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Search results

1000 results found for “Thyrostimulin”

Name

Description

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  • View Data Sheet

    Name :

    TNNI3 Human, (1-210)

    Description:

    Cardiac Troponin-I Human Recombinant (1-210 a.a.)

    Troponin I cardiac muscle, Cardiac troponin I, TNNI3, TNNC1, CMH7, RCM1, cTnI, CMD2A, MGC116817.

    Product # :

    PRO-2591

    Price :

    Quantity :

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    Description

    TNNI3 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 233 amino acids (1-210 a.a) and having a molecular mass of 26.4 kDa.TNNI3 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    TNNI3 protein solution (0.25mg/ml) contains 30% glycerol, 20mM Tris-HCl buffer (pH 7.5), 0.1M NaCl, 0.1mMPMSF & 1mM DTT.

    Purity

    Greater than 90.0% as determined by both SDS-PAGE.

    Citations

    More Info

    • Introduction

      Troponin I (TnI), troponin T (TnT) and troponin C (TnC) form the troponin complex of the thin filaments of striated muscle. TnI acts as the inhibitory subunit by blocking actin-myosin interactions and thereby mediating striated muscle relaxation. The TnI subfamily contains 3 genes: TnI-skeletal-fast-twitch, TnI-skeletal-slow-twitch, and TnI-cardiac. The TNNI3 gene encodes the TnI-cardiac protein and isexpressed solely in cardiac muscle tissues. Mutations in the TNNI3 gene cause familial hypertrophic cardiomyopathy type 7 (CMH7) and familial restrictive cardiomyopathy (RCM).

    • Synonyms

      Troponin I cardiac muscle, Cardiac troponin I, TNNI3, TNNC1, CMH7, RCM1, cTnI, CMD2A, MGC116817.

    • 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).Avoid multiple freeze-thaw cycles.

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MGSMADGSSD AAREPRPAPA PIRRRSSNYR AYATEPHAKK KSKISASRKL QLKTLLLQIA KQELEREAEERRGEKGRALS TRCQPLELAG LGFAELQDLC RQLHARVDKV DEERYDIEAK VTKNITEIAD LTQKIFDLRG KFKRPTLRRV RISADAMMQALLGARAKESL DLRAHLKQVK KEDTEKENRE VGDWRKNIDA LSGMEGRKKK FES

    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.

    Cardiac Troponin I
  • View Data Sheet

    Name :

    RGS2 Human

    Description:

    Regulator of G-Protein Signaling 2 Human Recombinant

    Regulator of G-protein Signaling 2 24kDa, G0S8, G0/G1 switch regulatory protein 8, Cell growth-inhibiting gene 31 protein, RGS2.

    Product # :

    PRO-182

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    Description

    RGS2 produced in E.Coli is a single, non-glycosylated polypeptide chain containing 231 amino acids (1-211a.a.) and having a molecular mass of 26.5 kDa. RGS2 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The RGS2 protein solution (0.25mg/1ml) is formulated in 20mM Tris-HCl buffer (pH8.0), 100mM NaCl, 2mM DTT and 10% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      RGS2 belongs to the RGS family which are regulatory molecules that act as GTPase activating proteins for G alpha subunits of heterotrimeric G proteins. RGS2 inhibits signal transduction by increasing the GTPase activity of G protein alpha subunits and as a result driving them into their inactive GDP-bound form.

    • Synonyms

      Regulator of G-protein Signaling 2 24kDa, G0S8, G0/G1 switch regulatory protein 8, Cell growth-inhibiting gene 31 protein, RGS2.

    • 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 MQSAMFLAVQ HDCRPMDKSA GSGHKSEEKR EKMKRTLLKD WKTRLSYFLQ NSSTPGKPKT GKKSKQQAFI KPSPEEAQLW SEAFDELLAS KYGLAAFRAF LKSEFCEENI EFWLACEDFK KTKSPQKLSS KARKIYTDFI EKEAPKEINI DFQTKTLIAQ NIQEATSGCF TTAQKRVYSL MENNSYPRFL ESEFYQDLCK KPQITTEPHA T

    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.

    Rgs2 Human
  • View Data Sheet

    Name :

    CD90 Thy-1.1 Antibody

    Description:

    Thy-1.1 (CD90), Rat Anti-Mouse

    CD-90, CD90, THY-1, THY1, Theta Antigen.

    Product # :

    ANT-140

    Price :

    Quantity :

    Shipping Method :

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    • formulation
    • More Info
    • Citations

    Formulation

    1mg/ml in PBS (after reconstitution).

    Citations

    More Info

    • Introduction

      CD-90 plays a role in cell-cell or cell-ligand interactions during synaptogenesis and other events in the brain Thy-1 is the designation for a major cell surface glycoprotein characteristic to T cells,. The Thy-1 glycoproteins are constituents of thymocytes and neurons and probably are involved in cell-cell interactions. Human Thy-1 homolog maps to chromosome 11 because that is where T3D is found, in the mouse T3D and Thy-1 map to chromosome 9 along with certain other loci that are on human 11q.

