derepression of transcription by RNA polymerase II, probably by its interface with ELL.

    • Synonyms

      SNF8 ESCRT-II complex subunit homolog (S. cerevisiae), ESCRT-II complex subunit VPS22, ELL-associated protein of 30 kDa, EAP30 subunit of ELL complex, vacuolar-sorting protein SNF8, EAP30, VPS22, Dot3.

    • 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 MGSHMHRRGV GAGAIAKKKL AEAKYKERGT VLAEDQLAQM SKQLDMFKTN LEEFASKHKQ EIRKNPEFRV QFQDMCATIG VDPLASGKGF WSEMLGVGDF YYELGVQIIE VCLALKHRNG GLITLEELHQ QVLKGRGKFA QDVSQDDLIR AIKKLKALGT GFGIIPVGGT YLIQSVPAEL NMDHTVVLQL AEKNGYVTVS EIKASLKWET ERARQVLEHL LKEGLAWLDL QAPGEAHYWL PALFTDLYSQ EITAEEAREA LP

    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.

    Snf8 Human
  • View Data Sheet

    Name :

    ST3GAL5 Human

    Description:

    ST3 Beta-Galactoside Alpha-2,3-Sialyltransferase 5 Human Recombinant

    ST3 Beta-Galactoside Alpha-2,3-Sialyltransferase 5, SIAT9, Sialyltransferase 9 (CMP-NeuAc:Lactosylceramide Alpha-2,3-Sialyltransferase; GM3 Synthase), Ganglioside GM3 Synthase, ST3GalV, CMP-NeuAc:Lactosylceramide Alpha-2,3-Sialyltransferase, ST3Gal V, EC 2.4.99.9, SATI, SIATGM3S, Alpha 2,3-Sialyltransferase V, Lactosylceramide Alpha-2,3-Sialyltransferase, Sialyltransferase 9, ST3GALV, GM3 Synthase.

    Product # :

    ENZ-755

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    Description

    ST3GAL5 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 359 amino acids (83-418a.a) and having a molecular mass of 41kDa. ST3GAL5 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    ST3GAL5 protein solution (1mg/ml) containing In 20mM Tris-HCl buffer (pH 8.0), 10% glycerol and 0.4M Urea.

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      ST3 Beta-Galactoside Alpha-2,3-Sialyltransferase 5, also know as ST3GAL5 belongs to the glycosyltransferase family 29 and localized to the Golgi apparatus. ST3GAL5 is known to play a part in the induction of cell differentiation, modulation of cell proliferation, maintenance of fibroblast morphology, signal transduction, and integrin-mediated cell adhesion. ST3GAL5 is a type II membrane protein which catalyzes the formation of GM3 with lactosylceramide as the substrate. Mutation in this ST3GAL5 has been connected with Amish infantile epilepsy syndrome. Transcript variants encoding various isoforms have been found for this gene.

    • Synonyms

      ST3 Beta-Galactoside Alpha-2,3-Sialyltransferase 5, SIAT9, Sialyltransferase 9 (CMP-NeuAc:Lactosylceramide Alpha-2,3-Sialyltransferase; GM3 Synthase), Ganglioside GM3 Synthase, ST3GalV, CMP-NeuAc:Lactosylceramide Alpha-2,3-Sialyltransferase, ST3Gal V, EC 2.4.99.9, SATI, SIATGM3S, Alpha 2,3-Sialyltransferase V, Lactosylceramide Alpha-2,3-Sialyltransferase, Sialyltransferase 9, ST3GALV, GM3 Synthase.

    • 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).Please avoid freeze thaw cycles.

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MGSLKLNYTT EECDMKKMHY VDPDHVKRAQ KYAQQVLQKE CRPKFAKTSM ALLFEHRYSV DLLPFVQKAP KDSEAESKYD PPFGFRKFSS KVQTLLELLP EHDLPEHLKA KTCRRCVVIG SGGILHGLEL GHTLNQFDVV IRLNSAPVEG YSEHVGNKTT IRMTYPEGAP LSDLEYYSND LFVAVLFKSV DFNWLQAMVK KETLPFWVRL FFWKQVAEKI PLQPKHFRIL NPVIIKETAF DILQYSEPQS RFWGRDKNVP TIGVIAVVLA THLCDEVSLA GFGYDLNQPR TPLHYFDSQC MAAMNFQTMH NVTTETKFLL KLVKEGVVKD LSGGIDREF

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    St3Gal5 Human
  • View Data Sheet

    Name :

    PFN1 Human

    Description:

    Profilin-1 Human Recombinant

    Profilin-1, Profilin I, PFN1.

