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Search results

1000 results found for “Melanotan”

Name

Description

Product #

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  • View Data Sheet

    Name :

    Midkine Human

    Description:

    Midkine Human Recombinant

    NEGF-2, Neurite Growth-Promoting Factor 2, MK, Neurite outgrowth-promoting protein, Midgestation and kidney protein, Amphiregulin-associated protein, ARAP, Neurite outgrowth-promoting factor 2, FLJ27379, Midkine, MK1, NEGF2.

    Product # :

    CYT-192

    Price :

    Quantity :

    Shipping Method :

    Room Temp Icon

    Shipped at Room temp

    Add To Cart

    More Info

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    • source
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    Description

    Midkine Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 123 amino acids and having a molecular mass of 13.4kDa. The Midkine 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 95.0% as determined by:
    (a) Analysis by RP-HPLC.
    (b) Analysis by SDS-PAGE.

    Biological Activity

    Determined by its ability to chemoattract human neutrophils using a concentration range of 0.1-10 ng/ml corresponding to a specific activity of 100,000-10,000,000IU/mg.

    Citations

    More Info

    • Introduction

      Midkine (MK) is the product of a retinoic acid responsive gene. It contains 121 amino acid residues including 10 conserved cysteine residues, all of which appear to be disulphide linked.
      Midkine is expressed during embryogenesis, showing an expression pattern that suggests functions in neurogenesis, cell migration, secondary organogenetic induction, and mesoderm-epithelial interaction.
      The widespread downregulation of MK in the adult human is reverted in a number of cancers, in which polypeptides are able to act as both transforming growth factors and promoters of angiogenesis.
      Midkine (MK), induces chemotaxis of human neutrophils and was found to trigger mobilization of intracellular calcium of these cells.
      Midkine induces histamine release from rat peritoneal mast cells with a rapid response in a dose dependent manner.
      Midkine is also a potent stimulator of collagen and glycosaminoglycan synthesis.

    • Synonyms

      NEGF-2, Neurite Growth-Promoting Factor 2, MK, Neurite outgrowth-promoting protein, Midgestation and kidney protein, Amphiregulin-associated protein, ARAP, Neurite outgrowth-promoting factor 2, FLJ27379, Midkine, MK1, NEGF2.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Amino Acid Sequence

      VAKKKDKVKK GGPGSECAEW AWGPCTPSSK DCGVGFREGT CGAQTQRIRC RVPCNWKKEF GADCKYKFEN WGACDGGTGT KVRQGTLKKA RYNAQCQETI RVTKPCTPKT KAKAKAKKGK GKD.

    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.

    Midkine Human
  • View Data Sheet

    Name :

    PARK7 Mouse

    Description:

    Parkinson Disease Protein 7 Mouse Recombinant

    Protein deglycase DJ-1, Parkinson disease protein 7 homolog.

    Product # :

    PRO-2226

    Price :

    Quantity :

    Shipping Method :

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    Shipped with Ice Packs

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    Description

    PARK7 Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 212 amino acids (1-189 a.a) and having a molecular mass of 22.4kDa. PARK7 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    PARK7 protein solution (0.5mg/ml) containing Phosphate Buffered Saline (pH 7.4), 20% glycerol and 1mM DTT.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      The PARK7 is a ubiquitously expressed protein involved in various cellular processes including spermatogenesis and fertilization, cancer, RNA-binding, androgen-receptor signaling and oxidative stress. Mutations in the PARK7 are the cause of autosomal recessive early-onset Parkinson’s disease 7 (Park7).

    • Synonyms

      Protein deglycase DJ-1, Parkinson disease protein 7 homolog.

    • 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 MGSMASKRAL VILAKGAEEM ETVIPVDVMR RAGIKVTVAG LAGKDPVQCS RDVMICPDTS LEDAKTQGPY DVVVLPGGNL GAQNLSESPM VKEILKEQES RKGLIAAICA GPTALLAHEV GFGCKVTTHP LAKDKMMNGS HYSYSESRVE KDGLILTSRG PGTSFEFALA IVEALVGKDM ANQVKAPLVL KD.

    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.

    Park7 Mouse
  • View Data Sheet

    Name :

    M CSF Human

    Description:

    Macrophage-Colony Stimulating Factor Human Recombinant

    Macrophage Colony Stimulating Factor, CSF-1, Lanimostim, MCSF, MGC31930, M-CSF.

    Product # :

    CYT-308

    Price :

    Quantity :

    Shipping Method :

    Room Temp Icon

    Shipped at Room temp

    Add To Cart

    More Info

    • description
    • source
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    • Citations

    Description

    Macrophage Colony Stimulating Factor Human Recombinant produced in E.coli is a disulfide linked homodimer, non-glycosylated, polypeptide chain containing 2 x 159 amino acids and having a total molecular mass of 37.1 KD. MCSF is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The MCSF protein was lyophilized with 10mM sodium Phosphate, pH-8.0 & 50mM NaCl.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Biological Activity

    The ED50, calculated by the dose-dependent stimulation of the proliferation of murine M-NFS-60 indicator cells was found to be 1.15ng/ml corresponding to a specific activity of 8.7x105 Units/mg.

    Citations

    More Info

    • Introduction

      Granulocyte/Macrophage Colony-Stimulating Factors are cytokines that act in hematopoiesis by controlling the production, differentiation, and function of 2 related white cell populations of the blood, the granulocytes and the monocytes-macrophages. MCSF induces cells of the monocyte/macrophage lineage. MCSF plays a role in immunological defenses, bone metabolism, lipoproteins clearance, fertility and pregnancy.

    • Synonyms

      Macrophage Colony Stimulating Factor, CSF-1, Lanimostim, MCSF, MGC31930, M-CSF.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Amino Acid Sequence

      MEEVSEYCSH MIGSGHLQSL QRLIDSQMET SCQITFEFVD QEQLKDPVCY LKKAFLLVQD IMEDTMRFRD NTPNAIAIVQ LQELSLRLKS CFTKDYEEHD KACVRTFYET PLQLLEKVKN VFNETKNLLD KDWNIFSKNC NNSFAECSSQ GHERQSEGS.

    • Background

      M-CSF (Macrophage-Colony Stimulating Factor) Human Recombinant: Unraveling Its Role in Macrophage Biology and Beyond

      Abstract:

      M-CSF (Macrophage-Colony Stimulating Factor), also known as Lanimostim, MCSF, or MGC31930, is a crucial growth factor that regulates the development, proliferation, and function of macrophages.

      This research paper aims to provide a comprehensive analysis of the molecular characteristics, signaling pathways, and diverse physiological functions of M-CSF. Additionally, it explores the therapeutic implications of M-CSF in various diseases and disorders.

      Synonyms such as Lanimostim, MCSF, and MGC31930 associated with the protein are discussed throughout the paper to highlight their relevance in scientific literature.

      Introduction:

      1. M-CSF, also known as Lanimostim, MCSF, or MGC31930, is a growth factor that plays a critical role in the regulation of macrophage biology. This section introduces M-CSF and its synonyms, highlighting their significance and relevance in scientific research.

      Molecular Characteristics of M-CSF:

      1. This section explores the molecular characteristics of M-CSF, including its primary amino acid sequence, protein structure, and post-translational modifications. The importance of these factors in determining M-CSF's biological activity and receptor binding is discussed.

      Signaling Pathways Activated by M-CSF:

      1. M-CSF activates specific signaling pathways upon binding to its receptor, leading to diverse cellular responses. This section focuses on the activation of the MAPK/ERK and PI3K/Akt pathways. The downstream effectors and transcriptional regulators involved in mediating M-CSF's cellular responses are also discussed.