    • Synonyms

      CD-90, CD90, THY-1, THY1, Theta Antigen.

    • Solubility

      Reconstitute with of H20. Mix gently, wash the sides of the vial and wait 30-60 seconds before use.

    • Immunogen

      Purified mouse LN T cells.

    • Ig Subclass

      Rat IgM.

    • Clone

      mThy-1.1.

    • Applications

      Cytotoxic and staining antibody. For staining, use 10µl/1,000,000 cells. Exact titer for cytotoxicity should be determined by the investigator.

    • Available Conjugates

      This antibody is only available as purified antibody.

    • Type

      Rat Anti Mouse Monoclonal.

    • Storage Procedures

      Lyophilized: store at 4oC. After reconstitution, if not intended for use within a month, aliquot and store at -20oC.

    • Purification Method

      boric acid precipitation.

    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.

    Cd90 Thy 11 Antibody
  • View Data Sheet

    Name :

    T.pallidum p47 (Partial)

    Description:

    Treponema pallidum p47 (Partial) Recombinant

    Product # :

    TRP-249

    Price :

    Quantity :

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    Description

    The E.Coli derived recombinant protein is fused at the C- terminus with a 6xHis Tag and contains the T.Pallidum p47 immunodominant regions.

    Source

    Escherichia Coli.

    Formulation

    70mM Tris-HCl pH8.0, 50mM NaCl, 50% Glycerol and 1.5M urea.

    Purity

    Treponema Pallidum protein is >95% pure as determined by 10% PAGE (coomassie staining).

    Citations

    More Info

    • Introduction

      Treponema pallidum is a gram-negative spirochaete bacterium and is considered to be metabolically crippled. There are at least four known subspecies: T. pallidum pallidum, T. pallidum pertenue, T. pallidum carateum and T. pallidum endemicum. The helical structure of T. pallidum pallidum allows it to move in a corkscrew motion through viscous mediums such as mucus. Treponema pallidum subsp. pallidum has one of the smallest bacterial genomes at 1.14 million base pairs (Mb) and has limited metabolic capabilities, reflecting its adaptation through genome reduction to the rich environment of mammalian tissue.

    • Stability

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

    • Applications

      Treponema Pallidum protein is suitable for ELISA and Western blots, excellent antigen for detection of T.Pallidum with minimal specificity problems.

    • Specificity

      Immunoreactive with sera of T.Pallidum infected individuals.

    • Purification Method

      Treponema Pallidum protein was purified by proprietary chromatographic technique.

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

    Tpallidum P47 Partial
  • View Data Sheet

    Name :

    Thrombin

    Description:

    Human Thrombin

    Product # :

    PRO-339

    Price :

    Quantity :

    Shipping Method :

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    • description
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    Description

    Thrombin was purified from human plasma.

    Source

    Human Plasma.

    Formulation

    Lyophilized protein containing mannitol, sodium chloride, calcium chloride.

    Biological Activity

    The specific activity was found to be 116 US Units/mg protein.

    Citations

    More Info

    • Introduction

      Thrombin enzyme (Activated Factor IIa) is an important clotting promoter that controls the transformation of soluble fibrinogen to insoluble active fibrin strands. Thrombin is a coagulation protein and a serine protease (EC 3.4.21.5) that catalyzes many coagulation-related reactions. Thrombin triggers factor-XI, factor-V, Factor-XIII and factor-VIII. Thrombin endorses platelet activation, using activation of protease-activated receptors on the platelet. As a result of its high proteolytic specificity, thrombin has become an important biochemical protein. The thrombin cleavage site (Leu-Val-Pro-Arg-Gly-Ser) is widely used in linker regions of recombinant fusion protein constructs. After the purification of the fusion protein, thrombin is used to cleave between the Arginine and Glycine residues of the cleavage site, efficiently removing the purification tag from the protein of interest with a high degree of specificity.

    • Physical Appearance

      lyophilized powder.

    • Stability

      Lyophilized Human Thrombin although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution human thrombin 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 human thrombin in sterile a 0.9% NaCl solution at 500U/ml.

    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.

    Thrombin Human
  • View Data Sheet

    Name :

    M CSF Mouse

    Description:

    Macrophage-Colony Stimulating Factor Mouse Recombinant

    CSF-1, Lanimostim, MCSF, M-CSF.

    Product # :

    CYT-439

    Price :

    Quantity :

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    Description

    Macrophage Colony Stimulating Factor Mouse Recombinant produced in E.coli is a disulfide linked homodimer, non-glycosylated, polypeptide chain containing 2 x 156 amino acids and having a total molecular mass of 36.4 KD.MCSF is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The protein was lyophilized from a sterile (0.2µm) filtered solution containing 10mM sodium phosphate, 50mM sodium chloride, pH 7.5.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Biological Activity

    The ED50, as calculated by the dose-dependant stimulation of the proliferation of murine M-NFS-60 indicator cells is 1.33ng/ml corresponding to a specific activity of 7.5x105 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. CSF-1 induces cells of the monocyte/macrophage lineage. It plays a role in immunological defenses, bone metabolism, lipoproteins clearance, fertility and pregnancy.

