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Search results

1000 results found for “cytohesin”

Name

Description

Product #

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  • View Data Sheet

    Name :

    EMG1 Human

    Description:

    EMG1 Nucleolar Protein Human Recombinant

    EMG1 nucleolar protein homolog (S. cerevisiae), 18S rRNA Psi1248 methyltransferase, 18S rRNA (pseudouridine-N1-)-methyltransferase NEP1, Ribosome biogenesis protein NEP1, essential for mitotic growth 1, ribosomal RNA small subunit methyltransferase NEP1, Protein C2f, BWCNS, Grcc2f, NEP1, EC 2.1.1.-.

    Product # :

    PRO-1122

    Price :

    Quantity :

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    Description

    EMG1 Human Recombinant produced in E. coli is a single polypeptide chain containing 267 amino acids (1-244) and having a molecular mass of 29.1kDa.EMG1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    The EMG1 solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 100mM Nacl, 1mM DTT and 20% glycerol.

    Purity

    Greater than 95% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      EMG1 is a 244 aa protein which has a role in ribosome biogenesis. EMG1 is a key protein in the small ribosomal subunit assembly, controls methylation during ribosome synthesis and takes part in pre-18S rRNA processing. EMG1 is localized to the nucleolus and a mutation in this gene is linked with Bowen-Conradi syndrome.

    • Synonyms

      EMG1 nucleolar protein homolog (S. cerevisiae), 18S rRNA Psi1248 methyltransferase, 18S rRNA (pseudouridine-N1-)-methyltransferase NEP1, Ribosome biogenesis protein NEP1, essential for mitotic growth 1, ribosomal RNA small subunit methyltransferase NEP1, Protein C2f, BWCNS, Grcc2f, NEP1, 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 MGSMAAPSDG FKPRERSGGE QAQDWDALPP KRPRLGAGNK IGGRRLIVVL EGASLETVKV GKTYELLNCD KHKSILLKNG RDPGEARPDI THQSLLMLMD SPLNRAGLLQ VYIHTQKNVL IEVNPQTRIP RTFDRFCGLM VQLLHKLSVR AADGPQKLLK VIKNPVSDHF PVGCMKVGTS FSIPVVSDVR ELVPSSDPIV FVVGAFAHGK VSVEYTEKMV SISNYPLSAA LTCAKLTTAF EEVWGVI

    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.

    Emg1 Human
  • View Data Sheet

    Name :

    BD 3 Mouse

    Description:

    Beta Defensin-3 Mouse Recombinant

    Beta-defensin 3, BD-3, mBD-3, Defensin beta 3, Defb3, Bd3, MGC129397.

    Product # :

    CYT-036

    Price :

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    Description

    Beta Defensin-3 Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 41 amino acids and having a molecular mass of 4.6kDa. The BD-3 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The Mouse BD-3 was lyophilized from a 0.2µm filtered concentrated solution in PBS, pH7.4.

    Purity

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

    Biological Activity

    Measured by its antimicrobial activity against E. coli. The ED50 for this effect is typically 4-20µg/ml, corresponding to a specific activity of 50,000-250,000units/mg.

    Citations

    More Info

    • Introduction

      Defensins form a family of microbicidal and cytotoxic peptides made by neutrophils. Members of the defensin family are highly similar in protein sequence. This gene encodes defensin, beta 103A, which has broad spectrum antimicrobial activity and may play an important role in innate epithelial defense.

    • Synonyms

      Beta-defensin 3, BD-3, mBD-3, Defensin beta 3, Defb3, Bd3, MGC129397.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Amino Acid Sequence

      KKINNPVSCL RKGGRCWNRC IGNTRQIGSC GVPFLKCCKR K.

    • Background

      What is the molecular weight/Mw of BD3 Protein?
      BD3 Protein has a total Mw of 4.6kDa.

      What is the source or expression system of BD3 Protein?
      Escherichia Coli.

      What is the Purity of BD3 Protein?
      BD3 Protein is >98% pure as determined by SDS-PAGE.

      What is the Biological Activity of BD3 Protein?
      Measured by its antimicrobial activity against E. coli. The ED50 for this effect is typically 4-20µg/ml, corresponding to a specific activity of 50,000-250,000units/mg.

      What is the amino acid sequence of BD3 Protein?
      KKINNPVSCL RKGGRCWNRC IGNTRQIGSC GVPFLKCCKR K.

      What applications can BD3 Protein be used in?
      BD3 Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for BD3 Protein?
      The endotoxin level is minimal, BD3 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.

    Bd 3 Mouse
  • View Data Sheet

    Name :

    STXBP6 Human

    Description:

    Syntaxin Binding Protein 6 Human Recombinant

    Syntaxin-binding protein 6, Amisyn, STXBP6, HSPC156, Syntaxin Binding Protein 6.

    Product # :

    PRO-2056

    Price :

    Quantity :

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    Description

    STXBP6 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 233 amino acids (1-210 a.a.) and having a molecular mass of 25.9kDa.STXBP6 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    STXBP6 protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH8.0), 10% glycerol, 0.15M NaCl and 1mM DTT.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      Syntaxin-binding protein 6 (STXBP6) binds components of the SNARE complex and takes part in regulating SNARE complex configuration. STXBP6 forms non-fusogenic complexes with SNAP25 and STX1A and modulates the formation of SNARE complexes and exocytosis.

    • Synonyms

      Syntaxin-binding protein 6, Amisyn, STXBP6, HSPC156, Syntaxin Binding Protein 6.

    • Physical Appearance

      Sterile Filtered clear solution.

    • Stability

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

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MGSMSAKSAI SKEIFAPLDE RMLGAVQVKR RTKKKIPFLA TGGQGEYLTY ICLSVTNKKP TQASITKVKQ FEGSTSFVRR SQWMLEQLRQ VNGIDPNGDS AEFDLLFENA FDQWVASTAS EKCTFFQILH HTCQRYLTDR KPEFINCQSK IMGGNSILHS AADSVTSAVQ KASQALNERG ERLGRAEEKT EDLKNSAQQF AETAHKLAMK HKC.

    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.

    Stxbp6 Human
  • View Data Sheet

    Name :

    Super Leptin qA Ovine

    Description:

    Super Leptin Antagonist Ovine Recombinant

    Product # :

    CYT-1245

    Price :

    Quantity :

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    Description

    Super Leptin Antagonist Ovine Recombinant is a single polypeptide chain containing 146 amino acids, an additional Ala at N-terminus acids and having a molecular mass of ~ 16 kDa. Super Ovine Leptin Antagonist was mutated, resulting in D23L/L39A/D40A/F41A that was purified by proprietary chromatographic techniques.

    Source

    Escherichia coli.