      Physiological Functions of M-CSF:

      1. M-CSF plays critical roles in various physiological processes, particularly in macrophage development, survival, polarization, and immune regulation. This section provides an in-depth analysis of M-CSF's contributions to these processes, emphasizing its role in hematopoiesis, tissue homeostasis, wound healing, and host defense.

      Therapeutic Implications of M-CSF:

      1. The unique properties of M-CSF make it a promising therapeutic candidate for various diseases and disorders. This section discusses the potential applications of M-CSF in immunotherapy, tissue regeneration, cancer treatment, and autoimmune diseases. The challenges and future directions in utilizing M-CSF as a therapeutic agent are also explored.

      M-CSF in Disease Pathogenesis:

      1. M-CSF dysregulation is implicated in the pathogenesis of several diseases, including cancer, inflammation, and bone disorders. This section examines the role of M-CSF in promoting tumor progression, macrophage-mediated inflammation, osteoclast differentiation, and metabolic diseases. The therapeutic implications and targeting of M-CSF in disease management are also discussed.

      Conclusion:

      1. M-CSF, also known as Lanimostim, MCSF, or MGC31930, is a critical growth factor involved in macrophage biology and disease pathogenesis. Understanding the molecular characteristics, signaling pathways, and physiological functions of M-CSF contributes to the exploration of its therapeutic potential in various disorders.

    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.

    M Csf Human
  • View Data Sheet

    Name :

    RB1 Human

    Description:

    Retinoblastoma Associated Protein Human Recombinant

    RB, OSRC, RB-1, RB1, p105-Rb, OSTEOSARCOMA, RETINOBLASTOMA-RELATED,PP110, Retinoblastoma-associated protein.

    Product # :

    PRO-584

    Price :

    Quantity :

    Shipping Method :

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    Shipped at Room temp

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    • description
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    Description

    Retinoblastoma Human Recombinant fused with 6X His tag produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 146 amino acids and having a molecular mass of 16.5 kDa.The Retinoblastoma is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The RB1 was lyophilized from 1xPBS 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

      Retinoblastoma (RB) is an embryonic malignant neoplasm of retinal origin. It almost always presents in early childhood and is often bilateral. Spontaneous regression ('cure') occurs in some cases. Retinoblastoma acts as a regulator of other genes and forms a complex with adenovirus e1a and with sv40 large t antigen. Retinoblastoma acts as a tumor suppressor and modulats functionally certain cellular proteins with which t and e1a compete for pocket binding. Retinoblastoma is potent inhibitor of e2f-mediated trans-activation, recruits and targets histone methyltransferase suv39h1 leading to epigenetic transcriptional repression, inhibits the intrinsic kinase activity of taf1.

    • Synonyms

      RB, OSRC, RB-1, RB1, p105-Rb, OSTEOSARCOMA, RETINOBLASTOMA-RELATED,PP110, Retinoblastoma-associated protein.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Amino Acid Sequence

      MASFPSSPLRIPGGNIYISPLKSPYKISEGLPTPTKMTPRSRILVSIGESFG
      TSEKFQKINQMVCNSDRVLKRSAEGSNPPKPLKKLRFDIEGSDEADGSK
      HLPGESKFQQKLAEMTSTRTRMQKQKMNDSMDTSNKEEKHHHHHH.

    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.

    Rb1 Human
  • View Data Sheet

    Name :

    AsnRS

    Description:

    Asparagine tRNA Synthetase Brugia Malayi Recombinant

    Asparagine--tRNA ligase, cytoplasmic (EC:6.1.1.22), Asparaginyl-tRNA synthetase, AsnRS, Potentially protective 63 kDa antigen.

    Product # :

    ENZ-941

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    Description

    AsnRS Brugia Malayi Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 568 amino acids (including a 6xHis Tag at N-terminus) and having a molecular mass of 64.5kDa.The AsnRS is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    AsnRS 0.2µm filtered solution containing 20mM HEPES, pH7.4, 100mM NaCl, 5mM MgCl2, 5mM b-Mercaptoethanol and 10 % Glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      The AsnRS enzyme is a member of the ligases family, specifically those forming carbon-oxygen bonds in aminoacyl-tRNA and related compounds. An asparagine-tRNA ligase is an enzyme which catalyzes the chemical reaction: ATP + L-asparagine + tRNAAsn AMP + diphosphate + L-asparaginyl-tRNAAsn. The three substrates of the AsnRS enzyme are ATP, L-asparagine, and tRNA(Asn), whereas its three products are AMP, diphosphate, and L-asparaginyl-tRNA(Asn).

    • Synonyms

      Asparagine--tRNA ligase, cytoplasmic (EC:6.1.1.22), Asparaginyl-tRNA synthetase, AsnRS, Potentially protective 63 kDa antigen.

    • 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 MTVYICPETG DDGNDGSELK PLRTLYQAMI ITKSSKGDFL IRTKKDGKQV WEAASKTALK KSWKRYEQEM LKNEKVAAKM LEKDATEVGV KAALEEAKKV QIELDTSLSY ITGVKIRDLV KHRNERVCIK GWIHRMRRQG KSLMFFILRD GTGFLQVLLM DKLCQTYDAL TVNTECTVEI YGAIKEVPEG KEAPNGHELI ADFWKIIGNA PSGGIDNVLN EEASVDKMLD NRHLVIRGEN AAALLRLRAA ATRAMREHFY NAGYVEVAPP TLVQTQVEGG STLFNLDYFG EQSFLTQSSQ LYLETCIPTL GDVFLHCSVL QGGKISHSST LAEYAHVEAE CPFITLDDLM EKIEELVCDT VDRLLADEEA KKLLEHINPK FQPPERPFLR MEYKDAIKWL QEHNVENEFG NTFTYGEDIA EAAERFMTDT INKPILLNRF PSEIKAFYMQ RDAKDNTLTE SVDLLMPGVG EIVGGSMRIW KFDELSKAFK NVEIDPKPYY WYLDQRLYGT CPHGGYGLGL ERFICWLTNT NHIRDVCLYP RFVGRCVP.

    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.

    Asnrs
  • View Data Sheet

    Name :

    EGLN3 Human

    Description:

    Egl Nine Homolog 3 Human Recombinant

    Egl nine homolog 3 (C. elegans), Hypoxia-inducible factor prolyl hydroxylase 3, Prolyl hydroxylase domain-containing protein 3, HIF-PH3, PHD3, egl nine-like protein 3 isoform, HIF prolyl hydroxylase 3, EC 1.14.11.29, HPH-1, HPH-3.

    Product # :

    PRO-1143

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    Description

    EGLN3 Human Recombinant produced in E. coli is a single polypeptide chain containing 263 amino acids (1-239) and having a molecular mass of 29.8 kDa.EGLN3 is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    The EGLN3 solution (0.25mg/1ml) contains 20mM Tris-HCl buffer (pH 8.0), 300mM NaCl, 5mM DTT, 2mM EDTA and 50% glycerol.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      Egl Nine Homolog 3 (EGLN3) belongs to the EGLN family of prolyl hydroxylases. EGLN3 catalyzes hydroxylation of the ? subunit of hypoxia-inducible factor-?, which targets hypoxia-inducible factor-? for ubiquitination by a ubiquitin ligase complex containing the von Hippel-Lindau (VHL) tumor suppressor. EGLN3 is the most significant isozyme in limiting physiological activation of HIFs (especially HIF2A) in hypoxia. EGLN3 is activated in cardiovascular cells and Hela cells after exposure to hypoxia. In addition, EGLN3 hydroxylates PKM2 in hypoxia, thus limiting glycolysis. Under normoxia, EGLN3 hydroxylates and regulates the stability of ADRB2. EGLN3 is inhibited by polynitrogen compounds possibly by chelation to Fe2+ ions.

