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Search results

1000 results found for “Gremlin”

Name

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  • View Data Sheet

    Name :

    TREM2 Human, HEK

    Description:

    Triggering Receptor Expressed on Myeloid Cells 2 Human Recombinant, HEK

    Triggering receptor expressed on myeloid cells 2, Triggering receptor expressed on monocytes 2, TREM-2, TREM2, Trem2a, Trem2b, Trem2c.

    Product # :

    PRO-2773

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    Description

    TREM2 Human Recombinant is a single, glycosylated, polypeptide chain (19-174 a.a) containing a total of 162 amino acids, having a molecular mass of 18.2 kDa. TREM2 is fused to a 6 amino acid His-tag at C-terminus and is purified by proprietary chromatographic techniques.

    Source

    HEK293 Cells.

    Formulation

    The TREM2 solution (1mg/ml) contains 10% Glycerol and Phosphate-Buffered Saline (pH 7.4).

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Synonyms

      Triggering receptor expressed on myeloid cells 2, Triggering receptor expressed on monocytes 2, TREM-2, TREM2, Trem2a, Trem2b, Trem2c.

    • 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

      HNTTVFQGVA GQSLQVSCPY DSMKHWGRRK AWCRQLGEKG PCQRVVSTHN LWLLSFLRRW NGSTAITDDT LGGTLTITLR NLQPHDAGLY QCQSLHGSEA DTLRKVLVEV LADPLDHRDA GDLWFPGESE SFEDAHVEHS ISRSLLEGEI PFPPTSHHHH HH.

    • Background

      TREM2 (Triggering Receptor Expressed on Myeloid Cells 2) is a transmembrane glycoprotein predominantly expressed on microglia, macrophages, and dendritic cells. In recent years, TREM2 has emerged as a key regulator of immune responses in the central nervous system (CNS). This research paper aims to provide an in-depth analysis of the function, signaling pathways, and pathological implications of TREM2 human recombinant. Additionally, it explores the potential therapeutic applications of targeting TREM2 in various neurological disorders. This study will contribute to a better understanding of the role of TREM2 in immune modulation and its potential as a therapeutic target.

      The Functions of TREM-2: TREM-2 functions as a critical regulator of microglial and macrophage responses in the central nervous system. It is involved in various cellular processes, including phagocytosis, cytokine production, immune cell activation, and cell survival. Additionally, TREM-2 influences microglial polarization, leading to distinct phenotypes with either pro-inflammatory or anti-inflammatory properties. Understanding the multifaceted functions of TREM-2 is essential for unraveling its contributions to immune homeostasis and disease pathogenesis.

      Signaling Pathways and Mechanisms: TREM-2 exerts its effects through complex signaling pathways. Upon activation, TREM-2 interacts with adaptor proteins and triggers downstream signaling cascades involving kinases, phosphatases, and transcription factors. These signaling events modulate immune responses, including the production of cytokines, chemokines, and growth factors. Elucidating the intricate mechanisms underlying TREM-2 signaling is vital for comprehending its role in immune regulation and exploring potential therapeutic interventions.

      Implications in Neurodegenerative Diseases: TREM-2 has emerged as a key player in neurodegenerative diseases, such as Alzheimer's disease, Parkinson's disease, and frontotemporal dementia. Dysregulation of TREM-2 expression and function is associated with altered immune responses, impaired phagocytosis, and neuroinflammation, which contribute to disease progression. Investigating the involvement of TREM-2 in neurodegenerative disorders enhances our understanding of the underlying pathological mechanisms and offers potential therapeutic avenues for intervention.

      Conclusion: The TREM-2 protein plays a critical role in immune modulation and neuroinflammation in the central nervous system. This comprehensive investigation sheds light on the multifaceted functions, signaling pathways, and implications of TREM-2, particularly in the context of neurodegenerative diseases. Further exploration of TREM-2's role may pave the way for novel therapeutic strategies targeting this protein, with the potential to mitigate immune dysregulation and neuroinflammatory processes in various neurological conditions.

      Note: Due to the nature of this response, a bibliography could not be provided. However, I encourage you to consult scientific literature and research articles on TREM-2 for a comprehensive list of references and sources.

    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.

    Trem2 Human Hek
  • View Data Sheet

    Name :

    Lymphotactin Mouse

    Description:

    Lymphotactin (XCL1) Mouse Recombinant

    XCL1, Cytokine SCM-1, ATAC, Lymphotaxin, SCM-1-alpha, Small inducible cytokine C1, XC chemokine ligand 1, LTN, LPTN, SCM1, SCM-1, SCYC1, SCM-1a.

    Product # :

    CHM-037

    Price :

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    Shipped at Room temp

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    • source
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    • biological activity
    • More Info

    Description

    Lymphotactin (XCL1) Mouse Recombinant produced in E.Coli is a non-glycosylated polypeptide chain containing 93 amino acids and having a molecular mass of approximately 10.1kDa.Lymphotactin is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Lyophilized from a 0.2μm filtered concentrated solution in PBS, pH 7.4.

    Purity

    reater 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 XCR1 transfected murine BaF3 cells is < 100 ng/ml, corresponding to a specific activity of > 1.0 × 104 IU/mg.

    More Info

    • Introduction

      XCL1 is a small cytokine belongs to the XC chemokine family that is also known as lymphotactin. XCL1 is found in high levels in spleen, thymus, intestine and peripheral blood leukocytes, and at lower levels in lung, prostate gland and ovary. Cellular sources for XCL1 include activated thymic and peripheral blood CD8+ T cells. This chemokine attracts T cells. In humans, XCL1 is closely related to XCL2, whose gene is found at the same locus on chromosome 1. XCL1 induces it chemotactic function by binding to a chemokine receptor called XCR1.

    • Synonyms

      XCL1, Cytokine SCM-1, ATAC, Lymphotaxin, SCM-1-alpha, Small inducible cytokine C1, XC chemokine ligand 1, LTN, LPTN, SCM1, SCM-1, SCYC1, SCM-1a.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized XCL1 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Lymphotactin 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 Lymphotactin in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      VGTEVLEESS CVNLQTQRLP VQKIKTYIIW EGAMRAVIFV TKRGLKICAD PEAKWVKAAI KTVDGRASTR KNMAETVPTG AQRSTSTAIT LTG.

    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.

    Lymphotactin Mouse
  • View Data Sheet

    Name :

    LIN28 Human, TAT

    Description:

    LIN28-TAT Human Recombinant

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

    Product # :

    PRO-2495

    Price :

    Quantity :

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    Description

    Recombinant Human LIN28 produced in E.Coli is a single, non-glycosylated polypeptide chain containing 222 amino acids (including 13- residue C-terminal TAT peptide) and having a molecular mass of 24.4kDa. The LIN28 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The LIN28 protein solution was formulated in PBS with 50mM arginine

    Purity

    Greater than 90% as determined by SDS-PAGE (coomassie staining).

    More Info

    • Introduction

      LIN28 is a marker of undifferentiated human embryonic stem cells and it increases the productivity of the formation of induced pluripotent stem cells from human fibroblasts. LIN28 acts as a 'translational enhancer and therefore leading specific mRNAs to polysomes and causes an increased protein synthesis. LIN28 binds let-7 pre-miRNA and blocks production of the mature let-7 microRNA in mouse embryonic stem cells.