    • Synonyms

      CSF-1, Lanimostim, MCSF, M-CSF.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized M-CSF 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 M-CSF in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      MKEVSEHCSH MIGNGHLKVL QQLIDSQMET SCQIAFEFVD QEQLDDPVCY LKKAFFLVQD IIDETMRFKD NTPNANATER LQELSNNLNS CFTKDYEEQN KACVRTFHET PLQLLEKIKN FFNETKNLLE KDWNIFTKNC NNSFAKCSSR DVVTKP.

    • Background

      Macrophage-Colony Stimulating Factor Mouse Recombinant: An In-Depth Analysis

      Abstract:

      Macrophage-Colony Stimulating Factor (M-CSF) is a crucial cytokine involved in the regulation of macrophage biology, including their differentiation, survival, and function. This research paper provides an in-depth analysis of M-CSF Mouse Recombinant, focusing on its structure, signaling pathways, and diverse functions in the context of human research. Additionally, the paper explores the therapeutic potential of M-CSF modulation in various diseases.

      Introduction:

      M-CSF plays a vital role in the development and maintenance of macrophages, key immune cells involved in innate immunity and tissue homeostasis. This paper aims to provide a comprehensive analysis of M-CSF Mouse Recombinant, highlighting its importance in human macrophage biology and its potential therapeutic applications.

      Structure and Function of M-CSF:

      M-CSF is a homodimeric protein that binds to its receptor, CSF-1R, leading to the activation of downstream signaling pathways. It regulates the proliferation, survival, and activation of macrophages, influencing immune responses and tissue remodeling processes.

      Signaling Pathways:

      Upon binding to CSF-1R, M-CSF triggers various intracellular signaling pathways, including the MAPK pathway, PI3K/Akt pathway, and JAK/STAT pathway. These pathways regulate gene expression and mediate cellular responses, impacting macrophage functions.

      Role in Macrophage Development and Function:

      M-CSF is essential for the differentiation and maturation of macrophages from hematopoietic progenitor cells. It promotes the survival, proliferation, and activation of macrophages, enhancing their phagocytic activity, cytokine production, and antigen presentation capabilities.

      Therapeutic Potential:

      Given its crucial role in macrophage biology, M-CSF modulation has emerged as a potential therapeutic strategy. M-CSF inhibitors and CSF-1R antagonists have shown promise in the treatment of inflammatory and autoimmune diseases, as well as certain cancers. Targeting M-CSF signaling can modulate immune responses and affect disease progression.

      Clinical Applications and Future Directions:

      The therapeutic potential of M-CSF modulation is being explored in various clinical settings. Clinical trials investigating M-CSF inhibitors as monotherapy or combination therapy are underway in diseases such as rheumatoid arthritis and cancer. Future research should focus on understanding the intricate mechanisms of M-CSF signaling, optimizing therapeutic strategies, and developing personalized treatment approaches.

    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 Mouse
  • View Data Sheet

    Name :

    S100A8 Human

    Description:

    S100 Calcium Binding Protein A8 Human Recombinant

    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-800

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    Description

    S100A8 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 93 amino acids (1-93 a.a.) and having a molecular mass of 10.8 kDa. The S100A8 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The S100A8 solution (0.5mg/ml) contains 20mM Tris-HCl pH-8, 1mM DTT and 10% glycerol.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    Citations

    More Info

    • 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.

    • Physical Appearance

      Sterile Filtered clear colorless solution.

    • Stability

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

    • Amino Acid Sequence

      MLTELEKALN SIIDVYHKYS LIKGNFHAVY RDDLKKLLET ECPQYIRKKG ADVWFKELDI NTDGAVNFQE FLILVIKMGV AAHKKSHEES HKE.

    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.

    S100A8 Human
  • View Data Sheet

    Name :

    Resistin Rat, His

    Description:

    Resistin Rat Recombinant, His Tag

    Cysteine-rich secreted protein FIZZ3, Adipose tissue-specific secretory factor, ADSF, C/EBP-epsilon-regulated myeloid-specific secreted cysteine-rich protein, Cysteine-rich secreted protein A12-alpha-like 2, RSTN, XCP1, RETN1, MGC126603, MGC126609.

    Product # :

    CYT-458

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    Description

    Resistin Rat Recombinant is manufactured with N-terminal fusion of His tag. Resistin Rat Recombinant His-Tagged Fusion Protein is an 11.9 kDa protein containing 94 amino acid residues of the Resistin Rat and 16 additional amino acid residues – His Tag (underlined).

    Source

    Escherichia Coli.

    Formulation

    Filtered (0.4µm) and lyophilized from 0.5mg/ml in 20mM Tris pH 8.0.