    • Synonyms

      Egl nine homolog 3 (C. elegans), Hypoxia-inducible factor prolyl hydroxylase 3, Prolyl hydroxylase domain-containing protein 3, HIF-PH3, PHD3, egl nine-like protein 3 isoform, HIF prolyl hydroxylase 3, EC 1.14.11.29, HPH-1, HPH-3.

    • 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 MGSHMPLGHI MRLDLEKIAL EYIVPCLHEV GFCYLDNFLG EVVGDCVLER VKQLHCTGAL RDGQLAGPRA GVSKRHLRGD QITWIGGNEE GCEAISFLLS LIDRLVLYCG SRLGKYYVKE RSKAMVACYP GNGTGYVRHV DNPNGDGRCI TCIYYLNKNW DAKLHGGILR IFPEGKSFIA DVEPIFDRLL FFWSDRRNPH EVQPSYATRY AMTVWYFDAE ERAEAKKKFR NLTRKTESAL TED

    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.

    Egln3 Human
  • View Data Sheet

    Name :

    IL11RA Rat

    Description:

    Interleukin 11 Receptor Subunit Alpha Rat Recombinant

    Interleukin-11 receptor subunit alpha, IL-11 receptor subunit alpha, IL-11R subunit alpha, IL-11R-alpha, IL-11RA, Il11ra1.

    Product # :

    CYT-990

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    Description

    Interleukin 11 Receptor Subunit Alpha Rat Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 356 amino acids (24-371a.a.) and having a molecular mass of 39.2kDa (Molecular size on SDS-PAGE will appear at approximately 40-57kDa).IL11RA is fused with an 8 amino acids His tag at C-Terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    IL11RA protein solution (0.25mg/ml) contains Phosphate Buffered Saline (pH7.4) and 10% glycerol.

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

    SDS-PAGE

    IL11RA Rat - Product image 1

    Citations

    More Info

    • Introduction

      Interleukin 11 Receptor Subunit Alpha (IL11RA) which belongs to the hematopoietic cytokine receptor family is a receptor for interleukin-11. Interleukin 11 is a stromal cell-derived cytokine which is a member of a family of pleiotropic and redundant cytokines that employ the gp130 transducing subunit in their high affinity receptors. This specific receptor is quite similar to ciliary neurotrophic factor, since both contain an extracellular region with a two-domain structure composed of an immunoglobulin-like domain and a cytokine receptor-like domain. The receptor systems for IL6, LIF, OSM, CNTF, IL11 and CT1 are able to utilize IL6ST for initiating signal transmission. The IL11/IL11RA/IL6ST complex is involved in the control of proliferation and/or differentiation of skeletogenic progenitor or additional mesenchymal cells.

    • Synonyms

      Interleukin-11 receptor subunit alpha, IL-11 receptor subunit alpha, IL-11R subunit alpha, IL-11R-alpha, IL-11RA, Il11ra1.

    • 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

      TPCPQAWGPP GVQYGQPGRP VMLCCPGVNA GTPVSWFRDG DSRLLQGPDS GLGHRLVLAQ VDSRDEGTYV CRTLDGVFGG MVTLKLGSPP ARPEVSCQAV DYENFSCTWS PGRVSGLPTR YLTSYRKKTL PGAESQRESP STGPWPCPQD PLEASRCVVH GAEFWSEYRI NVTEVNPLGA STCLLDVRLQ RILRPDPPQG LRVESVPGYP RRLHASWTYP ASWRRQPHFL LKFRLQYRPA QHPAWSTVEP IGLEELITDA VAGLPHAVRV SARDFLDAGT WSAWSPEAWG TPSTGPLRDE VPDGSRGHEQ KLEAAAQEDS PAPPSPSLQP DPRPLDHRDP LEQVAVLAVE HHHHHH.

    • Background

      What is the molecular weight/Mw of IL11RA RAT Protein?
      IL11RA RAT Protein has a total Mw of 39.2kDa.

      What is the source or expression system of IL11RA RAT Protein?
      Sf9, Baculovirus cells.

      What is the Purity of IL11RA RAT Protein?
      IL11RA RAT Protein is >85% pure as determined by SDS-PAGE.

      What is the Biological Activity of IL11RA RAT Protein?
      The biological functionality of IL11RA RAT Protein will be determined in the future.

      What is the amino acid sequence of IL11RA RAT Protein?
      TPCPQAWGPP GVQYGQPGRP VMLCCPGVNA GTPVSWFRDG DSRLLQGPDS GLGHRLVLAQ VDSRDEGTYV CRTLDGVFGG MVTLKLGSPP ARPEVSCQAV DYENFSCTWS PGRVSGLPTR YLTSYRKKTL PGAESQRESP STGPWPCPQD PLEASRCVVH GAEFWSEYRI NVTEVNPLGA STCLLDVRLQ RILRPDPPQG LRVESVPGYP RRLHASWTYP ASWRRQPHFL LKFRLQYRPA QHPAWSTVEP IGLEELITDA VAGLPHAVRV SARDFLDAGT WSAWSPEAWG TPSTGPLRDE VPDGSRGHEQ KLEAAAQEDS PAPPSPSLQP DPRPLDHRDP LEQVAVLAVE HHHHHH.
      What applications can IL11RA RAT Protein be used in?
      IL11RA RAT Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for IL11RA RAT Protein?
      The endotoxin level is minimal, IL11RA RAT Protein was purified using conventional chromatography techniques.

      Who supplies recombinant IL11RA RAT 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 IL11RA RAT?
      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.

    Il11Ra Rat
  • View Data Sheet

    Name :

    CAMP Human

    Description:

    Cathelicidin Antimicrobial Peptide Human Recombinant

    CAP-18, CAP18, CRAMP, FALL-39, FALL39, HSD26, LL37, 18 kDa cationic antimicrobial protein, FALL-39 peptide antibiotic, Cathelicidin antimicrobial peptide.

    Product # :

    PRO-1405

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    Description

    CAMP Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 163 amino acids (34-173 a.a.) and having a molecular mass of 18.4kDa.CAMP is fused to a 23 amino acid His-tag at N-terminus.

    Source

    Escherichia Coli.

    Formulation

    CAMP protein solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.4M UREA and 10% glycerol.

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      CAMP belongs to the antimicrobial peptide family, contains highly conserved N-terminal signal peptide, a cathelin domain and a structurally variable cationic antimicrobial peptide that produced by extracellular proteolysis from the C-terminus. CAMP has numerous functions besides the antimicrobial activity such as: cell chemotaxis, immune mediator induction and inflammatory response regulation.

    • Synonyms

      CAP-18, CAP18, CRAMP, FALL-39, FALL39, HSD26, LL37, 18 kDa cationic antimicrobial protein, FALL-39 peptide antibiotic, Cathelicidin antimicrobial peptide.

    • 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 MGSQVLSYKE AVLRAIDGIN QRSSDANLYR LLDLDPRPTM DGDPDTPKPV SFTVKETVCP RTTQQSPEDC DFKKDGLVKR CMGTVTLNQA RGSFDISCDK DNKRFALLGD FFRKSKEKIG KEFKRIVQRI KDFLRNLVPR TES.