    Product # :

    PRO-528

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    Description

    PFN1 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 140 amino acids (1-140 a.a.) and having a molecular mass of 15kDa.The PFN1 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The PFN1 protein solution contains 20mM Tris-HCl buffer (pH8.0) and 10% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      Profilin1 (PFN1) is a ubiquitous actin monomer-binding protein which is a member of the profilin family. PFN1 significantly boosts skin wound healing in-vitro and in-vivo which may be mediated by purinergic receptors. PFN1 is also active in endothelial cell migration and vessel sprouting. PFN1 is thought to control actin polymerization in response to extracellular signals. PFN1 binds to actin and affects the formation of the cytoskeleton. In addition, PFN1 has an important role in the regulation of epithelial cell-cell adhesion. At high concentrations, profilin averts the polymerization of actin, while at low concentrations it enhances the polymerization. PFN1 gene deletion is linked to Miller-Dieker syndrome.

    • Synonyms

      Profilin-1, Profilin I, PFN1.

    • 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

      MAGWNAYIDN LMADGTCQDA AIVGYKDSPS VWAAVPGKTF VNITPAEVGV LVGKDRSSFY VNGLTLGGQK CSVIRDSLLQ DGEFSMDLRT KSTGGAPTFN VTVTKTDKTL VLLMGKEGVH GGLINKKCYE MASHLRRSQY.

    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.

    Pfn1 Human
  • View Data Sheet

    Name :

    GSTK1 Human

    Description:

    Glutathione S-Transferase Kappa 1 Human Recombinant

    GST13, GST13-13, GSTK1-1, GST class-kappa, EC 2.5.1.18, Glutathione S-transferase kappa 1, Glutathione S-transferase subunit 13, hGSTK1, GSTK1.

    Product # :

    ENZ-476

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    Description

    GSTK1 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 226 amino acids (1-226 a.a.) and having a molecular mass of 25.5 kDa. GSTK1 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    GSTK1 solution containing 20mM Tris pH-8, 1mM DTT and 10% glycerol.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      GSTK1 is involved in cellular detoxification. GSTK1 is localized to the peroxisome and catalyzes the conjugation of the thiol group of glutathione (GSH) to the electrophilic groups of a broad range of hydrophobic substrates, leading to an easier removal of the latter from the cells.

    • Synonyms

      GST13, GST13-13, GSTK1-1, GST class-kappa, EC 2.5.1.18, Glutathione S-transferase kappa 1, Glutathione S-transferase subunit 13, hGSTK1, GSTK1.

    • 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

      MGPLPRTVEL FYDVLSPYSW LGFEILCRYQ NIWNINLQLR PSLITGIMKD SGNKPPGLLP RKGLYMANDL KLLRHHLQIP IHFPKDFLSV MLEKGSLSAM RFLTAVNLEH PEMLEKASRE LWMRVWSRNE DITEPQSILA AAEKAGMSAE QAQGLLEKIA TPKVKNQLKE TTEAACRYGA FGLPITVAHV DGQTHMLFGS DRMELLAHLL GEKWMGPIPP AVNARL.

    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.

    Gstk1 Human
  • View Data Sheet

    Name :

    GSTT2 Human

    Description:

    Glutathione S-Transferase Theta-2 Human Recombinant

    Glutathione S-transferase theta 2, GST class-theta-2, GSTT2B, Glutathione S-transferase theta-2B, EC 2.5.1.18.

    Product # :

    ENZ-593

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    Description

    GSTT2 Recombinant produced in E. coli is a single polypeptide chain containing 264 amino acids (1-244) and having a molecular mass of 29.6kDa.GSTT2 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    The GSTT2 solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 100mM Nacl,
    1mM DTT and 10% glycerol.

    Purity

    Greater than 95% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      GSTT2 belongs to the glutathione s-transferase (GST) family of proteins. There are eight GST proteins families, named alpha, kappa, mu, omega, pi, sigma, theta and zeta. Each one of the GST families has several proteins with different functions throughout the cell. The theta type members GSTT1 and GSTT2 have a 55% aa sequence homology and hold a vital role in human carcinogenesis. The theta genes are structurally similar – each has five exons with identical exon/intron boundaries.