    Purity

    Greater than 95% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      Resistin, a product of the RSTN gene, is a peptide hormone belonging to the class of cysteine-rich secreted proteins (monomeric peptide contains 11 cysteine residues) referred to as the RELM family, and is also described as ADSF (Adipose Tissue-Specific Secretory Factor) or FIZZ3 (Found in Inflammatory Zone 3). Mouse resistin is expressed as a 114 amino acid prepeptide; its hydrofobic Nterminal 20 amino acid signal peptide is cleaved before its secretion. Mouse resistin circulates in blood as a homodimeric protein consisting of two 94 amino acid polypeptides, which are disulfide-linked via Cys26.
      Resistin may be an important link between obesity. Mouse resistin, specifically produced and secreted by adipocyte, acts on skeletal muscle myocytes, hepatocytes and adipocytes themselves so that it reduces their sensitivity. Steppan et al. have suggested that resistin suppressed the ability to stimulate glucose uptake. They have also suggested that resistin was present at elevated levels in blood of obese mice, and was down regulated by fasting and by antidiabetic drugs. Way et al., on the other hand, have found that resistin expression is severely suppressed in obesity.
      Other studies have shown that mouse resistin increases during the differentiation of adipocytes, but it also seems to inhibit adipogenesis. In contrast, the human adipogenic differentiation is likely to be associated with a down regulation of resistin gene expression.

    • Synonyms

      Cysteine-rich secreted protein FIZZ3, Adipose tissue-specific secretory factor, ADSF, C/EBP-epsilon-regulated myeloid-specific secreted cysteine-rich protein, Cysteine-rich secreted protein A12-alpha-like 2, RSTN, XCP1, RETN1, MGC126603, MGC126609.

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

    • Amino Acid Sequence

      MRGSHHHHHH GMASHMPSMS LCPMDEAISK KINQDFSSLL PAAMKNTVLH CWSVSSRGRL ASCPEGTTVT SCSCGSGCGS WDVREDTMCH CQCGSIDWTA ARCCTLRVGS.

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

    Resistin Rat
  • View Data Sheet

    Name :

    Procalcitonin Human, His

    Description:

    Procalcitonin Human Recombinant, His Tag

    Procalcitonin, PCT.

    Product # :

    HOR-295

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    Description

    Procalcitonin Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 114 amino acids fragment (3-116) having a molecular mass of 17.13 kDa and an amino-terminal hexahistidine tag. The PCT is purified by standard chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    PCT is supplied in 20mM Tris-HCl pH 8.0 and 50% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      Procalcitonin is a peptide hormone mainly produced by the C cells of the thyroid and certain endocrine cells of the lung. Under normal expression conditions, procalcitonin is immediately cleaved into three specific fragments, an N terminal residue, calcitonin and katacalcin. Levels of unprocessed procalcitonin rise significantly after bacterial infection, trauma or shock.

    • Synonyms

      Procalcitonin, PCT.

    • 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.Please 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.

    Procalcitonin Human His
  • View Data Sheet

    Name :

    IL1A Mouse, His

    Description:

    Interleukin-1 alpha Mouse Recombinant, His Tag

    Interleukin-1 alpha, IL-1 alpha, Il1a.

    Product # :

    CYT-848

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    Description

    IL 1 alpha Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 179 amino acids (115-270 a.a) and having a molecular mass of 20.4kDa.IL 1 alpha is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    IL 1 alpha protein solution (1mg/ml) containing Phosphate buffered saline (pH7.4) and 10% glycerol.

    Purity

    Greater than 85% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      Interleukin-1 alpha is a proinflammatory cytokine produced by a wide variety of cell types, including macrophages, osteoblasts, monocytes and hepatocytes. Circulating levels of are normally low and only rise after stimulation by agents such as those produced byinflammation, infection or microbial endotoxins. IL-1 alpha possesses a wide variety of biological activities and exerts its effects by binding to specific cell surface receptors.

    • Synonyms

      Interleukin-1 alpha, IL-1 alpha, Il1a.

    • 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 MGSSAPYTYQ SDLRYKLMKL VRQKFVMNDS LNQTIYQDVD KHYLSTTWLN DLQQEVKFDM YAYSSGGDDS KYPVTLKISD SQLFVSAQGE DQPVLLKELP ETPKLITGSE TDLIFFWKSI NSKNYFTSAA YPELFIATKE QSRVHLARGL PSMTDFQIS.

    • Background

      What is the molecular weight/Mw of IL1A MOUSE, HIS Protein?
      IL1A MOUSE, HIS Protein has a total Mw of 20.4kDa.

      What is the source or expression system of IL1A MOUSE, HIS Protein?
      Escherichia Coli.

      What is the Purity of IL1A MOUSE, HIS Protein?
      IL1A MOUSE, HIS Protein is >85% pure as determined by SDS-PAGE.

      What is the Biological Activity of IL1A MOUSE, HIS Protein?
      The biological functionality of IL1A MOUSE, HIS Protein will be determined in the future.