    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.

    Camp Human
  • View Data Sheet

    Name :

    TNFRSF10D Human

    Description:

    TRAIL Receptor-4 Human Recombinant

    Tumor necrosis factor receptor superfamily member 10D, CD264, DCR2, TRAIL-R4, TRAILR4, TRUNDD, Decoy receptor 2, TNF-related apoptosis-inducing ligand receptor 4, TRAIL receptor 4, TRAIL receptor with a truncated death domain.          

    Product # :

    CYT-1045

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    Description

    TNFRSF10D produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 395 amino acids (56-211a.a.) and having a molecular mass of 73.8kDa. (Molecular size on SDS-PAGE will appear at approximately 40-57kDa).TNFRSF10D is expressed with a 239 amino acid hIgG-His tag at C-Terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    TNFRSF10D protein solution (0.5mg/ml) contains phosphate buffered saline (pH7.4) and 10% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    Biological Activity

    Measured in a neutralizing assay using Jurkat human T lymphocyte. The ED50 for this effect is less or equal to 10 ng/ml in the presence of 2ng/ml TRAIL.

     

    Citations

    More Info

    • Introduction

      TRAIL Receptor-4 Human Recombinant or TNFRSF10D, is part of the TNF-receptor superfamily. TNFRSF10D has atruncated cytoplasmic death domai , an extracellular TRAIL-binding domain and a transmembrane domain. The protein can prevent from TRAIL-mediated apoptosis on cells with TRAIL R1 and/or TRAIL R2.

    • Synonyms

      Tumor necrosis factor receptor superfamily member 10D, CD264, DCR2, TRAIL-R4, TRAILR4, TRUNDD, Decoy receptor 2, TNF-related apoptosis-inducing ligand receptor 4, TRAIL receptor 4, TRAIL receptor with a truncated death domain.

    • 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

      ATIPRQDEVP QQTVAPQQQR RSLKEEECPA GSHRSEYTGA CNPCTEGVDY TIASNNLPSC LLCTVCKSGQ TNKSSCTTTR DTVCQCEKGS FQDKNSPEMC RTCRTGCPRG MVKVSNCTPR SDIKCKNESA ASSTGKTPAA EETVTTILGM LASPYHVEPK SCDKTHTCPP CPAPELLGGP
      SVFLFPPKPK DTLMISRTPE VTCVVVDVSH EDPEVKFNWY VDGVEVHNAK TKPREEQYNS TYRVVSVLTV LHQDWLNGKE YKCKVSNKAL PAPIEKTISK AKGQPREPQV YTLPPSRDEL TKNQVSLTCL VKGFYPSDIA VEWESNGQPE NNYKTTPPVL DSDGSFFLYS KLTVDKSRWQ
      QGNVFSCSVM HEALHNHYTQ KSLSLSPGKH HHHHH.

    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.

    Tnfrsf10D
  • View Data Sheet

    Name :

    LCN2 Rat

    Description:

    Neutrophil Gelatinase Associated Lipocalin/Lipocalin-2 Rat Recombinant

    Neutrophil gelatinase-associated lipocalin, NGAL, Alpha-2-microglobulin-related protein, Alpha-2U globulin-related protein, Lipocalin-2, Siderocalin LCN2, p25.

    Product # :

    ENZ-920

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    Description

    LCN2 Rat Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 201 amino acids (21-198 a.a) and having a molecular mass of 22.9kDa. LCN2 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    LCN2 protein solution (0.25mg/ml) containing Phosphate Buffered Saline (pH7.4) and 20% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      Lipocalin-2 also called Neutrophil Gelatinase Associated Lipocalin (NGAL) belongs to a family of lipocans which include 25 proteins (including a1-microglobulin and b-lactoglobulin), which are characterized by their ability to bind small lipophilic substances in their hydrophobic core. They thereby serve as transporters of substances like retinal, biliverdins & prostaglandins. There are indications that NGAL is involved in modulation of the inflammatory response and is found in the plasma of patients after stroke.

    • Synonyms

      Neutrophil gelatinase-associated lipocalin, NGAL, Alpha-2-microglobulin-related protein, Alpha-2U globulin-related protein, Lipocalin-2, Siderocalin LCN2, p25.

    • 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 MGSQDSTQNL IPAPPLISVP LQPGFWTERF QGRWFVVGLA ANAVQKERQS RFTMYSTIYE LQEDNSYNVT SILVRGQGCR YWIRTFVPSS RPGQFTLGNI HSYPQIQSYD VQVADTDYDQ FAMVFFQKTS ENKQYFKVTL YGRTKGLSDE LKERFVSFAK SLGLKDNNIV FSVPTDQCID N.

    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.

    Lcn2 Rat
  • View Data Sheet

    Name :

    PTPN7 Human

    Description:

    Protein Tyrosine Phosphatase Non Receptor Type-7 Human Recombinant

    Protein tyrosine phosphatase non-receptor type 7, HEPTP, LC-PTP, Hematopoietic protein-tyrosine phosphatase, Protein-tyrosine phosphatase LC-PTP, PTPNI, LPTP, BPTP-4, dual specificity phosphatase 1, protein-tyrosine phosphatase non-receptor-type, stress induced, EC 3.1.3.48.

    Product # :

    PKA-025

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    Description

    PTPN7 Human Recombinant produced in E. coli is a single polypeptide chain containing 384 amino acids (1-360) and having a molecular mass of 43.1kDa.PTPN7 is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    The PTPN7 solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 100mM NaCl, 1mM DTT and 20% glycerol.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      PTPN7 performs specifically on tyrosine-phosphorylated MAPK1. PTPN7 takes part in the regulation of signal transduction and T and B-lymphocyte development.

    • Synonyms

      Protein tyrosine phosphatase non-receptor type 7, HEPTP, LC-PTP, Hematopoietic protein-tyrosine phosphatase, Protein-tyrosine phosphatase LC-PTP, PTPNI, LPTP, BPTP-4, dual specificity phosphatase 1, protein-tyrosine phosphatase non-receptor-type, stress induced, EC 3.1.3.48.

    • 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 MGSHMVQAHG GRSRAQPLTL SLGAAMTQPP PEKTPAKKHV RLQERRGSNV ALMLDVRSLG AVEPICSVNT PREVTLHFLR TAGHPLTRWA LQRQPPSPKQ LEEEFLKIPS NFVSPEDLDI PGHASKDRYK TILPNPQSRV CLGRAQSQED GDYINANYIR GYDGKEKVYI ATQGPMPNTV SDFWEMVWQE EVSLIVMLTQ LREGKEKCVH YWPTEEETYG PFQIRIQDMK ECPEYTVRQL TIQYQEERRS VKHILFSAWP DHQTPESAGP LLRLVAEVEE SPETAAHPGP IVVHCSAGIG RTGCFIATRI GCQQLKARGE VDILGIVCQL RLDRGGMIQT AEQYQFLHHT LALYAGQLPE EPSP

    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.

    Ptpn7 Human
  • View Data Sheet

    Name :

    NUCB2 Human

    Description:

    Nucleobindin-2 Human Recombinant

    Nucleobindin-2, DNA-binding protein NEFA, Gastric cancer antigen Zg4, NUCB2, NEFA, Nesfatin.

    Product # :

    PRO-492

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    Description

    The Recombinant Human NUCB2 (Nesfatin) produced in E.coli has a molecular mass of 9.7kDa containing 82 amino acid residues of the human NUCB2.