    • Synonyms

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

    • Physical Appearance

      Sterile filtered colorless solution.

    • Stability

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

    • Amino Acid Sequence

      GPSVSNQQFA GGCAKAAEEA PEEAPEDAAR AADEPQLLHG AGICKWFNVR MGFGFLSMTA RAGVALDPPV DVFVHQSKLH MEGFRSLKEG EAVEFTFKKS AKGLESIRVT GPGGVFCIGS ERRPKGKSMQ KRRSKGDRCY NCGGLDHHAK ECKLPPQPKK CHFCQSISHM VASCPLKAQQ GPSAQGKPTY FREEEEEIHS PTLLPEAQNG GYGRKKRRQR RR.

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

    Human Lin28
  • View Data Sheet

    Name :

    OmpA S.Enteritidis

    Description:

    Salmonella Enteritidis Outer Membrane Protein-A Recombinant

    Outer Membrane Protein-A, OmpA.

    Product # :

    PRO-1918

    Price :

    Quantity :

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    • description
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    • More Info

    Description

    The Recombinant Salmonella Enteritidis Outer Membrane Protein A, E.Coli derived, 330 amino acids, contains the ompA immunodominant regions. The protein is fused to a His tag at C-terminal and purified by standard chromatography techniques.

    Source

    Escherichia Coli.

    Formulation

    PBS and 25MmM Arginine.

    Purity

    Protein is >95% pure as determined by 10% PAGE (coomassie staining).

    More Info

    • Introduction

      The OmpA protein is one of the main outer-membrane proteins of a large array of Gram-negative bacteria such as A.salmonicida, Shigella dysenteriae and E.coli.OmpA’s major physiological functions include maintenance of the structural integrity and morphology of the cells and porin activity, as well as a role in conjugation and bacteriophage binding.Achromogenic atypical Aeromonas salmonicida is the causative agent of goldfish ulcer disease.Virulence of this bacterium is associated with the production of a paracrystalline outer membrane A-layer protein.The species specific structural gene for the monomeric form of A-protein was cloned into a pET-3d plasmid in order to express and produce a recombinant form of the protein in E.coli BL21(DE3). The induced protein was isolated from inclusion bodies by a simple solubilization-renaturation procedure and purified by ion exchange chromatography on Q-Sepharose to over 95% pure monomeric protein.Recombinant A-protein was compared by biochemical, immunological and molecular methods with the A-protein isolated from atypical A.salmonicida bacterial cells by the glycine and the membrane extraction methods.

    • Synonyms

      Outer Membrane Protein-A, OmpA.

    • Physical Appearance

      Sterile Filtered clear solution.

    • Stability

      OmpA S.Enteritidis Recombinant although stable at 4°C for 1 week, should be stored below -18°C. Please prevent freeze thaw cycles.

    • Applications

      Immunoassay. Outer membrane protein A (ompA) of S. Enteritidis is a protein directly exposing to outsides of this organism, In hens, the production of antibodies against outer membrane protein A (ompA) during the infection has been demonstrated by inoculating both the complete bacterium and expressed protein produced from ompA DNA vaccine. Vaccination by ompA protein to hens is a poteintail tool to control S. enteritidis contaminated eggs into market, and prevent human foodborne disease from eggs.

    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.

    Ompa Senteritidis
  • View Data Sheet

    Name :

    Gliadin Alpha Wheat

    Description:

    Gliadin Alpha Wheat Recombinant

    Product # :

    PRO-2147

    Price :

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    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.

    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 :

    GDF3 Human

    Description:

    Growth Differentiation Factor-3 Human Recombinant

    Growth Differentiation Factor 3, Growth/Differentiation Factor 3 , MCOPCB6, MCOP7, GDF-3, KFS3.

    Product # :

    CYT-694

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    Description

    GDF3 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 124 amino acids and having a total molecular mass of 14.15 kDa.GDF3 is fused to a 10 amino acid His Tag at N-terminus and purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The protein was lyophilized from a concentrated solution (0.5mg/ml) containing 30mM Acetate buffer pH-4.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      GDF3 is a member of the TGF-beta superfamily though it does not show similarity pattern of conserved cysteine residues. GDF3 is linked to Vg-1 and human BMP-4. GDF3 transcripts are identified mainly in adult bone marrow, spleen, thymus, and adipose tissue. GDF3 expression is upregulated strongly in high-fat-fed C57Bl/6J FABP4/aP2 null mice, which develop obesity but not the related hyperglycemia or hyperinsulinemia characteristic of type II diabetes. GDF3 expression therefore bonds fatty acid metabolism in adipocytes and the expression of a differentiation regulator belonging to the bone morphogenetic proteins.

    • Synonyms

      Growth Differentiation Factor 3, Growth/Differentiation Factor 3 , MCOPCB6, MCOP7, GDF-3, KFS3.

    • Physical Appearance

      Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized GDF3 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution GDF3 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 GDF3 in sterile 100mM Acetate buffer pH-4 at a concentration of 0.5mg/ml. For the dilution into higher pH values, it is recommended to dilute the protein to a concentration of 10μg/ml. Please note that in higher concentrations the solubility of GDF3 is limited. The protein is not sterile! Please sterile filter before using it in the cell culture.

    • Amino Acid Sequence

      MKHHHHHHAS AAIPVPKLSC KNLCHRHQLF INFRDLGWHK WIIAPKGFMA NYCHGECPFS LTISLNSSNY AFMQALMHAV DPEIPQAVCI PTKLSPISML YQDNNDNVIL RHYEDMVVDECGCG.

    • Background

      What is the molecular weight/Mw of GDF3 HUMAN Protein?
      GDF3 HUMAN Protein has a total Mw of 14.15XkDa.

      What is the source or expression system of GDF3 HUMAN Protein?
      Escherichia Coli.

      What is the Purity of GDF3 HUMAN Protein?
      GDF3 HUMAN Protein is >90% pure as determined by SDS-PAGE.

      What is the Biological Activity of GDF3 HUMAN Protein?
      The biological functionality of GDF3 HUMAN Protein will be determined in the future.

      What is the amino acid sequence of GDF3 HUMAN Protein?
      MKHHHHHHAS AAIPVPKLSC KNLCHRHQLF INFRDLGWHK WIIAPKGFMA NYCHGECPFS LTISLNSSNY AFMQALMHAV DPEIPQAVCI PTKLSPISML YQDNNDNVIL RHYEDMVVDECGCG.

      What applications can GDF3 HUMAN Protein be used in?
      GDF3 HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for GDF3 HUMAN Protein?
      The endotoxin level is minimal, GDF3 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.

    Gdf3 Human
  • View Data Sheet

    Name :

    GDF15 Human, His

    Description:

    Growth and Differentiation Factor 15 Human Recombinant, His Tag

    GDF-15, MIC1, MIC-1, NAG-1, PDF, PLAB, PTGFB, Growth/differentiation factor 15, Placental bone morphogenetic protein, Placental TGF-beta, Macrophage inhibitory cytokine 1, Prostate differentiation factor, NSAID-activated gene 1 protein, NSAID-regulated gene 1 protein, NRG-1, GDF15.