      What is the amino acid sequence of IL1A MOUSE, HIS Protein?
      MGSSHHHHHH SSGLVPRGSH MGSSAPYTYQ SDLRYKLMKL VRQKFVMNDS LNQTIYQDVD KHYLSTTWLN DLQQEVKFDM YAYSSGGDDS KYPVTLKISD SQLFVSAQGE DQPVLLKELP ETPKLITGSE TDLIFFWKSI NSKNYFTSAA YPELFIATKE QSRVHLARGL PSMTDFQIS.

      What applications can IL1A MOUSE, HIS Protein be used in?
      IL1A MOUSE, HIS Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for IL1A MOUSE, HIS Protein?
      The endotoxin level is minimal, IL1A MOUSE, 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.

    Il 1 Alpha Mouse His
  • View Data Sheet

    Name :

    IL3 Mouse

    Description:

    Interleukin-3 Mouse Recombinant

    MCGF (Mast cell growth factor), Multi-CSF, HCGF, P-cell stimulation factor, IL-3, MGC79398, MGC79399.

    Product # :

    CYT-371

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    Description

    Interleukin-3 mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 135 amino acids and having a molecular mass of 15100 Dalton. The IL-3 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Lyophilized from a concentrated (1mg/ml) solution in water containing no additives.

    Purity

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

    Biological Activity

    The ED50 as determined by the dose-dependant stimulation of murine M-NFS-60 cells is < 0.05 ng/ml, corresponding to a Specific Activity of 20,000,000IU/mg.

    Citations

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    • Introduction

      Interleukin-3 is a pleiotropic cytokine produced primarily by activated T cells.
      IL-3 is thought to function via specific cell surface receptors to stimulate the proliferation, differentiation and survival of haematopoietic cell lines. IL-3 has also been shown to affect the functional activity of a variety of other cell types including mast cells, eosinophils, megakaryocytes and basophils.

    • Synonyms

      MCGF (Mast cell growth factor), Multi-CSF, HCGF, P-cell stimulation factor, IL-3, MGC79398, MGC79399.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Amino Acid Sequence

      The sequence of the first five N-terminal amino acids was determined and was found to be Met-Asp-Thr-His-Arg.

    • Background

      What is the molecular weight/Mw of IL3 MOUSE Protein?
      IL3 MOUSE Protein has a total Mw of 15.1kDa.

      What is the source or expression system of IL3 MOUSE Protein?
      Escherichia Coli.

      What is the Purity of IL3 MOUSE Protein?
      IL3 MOUSE Protein is >97% pure as determined by SDS-PAGE.

      What is the Biological Activity of IL3 MOUSE Protein?
      The ED50 as determined by the dose-dependant stimulation of murine M-NFS-60 cells is < 0.05 ng/ml, corresponding to a Specific Activity of 20,000,000IU/mg.

      What is the amino acid sequence of IL3 MOUSE Protein?
      The sequence of the first five N-terminal amino acids was determined and was found to be Met-Asp-Thr-His-Arg.

      What applications can IL3 MOUSE Protein be used in?
      IL3 MOUSE Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for IL3 MOUSE Protein?
      The endotoxin level is minimal, IL3 MOUSE Protein was purified using conventional chromatography techniques.

      Who supplies recombinant IL3 MOUSE that is in stock and available to order?
      ProSpec has the protein in stock and available for immediate delivery.

      Where can I order bulk mg quantities of IL3 MOUSE?
      ProSpec supplies bulk mg quantities at affordable prices that meets research and academic budgets.

    • Protein content

      Protein quantitation was carried out by two independent methods1. UV spectroscopy at 280 nm using the absorbency value of 0.154 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 IL3 as a Reference Standard.

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

    Il 3 Mouse
  • View Data Sheet

    Name :

    Betacellulin His Human

    Description:

    Betacellulin Human Recombinant, His Tag

    Betacellulin, Probetacellulin. 

    Product # :

    CYT-077

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    • sds-page
    • Citations

    Description

    BTC Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 101 amino acids (32-111) and having a molecular mass of 11.3 kDa.BTC is fused to a 21 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    The BTC solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 5mM DTT, 0.2M NaCl and 20% glycerol.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    sds-page

    Betacellulin-sds-page - Product image 1

    Citations

    More Info

    • Introduction

      Btc is a potent mitogen for retinal pigment epithelial cells and vascular smooth muscle cells. The effects of betacellulin are probably mediated by the egf receptor and other related receptors.

    • Synonyms

      Betacellulin, Probetacellulin.

    • 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 MDGNSTRSPE TNGLLCGDPE ENCAATTTQS KRKGHFSRCP KQYKHYCIKG RCRFVVAEQT PSCVCDEGYI GARCERVDLF Y

    • Background

      What is the molecular weight/Mw of BETACELLULIN Protein?
      BETACELLULIN Protein has a total Mw of 11.3kDa.