    Formulation

    The protein was lyophilized from a concentrated (1mg/ml) solution with 0.003mM NaHCO3.

    Purity

    Greater than 98.0% as determined by:

    (a) Gel filtration analysis.

    (b) Analysis by SDS-PAGE.

    Biological Activity

    ProSpec’s super Ovine leptin antagonist is capable of inhibiting leptin-induced proliferation of BAF/3 cells stably transfected with the long form of human leptin receptor. Super Ovine leptin antagonist also inhibits various leptin effects in several in vitro bioassays.

    Citations

    More Info

    • Physical Appearance

      White lyophilized (freeze-dried) powder.

    • Stability

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

    • Solubility

      It is recommended to reconstitute the lyophilized Super Leptin Antagonist in sterile water or sterile 0.4% NaHCO3 adjusted to pH 10, 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-Arg.

    • Background

      Leptin is a hormone which mainly produced by adipocytes. Leptin’s main part is to regulate long-term energy balance. Leptin is encoded by the LEP gene. Leptin receptors are expressed by various brain and peripheral cell types. leptin levels influence satiety, appetite and triggers behaviours which save energy. When leptin levels are high, the brain interprets that energy reserves are high, whereas low leptin levels means that energy reserves are low, in the process adapting the organism to starvation through a variety of metabolic, neurobiochemical, endocrine and behavioral change.

    • Protein content

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

    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 Super Antagonist Ovine
  • View Data Sheet

    Name :

    IL6 Mouse

    Description:

    Interleukin-6 Mouse Recombinant

    IFN-b2, B cell differentiation factor (BCDF), BSF-2, HPGF, HSF, MGI-2, IL-6, Interleukin HP-1, B-cell hybridoma growth factor.

    Product # :

    CYT-350

    Price :

    Quantity :

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    • Citations

    Description

    Interleukin-6 Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 187 amino acids and having a molecular mass of 21709 Dalton. The IL-6 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Lyophilized from a 0.2µm filtered concentrated solution in PBS, 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 the dose-dependant stimulation of the proliferation of IL-6-dependent murine 7TD1 cells is < 0.02 ng/ml, corresponding to a specific activity of > 50,000,000 units/mg.

    Citations

    More Info

    • Introduction

      Interleukin-6 is a potent pro-inflammatory cytokine primarily produced by activated T cells and an assortment of other cells including endothelial cells and macrophages. IL-6 affects B and T lymphocytes and has been shown to have a role in host defense, acute phase reactions, immune responses and hematopoiesis.

    • Synonyms

      IFN-b2, B cell differentiation factor (BCDF), BSF-2, HPGF, HSF, MGI-2, IL-6, Interleukin HP-1, B-cell hybridoma growth factor.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized Interleukin-6 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IL6 should be stored at 4°C between 2-7 days and for future use below -18°C.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.

    • Solubility

      It is recommended to reconstitute the lyophilized Mouse Il-6 in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      FPTSQVRRGD FTEDTTPNRP VYTTSQVGGL ITHVLWEIVE MRKELCNGNS DCMNNDDALA ENNLKLPEIQ RNDGCYQTGY NQEICLLKIS SGLLEYHSYL EYMKNNLKDN KKDKARVLQR DTETLIHIFN QEVKDLHKIV LPTPISNALL TDKLESQKEW LRTKTIQFIL KSLEEFLKVT LRSTRQT.

    • Background

      Research Paper on Interleukin-6 Mouse Recombinant

      Abstract:

      Interleukin-6 (IL-6) Mouse Recombinant stands at the forefront of immunological exploration, unraveling the intricacies of immune modulation. This research paper delves into its molecular attributes and implications within the realm of immunological studies. By examining its functions, synonyms like DIF, TNFA, and TNFSF2, and potential applications, we gain insights into its pivotal role in shaping immune responses.

      Introduction:

      IL-6 Mouse Recombinant has emerged as a linchpin in immunological research. This paper seeks to comprehensively elucidate its molecular characteristics and the impact it bears on immune mechanisms.

      Molecular Architecture and Insights:

      Delving into the molecular makeup of IL-6 Mouse Recombinant, we unveil its crucial role in immune signaling. Its interactions and functions contribute significantly to orchestrating immune responses.

      Navigating Immune Dynamics:

      The well-established influence of IL-6 on immune cell activation and inflammation is a cornerstone. IL-6 Mouse Recombinant allows for a more intricate exploration of these immune processes, augmenting our understanding of cytokine-mediated functions.

      Synonyms and Network Connections:

      Understanding the synonyms associated with IL-6, such as DIF, TNFA, and TNFSF2, amplifies our grasp of immune signaling networks. IL-6 Mouse Recombinant aids in unraveling the complexity of these interconnected pathways.

      Potential Applications in Research and Beyond:

      Beyond the confines of research, IL-6 Mouse Recombinant holds promise in deciphering immune-related diseases. Its significance extends to potential therapeutic interventions and diagnostic applications.

      Clinical Implications and Future Prospects:

      The clinical relevance of IL-6 Mouse Recombinant is underscored by its role in diseases characterized by altered IL-6 signaling. Unearthing its therapeutic potential paves the way for innovative strategies in disease management.

      Conclusion:

      Within the realm of immunology, IL-6 Mouse Recombinant assumes a pivotal role. Its molecular insights, fundamental functions, and potential applications position it as a cornerstone in advancing our comprehension of immune regulation.

      What is the molecular weight/Mw of IL6 MOUSE Protein?
      IL6 MOUSE Protein has a total Mw of 21.7kDa.

      What is the source or expression system of IL6 MOUSE Protein?
      Escherichia Coli.

      What is the Purity of IL6 MOUSE Protein?
      IL6 MOUSE Protein is >96% pure as determined by SDS-PAGE.

      What is the Biological Activity of IL6 MOUSE Protein?
      The ED50 as determined by the dose-dependant stimulation of the proliferation of IL-6-dependent murine 7TD1 cells is < 0.02 ng/ml, corresponding to a specific activity of > 50,000,000 units/mg.

      What is the amino acid sequence of IL6 MOUSE Protein?
      FPTSQVRRGD FTEDTTPNRP VYTTSQVGGL ITHVLWEIVE MRKELCNGNS DCMNNDDALA ENNLKLPEIQ RNDGCYQTGY NQEICLLKIS SGLLEYHSYL EYMKNNLKDN KKDKARVLQR DTETLIHIFN QEVKDLHKIV LPTPISNALL TDKLESQKEW LRTKTIQFIL KSLEEFLKVT LRSTRQT.

      What applications can IL6 MOUSE Protein be used in?
      IL6 MOUSE Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for IL6 MOUSE Protein?
      The endotoxin level is minimal, IL6 MOUSE Protein was purified using conventional chromatography techniques.