    Source

    Escherichia Coli.

    Formulation

    The NUCB2 protein was lyophilized from a 0.2µm filtered concentrated solution in 1×PBS, 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

      Nucleobindin-2 (also known as NUCB2 or Nesfatin) is a EF-hand calcium-binding protein. Nucleobindin-2 takes part in calcium homeostasis and is a multifunctional protein that interacts with Ca(2+) nucleic acids & various regulatory proteins in different signaling pathways. NUCB2 (Nesfatin) is localized in neuronal perikarya and dendrites of mouse brain.

    • Synonyms

      Nucleobindin-2, DNA-binding protein NEFA, Gastric cancer antigen Zg4, NUCB2, NEFA, Nesfatin.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized NUCB2 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution NUCB2 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 NUCB2 in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      VPIDIDKTKV QNIHPVESAK IEPPDTGLYY DEYLKQVIDV LETDKHFREK LQKADIEEIK SGRLSKELDL VSHHVRTKLD EL.

    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.

    Nucb2 Human
  • View Data Sheet

    Name :

    KRT8 Antibody

    Description:

    Cytokeratin 8, Mouse Anti Human

    Keratin type II cytoskeletal 8, Cytokeratin-8, CK-8, Keratin-8, K8, KRT8, CYK8, KO, CK8, K2C8, CARD2.

    Product # :

    ANT-470

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    Formulation

    1mg/ml containing PBS, pH-7.4, 10% Glycerol and 0.02% Sodium Azide.

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    • Introduction

      Cytokeratin 8 (KRT8) belongs to the type II keratin family clustered on the long arm of chromosome 12. Type I and type II keratins heteropolymerize to form intermediate-sized filaments in the cytoplasm of epithelial cells. KRT8 typically dimerizes with keratin 18 to form an intermediate filament in simple single-layered epithelial cells. KRT8 has a role in retaining cellular structural integrity and also functions in signal transduction and cellular differentiation. KRT8 gene mutations cause cryptogenic cirrhosis.

    • Synonyms

      Keratin type II cytoskeletal 8, Cytokeratin-8, CK-8, Keratin-8, K8, KRT8, CYK8, KO, CK8, K2C8, CARD2.

    • Physical Appearance

      Sterile filtered colorless solution.

    • Immunogen

      Anti-human KRT8 mAb, clone PAT3D11A, is derived from hybridization of mouse F0 myeloma cells with spleen cells from BALB/c mice immunized with a recombinant human KRT8 protein purified from E. coli.

    • Ig Subclass

      Mouse IgG3 heavy chain and Kappa light chain.

    • Clone

      PAT3D11A.

    • Applications

      The antibody has been tested by ELISA, Western blot analysis to assure specificity and reactivity. Since application varies, however, each investigation should be titrated by the reagent to obtain optimal results. Recommended starting dilution is 1:1000.

    • Type

      Mouse Anti Human Monoclonal.

    • Storage Procedures

      For periods up to 1 month store at 4°C, for longer periods of time, store at -20°C. Prevent freeze thaw cycles.

    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.

    Krt8 Antibody
  • View Data Sheet

    Name :

    HAO1 Mouse

    Description:

    Hydroxyacid Oxidase 1 Mouse Recombinant

    (S)-2-hydroxy-acid oxidase; EC 1.1.3.15, Glycolate oxidase, GOX, GOX1MGC142227;GOXMGC142225, HAO1, HAO-1, HAOX1, hydroxyacid oxidase (glycolate oxidase) 1, hydroxyacid oxidase 1, Hydroxyacid Oxidase1, Hydroxyacid Oxidase-1.

    Product # :

    ENZ-1104

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    Description

    HAO1 Mouse Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 393 amino acids (1-370) and having a molecular mass of 43.4 kDa.HAO1 is fused to a 23 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    HAO1 protein (1mg/ml) is containing Phosphate Buffered Saline (pH 7.4) and 10% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    Biological Activity

    Specific activity is > 1,000 pmol/min/ug, and defined as the amount of enzyme that oxidize glyoxylate at pH 8.0 at 25C.

    Citations

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    • Introduction

      Hydroxyacid Oxidase 1 (HAO1) is a part of the superfamily of the alpha hydroxy acid oxidases (HAO) enzymes. HAO1 catalyses the FMN mediated oxidation of glycolate to glyoxylate and glyoxylate to oxalate by reducing oxygen to hydrogen peroxide. HAO1 is expressed mainly in the liver and pancreas and is most active on twocarbon substrates such as glycolate. HAO1 isthe main cause of hyperoxaluria, a disorder in which large deposits of calcium oxalate form kidney stones.

    • Synonyms

      (S)-2-hydroxy-acid oxidase; EC 1.1.3.15, Glycolate oxidase, GOX, GOX1MGC142227;
      GOXMGC142225, HAO1, HAO-1, HAOX1, hydroxyacid oxidase (glycolate oxidase) 1, hydroxyacid oxidase 1, Hydroxyacid Oxidase1, Hydroxyacid Oxidase-1.

    • 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 MGSMLPRLVC ISDYEQHVRS VLQKSVYDYY RSGANDQETL ADNIQAFSRW KLYPRMLRNV ADIDLSTSVL GQRVSMPICV GATAMQCMAH VDGELATVRA CQTMGTGMML SSWATSSIEE VAEAGPEALR WMQLYIYKDR EISRQIVKRA EKQGYKAIFV TVDTPYLGNR IDDVRNRFKL PPQLRMKNFE TNDLAFSPKG NFGDNSGLAE YVAQAIDPSL SWDDITWLRR LTSLPIVVKG ILRGDDAKEA VKHGVDGILV SNHGARQLDG VPATIDVLPE IVEAVEGKVE VFLDGGVRKG TDVLKALALG AKAVFVGRPI IWGLAFQGEK GVQDVLEILK EEFRLAMALS GCQNVKVIDK TLVRKNPLAV SKI.

    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.

    Hao1 Mouse
  • View Data Sheet

    Name :

    TNF alpha human

    Description:

    Tumor Necrosis Factor-Alpha Human Recombinant

    TNF-alpha, Tumor necrosis factor ligand superfamily member 2, TNF-a, Cachectin, DIF, TNFA, TNFSF2.

    Product # :

    CYT-223

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    Description

    Tumor Necrosis Factor-a Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 158 amino acids (157 a.a. of the mature human TNF-alpha and an N-terminal methionine) and having a molecular mass of 17.5kDa. The TNF-alpha is purified by standard chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    TNF-a Human was lyophilized from a concentrated 1mg/ml solution containing 20mM PB, pH-7.2, and 100mM NaCl.

    Purity

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

    Biological Activity

    The Specific Activity is >5.0×107 IU/mg as determined by the cytolysis of murine L929 cells in the presence of Actinomycin D.

    Citations

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    • Introduction

      Tumor necrosis factor is a cytokine involved in systemic inflammation and is a member of a group of cytokines that all stimulate the acute phase reaction. TNF is mainly secreted by macrophages.
      TNF causes apoptotic cell death, cellular proliferation, differentiation, inflammation, tumorigenesis and viral replication, TNF is also involved in lipid metabolism, and coagulation. TNF's primary role is in the regulation of immune cells.
      Dysregulation and, in particular, overproduction of TNF have been implicated in a variety of human diseases- autoimmune diseases, INS resistance, and cancer.