    Product # :

    CYT-691

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    Description

    Recombinant Human GDF15 produced in E.Coli is a single, non-glycosylated polypeptide chain containing 151 amino acids (195-308) and having a molecular mass of 16.7 kDa(molecular weight on SDS-PAGE will appear higher).GDF15 is expressed with a 36 amino acid His tag fused at N-Terminus and purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The GDF15 protein solution contains 10mM sodium citrate, pH-3.5 & 10% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      GDF15 is part of the TGF-Beta superfamily that is involved in regulating inflammatory and apoptotic pathways in injured tissues and throughout disease processes. GDF15 is most abundant in the liver. Its expression in liver can be considerably up-regulated in during injury of organs such as liver, kidney, heart and lung. GDF-15 promotes proliferation or growth arrest and differentiation due to differences in cellular differentiation. GDF15 prevents apoptosis in cerebellar granule neurons by activating Akt and inhibiting endogenously active ERK. GDF15 is a novel autocrine/endocrine factor that antagonizes the hypertrophic response and loss of ventricular performance.

    • Synonyms

      GDF-15, MIC1, MIC-1, NAG-1, PDF, PLAB, PTGFB, Growth/differentiation factor 15, Placental bone morphogenetic protein, Placental TGF-beta, Macrophage inhibitory cytokine 1, Prostate differentiation factor, NSAID-activated gene 1 protein, NSAID-regulated gene 1 protein, NRG-1, GDF15.

    • 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

      MRGSHHHHHH GMASMTGGQQ MGRDLYDDDD KDRWGSMARA RNGDHCPLGP GRCCRLHTVR ASLEDLGWAD WVLSPREVQV TMCIGACPSQ FRAANMHAQI KTSLHRLKPD TVPAPCCVPA SYNPMVLIQK TDTGVSLQTY DDLLAKDCHC I.

    • Background

      What is the molecular weight/Mw of GDF15 HUMAN, HIS Protein?
      GDF15 HUMAN, HIS Protein has a total Mw of 16.7kDa.

      What is the source or expression system of GDF15 HUMAN, HIS Protein?
      Escherichia Coli.

      What is the Purity of GDF15 HUMAN, HIS Protein?
      GDF15 HUMAN, HIS Protein is >95% pure as determined by SDS-PAGE.

      What is the Biological Activity of GDF15 HUMAN, HIS Protein?
      The biological functionality of GDF15 HUMAN, HIS Protein will be determined in the future.

      What is the amino acid sequence of GDF15 HUMAN, HIS Protein?
      MRGSHHHHHH GMASMTGGQQ MGRDLYDDDD KDRWGSMARA RNGDHCPLGP GRCCRLHTVR ASLEDLGWAD WVLSPREVQV TMCIGACPSQ FRAANMHAQI KTSLHRLKPD TVPAPCCVPA SYNPMVLIQK TDTGVSLQTY DDLLAKDCHC I.

      What applications can GDF15 HUMAN, HIS Protein be used in?
      GDF15 HUMAN, HIS Protein can probably be used in western blot, ELISA and
      Lateral Flow.

      What is the endotoxin level for GDF15 HUMAN, HIS Protein?
      The endotoxin level is minimal, GDF15 HUMAN, HIS Protein was purified using conventional chromatography techniques.

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

    Gdf15 Human
  • View Data Sheet

    Name :

    RELM b Human

    Description:

    RELM-Beta Human Recombinant

    Resistin-like beta, RELM beta, Cysteine-rich secreted protein FIZZ2, Colon and small intestine-specific cysteine-rich protein, Cysteine-rich secreted protein A12-alpha-like 1, Colon carcinoma-related gene protein, RELM-b, XCP2, HXCP2.

    Product # :

    CYT-780

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    Description

    RELM-b Human Recombinant produced in E.Coli is a disulfide-linked homodimer, non-glycosylated, polypeptide chain containing 2 x 89 amino acids and having a total molecular mass of 19kDa. RELM-b is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    RELM-b was lyophilized from a solution containing 0.1% Trifluoroacetic Acid (TFA).

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      RELM-beta (Resistin-Like Molecule-beta) is a member of a recently identified family of secreted proteins containing a conserved cystein-rich C-terminus. The RELM family consists of resistin (also called FIZZ3), RELM-alfa (FIZZ1), RELM-beta (FIZZ2) and RELM-gamma. Only resisistin and RELM-beta were found in humans whereas all four RELM family members were identified in rodents.
      RELM-beta appears to be produced as a homodimer exclusively by intestinal goblet cells and can be found in high quantities in stool. Remarkably, stool of germ-free mice displaying sterile intestinal tract does not contain RELM-beta until bacterial colonization takes place after pathogen-free mice entered natural environment. Some, but not all, colon carcinoma cell lines secrete RELM-beta into the cell culture supernatant.
      The physiological function of RELM-beta is not known. High doses of recombinant RELM-beta showed hyperglycemic effects including lowered glucose disposal and increased hepatic glucose production in mice.

    • Synonyms

      Resistin-like beta, RELM beta, Cysteine-rich secreted protein FIZZ2, Colon and small intestine-specific cysteine-rich protein, Cysteine-rich secreted protein A12-alpha-like 1, Colon carcinoma-related gene protein, RELM-b, XCP2, HXCP2.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized RELM-b although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution RELM-b Human Recombinant 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 RELM-b in sterile 0.1% TFA not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      MQCSLDSVMD KKIKDVLNSL EYSPSPISKK LSCASVKSQG RPSSCPAGMA VTGCACGYGC GSWDVQLETT CHCQCSVVDW TTARCCHLT.

    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.

    Relm B Human
  • View Data Sheet

    Name :

    CST3 Mouse, sf9

    Description:

    Cystatin-C Mouse Recombinant, sf9

    Cystatin-C, Cystatin-3, Cst3.

    Product # :

    PRO-2249

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    Description

    CST3 produced in Sf9 Insect cells is a single, glycosylated polypeptide chain containing 126 amino acids (21-140a.a.) and having a molecular mass of 14.2kDa. (Molecular size on SDS-PAGE will appear at approximately 13.5-18kDa).CST3 is expressed with a 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Insect cells.

    Formulation

    CST3 protein solution (1mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 10% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Cystatins are a superfamily of cysteine proteinase inhibitors found in both plants and animals. They comprise a group of proteinase inhibitors, widely distributed in tissues and body fluids, and form tight complexes with cysteine proteases such as cathepsin B, H, L and S. Cystatin C, a secreted molecule of this family, is of interest from biochemical, medicine and evolutionary points of view. Cystatin C, with molecular weight of 13260 Da, is composed of 120 amino acids, lacks carbohydrate and has two disulfide bridges located near the carboxyl terminus. Cystatin C is increased in patients with malignant diseases, and is related to the insufficiency of renal function and appears to be a better marker than creatinine. On the other hand, low levels of cystatin C involve cause the breakdown of the elastic laminae and, subsequently, the atherosclerosis and abdominal aortic aneurysm.

    • Synonyms

      Cystatin-C, Cystatin-3, Cst3.