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

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

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

      What is the amino acid sequence of BETACELLULIN Protein?
      MGSSHHHHHH SSGLVPRGSH MDGNSTRSPE TNGLLCGDPE ENCAATTTQS KRKGHFSRCP KQYKHYCIKG RCRFVVAEQT PSCVCDEGYI GARCERVDLF Y

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

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

    Btc His Human
  • View Data Sheet

    Name :

    CRH Human (13-87)

    Description:

    Corticotropin Releasing Hormone (13-87 a.a.) Human Recombinant

    CRF, Corticotropin-Releasing Factor.

    Product # :

    HOR-054

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    Description

    The CRH Human is created as a recombinant protein with a 4kda N-terminal fusion of His Tag. The CRH His-Tagged Fusion Protein, produced in E. coli, is a 15kDa protein containing 75 amino acid residues of the CRH Human, 13-87 amino acids.

    Source

    Escherichia Coli.

    Formulation

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

    Purity

    Greater than 90% as determined by SDS-PAGE.

    Citations

    More Info

    • Synonyms

      CRF, Corticotropin-Releasing Factor.

    • Physical Appearance

      Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Store lyophilized CRH at -20°C. Aliquot the product after reconstitution to avoid repeated freezing/thawing cycles. Reconstituted protein can be stored at 4°C for a limited period of time; it does not show any change after two weeks at 4°C.

    • Solubility

      It is recommended to add deionized water to prepare a working stock solution of approximately 0.5mg/ml and let the lyophilized pellet dissolve completely. Product is not sterile! Please filter the product by an appropriate sterile filter before using it on cell culture.

    • Background

      CRH is a neuropeptide which regulates body's response to stress. CRH stimulates the release of ACTH from the pituitary gland which triggers the adrenal glands to produce cortisol. CRH takes part in the hypothalamic-pituitary-adrenal axis which controls the production of cortisol and other glucocorticoids. CRH is synthesized in different tissues such as the brainstem, hypothalamus and peripheral organs. In Pregnancy, CRH regulates parturition and fetal development.

    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.

    Crh Protein
  • View Data Sheet

    Name :

    Tissue Factor Human, Active

    Description:

    Coagulation Factor III Active Human Recombinant

    Tissue factor, TF, Coagulation factor III, CD142.

    Product # :

    PRO-2845

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    Description

    Recombinant Human Tissue Factor Active is a glycosylated, polypeptide chain containing 225 amino acids and having a total molecular mass of 45.0kDa. Coagulation Factor III is fused at C-terminus & is purified by proprietary chromatographic techniques.

    Source

    CHO cells.

    Formulation

    Lyophilized from a 0.2μm filtered solution in 20mM Tris and 150mM NaCl, pH 8.0.

    Purity

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

    Biological Activity

    The ED50 was determined by its ability to activate fluorogenic peptide substrate Boc-VPR-AMC cleavage, when bound in 1:1 complex with Coagulation Factor VII.

    Citations

    More Info

    • Synonyms

      Tissue factor, TF, Coagulation factor III, CD142.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Amino Acid Sequence

      SGTTNTVAAY NLTWKSTNFK TILEWEPKPV NQVYTVQIST KSGDWKSKCF YTTDTECDLT DEIVKDVKQT YLARVFSYPA GNVESTGSAG EPLYENSPEF TPYLETNLGQ PTIQSFEQVG TKVNVTVEDE RTLVRRNNTF LSLRDVFGKD LIYTLYYWKS SSSGKKTAKT NTNEFLIDVD KGENYCFSVQ AVIPSRTVNR KSTDSPVECM GQEKGEFREH HHHHH.

    • Background

      Tissue Factor is the main initiator of the extrinsic blood coagulation pathway. after vascular injury, Tissue Factor binds circulating Factor VII/VIIa, forming the TF–FVIIa complex, which activates Factors IX and X, leading to thrombin generation and fibrin clot formation. Tissue Factor also participates in cell signalling influencing inflammation, angiogenesis, wound healing, and tumor progression.

      What is the molecular weight / Mw of Tissue Factor Protein?
      Tissue Factor Protein has a total Mw of 45kDa.

      What is the source or expression system of Tissue Factor Protein?
      CHO Cells

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

      What is the Biological Activity of Tissue Factor Protein?
      The enzymatic activity was determined by its ability to activate fluorogenic peptide substrate Boc-VPR-AMC cleavage, when bound in 1:1 complex with Coagulation Factor VII.

      What is the amino acid sequence of Tissue Factor Protein?
      SGTTNTVAAY NLTWKSTNFK TILEWEPKPV NQVYTVQIST KSGDWKSKCF YTTDTECDLT DEIVKDVKQT YLARVFSYPA GNVESTGSAG EPLYENSPEF TPYLETNLGQ PTIQSFEQVG TKVNVTVEDE RTLVRRNNTF LSLRDVFGKD LIYTLYYWKS SSSGKKTAKT NTNEFLIDVD KGENYCFSVQ AVIPSRTVNR KSTDSPVECM GQEKGEFREH HHHHH

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

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

    Tissue Factor Human, Active
  • View Data Sheet

    Name :

    TGFB2 Human, HEK

    Description:

    Transforming Growth Factor-Beta 2 Human Recombinant, HEK

    Transforming growth factor, beta 2, cetermin, Glioblastoma-derived T-cell suppressor factor, polyergin, G-TSF, TGF-beta2, TGF-beta-2, transforming growth factor beta-2, BSC-1 cell growth inhibitor, TGFB-2.