    • Synonyms

      Glutathione S-transferase theta 2, GST class-theta-2, GSTT2B, Glutathione S-transferase theta-2B, EC 2.5.1.18.

    • 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 MGLELFLDLV SQPSRAVYIF AKKNGIPLEL RTVDLVKGQH KSKEFLQINS LGKLPTLKDG DFILTESSAI LIYLSCKYQT PDHWYPSDLQ ARARVHEYLG WHADCIRGTF GIPLWVQVLG PLIGVQVPEE KVERNRTAMD QALQWLEDKF LGDRPFLAGQ QVTLADLMAL EELMQPVALG YELFEGRPRL AAWRGRVEAF LGAELCQEAH SIILSILEQA AKKTLPTPSP EAYQAMLLRI ARIP

    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.

    Gstt2 Human
  • View Data Sheet

    Name :

    GSTZ1 Human

    Description:

    Glutathione Transferase Zeta 1 Human Recombinant

    MAAI, GSTZ-1, MAI, Maleylacetone Isomerase, EC 2.5.1.18, Maleylacetoacetate isomerase, Glutathione S-transferase zeta 1, EC 5.2.1.2, GSTZ1-1, MGC2029, GSTZ1.

    Product # :

    ENZ-494

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    Description

    GSTZ1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 236 amino acids (1-216 a.a.) and having a molecular mass of 26.2 kDa. The GSTZ1 is fused to a 20 amino acid His-Tag at N-terminus and purified by conventional chromatography.

    Source

    Escherichia Coli.

    Formulation

    The GSTZ1 protein solution contains 1x PBS pH-7.4 and 10% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      GSTZ1 is part of the glutathione S-transferase super-family which encodes multifunctional enzymes vital in the detoxification of electrophilic molecules, including carcinogens, mutagens, and several therapeutic drugs, by conjugation with glutathione. GSTZ1 participates in the catabolism of phenylalanine and tyrosine. Thus defects in GSTZ1 cause harsh metabolic disorders including alkaptonuria, phenylketonuria and tyrosinaemia. GSTZ1 is a bifunctional protein which has minimal glutathione-conjugating activity with 7-chloro-4-nitrobenz-2-oxa-1,3-diazole and maleylacetoacetate isomerase activity. GSTZ1 has low glutathione peroxidase activity with T-butyl and cumene hydroperoxides. GSTZ1 catalyzes the glutathione dependent oxygenation of dichloroacetic acid to glyoxylic acid.

    • Synonyms

      MAAI, GSTZ-1, MAI, Maleylacetone Isomerase, EC 2.5.1.18, Maleylacetoacetate isomerase, Glutathione S-transferase zeta 1, EC 5.2.1.2, GSTZ1-1, MGC2029, GSTZ1.

    • 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 MQAGKPILYS YFRSSCSWRV RIALALKGID YETVPINLIK DGGQQFSKDF QALNPMKQVP TLKIDGITIH QSLAIIEYLE ETRPTPRLLP QDPKKRASVR MISDLIAGGI QPLQNLSVLK QVGEEMQLTW AQNAITCGFN ALEQILQSTA GIYCVGDEVT MADLCLVPQV ANAERFKVDL TPYPTISSIN KRLLVLEAFQ VSHPCRQPDT PTELRA.

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    Gstz1 Human
  • View Data Sheet

    Name :

    WARS Human

    Description:

    Tryptophanyl-tRNA Synthetase Human Recombinant

    GAMMA-2, IFI53, IFP53, WRS, WARS, TrpRS, hWRS, EC=6.1.1.2, Tryptophanyl-tRNA synthetase, INF-induced protein 53, Tryptophan--tRNA ligase, GAMMA-2.

    Product # :

    ENZ-545

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    Description

    WARS Recombinant Human produced in E.Coli is a single, non-glycosylated polypeptide chain containing 491 amino acids (1-471 a.a.) and having a molecular mass of 55.3 kDa. The WARS 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-HCl pH-8, 1mM DTT, 0.1M NaCl, 1mM DTT & 10% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      WARS is part of the class I tRNA synthetase family. 2 types of tryptophanyl tRNA synthetase exist, a cytoplasmic form, called WARS, and a mitochondrial form, called WARS2. WARS catalyzes the aminoacylation of tRNA(trp) with tryptophan and is induced by INF. WARS controls ERK, Akt, and eNOS activation pathways that are related with angiogenesis, cytoskeletal reorganization and shear stress-responsive gene expression.