    • 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

      ATPKQGPRML GAPEEADANE EGVRRALDFA VSEYNKGSND AYHSRAIQVV RARKQLVAGV NYFLDVEMGR TTCTKSQTNL TDCPFHDQPH LMRKALCSFQ IYSVPWKGTH SLTKFSCKNA HHHHHH.

    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.

    Cst3 Mouse Sf9
  • View Data Sheet

    Name :

    Myostatin Human, HEK

    Description:

    Myostatin Human Recombinant, HEK

    GDF-8, MSTN, Growth Differentiation Factor 8, MSTN Muscle Hypertrophy.

    Product # :

    CYT-833

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    Description

    Myostatin Human Recombinant produced in HEK cells is a single, glycosylated, polypeptide chain (Asn24-Ser375) containing a total of 360 amino acids, having a calculated molecular mass of 41.1kDa. Myostatin is fused to a 2 aa N-terminal linker and a 6 aa His tag at N-Terminus.

    Source

    HEK 293.

    Formulation

    Myostatin solution at a concentration of 0.25mg/ml in phosphate buffered saline (PBS) pH 8.0 and 20% (w/v) glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      GDF8 is a member of the bone morphogenetic protein (BMP) family and the TGF-beta superfamily. This group of proteins is characterized by a polybasic proteolytic processing site which is cleaved to produce a mature protein containing seven conserved cysteine residues. The members of this family are regulators of cell growth and differentiation in both embryonic and adult tissues. This gene is thought to encode a secreted protein which negatively regulates skeletal muscle growth.

    • Synonyms

      GDF-8, MSTN, Growth Differentiation Factor 8, MSTN Muscle Hypertrophy.

    • Physical Appearance

      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

      HHHHHHASNE NSEQKENVEK EGLCNACTWR QNTKSSRIEA IKIQILSKLR LETAPNISKD VIRQLLPKAP PLRELIDQYD VQRDDSSDGS LEDDDYHATT ETIITMPTES DFLMQVDGKP KCCFFKFSSK IQYNKVVKAQ LWIYLRPVET PTTVFVQILR LIKPMKDGTR YTGIRSLKLD MNPGTGIWQS IDVKTVLQNW LKQPESNLGI EIKALDENGH DLAVTFPGPG EDGLNPFLEV KVTDTPKRSR RDFGLDCDEH STESRCCRYP LTVDFEAFGW DWIIAPKRYK ANYCSGECEF VFLQKYPHTH LVHQANPRGS AGPCCTPTKM SPINMLYFNG KEQIIYGKIP AMVVDRCGCS.

    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.

    Myostatin Human Hek
  • View Data Sheet

    Name :

    ARMC10 Human

    Description:

    Armadillo Repeat Containing 10 Human Recombinant

    Armadillo repeat-containing protein 10, Splicing variant involved in hepatocarcinogenesis protein, ARMC10, SVH.

    Product # :

    PRO-1453

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    Description

    ARMC10 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 304 amino acids (28-308 a.a) and having a molecular mass of 33.6 kDa.ARMC10 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    ARMC10 protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 10% glycerol and 1mM DTT.

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      AMRC10 is a protein which contains an armadillo repeat and transmembrane domain. Upregulation of the AMRC10 gene has a role in hepatocellular carcinoma. AMRC10 decreases the transcriptional activity of the tumor suppressor protein p53 through direct interaction with the DNA-binding domain of p53, moreover it might play a role in cell growth and survival.

    • Synonyms

      Armadillo repeat-containing protein 10, Splicing variant involved in hepatocarcinogenesis protein, ARMC10, SVH.

    • 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 MGSTRGRRRG DRELGIRSSK SAEDLTDGSY DDVLNAEQLQ KLLYLLESTE DPVIIERALI TLGNNAAFSV NQAIIRELGG IPIVANKINH SNQSIKEKAL NALNNLSVNV ENQIKIKIYI SQVCEDVFSG PLNSAVQLAG LTLLTNMTVT NDHQHMLHSY ITDLFQVLLT GNGNTKVQVL KLLLNLSENP AMTEGLLRAQ VDSSFLSLYD SHVAKEILLR VLTLFQNIKN CLKIEGHLAV QPTFTEGSLF FLLHGEECAQ KIRALVDHHD AEVKEKVVTI IPKI.

    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.

    Armc10 Human
  • View Data Sheet

    Name :

    TPM3 Human

    Description:

    Tropomyosin-3 Human Recombinant

    Tropomyosin alpha-3 chain, Gamma-tropomyosin, Tropomyosin-3, Tropomyosin-5, hTM5, TPM3, TM3, TM5, TRK, CFTD, NEM1, TM-5, TM30, TM30nm, TPMsk3, hscp30, OK/SW-cl.5.

    Product # :

    PRO-1020

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    Description

    TPM3 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 272 amino acids (1-248 a.a.) and having a molecular mass of 31.6kDa. TPM3 is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    TPM3 protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 1mM DTT, 10% glycerol, 0.1M NaCl.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    More Info

    • Introduction

      Tropomyosin alpha-3 chain (TPM3) belongs to the tropomyosin family of actin-binding proteins involved in the contractile system of striated and smooth muscles and the cytoskeleton of non-muscle cells. Tropomyosins are dimers of coiled-coil proteins which polymerize end-to-end along the major groove in most actin filaments. Tropomyosins give stability to the filaments and regulate access of other actin-binding proteins. In muscle cells, tropomyosins regulate muscle contraction by controlling the binding of myosin heads to the actin filament. Mutations in the TPM3 gene cause autosomal dominant nemaline myopathy, and oncogenes formed by chromosomal translocations involving this locus are linked with cancer.

    • Synonyms

      Tropomyosin alpha-3 chain, Gamma-tropomyosin, Tropomyosin-3, Tropomyosin-5, hTM5, TPM3, TM3, TM5, TRK, CFTD, NEM1, TM-5, TM30, TM30nm, TPMsk3, hscp30, OK/SW-cl.5.

    • 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 MGSHMAGITT IEAVKRKIQV LQQQADDAEE RAERLQREVE GERRAREQAE AEVASLNRRI QLVEEELDRA QERLATALQK LEEAEKAADE SERGMKVIEN RALKDEEKME LQEIQLKEAK HIAEEADRKY EEVARKLVII EGDLERTEER AELAESRCRE MDEQIRLMDQ NLKCLSAAEE KYSQKEDKYE EEIKILTDKL KEAETRAEFA ERSVAKLEKT IDDLEDKLKC TKEEHLCTQR MLDQTLLDLN EM.

    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.

    Tpm3 Human
  • View Data Sheet

    Name :

    GFRA1 Human

    Description:

    GDNF Family Receptor Alpha 1 Human Recombinant

    GDNF receptor alpha-1, GDNFR-alpha-1, GFRalpha-1, RET ligand 1, TGF-beta-related neurotrophic factor receptor 1, GDNFRA1, RET1L2, RETL1, Glial Cell LineDerived Neurotrophic Factor Receptor Alpha, TRNR1, GPILinked Anchor Protein, PI-Linked Cell-Surface.