    Product # :

    CYT-112

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    Description

    TGF-b 2 Human Recombinant produced in HEK cells is a non-glycosylated homodimer, having a total molecular weight of 25kDa.The TGF-b 2 is purified by proprietary chromatographic techniques.

    Source

    HEK.

    Formulation

    TGF-b 2 was lyophilized from a 0.2µm filtered solution containing 50mM sodium acetate pH 4.5.

    Purity

    Greater than 95% as obsereved by SDS-PAGE.

    Biological Activity

    The specific activity was determined by the dose-dependent inhibition of IL-4 induced proliferation of mouse HT-2 cells (BALB/c spleen activated by sheep erythrocytes in the presence of IL-2), the ED50 is 0.16ng/ml.

    Citations

    More Info

    • Introduction

      TGFB2 is a 27.08 kDa protein having two identical 118 amino acid peptide chains linked by a single disulfide bond. TGFB2 is part of a family of five related cytokines that have an extensive variation of normal and neoplastic cells, indicating the importance of these homo-dimmer proteins as multi-functional regulators of cellular activity. The three mammalian isoforms of TGF-beta (TGFb1, TGFb2 and TGFb3) signal through the same receptor and stimulate similar biological responses. They are involved in physiological processes as embryogenesis, tissue remodelling and wound healing.

    • Synonyms

      Transforming growth factor, beta 2, cetermin, Glioblastoma-derived T-cell suppressor factor, polyergin, G-TSF, TGF-beta2, TGF-beta-2, transforming growth factor beta-2, BSC-1 cell growth inhibitor, TGFB-2.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized TGF-b 2 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution TGF-b 2 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 TGF-b 2 in sterile solution containing 20% ethanol, 50mM sodium acetate and 75mM acetic acid.

    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.

    Tgf B 2 Human Hek
  • View Data Sheet

    Name :

    Leptin-B Tilapia

    Description:

    Leptin-B Tilapia Recombinant

    Product # :

    CYT-1110

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    Description

    Leptin-B Tilapia Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 152 amino acids and having a molecular mass of 15,243 Dalton. The Leptin-B Tilapia is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Lyophilized from a concentrated (1mg/ml) solution containing NaHCO3 at 1:2 salt: protein ratio.

    Purity

    Greater than 95.0% as determined by:
    (a) Gel filtration analysis.
    (b) Analysis by SDS-PAGE.

    Biological Activity

    Tilapia leptins were found to be biologically active in promoting proliferation of BAF/3 cells stably transfected with the long form of human leptin receptor, but their activity was lower than that of mammalian leptin. Furthermore, the Tilapia leptins were biologically active in promoting STAT‐LUC activation in COS7 cells transfected with Tilapia leptin receptor but not in cells transfected with human leptin receptor. Tilapia Leptin A was more active than Tilapia Leptin B.

    Citations

    More Info

    • Introduction

      Leptin is a protein hormone. It is mainly produced in adipose cells that regulate energy homeostasis by restraining hunger. Leptin ties to nuclear receptors in the hypothalamus (arcuate nucleus). Similar to insulin resistance in type II diabetes, in obesity there is a decrease in the sensitivity towards leptin, ending in a failure to identify satiety, even in high levels of energy stores or leptin itself. Full-length cDNA encoding 2 leptin sequences (tLepA and tLepB) and 1 leptin receptor sequence (tLepR) exists in tilapia (Oreochromis niloticus). The full-length cDNA of tLepR is 3423 bp, encoding a protein of 1140 amino acid which contained all functionally important domains conserved among vertebrate leptin receptors. The cDNAs of tLepA and tLepB are 486 bp and 459 bp in length, encoding proteins of 161 aa and 152 aa, respectively. The three-dimensional structures of tLepA and tLepB demonstrates strong conservation of tertiary structure with that of human leptin comprised of 4 helixes.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Solubility

      It is recommended to reconstitute the lyophilized Leptin-B Tilapia in sterile water or 0.4% NaHCO3 adjusted to pH 8-9, not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      The first six N-terminal amino acids of recombinant Tilapia leptin B are Ala-Leu-Leu-Thr-Lys-Gly.

    • Protein content

      Protein quantitation was carried out by UV spectroscopy at 280 nm using the absorbency value of 0.19 for 1 mg/ml Leptin-B Tilapia as the extinction coefficient for a 0.1% (1mg/ml) solution at pH 8.0. This value is calculated by the DNAman computer analysis program of protein sequences.

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

    Leptin B
  • View Data Sheet

    Name :

    TGFB1 Human, HEK

    Description:

    Transforming Growth Factor-Beta 1 Human Recombinant, HEK

    Transforming growth factor beta-1, TGF-beta-1, CED, DPD1, TGFB, TGF-b 1, LAP, TGFB1.