      Who supplies recombinant IL6 MOUSE 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 IL6 MOUSE?
      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.

    Il 6 Mouse
  • View Data Sheet

    Name :

    CCL17 Mouse

    Description:

    Thymus and Activation Regulated Chemokine (CCL17) Mouse Recombinant

    C-C motif chemokine 17, Small-inducible cytokine A17, Thymus and activation-regulated chemokine, CC chemokine TARC, ABCD-2, CCL17, CCL-17, SCYA17, TARC, A-152E5.3, MGC138271, MGC138273.

    Product # :

    CHM-270

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    Description

    TARC Mouse Recombinant produced in E.Coli is a non-glycosylated, Polypeptide chain containing 70 amino acids and having a molecular mass of 7.9kDa. The TARC Mouse is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The protein was lyophilized from a 0.2µm filtered concentrated solution in 1×PBS, pH7.4.

    Purity

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

    Biological Activity

    The ED50 as determined by its ability to chemoattract BaF3 mouse pro-B cells transfected with human CCR4 is typically 2-10 ng/ml.

    Citations

    More Info

    • Introduction

      TARC cDNA encodes a 94 amino acid precursor protein with a 23 amino acid residue signal peptide that is cleaved off to generate the 71 amino acid residue mature secreted protein. Along with CC chemokine family members, CCL-17 has approximately 24-29% amino acid sequence identity with RANTES, MIP-1a, MIP-1b, MCP-1, MCP-2, MCP-3 and I-309. TARC is expressed in thymus, and at a lower level in the lung, colon, and small intestine. TARC is in addition transiently expressed in stimulated peripheral blood mononuclear cells. Recombinant TARC has been shown to be chemotactic for T cell lines but not monocytes or neutrophils. CCL-17 was recently identified to be a specific functional ligand for CCR4, a receptor that is selectively expressed on T cells. CCL17 is one of quite a few Cys-Cys (CC) cytokine genes clustered on the q arm of chromosome 16. CCL17 shows chemotactic activity for T lymphocytes, but not monocytes or granulocytes. CCL17 binds to chemokine receptors CCR4 and CCR8. This chemokine plays important roles in T cell development in thymus as well as in trafficking and activation of mature T cells.

    • Synonyms

      C-C motif chemokine 17, Small-inducible cytokine A17, Thymus and activation-regulated chemokine, CC chemokine TARC, ABCD-2, CCL17, CCL-17, SCYA17, TARC, A-152E5.3, MGC138271, MGC138273.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Amino Acid Sequence

      ARATNVGREC CLDYFKGAIP IRKLVSWYKT SVECSRDAIV FLTVQGKLIC ADPKDKHVKK AIRLVKNPRP.

    • Background

      What is the molecular weight/Mw of CCL17 MOUSE Protein?
      CCL17 MOUSE Protein has a total Mw of 7.9kDa.

      What is the source or expression system of CCL17 MOUSE Protein?
      Escherichia Coli.

      What is the Purity of CCL17 MOUSE Protein?
      CCL17 MOUSE Protein is > 97% pure as determined by SDS-PAGE.

      What is the Biological Activity of CCL17 MOUSE Protein?
      The ED50 as determined by its ability to chemoattract BaF3 mouse pro-B cells transfected with human CCR4 is typically 2-10 ng/ml.

      What is the amino acid sequence of CCL17 MOUSE Protein?
      ARATNVGREC CLDYFKGAIP IRKLVSWYKT SVECSRDAIV FLTVQGKLIC ADPKDKHVKK AIRLVKNPRP.

      What applications can CCL17 MOUSE Protein be used in?
      CCL17 MOUSE Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for CCL17 MOUSE Protein?
      The endotoxin level is minimal, CCL17 MOUSE Protein was purified using conventional chromatography techniques.

      Who supplies recombinant CCL17 MOUSE 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 CCL17 MOUSE?
      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.

    Tarc Mouse
  • View Data Sheet

    Name :

    TCL1A Human

    Description:

    T-cell Leukemia/Lymphoma 1A Human Recombinant

    T-cell leukemia/lymphoma protein 1A, Protein p14 TCL1, Oncogene TCL-1, Oncogene TCL1, TCL1A, TCL1.

    Product # :

    PRO-726

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    Description

    TCL1A Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 114 amino acids (1-114 a.a.) and having a molecular mass of 13.4kDa.The TCL1A is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The TCL1A protein solution contains 50mM Tris-HCl buffer (pH7.5) and 10% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      TCL1A (T-cell leukemia/lymphoma 1A) is a protein with a possible role in intracellular regulation of T cell signaling. TCL1A enhances cell proliferation, stabilizes mitochondrial membrane potential and promotes cell survival. TCL1A is restricted in the T-cell lineage to immature thymocytes and activated peripheral lymphocytes. TCL1A is preferentially expressed early in T and B-lymphocyte differentiation. Chromosomal anomalies activating TCL1A are found in chronic T-cell leukemias (T-CLL).
      TCL1A enhances the phosphorylation and activation of AKT1, AKT2 and AKT3. TCL1A promotes nuclear translocation of AKT1. TCL1A binds to the pleckstrin homology domain of Akt (protein kinase B) family proteins, which facilitates Akt dimerization and activity. By increasing Akt activity, TCL1A can enhance the serine/threonine phosphorylation of major Akt signaling substrates, for example Ikk complex, mTOR, BAD, p70S6 kinase, FOXO transcription factors and GSK3b. These substrates regulate cellular differentiation, growth, survival, and metabolism.

    • Synonyms

      T-cell leukemia/lymphoma protein 1A, Protein p14 TCL1, Oncogene TCL-1, Oncogene TCL1, TCL1A, TCL1.

    • 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

      MAECPTLGEA VTDHPDRLWA WEKFVYLDEK QHAWLPLTIE IKDRLQLRVL LRREDVVLGR PMTPTQIGPS LLPIMWQLYP DGRYRSSDSS FWRLVYHIKI DGVEDMLLEL LPDD.

    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.

    Tcl1A Human
  • View Data Sheet

    Name :

    PF 4 Protein

    Description:

    Platelet Factor-4 Human (CXCL4)

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

    Product # :

    CHM-234

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    Description

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

    Source

    Human Platelets.

    Formulation

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

    Purity

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

    Citations

    More Info

    • Introduction

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

    • Synonyms

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

    • Physical Appearance

      Sterile Filtered white lyophilized powder.

    • Stability

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

    • Solubility

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

    • Amino Acid Sequence

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

    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.

    Pf 4 Human
  • View Data Sheet

    Name :

    TFF1 Human

    Description:

    Trefoil Factor-1 Human Recombinant

    TFF-1, TFF1, pS2, BCEI, HPS, HP1.A, pNR-2, D21S21, pS2 protein, Trefoil factor 1, Breast cancer estrogen-inducible protein.