    • Synonyms

      TNF-alpha, Tumor necrosis factor ligand superfamily member 2, TNF-a, Cachectin, DIF, TNFA, TNFSF2.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Amino Acid Sequence

      MVRSSSRTPS DKPVAHVVAN PQAEGQLQWL NRRANALLAN GVELRDNQLV VPSEGLYLIY SQVLFKGQGC PSTHVLLTHT ISRIAVSYQT KVNLLSAIKS PCQRETPEGA E AKPWYEPIY LGGVFQLEKG DRLSAEINRP DYLDFAESGQ VYFGIIAL.

    • Background

      TNF Alpha Human: An Overview of Its Role and Importance in Immunology

      TNF alpha human, also known as Tumor Necrosis Factor-alpha, is a critical cytokine in the immune system. Macrophages mainly produce this protein, and it plays a key role in inflammation and the acute phase reaction.

      This protein is involved in various cellular functions, including cell death, differentiation, proliferation, and immune regulation.

      Production and Properties

      Tumor Necrosis Factor-alpha is produced recombinantly in E. coli and consists of a single, non-glycosylated polypeptide chain. It includes 157 amino acids of the mature human TNF-alpha and an N-terminal methionine, resulting in a molecular mass of approximately 17.5 kDa.

      Furthermore, the protein is purified through standard chromatographic techniques to ensure high purity and biological activity.

      Solubility and Usage

      The lyophilized form of TNF appears as a sterile, white powder. It is recommended to reconstitute this powder in sterile water to achieve a solution of no less than 100µg/ml.

      This solution can then be further diluted for various experimental applications. TNF alpha is used extensively in research, particularly for studying its effects on cell signaling and immune response.

      Storage and Stability

      For long-term storage, TNF should be kept desiccated below -18°C. Once reconstituted, it should be used within a week if stored at 4°C or kept below -18°C for future use. Avoiding freeze-thaw cycles is crucial to maintain the protein's functionality.

      Biological Role and Implications

      TNF alpha human is involved in the regulation of immune cells and is known for its role in inflammatory processes.

      Dysregulation of TNF alpha production is linked to various diseases, such as autoimmune disorders, insulin resistance, and cancer. It is also a target for therapeutic interventions, particularly in conditions like rheumatoid arthritis and inflammatory bowel disease.

      Mechanism of Action

      TNF alpha can induce fever, apoptotic cell death, and can inhibit tumorigenesis and viral replication. Moreover, it is a potent mediator of the acute phase reaction, which influences the activity of various cells involved in systemic inflammation.

      Research and Clinical Importance

      Scientific research on TNF has provided insights into its complex role in disease mechanisms. Its interaction with receptors such as TNFRSF1A underscores its multifaceted effects across different organ systems, from liver function to brain activity.

      Ongoing studies continue to explore its therapeutic potential, especially how it can be modulated to treat diseases without harmful side effects.

      In essence, TNF alpha human is a versatile and powerful component of the immune system, important for both health and disease. Understanding its pathways and functions helps scientists develop better treatments for various inflammatory and autoimmune diseases.



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

    Tnf Alpha Human
  • View Data Sheet

    Name :

    KRT18 Antibody

    Description:

    Cytokeratin 18, Mouse Anti Human

    Keratin type I cytoskeletal 18, Cytokeratin-18, CK-18, Keratin-18, K18, KRT18,CYK18,Cell proliferation-inducing gene 46 protein.

    Product # :

    ANT-025

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    Formulation

    1mg/ml containing PBS, pH-7.4, & 0.1% Sodium Azide.

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    • Introduction

      KRT18 encodes the type I intermediate filament chain keratin 18. Keratin 18, together with its filament partner keratin 8, are perhaps the most commonly found members of the intermediate filament gene family. They are expressed in single layer epithelial tissues of the body. Mutations in this gene have been linked to cryptogenic cirrhosis. Two transcript variants encoding the same protein have been found for this gene.

    • Synonyms

      Keratin type I cytoskeletal 18, Cytokeratin-18, CK-18, Keratin-18, K18, KRT18,CYK18,Cell proliferation-inducing gene 46 protein.

    • Physical Appearance

      Sterile filtered colorless solution.

    • Immunogen

      Anti-human KRT18 mAb, is derived from hybridization of mouse FO myeloma cells with spleen cells from BALB/c mice immunized with recombinant human KRT18 amino acids 79-430 purified from E. coli.

    • Ig Subclass

      Mouse IgG2b heavy chain and k light chain.

    • Clone

      PAT2G3AT.

    • Applications

      KRT18 antibody has been tested by ELISA, Western blot and Immunofluorescence analysis to assure specificity and reactivity. Since application varies, however, each investigation should be titrated by the reagent to obtain optimal results. Recommended dilution range for Western blot analysis and Immunofluorescence is 1:250 ~ 1000.
      Recommended starting dilution is 1:500.

    • Type

      Mouse Anti Human Monoclonal.

    • Storage Procedures

      For periods up to 1 month store at 4°C, for longer periods of time, store at -20°C. Prevent freeze thaw cycles.

    • Purification Method

      KRT18 antibody was purified from mouse ascitic fluids by protein-G affinity chromatography.

    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.

    Krt18 Antibody
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    Name :

    KRT23 Antibody

    Description:

    Cytokeratin 23, Mouse Anti Human

    Keratin, type I cytoskeletal 23, Cytokeratin-23, CK-23, Keratin-23, K23, KRT23, CK23, HAIK1.

    Product # :

    ANT-081

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    Formulation

    1mg/ml containing PBS, pH-7.4, & 0.1% Sodium Azide.

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    • Introduction

      Cytokeratin 23 (KRT23) is a 422 amino acid intermediate filament protein. The human KRT23 gene is found on chromosome 17q21.2. Type I cytokeratins consist of acidic proteins which are organized in pairs of heterotypic keratin chains. The cytokeratin proteins have an essential role in differentiation, plus tissue specialization and function, and epithelial cells structure maintenance. Cytokeratins are portrayed to be differentiation markers in a number of epithelial cancers.

    • Synonyms

      Keratin, type I cytoskeletal 23, Cytokeratin-23, CK-23, Keratin-23, K23, KRT23, CK23, HAIK1.

    • Immunogen

      Anti-human KRT23 mAb, is derived from hybridization of mouse FO myeloma cells with spleen cells from BALB/c mice immunized with recombinant human KRT23 amino acids 271-422 purified from E. coli.

    • Ig Subclass

      Mouse IgG1 heavy chain and k light chain.

    • Clone

      PAT2F6AT.

    • Applications

      KRT23 antibody has been tested by ELISA, Western blot analysis to assure specificity and reactivity. Since application varies, however, each investigation should be titrated by the reagent to obtain optimal results. Recommended dilution range for Western blot analysis is 1:500 ~ 1:3000.

    • Type

      Mouse Anti Human Monoclonal.

    • Storage Procedures

      For periods up to 1 month store at 4°C, for longer periods of time, store at -20°C. Prevent freeze thaw cycles.

    • Purification Method

      KRT23 antibody was purified from mouse ascitic fluids by protein-G affinity chromatography.

    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.

    Krt23 Antibody
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    Name :

    GSTT1 Antibody

    Description:

    Glutathione S-Transferase Theta-1, Mouse Anti Human

    Glutathione S-transferase theta-1, GST class-theta-1, Glutathione transferase T1-1, GSTT1.

    Product # :

    ANT-591

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    Formulation

    1mg/ml containing PBS, pH-7.4, 10% Glycerol and 0.02% Sodium Azide.