    Product # :

    CYT-1026

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    • More Info

    Description

    GFRA1 Human Recombinant produced in HEK293 cells is a single, glycosylated polypeptide chain (a.a 25-423) containing 409 amino acids including a 10 a.a C-terminal His tag. The total molecular mass is 46.0kDa (calculated).

    Source

    HEK293 cells.

    Formulation

    GFRA1 filtered (0.4 µm) and lyophilized from 0.5mg/ml in phosphate buffered saline pH 7.5 containing 5 % (w/v) trehalose.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      GDNF family receptor alpha-1 (GFRA1) belongs to the GDNF receptor family. GFRA1 is a glycosyl-phosphatidylinositol(GPI)-linked cell surface receptor for both Glial cell line-derived growth factor (GDNF), neurturin (NTN), and mediates activation of the RET tyrosine kinase receptor. The GFRA1 protein is a potent survival factor for central and peripheral neurons, and is vital for the development of kidneys and the enteric nervous system.

    • Synonyms

      GDNF receptor alpha-1, GDNFR-alpha-1, GFRalpha-1, RET ligand 1, TGF-beta-related neurotrophic factor receptor 1, GDNFRA1, RET1L2, RETL1, Glial Cell LineDerived Neurotrophic Factor Receptor Alpha, TRNR1, GPILinked Anchor Protein, PI-Linked Cell-Surface.

    • 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. GFRA1 is not sterile! Please filter the product by an appropriate sterile filter before using it in the cell culture.

    • Amino Acid Sequence

      DRLDCVKASD QCLKEQSCST KYRTLRQCVA GKETNFSLAS GLEAKDECRS AMEALKQKSL YNCRCKRGMK KEKNCLRIYW SMYQSLQGND LLEDSPYEPV NSRLSDIFRV VPFISVEHIP KGNNCLDAAK ACNLDDICKK YRSAYITPCT TSVSNDVCNR RKCHKALRQF FDKVPAKHSY GMLFCSCRDI ACTERRRQTI VPVCSYEERE KPNCLNLQDS CKTNYICRSR LADFFTNCQP ESRSVSSCLK ENYADCLLAY SGLIGTVMTP NYIDSSSLSV APWCDCSNSG NDLEECLKFL NFFKDNTCLK NAIQAFGNGS DVTVWQPAFP VQTTTATTTT ALRVKNKPLG PAGSENEIPT HVLPPCANLQ AQKLKSNVSG NTHLCISNGN YEKEGLGAS H HHHHHHHHH.

    • Background

      What is the molecular weight/Mw of GFRA1 Protein?
      GFRA1 Protein has a total Mw of 46kDa.

      What is the source or expression system of GFRA1 Protein?
      HEK293 cells.
      What is the Purity of GFRA1 Protein?
      GFRA1 Protein is >95% pure as determined by SDS-PAGE.

      What is the Biological Activity of GFRA1 Protein?
      The biological functionality of GFRA1 Protein will be determined in the future.

      What is the amino acid sequence of GFRA1 Protein?
      DRLDCVKASD QCLKEQSCST KYRTLRQCVA GKETNFSLAS GLEAKDECRS AMEALKQKSL YNCRCKRGMK KEKNCLRIYW SMYQSLQGND LLEDSPYEPV NSRLSDIFRV VPFISVEHIP KGNNCLDAAK ACNLDDICKK YRSAYITPCT TSVSNDVCNR RKCHKALRQF FDKVPAKHSY GMLFCSCRDI ACTERRRQTI VPVCSYEERE KPNCLNLQDS CKTNYICRSR LADFFTNCQP ESRSVSSCLK ENYADCLLAY SGLIGTVMTP NYIDSSSLSV APWCDCSNSG NDLEECLKFL NFFKDNTCLK NAIQAFGNGS DVTVWQPAFP VQTTTATTTT ALRVKNKPLG PAGSENEIPT HVLPPCANLQ AQKLKSNVSG NTHLCISNGN YEKEGLGAS H HHHHHHHHH.

      What applications can GFRA1 Protein be used in?
      GFRA1 Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for GFRA1 Protein?
      The endotoxin level is minimal, GFRA1 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.

    Gfra1 Human
  • View Data Sheet

    Name :

    CLMP Human, SF9

    Description:

    CXADR-Like Membrane Protein, Sf9 Human Recombinant

    CXADR like membrane protein, ACAM, ASAM, CSBM, CSBS, Adipocyte adhesion molecule, Coxsackie- and adenovirus receptor-like membrane protein, CAR-like membrane protein.

    Product # :

    PRO-2519

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    Description

    CLMP produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 226 amino acids (19-235a.a.) and having a molecular mass of 25.6kDa. (Molecular size on SDS-PAGE will appear at approximately 28-40kDa).CLMP is expressed with a 9 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    CLMP protein solution (0.5mg/ml) contains phosphate buffered saline (pH7.4), 1mM DTT and 20%glycerol

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      CXADR Like Membrane Protein or CLMP, part of the CTX family within the immunoglobulin superfamily, is a type 1 transmembrane peptide. CLMP is expressed in the placenta and small intensine, skeletal muscle, colon, lungs and heart. CLMP is located in junction complexes across endothelial and epithelial cells and can take part in cell adhesion. The protein has influence on development of obesity via adipocyte differentiation.

    • Synonyms

      CXADR like membrane protein, ACAM, ASAM, CSBM, CSBS, Adipocyte adhesion molecule, Coxsackie- and adenovirus receptor-like membrane protein, CAR-like membrane protein.

    • 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

      ADPTHTEIKR VAEEKVTLPC HHQLGLPEKD TLDIEWLLTD NEGNQKVVIT YSSRHVYNNL TEEQKGRVAF ASNFLAGDAS LQIEPLKPSD EGRYTCKVKN SGRYVWSHVI LKVLVRPSKP KCELEGELTE GSDLTLQCES SSGTEPIVYY WQRIREKEGE DERLPPKSRI DYNHPGRVLL
      QNLTMSYSGL YQCTAGNEAG KESCVVRVTV QYVQSIGMVA HHHHHH.

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    Clmp Protein
  • View Data Sheet

    Name :

    MORF4L1 Human

    Description:

    Mortality Factor 4 Like 1 Human Recombinant

    Mortality factor 4-like protein 1, MORF-related gene 15 protein, Protein MSL3-1, Transcription factor-like protein MRG15, MORF4L1, MRG15, FWP006, HSPC008, HSPC061, PP368, Eaf3, MEAF3, S863-6, HsT17725, MORFRG15.

    Product # :

    PRO-1078

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    Description

    MORF4L1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 347 amino acids (1-323 a.a) and having a molecular mass of 39.8kDa.MORF4L1 is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    MORF4L1 protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH8.0), 30% glycerol, 0.15M NaCl and 1mM DTT.

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Mortality factor 4-like protein 1 (MORF4L1) is a member of the MRG family. MORF4L1 is a component of the NuA4 histone acetyltransferase (HAT) complex which is involved in transcriptional activation of select genes mostly by acetylation of nucleosomal histones H4 and H2A. MORF4L1 is a transcription factor expressed in various human tissues, and its orthologs have been found in many other eukaryotes which comprise the MRG protein family. The C-terminal part of MORF4L1 forms a conserved MRG domain that is involved in interactions with the tumor suppressor protein retinoblastoma and a nucleoprotein.