    Product # :

    CYT-586

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    Description

    TFF-1 Human Recombinant produced in E.Coli is a homodimer, non-glycosylated, polypeptide chain containing 2 x 60 amino acids which includes a 40 amino acid trefoil motif containing 3 conserved intramolecular disulfide bonds and having a total molecular mass of 13.2 kDa. TFF-1 Human Recombinant is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The Human TFF1 protein was lyophilized from a 0.2µm filtered concentrated solution in 20mM PB, pH 7.4 and 150mM NaCl.

    Purity

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

    Biological Activity

    The ED50 as determined by a chemotaxis bioassay using human MCF-7 cells is less than 10µg/ml, corresponding to a specific activity of >100 IU/mg.

    Citations

    More Info

    • Introduction

      The Trefoil Factor peptides (TFF1, TFF2 and TFF3) are stable secretory proteins expressed in the gastrointestinal tract (gastric mucosa), and are involved in intestinal mucosal defense and repair. TFF1 is an essential protein for normal differentiation of the antral and pyloric gastric mucosa and functions as a gastric-specific tumor suppressor gene. TFF1 is a stabilizer of the mucous gel overlying the gastrointestinal mucosa that provides a physical barrier against various noxious agents. TFF1 protects the mucosa from isults, stabilizes the mucus layer, & affects healing of the epithelium. TFF1 is commonly expressed in tumors. TFF1 is related with the cell membrane of MCF-7 cells. High levels of TFF1 and TFF2 are found in serum from inflammatory bowel disease.

    • Synonyms

      TFF-1, TFF1, pS2, BCEI, HPS, HP1.A, pNR-2, D21S21, pS2 protein, Trefoil factor 1, Breast cancer estrogen-inducible protein.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized TFF1 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution TFF1 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 TFF1 in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      EAQTETCTVAPRERQNCGFPGVTPSQCANKGCCFDDTVRGVPWCFY
      PNTIDVPPEEECEF.

    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.

    Tff1 Human
  • View Data Sheet

    Name :

    CANX Human

    Description:

    Calnexin Human Recombinant

    Calnexin, Major histocompatibility complex class I antigen-binding protein p88, p90, IP90, CANX, CNX, FLJ26570.

    Product # :

    PRO-725

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    Description

    CANX Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 462 amino acids (21-481 a.a.) and having a molecular mass of 52.5kDa.The CANX is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The CANX protein solution contains 20mM Tris-HCl buffer (pH8.0), 1mM DTT and 20% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      Calnexin (CANX) belongs to the calnexin family of molecular chaperones. Calnexin is a calcium-binding, ER-associated protein that interacts briefly with newly synthesized N-linked glycoproteins, facilitating protein folding and assembly. Calnexin may also have a key role in the quality control of protein folding by retaining incorrectly folded protein subunits within the ER for degradation. Calnexin grants long-term protection of wild-type Shaker protein from ER-associated degradation. Polypeptide substrate recognition by Calnexin requires specific conformations of the Calnexin protein. Calnexin dwindles with aging and might contribute to a cytoprotection in an array of human age-related diseases.

    • Synonyms

      Calnexin, Major histocompatibility complex class I antigen-binding protein p88, p90, IP90, CANX, CNX, FLJ26570.

    • 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

      MHDGHDDDVI DIEDDLDDVI EEVEDSKPDT TAPPSSPKVT YKAPVPTGEV YFADSFDRGT LSGWILSKAK KDDTDDEIAK YDGKWEVEEM KESKLPGDKG LVLMSRAKHH AISAKLNKPF LFDTKPLIVQ YEVNFQNGIE CGGAYVKLLS KTPELNLDQF HDKTPYTIMF GPDKCGEDYK LHFIFRHKNP KTGIYEEKHA KRPDADLKTY FTDKKTHLYT LILNPDNSFE ILVDQSVVNS GNLLNDMTPP VNPSREIEDP EDRKPEDWDE RPKIPDPEAV KPDDWDEDAP AKIPDEEATK PEGWLDDEPE YVPDPDAEKP EDWDEDMDGE WEAPQIANPR CESAPGCGVW QRPVIDNPNY KGKWKPPMID NPSYQGIWKP RKIPNPDFFE DLEPFRMTPF SAIGLELWSM TSDIFFDNFI ICADRRIVDD WANDGWGLKK AADGAAEPGV VGQMIEAAEE RP.

    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.

    Canx Human
  • View Data Sheet

    Name :

    CAPS Human

    Description:

    Calcyphosine Human Recombinant

    Calcyphosin, Calcyphosine, CAPS, CAPS1, MGC126562.

    Product # :

    PRO-117

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    Description

    CAPS Human Recombinant fused with a 20 amino acid His tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 209 amino acids (1-189 a.a.) and having a molecular mass of 23.1kDa. The CAPS is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The CAPS solution (1 mg/ml) contains 20mM Tris-HCl buffer (pH8.0), 10% glycerol, 2mM DTT and 100mM NaCl.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      Calcyphosine (CAPS) is a calcium-binding protein containing four EF-hand domains. CAPS protein was originally identified as thyroid protein p24 which is found in a number of epithelium and in some cells of the central nervous system. CAPS may have a role in the regulation of ion transport. In the thyroid follicular cells, CAPS is synthesized and phosphorylated in response to stimulation by thyrotropin and cAMP agonists.

    • Synonyms

      Calcyphosin, Calcyphosine, CAPS, CAPS1, MGC126562.

    • 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 MDAVDATMEK LRAQCLSRGA SGIQGLARFF RQLDRDGSRS LDADEFRQGL AKLGLVLDQA EAEGVCRKWD RNGSGTLDLE EFLRALRPPM SQAREAVIAA AFAKLDRSGD GVVTVDDLRG VYSGRAHPKV RSGEWTEDEV LRRFLDNFDS SEKDGQVTLA EFQDYYSGVS ASMNTDEEFV AMMTSAWQL.

    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.

    Caps Human
  • View Data Sheet

    Name :

    Flt3 Ligand Porcine

    Description:

    Flt3 Ligand Porcine Recombinant

    Fms-related tyrosine kinase 3 ligand, FLK2, STK1, CD135, Stem Cell Tyrosine Kinase 1, FLT3LG, Flt3.

    Product # :

    CYT-1041

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    Description

    Flt3-Ligand Porcine Recombinant produced in E.Coli is a non-glycosylated, polypeptide chain containing 155 amino acids and having a molecular mass of approximately 17.3kDa. Flt3-Ligand is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The protein is lyophilized with 10mM Sodium Phosphate pH-7.5.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      FLT3 ligand is a receptor for the fl cytokine has a tyrosine-protein kinase activity & a growth factor that regulates proliferation of early hematopoietic cells. Flt3-Ligand synergizes with other CSFs and interleukins to induce growth and differentiation.