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    • Introduction

      GSTT1 belongs to a superfamily of proteins which catalyze the conjugation of reduced glutathione to a variety of electrophilic and hydrophobic compounds. GSTT1 is one of the GSTs’ four main classes: alpha, mu, pi and theta (which includes GSTT1 and GSTT2). GSTT1 is involved in activation and detoxification reactions and catalyzes the conjugation of industrial chemicals, such as epoxybutane, ethylene oxides, halomethane with glutathione. GSTT1 is found in erythrocytes, at low levels in the liver as well as in Clara and ciliated cells at the alveolar/bronchiolar junction in the lung. The GSTT1 gene is deficient in 38% of the population. The GSTTI enzyme deficiency might influence the individual risk for development of acquired aplastic anemia and acute myeloid leukemia. The presence or absence of the GSTT1 gene is concurrent with GSST1+ (the conjugator) and GSTT1- (the non-conjugator) phenotypes correspondingly. The GSTT1+ phenotype is able to catalyze the glutathione conjugation of dichloromethane. GSTT1-null genotypes are seen as having a higher risk of developing leukoplakia. Germline genetic polymorphism in GSTT1 is linked to breast cancer.

    • Synonyms

      Glutathione S-transferase theta-1, GST class-theta-1, Glutathione transferase T1-1, GSTT1.

    • Physical Appearance

      Sterile filtered colorless solution.

    • Immunogen

      Anti-human GSTT1 mAb, is derived from hybridization of mouse F0 myeloma cells with spleen cells from BALB/c mice immunized with recombinant human GSTT1 amino acids 1-240 purified from E. coli.

    • Ig Subclass

      Mouse IgG2b heavy chain and k light chain.

    • Clone

      PAT38D11AT.

    • Applications

      GSTT1 antibody has been tested by ELISA, Western blot analysis, ICC/IF and Flow cytometry to assure specificity and reactivity. Since application varies, however, each investigation should be titrated by the reagent to obtain optimal results.

    • Type

      Mouse Anti Human Monoclonal.

    • Storage Procedures

      For periods up to 1 month store at 4°C, for longer periods of time, store at -20°C. Prevent freeze thaw cycles.

    • Purification Method

      GSTT1 antibody was purified from mouse ascitic fluids by protein-A affinity chromatography.

    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.

    Gstt1 Antibody
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    Name :

    YWHAQ Antibody

    Description:

    Tyr-3/Trp- 5 Monooxygenase Activation Protein Theta, Mouse Anti Human

    14-3-3 theta, 14-3-3 tau, 14-3-3 T-cell, HS1, YWHAQ, 1C5, 14-3-3 Tau, Tyr-3/Trp- 5 Monooxygenase Activation Protein Theta.

    Product # :

    ANT-387

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    Formulation

    1mg/ml containing PBS, pH-7.4, 10% glycerol & 0.02% Sodium Azide.

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    • Introduction

      The 14-3-3 family of proteins plays a key regulatory role in signal transduction, checkpoint control, apoptotic and nutrient-sensing pathways. 14-3-3 proteins are highly conserved and ubiquitously expressed. There are at least seven isoforms, β, γ, ε, σ, ζ, τ and η that have been identified in mammals. The 14-3-3 tau, a subtype of the 14-3-3 family of proteins, was found in T Cells, brain and testes. This 14-3-3 tau is upregulated in patients with amyotrophic lateral sclerosis.

    • Synonyms

      14-3-3 theta, 14-3-3 tau, 14-3-3 T-cell, HS1, YWHAQ, 1C5, 14-3-3 Tau, Tyr-3/Trp- 5 Monooxygenase Activation Protein Theta.

    • Immunogen

      Anti-human YWHAQ mAb is derived from hybridization of mouse F0 myeloma cells with spleen cells from BALB/c mice immunized with recombinant human YWHAQ amino acids 1-245 purified from E. coli.

    • Ig Subclass

      Mouse IgG1 heavy chain and κ light chain.

    • Clone

      PAT1A1AT.

    • Applications

      YWHAQ antibody has been tested by ELISA and Western blot analysis to assure specificity and reactivity. Since application varies, however, each investigation should be titrated by the reagent to obtain optimal results. Recommended dilution range for Western blot analysis is 1:1000 ~ 2000. Recommended starting dilution is 1:1000.

    • Type

      Mouse Anti Human Monoclonal.

    • Storage Procedures

      For periods up to 1 month store at 4°C, for longer periods of time, store at -20°C. Prevent freeze thaw cycles.

    • Purification Method

      YWHAQ antibody was purified from mouse ascitic fluids by protein-G affinity chromatography.

    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.

    Ywhaq Antibody
  • View Data Sheet

    Name :

    CST3 Mouse

    Description:

    Cystatin-C Mouse Recombinant

    Post G-globulin, CST 3, CST3, Gamma-Trace, Cystatin 3, Amyloid Angiopathy and Cerebral Hemorrhage, Cystatin-C precursor, neuroendocrine basic polypeptide.

    Product # :

    PRO-597

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    Description

    Cystatin-C Murine Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 134 amino acids and having a molecular mass of 15kDa. The Mouse Cystatin-C is fused to His tag at N-Terminus.The Mouse Cystatin-C is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The sterile filtered concentrated (0.5mg/ml) protein solution was lyophilized with 20mM Tris & 50mM NaCl pH-7.5.

    Purity

    Greater than 95% as determined by SDS-PAGE.

    Citations

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    • 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

      Post G-globulin, CST 3, CST3, Gamma-Trace, Cystatin 3, Amyloid Angiopathy and Cerebral Hemorrhage, Cystatin-C precursor, neuroendocrine basic polypeptide.

    • Physical Appearance

      Sterile 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.

    • Solubility

      Add deionized water to a working concentration of 0.5mg/ml and let the lyophilized pellet dissolve completely.

    • Amino Acid Sequence

      MRGSHHHHHH GMASATPKQG PRMLGAPEEA DANEEGVRRA LDFAVSEYNK GSNDAYHSRA IQVVRARKQL VAGVNYFLDV EMGRTTCTKS QTNLTDCPFH DQPHLMRKAL CSFQIYSVPW KGTHSLTKFSCKNA.

    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.

    Cystatin C Mouse
  • View Data Sheet

    Name :

    S100A8 Human, His

    Description:

    S100 Calcium Binding Protein A8 Human Recombinant, His Tag

    Calgranulin A, MRP8, CAGA, CGLA, CFAG, Protein S100-A8, S100 calcium-binding protein A8, Migration inhibitory factor-related protein 8, MRP-8, p8, Cystic fibrosis antigen, Leukocyte L1 complex light chain, Calprotectin L1L subunit, Urinary stone protein band A, S100A8, MIF, NIF, L1Ag, CP-10, MA387, 60B8AG.

    Product # :

    PRO-150

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    Description

    The Recombinant Human S100A8 produced in E.coli has a molecular mass of 12.08kDa containing 103 amino acid residues of the human S100A8 and fused to a 10 a.a. His tag at N-terminus.

    Source

    Escherichia Coli.

    Formulation

    S100A8 was filtered (0.4µm) and lyophilized in 0.5mg/ml in 20mM Tris and 100mM NaCl, pH 7.5.