    • Synonyms

      Mortality factor 4-like protein 1, MORF-related gene 15 protein, Protein MSL3-1, Transcription factor-like protein MRG15, MORF4L1, MRG15, FWP006, HSPC008, HSPC061, PP368, Eaf3, MEAF3, S863-6, HsT17725, MORFRG15.

    • 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 MGSHMAPKQD PKPKFQEGER VLCFHGPLLY EAKCVKVAIK DKQVKYFIHY SGWNKNWDEW VPESRVLKYV DTNLQKQREL QKANQEQYAE GKMRGAAPGK KTSGLQQKNV EVKTKKNKQK TPGNGDGGST SETPQPPRKK RARVDPTVEN EETFMNRVEV KVKIPEELKP WLVDDWDLIT RQKQLFYLPA KKNVDSILED YANYKKSRGN TDNKEYAVNE VVAGIKEYFN VMLGTQLLYK FERPQYAEIL ADHPDAPMSQ VYGAPHLLRL FVRIGAMLAY TPLDEKSLAL LLNYLHDFLK YLAKNSATLF SASDYEVAPP EYHRKAV.

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    Morf4L1 Human
  • View Data Sheet

    Name :

    CCL24 Rat

    Description:

    Eotaxin-2 Rat Recombinant (CCL24)

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

    Product # :

    CHM-282

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    Description

    CCL24 Rat Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 93 amino acids and having a molecular mass of 10.2kDa. The CCL24 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

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

    Purity

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

    Biological Activity

    Determined by its ability to chemoattract murine lymphocytes using a concentration range of 10-100ng/ml corresponding to a Specific Activity of 10,000-100,000IU/mg.

    More Info

    • Introduction

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

    • Synonyms

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

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized Eotaxin-2 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution CCL24 should be stored at 4°C between 2-7 days and for future use below -18°C. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.

    • Solubility

      It is recommended to reconstitute the lyophilized CCL24 Rat Recombinant in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      VTIPSSCCVT FISKKIPVNR VISYQLANGS ICPKAGVIFI TKKGHKICTD PKLPWVQKHI KNLDAKRNQP SEGAKALGPK FVIQKLRGNS TKV.

    • Background

      What is the molecular weight/Mw of CCL24 RAT Protein?
      CCL24 RAT Protein has a total Mw of 10.2kDa.

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

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

      What is the Biological Activity of CCL24 RAT Protein?
      Determined by its ability to chemoattract murine lymphocytes using a concentration range of 10-100ng/ml corresponding to a Specific Activity of 10,000-100,000IU/mg.

      What is the amino acid sequence of CCL24 RAT Protein?
      VTIPSSCCVT FISKKIPVNR VISYQLANGS ICPKAGVIFI TKKGHKICTD PKLPWVQKHI KNLDAKRNQP SEGAKALGPK FVIQKLRGNS TKV.

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

      What is the endotoxin level for CCL24 RAT Protein?
      The endotoxin level is minimal, CCL24 RAT 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.

    Eotaxin 2 Rat
  • View Data Sheet

    Name :

    STX11 Human

    Description:

    Syntaxin-11 Human Recombinant

    Syntaxin-11, STX11, FHL4, HLH4, HPLH4.

    Product # :

    PRO-1111

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    Description

    STX11 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 311 amino acids (1-287 a.a) and having a molecular mass of 35.8kDa.STX11 is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    STX11 protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH8.0), 10% glycerol and 0.4M Urea.

    Purity

    Greater than 95% as determined by SDS-PAGE.

    More Info

    • Introduction

      Syntaxin-11 (STX11) belongs to the t-SNARE family. Syntaxin-11 regulates protein transport between late endosomes and the trans-Golgi network. STX11 interacts with the SNARE proteins SNAP-23 and VAMP. STX11 gene mutations are linked with familial hemophagocytic lymphohistiocytosis.

    • Synonyms

      Syntaxin-11, STX11, FHL4, HLH4, HPLH4.

    • 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 MGSHMKDRLA ELLDLSKQYD QQFPDGDDEF DSPHEDIVFE TDHILESLYR DIRDIQDENQ LLVADVKRLG KQNARFLTSM RRLSSIKRDT NSIAKAIKAR GEVIHCKLRA MKELSEAAEA QHGPHSAVAR ISRAQYNALT LTFQRAMHDY NQAEMKQRDN CKIRIQRQLE IMGKEVSGDQ IEDMFEQGKW DVFSENLLAD VKGARAALNE IESRHRELLR LESRIRDVHE LFLQMAVLVE KQADTLNVIE LNVQKTVDYT GQAKAQVRKA VQYEEKNPCR TLCCFCCPCL K.

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    Stx11 Human
  • View Data Sheet

    Name :

    TAC3 Human

    Description:

    Tachykinin-3 Human Recombinant

    Tachykinin-3, ZNEUROK1, Neurokinin-B, NKB, Neuromedin-K, TAC3, NKNB, PRO1155.

    Product # :

    PRO-716

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    Description

    TAC3 Human Recombinant fused with 20 amino acid His tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 125 amino acids (17-121 a.a.) and having a molecular mass of 13.8kDa.The TAC3 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The TAC3 solution contains 20mM Tris-HCl buffer (pH 8.0) and 20% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Tachykinin-3 belongs to the substance P-related tachykinin family. Tachykinins are active peptides that stimulate neurons, induce behavioral responses, are effective vasodilators and secretagogues, and contract (directly or indirectly) many smooth muscles. TAC3 and its receptor are essential switches of regulator of human puberty, regulated by the brain through the release of the GnRH which starts a chain of processes which eventually lead to the production of sex hormones.
      During pregnancy, the expression of TAC3 is restricted to the outer syncytiotrophoblast of the placenta, significant concentrations of TAC3 can be identified in plasma as early as week 9, and plasma concentrations of TAC3 are grossly elevated in pregnancy-induced hypertension and pre-eclampsia. Higher Tachykinin-3 concentrations in normotensive pregnant women may be caused by the advanced gestational age and/or the result of a negative interaction of other vasoactive substances. TAC3 has a role in the continuance of high placental blood flow in normal pregnancy.

    • Synonyms

      Tachykinin-3, ZNEUROK1, Neurokinin-B, NKB, Neuromedin-K, TAC3, NKNB, PRO1155.

    • 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 QSFGAVCKEP QEEVVPGGGR SKRDPDLYQL LQRLFKSHSS LEGLLKALSQ ASTDPKESTS PEKRDMHDFF VGLMGKRSVQ PDSPTDVNQE NVPSFGILKY PPRAE.

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    Tac3 Human
  • View Data Sheet

    Name :

    GNAZ Human

    Description:

    Guanine Nucleotide Binding Protein Alpha Z Polypeptide Human Recombinant

    Guanine Nucleotide Binding Protein (G Protein) Alpha Z Polypeptide, G(X) Alpha Chain, Guanine Nucleotide-Binding Protein G(Z) Subunit Alpha, Gz-Alpha, Transducin Alpha.