    • Synonyms

      Fms-related tyrosine kinase 3 ligand, FLK2, STK1, CD135, Stem Cell Tyrosine Kinase 1, FLT3LG, Flt3.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized Porcine Flt3-Ligand although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Flt3-Ligand 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 Flt3-L in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      MSPDCSFPHS PISSTFANTI RQLSDYLLQD YPVTVASNLQ DDELCGAFWR LVLAQRWMGQ LKTVAGSQMQ KLLEAVNTEI VFVTSCALQP LPSCLRFVQA NISHLLQDTS QQLVALKPWI TRRNFSRCLE LQCQPDPSTL LPPRSPGALE ATSLP.

    • Background

      What is the molecular weight/Mw of FLT3 LIGAND PORCINE Protein?
      FLT3 LIGAND PORCINE Protein has a total Mw of 17.3kDa.

      What is the source or expression system of FLT3 LIGAND PORCINE Protein?
      Escherichia Coli.

      What is the Purity of FLT3 LIGAND PORCINE Protein?
      FLT3 LIGAND PORCINE Protein is >95% pure as determined by SDS-PAGE.

      What is the Biological Activity of FLT3 LIGAND PORCINE Protein?
      The biological functionality of FLT3 LIGAND PORCINE Protein will be determined in the future.

      What is the amino acid sequence of FLT3 LIGAND PORCINE Protein?
      MSPDCSFPHS PISSTFANTI RQLSDYLLQD YPVTVASNLQ DDELCGAFWR LVLAQRWMGQ LKTVAGSQMQ KLLEAVNTEI VFVTSCALQP LPSCLRFVQA NISHLLQDTS QQLVALKPWI TRRNFSRCLE LQCQPDPSTL LPPRSPGALE ATSLP.

      What applications can FLT3 LIGAND PORCINE Protein be used in?
      FLT3 LIGAND PORCINE Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for FLT3 LIGAND PORCINE Protein?
      The endotoxin level is minimal, FLT3 LIGAND PORCINE 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.

    Flt3 Ligand Porcine
  • View Data Sheet

    Name :

    PIN4 Human

    Description:

    Peptidyl-Prolyl Cis/Trans Isomerase NIMA-Interacting 4 Human Recombinant

    Peptidyl-prolyl cis-trans isomerase NIMA-interacting 4, Parvulin-14, Par14, hPar14, Parvulin-17, Par17, hPar17, Peptidyl-prolyl cis-trans isomerase Pin4, PPIase Pin4, Peptidyl-prolyl cis/trans isomerase EPVH, hEPVH, Rotamase Pin4, PIN4, EPVH, MGC138486.

    Product # :

    ENZ-106

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    Description

    PIN4 produced in E.Coli is a single, non-glycosylated polypeptide chain containing 176 amino acids (1-156 a.a.) and having a molecular mass of 18.8kDa.PIN4 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    PIN4 solution (1mg/ml) containing 20mM Tris-HCl buffer (pH8.0), 10% glycerol, 1mM DTT and 0.1mM PMSF.

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

    Biological Activity

    Specific activity is > 300 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

      Peptidyl-prolyl cis-trans isomerase NIMA-interacting 4 (PIN4) is a peptidyl-prolyl cis/trans isomerase (PPIase) which interacts with NIMA and is vital for cell cycle regulation. PIN4 has 2 different isoforms: PAR14 and PAR17. Furthermore, Pin4 protein binds to double-stranded DNA under physiological salt conditions.

    • Synonyms

      Peptidyl-prolyl cis-trans isomerase NIMA-interacting 4, Parvulin-14, Par14, hPar14, Parvulin-17, Par17, hPar17, Peptidyl-prolyl cis-trans isomerase Pin4, PPIase Pin4, Peptidyl-prolyl cis/trans isomerase EPVH, hEPVH, Rotamase Pin4, PIN4, EPVH, MGC138486.

    • 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 MPMAGLLKGL VRQLERFSVQ QQASKMPPKG KSGSGKAGKG GAASGSDSAD KKAQGPKGGG NAVKVRHILC EKHGKIMEAM EKLKSGMRFN EVAAQYSEDK ARQGGDLGWM TRGSMVGPFQ EAAFALPVSG MDKPVFTDPP VKTKFGYHII MVEGRK.

    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.

    Pin4 Human
  • View Data Sheet

    Name :

    KLRK1 Human

    Description:

    Killer Cell lectin-Like Receptor Subfamily K, Member 1 Human Recombinant

    CD314, D12S2489E, KLR, NKG2-D, NKG2D, Killer cell lectin-like receptor subfamily K member 1, NK cell receptor D, NKG2-D-activating NK receptor, CD314.

    Product # :

    PRO-1290

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    Description

    KLRK1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 168 amino acids (73-216 a.a.) and having a molecular mass of 19.2kDa. KLRK1 is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    KLRK1 protein solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH8.0), 10% glycerol and 0.4M Urea.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      Killer Cell lectin-Like Receptor Subfamily K, Member 1 (KLRK1) is an activating receptor which has recently generated considerable interest. The most fascinating of these, are a couple of closely related proteins known as MICA and MICB. These are cell-surface molecules distantly related to MHC class I proteins, and their genes have elements of heat shock promoters. Thus, MICA and MICB are expressed in the course of cell stress and are up-regulated in tumor cells and during viral infections. This receptor-ligand combination has a crucial role in the immune response to various pathologies.

    • Synonyms

      CD314, D12S2489E, KLR, NKG2-D, NKG2D, Killer cell lectin-like receptor subfamily K member 1, NK cell receptor D, NKG2-D-activating NK receptor, CD314.

    • 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 MGSMIWSAVF LNSLFNQEVQ IPLTESYCGP CPKNWICYKN NCYQFFDESK NWYESQASCM SQNASLLKVY SKEDQDLLKL VKSYHWMGLV HIPTNGSWQW EDGSILSPNL LTIIEMQKGD CALYASSFKG YIENCSTPNT YICMQRTV.

    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.

    Klrk1 Human
  • View Data Sheet

    Name :

    CDK16 Human

    Description:

    Cyclin-dependent kinase 16 Human Recombinant

    Cyclin-Dependent Kinase 16, PCTK1, Serine/Threonine-Protein Kinase,  Serine/Threonine-Protein Kinase PCTAIRE-1, Cell Division Protein Kinase 16, PCTAIRE Protein Kinase 1, PCTAIRE, PCTGAIRE, EC 2.7.11.22, EC 2.7.11, PCTAIRE-Motif Protein Kinase 1, PCTAIRE1.