    Citations

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    • Introduction

      S100A8 is a part of the S100 family of proteins containing 2 EF-hand calcium-binding motifs. S100 proteins are localized in the cytoplasm and/or nucleus of a broad range of cells, and participate in the regulation of cellular processes such as cell cycle progression and differentiation. S100A8 plays a role in the inhibition of casein kinase and as a cytokine. S100A8 altered expression is related with cystic fibrosis disease. S100A8 is a calcium-binding protein that has antimicrobial activity against bacteria and fungi.S100A8 is crucial for resistance towards invasion by pathogenic bacteria. S100A8 up-regulates transcription of genes that are under the control of NF-kappa-B. S100A8 plays a role in the development of endotoxic shock in response to bacterial lipopolysaccharide. S100A8 endorses tubulin polymerization and promotes phagocyte migration and infiltration of granulocytes at sites of wounding. S100A8 takes part as a pro-inflammatory mediator in acute and chronic inflammation and up-regulates the release of IL8 and cell-surface expression of ICAM1.

    • Synonyms

      Calgranulin A, MRP8, CAGA, CGLA, CFAG, Protein S100-A8, S100 calcium-binding protein A8, Migration inhibitory factor-related protein 8, MRP-8, p8, Cystic fibrosis antigen, Leukocyte L1 complex light chain, Calprotectin L1L subunit, Urinary stone protein band A, S100A8, MIF, NIF, L1Ag, CP-10, MA387, 60B8AG.

    • 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 0.5 mg/ml and let the lyophilized pellet dissolve completely. Product is not sterile! Please filter the product by an appropriate sterile filter before using it in the cell culture.

    • Amino Acid Sequence

      MKHHHHHHAS MLTELEKALN SIIDVYHKYS LIKGNFHAVY RDDLKKLLET ECPQYIRKKG ADVWFKELDI NTDGAVNFQEMLTELEKALN SIIDVYHKYS LIKGNFHAVY RDDLKKLLET ECPQYIRKKG ADVWFKELDI NTDGAVNFQE FLILVIKMGV AAHKKSHEES HKE.

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    S100A8 Human His
  • View Data Sheet

    Name :

    SCGN Human

    Description:

    Secretagogin Human Recombinant

    SCGN, EF-hand calcium binding protein, Setagin, SEGN, CALBL, SECRET, DJ501N12.8, Secretagogin.

    Product # :

    PRO-599

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    Description

    SCGN Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 296 amino acids (1-276 a.a.) and having a molecular mass of 34.2kDa. SCGN is fused to a 20 amino acid His tag at N-terminus and purified by standard chromatography techniques.

    Source

    Escherichia Coli.

    Formulation

    SCGN His-Tag (1mg/ml) protein is supplied in 20mM Tris HCl pH-8, 1mM DTT, 0.1M NaCl and 10% glycerol.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      SCGN is a secreted calcium-binding protein which is found in the cytoplasm. It is related to calbindin D-28K and calretinin. Secretagogin is involved in KCL-stimulated calcium flux and cell proliferation.
      Secretagogin plays a role in human non-functional pituitary adenomas.

    • Synonyms

      SCGN, EF-hand calcium binding protein, Setagin, SEGN, CALBL, SECRET, DJ501N12.8, Secretagogin.

    • Physical Appearance

      Sterile Filtered colorless liquid formulation.

    • 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 MDSSREPTLG RLDAAGFWQV WQRFDADEKG YIEEKELDAF FLHMLMKLGT DDTVMKANLH KVKQQFMTTQ DASKDGRIRM KELAGMFLSE DENFLLLFRR ENPLDSSVEF MQIWRKYDAD SSGFISAAEL RNFLRDLFLH HKKAISEAKL EEYTGTMMKI FDRNKDGRLD LNDLARILAL QENFLLQFKM DACSTEERKR DFEKIFAYYD VSKTGALEGP EVDGFVKDMM ELVQPSISGV DLDKFREILL RHCDVNKDGK IQKSELALCL GLKINP.

    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.

    Scgn Human
  • View Data Sheet

    Name :

    HMGN1 Human

    Description:

    High-Mobility Group Nucleosome Binding Domain 1 Human Recombinant

    HMG14, GC104230, High-Mobility Group Nucleosome Binding Domain 1.

    Product # :

    PRO-821

    Price :

    Quantity :

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

    Description

    HMGN1 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 108 amino acids (1-100 a.a.) and having a molecular mass of 11.7 kDa. HMGN1 protein is fused to an 8 amino acid His-Tag at C-terminus and purified by standard chromatography.

    Source

    Escherichia Coli.

    Formulation

    HMGN1 protein solution (0.5mg/ml) containing 20mM Tris-HCl pH-8, 1mM DTT, 0.1M NaCl, 0.1mM PMSF & 20% glycerol.

    Purity

    Greater than 95% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      HMGN1 binds to the inner side of the nucleosomal DNA therefore changing the interaction between the DNA and the histone octamer. HMGN1 participates in the development which maintains transcribable genes in an exceptional chromatin conformation. HMGN1 inhibits the phosphorylation of nucleosomal histones H3 and H2A by RPS6KA5/MSK1 and RPS6KA3/RSK2.

    • Synonyms

      HMG14, GC104230, High-Mobility Group Nucleosome Binding Domain 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

      MPKRKVSSAE GAAKEEPKRR SARLSAKPPA KVEAKPKKAA AKDKSSDKKV QTKGKRGAKG KQAEVANQET KEDLPAENGE TKTEESPASD EAGEKEAKSD LEHHHHHH.

    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.

    Hmgn1 Human
  • View Data Sheet

    Name :

    DLST Human

    Description:

    Dihydrolipoamide S-Succinyltransferase Human Recombinant

    dihydrolipoamide S-succinyltransferase (E2 component of 2-oxo-glutarate complex), Dihydrolipoamide succinyltransferase component of 2-oxoglutarate dehydrogenase complex, component E2, DLST, E2K, OGDC-E2, EC 2.3.1.61, EC 2.3.1.

    Product # :

    ENZ-083

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    Quantity :

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    More Info

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

    Description

    DLST is a Full-length cDNA coding for the mature form of the human OGDC-E2 protein having a molecular mass of 42,301 Dalton (pH 6.3).DLST protein is fused to a hexa-histidine purification tag.

    Source

    Sf9 insect cells.

    Formulation

    DLST (0.74mg/ml) is supplied in 20mM HEPES buffer pH-8.0, 200mM NaCl and 20% glycerol.

    Purity

    DLST purity was found to be greater than 75% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      DLST catalyzes the general transformation of 2-oxoglutarate to succinyl-CoA and CO(2). DLST holds multiple copies of 3 enzymatic components: 2-oxoglutarate dehydrogenase (E1), dihydrolipoamide succinyltransferase (E2) and lipoamide dehydrogenase (E3).

    • Synonyms

      dihydrolipoamide S-succinyltransferase (E2 component of 2-oxo-glutarate complex), Dihydrolipoamide succinyltransferase component of 2-oxoglutarate dehydrogenase complex, component E2, DLST, E2K, OGDC-E2, EC 2.3.1.61, EC 2.3.1.

    • Stability

      Store DLST at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. Avoid multiple freeze-thaw cycles.

    • Immunological Functions

      1. DLST binds IgG-type human auto-antibodies. 2. Standard ELISA test (checkerboard analysis of positive/negative sera panels); immunodot test with positive/negative sera panels.

    • coating concentration

      0.4-1.0 µg/ml (depending on the type of ELISA plate and coating buffer). Suitable for biotinylation and iodination.

    • Applications

      Western blot with anti-M2-Antigen autoantibody-positive patient sera or monoclonal
      anti-hexa-His-tag antibody.

    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.

    Dlst Human
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