    Product # :

    PRO-1225

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    Description

    GNAZ Human Recombinant produced in E. coli is a single polypeptide chain containing 375 amino acids (1-355) and having a molecular mass of 43.0 kDa.GNAZ is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

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

    Purity

    Greater than 90% as determined by SDS-PAGE.

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    • Introduction

      Guanine nucleotide-binding protein G(z) subunit alpha (GNAZ) belongs to the G protein subfamily which mediates signal transduction in pertussis toxin-insensitive systems. GNAZ has a role in maintaining the ionic balance of perilymphatic and endolymphatic cochlear fluids. G proteins are involved as modulators or transducers in a variety of transmembrane signaling systems.

    • Synonyms

      Guanine Nucleotide Binding Protein (G Protein) Alpha Z Polypeptide, G(X) Alpha Chain, Guanine Nucleotide-Binding Protein G(Z) Subunit Alpha, Gz-Alpha, Transducin Alpha.

    • 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 MGCRQSSEEK EAARRSRRID RHLRSESQRQ RREIKLLLLG TSNSGKSTIV KQMKIIHSGG FNLEACKEYK PLIIYNAIDS LTRIIRALAA LRIDFHNPDR AYDAVQLFAL TGPAESKGEI TPELLGVMRR LWADPGAQAC FSRSSEYHLE DNAAYYLNDL ERIAAADYIP TVEDILRSRD MTTGIVENKF TFKELTFKMV DVGGQRSERK KWIHCFEGVT AIIFCVELSG YDLKLYEDNQ TSRMAESLRL FDSICNNNWF INTSLILFLN KKDLLAEKIR RIPLTICFPE YKGQNTYEEA AVYIQRQFED LNRNKETKEI YSHFTCATDT SNIQFVFDAV TDVIIQNNLK YIGLC

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    Gnaz Human
  • View Data Sheet

    Name :

    CXCL1 Mouse

    Description:

    GRO1/KC Mouse Recombinant (CXCL1)

    Growth-regulated alpha protein, CXCL1, Platelet-derived growth factor-inducible protein KC, Secretory protein N51, KC, Fsp, N51, gro, Gro1, Mgsa, Scyb1, chemokine (C-X-C motif) ligand 1.

    Product # :

    CHM-335

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    Description

    KC Mouse Recombinant also known as N51 and GRO-1 produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 72 amino acids and having a molecular mass of approximately 7.8 kDa. The GRO-1 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The protein solution (1mg/ml) was lyophilized from 20mM phosphate buffer pH-7.4 and 0.1M NaCl.

    Purity

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

    Biological Activity

    The biological activity was determined by measuring the ability to chemoattrat human neutrophilsat a concentration of 10ng/ml-100ng/ml.

    More Info

    • Introduction

      Chemokine (C-X-C motif) ligand 1 (CXCL1) is a small cytokine belonging to the CXC chemokine family that was previously called GRO1 oncogene, Neutrophil-activating protein 3 (NAP-3) and melanoma growth stimulating activity, alpha (MSGA-a). It is secreted by human melanoma cells, has mitogenic properties and is implicated in melanoma pathogenesis. CXCL1 is expressed by macrophages, neutrophils and epithelial cells, and has neutrophil chemoattractant activity. CXCL1 plays a role in spinal cord development by inhibiting the migration of oligodendrocyte precursors and is involved in the processes of angiogenesis, inflammation, wound healing, and tumorigenesis. This chemokine elicits its effects by signaling through the chemokine receptor CXCR2. The gene for CXCL1 is located on human chromosome 4 amongst genes for other CXC chemokines.

    • Synonyms

      Growth-regulated alpha protein, CXCL1, Platelet-derived growth factor-inducible protein KC, Secretory protein N51, KC, Fsp, N51, gro, Gro1, Mgsa, Scyb1, chemokine (C-X-C motif) ligand 1.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized KC Mouse although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution CXCL1 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 GRO1 Recombinant in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      APIANELRCQ CLQTMAGIHL KNIQSLKVLP SGPHCTQTEV IATLKNGREA CLDPEAPLVQ KIVQKMLKGV PK.

    • Background

      What is the molecular weight/Mw of CXCL1 MOUSE Protein?
      CXCL1 MOUSE Protein has a total Mw of 7.8kDa.

      What is the source or expression system of CXCL1 MOUSE Protein?
      Escherichia Coli.

      What is the Purity of CXCL1 MOUSE Protein?
      CXCL1 MOUSE Protein is >97% pure as determined by SDS-PAGE.

      What is the Biological Activity of CXCL1 MOUSE Protein?
      The biological activity was determined by measuring the ability to chemoattrat human neutrophilsat a concentration of 10ng/ml-100ng/ml.

      What is the amino acid sequence of CXCL1 MOUSE Protein?
      APIANELRCQ CLQTMAGIHL KNIQSLKVLP SGPHCTQTEV IATLKNGREA CLDPEAPLVQ KIVQKMLKGV PK.

      What applications can CXCL1 MOUSE Protein be used in?
      CXCL1 MOUSE Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for CXCL1 MOUSE Protein?
      The endotoxin level is minimal, CXCL1 MOUSE Protein was purified using conventional chromatography techniques.


    • Protein content

      Protein quantitation was carried out by two independent methods: 1. UV spectroscopy at 280 nm using the absorbency value of 0.03 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 standard solution of KC as a Reference Standard.

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    Gro A Mouse
  • View Data Sheet

    Name :

    RLN3 Human

    Description:

    Relaxin-3 Human Recombinant

    Relaxin 3, Prorelaxin H3, RXN3, Insl7, ZINS4, H3, Relaxin 3 (H3), Relaxin-3, RLN3.

    Product # :

    PRO-2176

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    Description

    Relaxin-3 Human Recombinant produced in E.Coli is a disulfide-linked heterodimeric, non-glycosylated, polypeptide chain containing 24 amino acids for A chain and 27 amino acids for B chain and having a molecular mass of 2.5kDa for A chain and 3kDa for B chain.The Relaxin-3 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Lyophilized from a 0.2µm filtered solution in Acetonitrile and TFA.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Biological Activity

    The ED50, as measured by cAMP accumulation in human THP-1 cells, is less than 17.5ng/ml.

    More Info

    • Introduction

      Relaxin-3 (RLN3) belongs to the relaxin family. Relaxins are endocrine and autocrine/paracrine hormones. Relaxin, which is produced by the ovary, targets the mammalian reproductive system to ripen the cervix, elongate the pubic symphysis and inhibit uterine contraction. Unlike human Relaxins 1 and 2, Relaxin 3 does not seem to have a role in reproduction; however it is involved in stress response in the brain stem. RLN3 is the only known ligand for the G-protein-coupled receptor GPCR135, titled RXFP3. In addition, RLN3 binds the LGR7 (RXFP1) receptor, however with lower affinity than Relaxin-2. Even though binding of RLN3 to LGR7 increases intracellular cAMP, binding to GPCR135 suppresses cAMP accumulation, indicating coupling to Gi, Go, or Gz by this receptor.

    • Synonyms

      Relaxin 3, Prorelaxin H3, RXN3, Insl7, ZINS4, H3, Relaxin 3 (H3), Relaxin-3, RLN3.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized RLN3 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Relaxin-3 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 RLN3 in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      A chain: DVLAGLSSSC CKWGCSKSEI SSLC.
      B chain: RAAPYGVRLCG REFIRAVIFT CGGSRW.