    Product # :

    PKA-324

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    Description

    CDK16 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 362 amino acids (158-496aa) and having a molecular mass of 41.1kDa.CDK16 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    CDK16 protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.1M NaCl and 10% glycerol.

    Purity

    Greater than 95% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      CDK16 is a member of the CDK family of serine/threonine protein kinases which are known to regulate the cell cycle. These proteins have a core kinase domain flanked by unique amino- and carboxy- terminal domains. CDK16, which is expressed mainly in mammalian brain, cooperates with an assortment of proteins, and is a part of a multiple signal transduction cascade.

    • Synonyms

      Cyclin-Dependent Kinase 16, PCTK1, Serine/Threonine-Protein Kinase, Serine/Threonine-Protein Kinase PCTAIRE-1, Cell Division Protein Kinase 16, PCTAIRE Protein Kinase 1, PCTAIRE, PCTGAIRE, EC 2.7.11.22, EC 2.7.11, PCTAIRE-Motif Protein Kinase 1, PCTAIRE1.

    • 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 MGSGFGKLET YIKLDKLGEG TYATVYKGKS KLTDNLVALK EIRLEHEEGA PCTAIREVSL LKDLKHANIV TLHDIIHTEK SLTLVFEYLD KDLKQYLDDC GNIINMHNVK LFLFQLLRGL AYCHRQKVLH RDLKPQNLLI NERGELKLAD FGLARAKSIP TKTYSNEVVT LWYRPPDILL GSTDYSTQID MWGVGCIFYE MATGRPLFPG STVEEQLHFI FRILGTPTEE TWPGILSNEE FKTYNYPKYR AEALLSHAPR LDSDGADLLT KLLQFEGRNR ISAEDAMKHP FFLSLGERIH KLPDTTSIFA LKEIQLQKEA SLRSSSMPDS GRPAFRVVDT EF

    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.

    Cdk16 Human
  • View Data Sheet

    Name :

    TrxR Yeast

    Description:

    Thioredoxin Reductase (NADPH) Yeast Recombinant

    Thioredoxin Reductase (NADPH), NTR, TrxR.

    Product # :

    ENZ-278

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    Description

    Thioredoxin Reductase (NADPH) Yeast Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain having a molecular mass of 36 kDa. Thioredoxin Reductase is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Each mg of protein contains 20mM phosphate buffer pH 7.4.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Biological Activity

    The specific activity was found to be 5.8 IU/mg.

    Citations

    More Info

    • Introduction

      Thioredoxin reductase (TrxR/NTR), an enzyme belonging to the flavoprotein family of pyridine nucleotide-disulfide oxidoreductases. Thioredoxin reductase (TrxR), a component of the thioredoxin system, including thioredoxin (Trx) and NADPH, catalyzes the transfer of electrons from NADPH to Trx, acts as a reductant of disulfide-containing proteins and participates in the defense system against oxidative stresses.

    • Synonyms

      Thioredoxin Reductase (NADPH), NTR, TrxR.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      NTR although stable at 4°C for 3 weeks, should be stored desiccated below -18°C. Please prevent freeze thaw cycles.

    • Solubility

      It is recommended to reconstitute the lyophilized NTR in sterile 18MΩ-cm H2O.

    • Unit Definition

      One unit equals the change in absorbance at 412 nm per minute at 25°C using 0.2mM NADPH containing 5mM DTNB (pH 7.0).

    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 Reductase Yeast
  • View Data Sheet

    Name :

    CFL2 Human

    Description:

    Cofilin-2 Human Recombinant

    Cofilin-2, Cofilin- muscle isoform, CFL2, NEM7.

    Product # :

    PRO-912

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    Description

    CFL2 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 186 amino acids (1-166 a.a.) and having a molecular mass of 20.9kDa.CFL2 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    CFL2 protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 2mM DTT, 10% glycerol and 50mM NaCl.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      CFL2 protein is a member of the actin-binding proteins ADF family which contains 1 ADF-H domain. Cofilin is a broadly distributed intracellular actin-modulating protein which binds and depolymerizes filamentous F-actin and inhibits the polymerization of monomeric G-actin in a pH-dependent manner. Defects in the CFL2 gene are the cause of nemaline myopathy type 7 (NEM7).

    • Synonyms

      Cofilin-2, Cofilin- muscle isoform, CFL2, NEM7.

    • 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 MASGVTVNDE VIKVFNDMKV RKSSTQEEIK KRKKAVLFCL SDDKRQIIVE EAKQILVGDI GDTVEDPYTS FVKLLPLNDC RYALYDATYE TKESKKEDLV FIFWAPESAP LKSKMIYASS KDAIKKKFTG IKHEWQVNGL DDIKDRSTLG EKLGGNVVVS LEGKPL.

    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.

    Cfl2 Human
  • View Data Sheet

    Name :

    LHRH Protein

    Description:

    Luteinizing Hormone Releasing Hormone Human Recombinant

    LHRH, GRH, GNRH, LNRH.

    Product # :

    HOR-268

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    Description

    LHRH Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 92 amino acids (24-92 a.a.) and having a molecular mass of 10.3kDa.LHRH is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

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

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      GNRH1 also known as Luteinising-hormone releasing hormone (LHRH), is a peptide hormone responsible for the release of FSH and LH from the anterior pituitary. GNRH1 is synthesized and released by the hypothalamus.
      At the pituitary, GNRH1 stimulates the synthesis and secretion of the follicle-stimulating hormone (FSH) and luteinizing hormone (LH). These processes are controlled by the size and frequency of GNRH1 pulses, as well as by feedback from androgens and estrogens. Low requency GNRH1 pulses lead to FSH release, whereas high frequency GNRH1 pulses stimulate LH release.
      There are differences in GNRH1 secretion between males and females. In males, GNRH1 is secreted in pulses at a constant frequency, but in females the frequency of the pulses varies during the menstrual cycle and there is a large surge of GNRH1 just before ovulation.
      GNRH1 secretion is pulsatile in all vertebrates, and is necessary for correct reproductive function. Thus, a single hormone, GNRH1, controls a complex process of follicular growth, ovulation, and corpus luteum maintenance in the female, and spermatogenesis in the male.

    • Synonyms

      LHRH, GRH, GNRH, LNRH.

    • 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 MGSQHWSYGL RPGGKRDAEN LIDSFQEIVK EVGQLAETQR FECTTHQPRS PLRDLKGALE SLIEEETGQK KI.

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    Lhrh Human Recombinant
  • View Data Sheet

    Name :

    UBE2L3 Human His

    Description:

    Ubiquitin-Conjugating Enzyme E2L 3 Human Recombinant, His Tag

    Ubiquitin-conjugating enzyme E2 L3, EC 6.3.2.19, Ubiquitin-protein ligase L3,Ubiquitin carrier protein L3, UbcH7, E2-F1, L-UBC, UbcM4.