    • Synonyms

      GAMMA-2, IFI53, IFP53, WRS, WARS, TrpRS, hWRS, EC=6.1.1.2, Tryptophanyl-tRNA synthetase, INF-induced protein 53, Tryptophan--tRNA ligase, GAMMA-2.

    • 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 MPNSEPASLL ELFNSIATQG ELVRSLKAGN ASKDEIDSAV KMLVSLKMSY KAAAGEDYKA DCPPGNPAPT SNHGPDATEA EEDFVDPWTV QTSSAKGIDY DKLIVRFGSS KIDKELINRI ERATGQRPHH FLRRGIFFSH RDMNQVLDAY ENKKPFYLYT GRGPSSEAMH VGHLIPFIFT KWLQDVFNVP LVIQMTDDEK YLWKDLTLDQ AYSYAVENAK DIIACGFDIN KTFIFSDLDY MGMSSGFYKN VVKIQKHVTF NQVKGIFGFT DSDCIGKISF PAIQAAPSFS NSFPQIFRDR TDIQCLIPCA IDQDPYFRMT RDVAPRIGYP KPALLHSTFF PALQGAQTKM SASDPNSSIF LTDTAKQIKT KVNKHAFSGG RDTIEEHRQF GGNCDVDVSF MYLTFFLEDD DKLEQIRKDY TSGAMLTGEL KKALIEVLQP LIAEHQARRK EVTDEIVKEF MTPRKLSFDF Q.

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    Wars Human
  • View Data Sheet

    Name :

    Rhodanese Human

    Description:

    Thiosulfate Sulfurtransferase Human Recombinant

    EC 2.8.1.1, TST, MGC19578, RDS, Thiosulfate sulfurtransferase, Rhodanese.

    Product # :

    ENZ-459

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    Description

    Recombinant Human Rhodanese produced in E.Coli is a single, non-glycosylated polypeptide chain containing 317 amino acids (1-297 a.a) and having a molecular mass of 35.6 kDa. Rhodanese is fused to a 20 amino acid His-Tag at N-terminus and purified by conventional chromatography techniques.

    Source

    Escherichia Coli.

    Formulation

    The Rhodanese protein solution contains 20mM Tris-HCl, pH-8 and 10% Glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      Rhodanese is a mitochondrial matrix enzyme that is encoded by the nucleus. Rhodanese is involved in cyanide detoxification, the formation of iron-sulfur proteins, and the modification of sulfur-containing enzymes. Rhodanese catalyzes the chemical reaction of thiosulfate & cyanide to sulfite & thiocyanate (detoxification). Rhodanese is part of the transferase family of proteins. Rhodanese includes two highly conservative domains, identified as rhodanese homology domains. In mammals, the majority of cyanide is converted to thiocyanate. Rhodanese has weak mercaptopyruvate sulfurtransferase activity.

    • Synonyms

      EC 2.8.1.1, TST, MGC19578, RDS, Thiosulfate sulfurtransferase, Rhodanese.

    • 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 MVHQVLYRAL VSTKWLAESI RTGKLGPGLR VLDASWYSPG TREARKEYLE RHVPGASFFD IEECRDTASP YEMMLPSEAG FAEYVGRLGI SNHTHVVVYD GEHLGSFYAP RVWWMFRVFG HRTVSVLNGG FRNWLKEGHP VTSEPSRPEP AVFKATLDRS LLKTYEQVLE NLESKRFQLV DSRSQGRFLG TEPEPDAVGL DSGHIRGAVN MPFMDFLTED GFEKGPEELR ALFQTKKVDL SQPLIATCRK GVTACHVALA AYLCGKPDVA VYDGSWSEWF RRAPPESRVS QGKSEKA.

    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.

    Rhodanese Human
  • View Data Sheet

    Name :

    GH Rat

    Description:

    GH Rat Recombinant

    GH1, GH, GHN, GH-N, hGH-N,Pituitary GH, GH-1.