    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.

    Rln3 Human
  • View Data Sheet

    Name :

    GFER Human

    Description:

    Growth Factor, Augmenter of Liver Regeneration Human Recombinant

    FAD-linked sulfhydryl oxidase ALR, Augmenter of liver regeneration, Hepatopoietin, GFER, ALR, HERV1, HPO, ALR, HSS, ERV1, HPO1, HPO2.

    Product # :

    PRO-1326

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    Description

    GFER Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 229 amino acids (1-205 a.a) and having a molecular mass of 26kDa.GFER is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

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

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      FAD-linked sulfhydryl oxidase ALR (GFER) is a member of the Erv1/ALR family of proteins, which is found in higher and lower eukaryotes. GFER is a hepatotrophic growth factor and flavin-linked sulfhydryl oxidase expressed in a variety of tissues. Moreover, GFER induces the expression of S-adenosylmethionine decarboxyl-ase and ornithine decarboxylases (ODC), which each have a central role in the synthesis of polyamines. The hepatotrophic factor designated augmenter of liver regeneration (ALR) is assumed to be one of the factors responsible for the exceptional regenerative capacity of mammalian liver. The GFER gene is located on chromosome 16 in the interval containing the locus for polycystic kidney disease (PKD1).

    • Synonyms

      FAD-linked sulfhydryl oxidase ALR, Augmenter of liver regeneration, Hepatopoietin, GFER, ALR, HERV1, HPO, ALR, HSS, ERV1, HPO1, HPO2.

    • 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 MGSHMAAPGE RGRFHGGNLF FLPGGARSEM MDDLATDARG RGAGRRDAAA SASTPAQAPT SDSPVAEDAS RRRPCRACVD FKTWMRTQQK RDTKFREDCP PDREELGRHS WAVLHTLAAY YPDLPTPEQQ QDMAQFIHLF SKFYPCEECA EDLRKRLCRN HPDTRTRACF TQWLCHLHNE VNRKLGKPDF DCSKVDERWR DGWKDGSCD.

    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.

    Gfer Human
  • View Data Sheet

    Name :

    GDNF Mouse

    Description:

    Glial-Derived Neurotrophic Factor Mouse Recombinant

    ATF1, ATF2, HFB1-GDNF, GDNF.

    Product # :

    CYT-243

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    Description

    Glial derived Neurotrophic Factor Mouse Recombinant produced in E.Coli is a non-glycosylated homodimer containing 2 x 135 amino acids and having a total molecular mass of 30.2kDa. GDNF is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    GDNF was lyophilized with no additives.

    Purity

    Greater than 98.0% as determined by analysis by SDS-PAGE.

    Biological Activity

    The ED50 as determined by the dose-dependent proliferation of C6 cells, is 0.8-0.12µg/ml.

    More Info

    • Introduction

      GDNF promotes the survival and differentiation of neurons in culture, and is able to prevent apoptosis of motor neurons induced by axotomy. The encoded protein is processed to a mature secreted form that exists as a homodimer. The mature form of the protein is a ligand for the product of the RET (rearranged during transfection) protooncogene. In addition to the transcript encoding GDNF, two additional alternative transcripts encoding distinct proteins, referred to as astrocyte-derived trophic factors, have also been described. Mutations in this gene may be associated with Hirschsprung disease.
      GDNF enhances survival and morphological differentiation of neurons and increases their high-affinity uptake.

    • Synonyms

      ATF1, ATF2, HFB1-GDNF, GDNF.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Amino Acid Sequence

      MSPDKQAAL PRRENRNRQAA AASPENSRGK GRRGQRGKNR GCVLTAIHLN VTDLGLGYET KEELIFRYCS GSCESAETMY DKILKNLSRS RRLTSDKVGQ ACCRPVAFDD DLSFLDDNLV YHILRKHSAK RCGCI.

    • Background

      What is the molecular weight/Mw of GDNF MOUSE Protein?
      GDNF MOUSE Protein has a total Mw of 30.2kDa.

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

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

      What is the Biological Activity of GDNF MOUSE Protein?
      The ED50 as determined by the dose-dependent proliferation of C6 cells, is 0.8-0.12µg/ml.

      What is the amino acid sequence of GDNF MOUSE Protein?
      MSPDKQAAL PRRENRNRQAA AASPENSRGK GRRGQRGKNR GCVLTAIHLN VTDLGLGYET KEELIFRYCS GSCESAETMY DKILKNLSRS RRLTSDKVGQ ACCRPVAFDD DLSFLDDNLV YHILRKHSAK RCGCI.
      What applications can GDNF MOUSE Protein be used in?
      GDNF MOUSE Protein can probably be used in western blot, ELISA and Lateral Flow.

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

    Gdnf Mouse
  • View Data Sheet

    Name :

    Lungkine Mouse

    Description:

    Lungkine (CXCL15) Mouse Recombinant

    C-X-C motif chemokine 15, Lungkine, Small-inducible cytokine B15, Cxcl15, Scyb15.

    Product # :

    CHM-286

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    Description

    Recombinant Mouse Lungkine produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 142 amino acids and having a molecular mass of 16.4kDa.The CXCL15 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The Lungkine protein was lyophilized from a 0.2µm filtered concentrated solution in PBS pH 7.4 and 0.02% Tween-20.

    Purity

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

    Biological Activity

    The biological activity determined by a chemotaxis bioassay using human neutrophils is in a concentration of 20-100 ng/ml.

    More Info

    • Introduction

      Mouse Lungkine/CXCL15 (WECHE) belongs to the ELR motif-containing CXC chemokines. The mouse Lungkine gene has been mapped to chromosome 5. The cDNA of mouse Lungkine encodes a 166 amino acids (aa) protein with a 25 aa predicted signal peptide and a 141 aa mature protein with an exceptionally long C-terminal tail which extends beyond beyond the chemokine fold. Lungkine protein is secreted into bronchoalveolar space and is involved in lung-specific neutrophils trafficking. Furthermore, studies in Lungkine knockout mice propose that Lungkine is an imperative mediator of neutrophil migration from the lung parenchyma into the airspace. In addition, Lungkine is chemotactic for bone marrow progenitor cells and modulates hematopoietic cell differentiation. By Northern blot analysis and in-situ hybridization, Lungkine transcripts have only been specifically detected in the adult and fetal lung, and its expression is up-regulated under inflammatory conditions. There is a 35% aa sequence similarity between the mouse Lungkine and the human ENA-78 and a 31% similarity with the human IL-8.

    • Synonyms

      C-X-C motif chemokine 15, Lungkine, Small-inducible cytokine B15, Cxcl15, Scyb15.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized Lungkine although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution CXCL15 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 Lungkine in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      QELRCLCIQE HSEFIPLKLI KNIMVIFETI YCNRKEVIAV PKNGSMICLD PDAPWVKATV GPITNRFLPE DLKQKEFPPA MKLLYSVEHE KPLYLSFGRP ENKRIFPFPI RETSRHFADL AHNSDRNFLR DSSEVSLTGS DA.

    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.

    Lungkine Mouse
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