    Product # :

    ENZ-344

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    Description

    Ubiquitin-Conjugating Enzyme E2L 3 Human Recombinant produced in E.coli is an 18.9 kDa protein containing 162 amino acids.The UBE2L3 protein contains 6xHis tag and is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Lyophilized from a 0.2μm filtered concentrated (1 mg/ml) solution in 1X PBS and 1mM DTT, pH 7.5.

    Purity

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

    Citations

    More Info

    • Introduction

      Human Ubquitin Conjugating Enzyme 7 (UbcH7) is a class I enzyme which functions in the stress response and the control of transcription factors. The enzyme is ubiquitously expressed with high levels of expression seen in adult muscle. UbcH7 mediates the selective degradation of short-lived and abnormal proteins and is highly homologous to UbcH5. It has been demonstrated to participate in the ubiquitinylation of p53, c-Fos and NF-?B. UbcH7 is one of two E2s (UbcH5 being the other) with which HECT domain proteins interact with UbcH7 being able to efficiently substitute for UbcH5 in E6-AP-dependent ubiquitinylation.

    • Synonyms

      Ubiquitin-conjugating enzyme E2 L3, EC 6.3.2.19, Ubiquitin-protein ligase L3,Ubiquitin carrier protein L3, UbcH7, E2-F1, L-UBC, UbcM4.

    • Physical Appearance

      Sterile Filtered white lyophilized powder.

    • Stability

      Lyophilized UBE2L3 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution UBE2L3 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 UBE2L3 in sterile water not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      MHHHHHHAMAASRRLMKELEEIRKCGMKNFRNIQVDEANLLTWQGLIVP
      DNPPYDKGAFRIEINFPAEYPFKPPKITFKTKIYHPNIDEKGQVCLPVISAEN
      WKPATKTDQVIQSLIALVNDPQPEHPLRADLAEEYSKDRKKFCKNAEEFT
      KKYGEKRPVD.

    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.

    Ube2L3 Human His
  • View Data Sheet

    Name :

    CHMP2B Human

    Description:

    Chromatin Modifying Protein 2B Human Recombinant

    Chromatin modifying protein 2B, CHMP2.5, VPS2B, Vacuolar protein sorting-associated protein 2-2, hVps2-2, DMT1, DKFZp564O123, VPS2 homolog B.

    Product # :

    PRO-877

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    Description

    CHMP2B Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 233 amino acids (1-213) and having a molecular mass of 26.1 kDa.The CHMP2B is fused to a 20 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    CHMP2B protein 1mg/ml is supplied in 20mM Tris-HCL, pH-8, 0.1M NaCl, 2mM DTT and 20% Glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      CHMP2B is a member of the vacuolar sorting protein family. CHMP2B is a component of the ESCRT-III complex which is essential for sorting endosomal articles into multivesicular bodies (MVBs), and are also obligatory for the formation of these bodies. CHMP2B is usually found in brain, heart, skeletal muscle, small intestine, pancreas, lung, placenta and leukocytes.

    • Synonyms

      Chromatin modifying protein 2B, CHMP2.5, VPS2B, Vacuolar protein sorting-associated protein 2-2, hVps2-2, DMT1, DKFZp564O123, VPS2 homolog B.

    • 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 MASLFKKKTV DDVIKEQNRE LRGTQRAIIR DRAALEKQEK QLELEIKKMA KIGNKEACKV LAKQLVHLRK QKTRTFAVSS KVTSMSTQTK VMNSQMKMAG AMSTTAKTMQ AVNKKMDPQK TLQTMQNFQK ENMKMEMTEE MINDTLDDIF DGSDDEEESQ DIVNQVLDEI GIEISGKMAK APSAARSLPS ASTSKATISD EEIERQLKAL GVD

    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.

    Chmp2B Human
  • View Data Sheet

    Name :

    CLEC1B Human

    Description:

    C-type Lectin Domain Family 1, Member B Human Recombinant

    C-Type Lectin Domain Family 1, Member B, CLEC2, C-Type Lectin-Like Receptor 2, CLEC2B, CLEC-2, C-Type Lectin Domain Family 1 Member B, C-Type Lectin-Like Receptor-2, 1810061I13Rik, PRO1384, QDED721, C-type lectin domain family 1 member B, C-type lectin-like receptor 2.

    Product # :

    PRO-2185

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    Description

    CLEC1B Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 198 amino acids (55-229 a.a) and having a molecular mass of 23.1kDa. CLEC1B is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    CLEC1B protein solution (1mg/ml) containing 20mM Tris, PH 8.0 and 10% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      C-type Lectin Domain Family 1 Member B, also known as CLEC1B. NK-Natural killer cells express multiple calcium-dependent (C-type) lectin-like receptors, for instance CD94 (KLRD1; MIM 602894) and NKG2D (KLRC4; MIM 602893), which interact with major histocompatibility complex class I molecules and either inhibit or else activate cytotoxicity and cytokine secretion. CLEC1B is a C-type lectin-like receptor which is expressed in myeloid cells as well as in NK cells.

    • Synonyms

      C-Type Lectin Domain Family 1, Member B, CLEC2, C-Type Lectin-Like Receptor 2, CLEC2B, CLEC-2, C-Type Lectin Domain Family 1 Member B, C-Type Lectin-Like Receptor-2, 1810061I13Rik, PRO1384, QDED721, C-type lectin domain family 1 member B, C-type lectin-like receptor 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 MGSSVMQRNY LQGENENRTG TLQQLAKRFC QYVVKQSELK GTFKGHKCSP CDTNWRYYGD SCYGFFRHNL TWEESKQYCT DMNATLLKID NRNIVEYIKA RTHLIRWVGL SRQKSNEVWK WEDGSVISEN MFEFLEDGKG NMNCAYFHNG KMHPTFCENK HYLMCERKAG MTKVDQLP.

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    Clec1B Human
  • View Data Sheet

    Name :

    GSS Human

    Description:

    Glutathione Synthetase Human Recombinant

    Glutathione synthetase, GSH synthetase, GSH-S, Glutathione synthase, GSHS, MGC14098, GSS.

    Product # :

    ENZ-021

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    Description

    GSS Human Recombinant fused with a 20 amino acid His tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 494 amino acids (1-474 a.a.) and having a molecular mass of 54.5kDa. The GSS is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

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

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      Glutathione synthetase (GSS) is the second enzyme in the glutathione biosynthesis pathway. GSS catalyses the condensation of gamma-glutamylcysteine and glycine to form glutathione. Defects in the GSS are the cause of glutathione synthetase deficiency aka GSS deficiency or 5-oxoprolinuria or pyroglutamic aciduria, which is a severe form characterized by an increased rate of hemolysis and defective function of the central nervous system.