    Product # :

    CYT-296

    Price :

    Quantity :

    Shipping Method :

    Room Temp Icon

    Shipped at Room temp

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    More Info

    • description
    • source
    • formulation
    • purity
    • More Info
    • Citations

    Description

    GH Rat Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 190 amino acids and having a molecular mass of 21810 Dalton. GH is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The protein (1mg/ml) was lyophilized after extensive dialyses against 5mM phosphate buffer, 5mg mannitol and 1mg glycine.

    Purity

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

    Citations

    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 gGH 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 GHs, 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 GH locus. Mutations in or deletions of the gene lead to GH deficiency and short stature.

    • Synonyms

      GH1, GH, GHN, GH-N, hGH-N,Pituitary GH, GH-1.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    Growth Hormone Rat
  • View Data Sheet

    Name :

    T.Vaginalis P65 Antibody

    Description:

    Polyclonal Rabbit Anti Trichomonas Vaginalis P65 Antibody

    Product # :

    ANT-494

    Price :

    Quantity :

    Shipping Method :

    Ice Icon

    Shipped with Ice Packs

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    • description
    • formulation
    • purity
    • More Info
    • Citations

    Description

    The polyclonal antibody to Trichomonas vaginalis was collected from the rabbit igG and immunized with recombinant T. Vaginalis P65.

    Formulation

    50mM mg glycine, pH8.0.

    Purity

    Pure Rabbit IgG.

    Citations

    More Info

    • Introduction

      Trichomonas vaginalis, an anaerobic, flagellated protozoan parasite, is most dominant protozoan causing sexual transmitted disease. T. vaginalis induced vaginal tract infection occurs as multiple steps involving interactions between host macromolecules and protozoan virulent factor. Adhension protein P65 of T. vaginalis has a vital part in assisting the penetration into vaginal tract surface.

    • Physical Appearance

      Sterile Filtered clear 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.

    • Purification Method

      Purified by affinity chromatographic technique.

    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.

    Tvaginalis P65 Antibody
  • View Data Sheet

    Name :

    Resistin Human (64-110)

    Description:

    Resistin (64-110) Human Recombinant

    Cysteine-rich secreted protein FIZZ3, Adipose tissue-specific secretory factor, ADSF.

    Product # :

    CYT-1232

    Price :

    Quantity :

    Shipping Method :

    Room Temp Icon

    Shipped at Room temp

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    More Info

    • description
    • source
    • formulation
    • purity
    • More Info
    • Citations

    Description

    The Resistin Human is created as a recombinant protein with a 4kda N-terminal fusion of His Tag. The Resistin His-Tagged Fusion Protein, produced in E. coli, is a 12kDa protein containing 47 amino acid residues of the Resistin Human, 64-110 amino acids.

    Source

    Escherichia Coli.

    Formulation

    Each mg was lyophilized with 1xPBS, 0.4% SDS and 4mM DTT.

    Purity

    Greater than 80% as determined by SDS-PAGE.

    Citations

    More Info

    • Synonyms

      Cysteine-rich secreted protein FIZZ3, Adipose tissue-specific secretory factor, ADSF.

    • Physical Appearance

      Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Store lyophilized Resistin 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. Product is not sterile! Please filter the product by an appropriate sterile filter before using it on cell culture.

    • Background

      Human resistin is an adipokine primarily secreted by adipose tissue, mainly in response to obesity and inflammatory conditions.

      Resistin Function

      Resistin takes part in insulin resistance, which can be the cause of the development of type 2 diabetes. Resistin can also affect glucose metabolism and insulin signalling.

      Regulation

      Levels of resistin are influenced by factors such as inflammation, obesity and certain hormones. It tends to increase in conditions associated with obesity and metabolic syndrome.

      Clinical Relevance

      Elevated levels of resistin have been associated with obesity-related conditions, cardiovascular diseases, and metabolic disorders. Resisting is considered as a potential biomarker for these conditions.

      Resistin Mechanism

      Resistin promotes insulin resistance through different pathways such as the modulation of inflammatory processes and the inhibition of insulin signaling in target tissues like liver and muscle.

      Research

      Ongoing studies are exploring resistin’s role in metabolic regulation, the exact mechanisms of action of resistin and its potential as a therapeutic target for treating metabolic diseases.

      Overall, resistin is a critical factor in metabolic health, mainly in the context of diabetes and obesity.

    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.

    Resistin Human Protein
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