    • Synonyms

      Glutathione synthetase, GSH synthetase, GSH-S, Glutathione synthase, GSHS, MGC14098, GSS.

    • 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

      MGSSHHHHQH SSGLVPRGSH MATNWGSLLQ DKQQLEELAR QAVDRALAEG VLLRTSQEPT SSEVVSYAPF TLFPSLVPSA LLEQAYAVQM DFNLLVDAVS QNAAFLEQTL SSTIKQDDFT ARLFDIHKQV LKEGIAQTVF LGLNRSDYMF QRSADGSPAL KQIEINTISA SFGGLASRTP AVHRHVLSVL SKTKEAGKIL SNNPSKGLAL GIAKAWELYG SPNALVLLIA QEKERNIFDQRAIENELLAR NIHVIRRTFE DISEKGSLDQ DRRLFVDGQE IAVVYFRDGY MPRQYSLQNW EARLLLERSH AAKCPDIATQ LAGTKKVQQE LSRPGMLEML LPGQPEAVAR LRATFAGLYS LDVGEEGDQA IAEALAAPSR FVLKPQREGG GNNLYGEEMV QALKQLKDSE ERASYILMEK IEPEPFENCL LRPGSPARVV QCISELGIFG VYVRQEKTLV MNKHVGHLLR TKAIEHADGG VAAGVAVLDN PYPV.

    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.

    Gss Human
  • View Data Sheet

    Name :

    GST, His

    Description:

    Glutathione S-Transferase Recombinant, His Tag

    Glutathione S-Transferase, GST, Glutathione S-transferase class-mu 28 kDa isozyme, GST 28, EC 2.5.1.18, Sj28GST, Sj28 antigen.

    Product # :

    ENZ-451

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    • source
    • formulation
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    • biological activity
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    • Citations

    Description

    Recombinant Schistosoma japonicum GST full length protein contains a total of 244 amino acids (1-218 a.a.) expressed in E.coli, having a molecular mass of 28.3kDa. The GST protein is fused to a 20 amino acids His-Tag at N-terminus. The GST protein is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    GST is supplied in PBS pH 7.4 & 10% glycerol.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    Biological Activity

    >10 units/mg, & is defined as the amount of enzyme that conjugate 1.0 u mole of 1-chloro-2,4-dinitrobenzene (CDNB) with reduced glutathione per minute at pH-6.5 at 25C.

    Citations

    More Info

    • Introduction

      Antioxidant enzyme Glutathione S- Transferase (GST) is thought to do the primary cellular defense mechanism against reactive oxygen species. GST reduces lipid hydroperoxides through its Se-independent glutathione peroxidase activity. The enzyme also detoxifies lipid peroxidation end products such as 4-hydroxynonenal (4-HNE).
      The soluble GST is a 26 kDa protein which occurs as a dimer in all aerobic organisms. Each monomer has two domains, one that binds GSH and is an /-structure similar to thioredoxin and the other, all helical, that binds the hydrophobic substrate. The GST -fusion protein expression system is a widely used recombinant protein expression system that allows a peptide or a regulatory protein domain to be expressed as a fusion to the C-terminus of Schistosoma japonicum GST. Fusion proteins also possess GST -enzymatic activity and can undergo dimerization similar to in vivo. The fusion protein can be purified via GST -affinity column chromatography. In most cases, the desired peptides or domains are removed from GST by applying a specific protease that recognizes and cleaves the linker between the protein domain and GST. The technique has been widely used to generate different kinds of proteins for crystallization, molecular immunology studies, the production of vaccines and studies involving protein-protein and protein-DNA interactions.

    • Synonyms

      Glutathione S-Transferase, GST, Glutathione S-transferase class-mu 28 kDa isozyme, GST 28, EC 2.5.1.18, Sj28GST, Sj28 antigen.

    • 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 MSPILGYWKI KGLVQPTRLL LEYLEEKYEE HLYERDEGDK WRNKKFELGL EFPNLPYYID GDVKLTQSMAIIRYIADKHN MLGGCPKERA EISMLEGAVL DIRYGVSRIA YSKDFETLKV DFLSKLPEML KMFEDRLCHK TYLNGDHVTH PDFMLYDALDVVLYMDPMCL DAFPKLVCFK KRIEAIPQID KYLKSSKYIA WPLQGWQATF GGGDHPPKSD LVPR.

    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.

    Glutathione S Transferase His
  • View Data Sheet

    Name :

    GYG1 Human

    Description:

    Glycogenin-1 Human Recombinant

    Glycogenin-1, GYG1, GYG.

    Product # :

    ENZ-431

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    Description

    GYG1 Human Recombinant fused with a 32 amino acid His-T7 tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 365 amino acids (1-333 a.a.) and having a molecular mass of 41.2kDa.The GYG1 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The GYG1 solution contains 20mM Tris-HCl buffer (pH 8.0), 1mM DTT and 10% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      Glycogenin-1 (GYG1) is an enzyme involved in glycogen biosynthesis. GYG1 is the chief enzyme involved in glycogen polymerisation. Glycogenin-1 is vital for the function of self-glucosylates, using an inter-subunit mechanism, to form an oligosaccharide primer which acts as substrate for glycogen synthase. In addition, GYG1 has a role in regulating glycogen metabolism and the achievement of maximal glycogen levels in skeletal muscle. GYG1 mRNA and protein content and activity increase in the muscle during recovery from prolonged and exhaustive exercise. GYG1 is inactivated with glycogen catabolism which concurs with an increase in glycogenin gene expression as exercise and glycogenolysis advance. Glycogenin will remain covalently attached to the reducing end of the glycogen molecule.

    • Synonyms

      Glycogenin-1, GYG1, GYG.

    • 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

      MHHHHHHMAS MTGGQQMGRD LYDDDDKDRW GSMTDQAFVT LTTNDAYAKG ALVLGSSLKQ HRTTRRLVVL ATPQVSDSMR KVLETVFDEV IMVDVLDSGD SAHLTLMKRP ELGVTLTKLH CWSLTQYSKC VFMDADTLVL ANIDDLFDRE ELSAAPDPGW PDCFNSGVFV YQPSVETYNQ LLHLASEQGS FDGGDQGILN TFFSSWATTD IRKHLPFIYN LSSISIYSYL PAFKVFGASA KVVHFLGRVK PWNYTYDPKT KSVKSEAHDP NMTHPEFLIL WWNIFTTNVL PLLQQFGLVK DTCSYVNVED VSGAISHLSL GEIPAMAQPF VSSEERKERW EQGQADYMGA DSFDNIKRKL DTYLQ.

    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.

    Gyg1 Human
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