    Product # :

    CYT-1260

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    Description

    TGFB1 Human Recombinant produced in 293 cells is a glycosylated homodimer polypeptide chain containing 2 x 112 amino acids and having a total molecular mass of 25.0kDa. The TGFB1 is purified by proprietary chromatographic techniques.

    Source

    HEK 293 cells.

    Formulation

    Lyophilized from a sterile filtered solution containing TFA (0.1%).

    Purity

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

    Biological Activity

    The ED50 as determined by the dose-dependent inhibition of IL-4-induced proliferation of HT-2 cells is ≤ 0.05 ng/ml, corresponding to a specific activity of ≥ 2 x 107 units/mg.

    Citations

    More Info

    • Synonyms

      Transforming growth factor beta-1, TGF-beta-1, CED, DPD1, TGFB, TGF-b 1, LAP, TGFB1.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized TGFB1 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution TGFB1 Human 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 TGFB1 in sterile in 18MΩ-cm H2O at a concentration of 0.1 mg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      ALDTNYCFSS TEKNCCVRQL YIDFRKDLGW KWIHEPKGYH ANFCLGPCPY IWSLDTQYSK VLALYNQHNP GASAAPCCVP QALEPLPIVY YVGRKPKVEQ LSNMIVRSCK CS.

    • Background

      Transforming growth factor betas (TGF Betas) mediate many cell-cell interactions that occur during embryonic development. 3 TGF Betas have been identified in mammals: TGF Beta 1, TGF Beta 2 and TGF Beta 3. each are synthesized as precursor proteins that are very similar in that each is cleaved to yield a 112 amino acid polypeptide that remains associated with the latent portion of the molecule.

    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.

    Tgf Beta 1 Hek
  • View Data Sheet

    Name :

    IL1RA Human, His

    Description:

    Interleukin-1 Receptor Antagonist Human Recombinant, His Tag

    IRAP, IL1F3, IL1RA; IL-1ra3, ICIL-1RA, IL1RN, IL1 inhibitor, IL-1ra, MGC10430.

    Product # :

    CYT-481

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    Description

    IL1Ra Human Recombinant produced in E.Coli is single, a non-glycosylated, Polypeptide chain containing 152 amino acids fragment (26-177) and having a total molecular mass of 21.63kDa with an amino-terminal hexahistidine tag. The IL-1Ra His is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Interleukin-1Ra His-tag protein is supplied in 20mM Tris HCl (pH 8) and 50% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Citations

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    • Introduction

      IL-1Ra is the natural antagonist of the pro-inflammatory cytokines Interleukin-1? and Interleukin-1?. IL-1Ra is produced by a variety of cells including monocytes, macrophages, neutrophils and fibroblasts in response to the binding of various pro-inflammatory cytokines.

    • Synonyms

      IRAP, IL1F3, IL1RA; IL-1ra3, ICIL-1RA, IL1RN, IL1 inhibitor, IL-1ra, MGC10430.

    • 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. Please avoid freeze thaw cycles.

    • Background

      What is the molecular weight/Mw of IL 1RA HUMAN, HIS Protein?
      IL 1RA HUMAN, HIS Protein has a total Mw of 21.63kDa.

      What is the source or expression system of IL 1RA HUMAN, HIS Protein?
      Escherichia Coli.

      What is the Purity of IL 1RA HUMAN, HIS Protein?
      IL 1RA HUMAN, HIS Protein is >95% pure as determined by SDS-PAGE.

      What is the Biological Activity of IL 1RA HUMAN, HIS Protein?
      The biological functionality of IL 1RA HUMAN, HIS Protein will be determined in the future.

      What is the amino acid sequence of IL 1RA HUMAN, HIS Protein?
      IL 1RA HUMAN, HIS Protein is composed from 152 amino acids.

      What applications can IL 1RA HUMAN, HIS Protein be used in?
      IL 1RA HUMAN, HIS Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for IL 1RA HUMAN, HIS Protein?
      The endotoxin level is minimal, IL 1RA HUMAN, HIS Protein was purified using conventional chromatography techniques.

      Who supplies recombinant IL 1RA HUMAN, HIS 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 IL 1RA HUMAN, HIS?
      ProSpec supplies bulk mg quantities at affordable prices that meets research and academic budgets.

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

    Il 1Ra Human His
  • View Data Sheet

    Name :

    T.pallidum p47

    Description:

    Treponema pallidum p47 Recombinant

    Product # :

    TRP-243

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    Description

    The E.Coli derived recombinant protein contains the T.Pallidum p47 immunodominant regions. The protein contains beta-galactosidase (114 kDa) fused at the N- terminus.

    Source

    Escherichia Coli.

    Formulation

    8M urea, 10mM Tris-HCl pH 8.0, 1mM EDTA and 1mM DTT.

    Purity

    Treponema Pallidum protein is >95% pure as determined by SDS-PAGE.

    Citations

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    • Introduction

      Treponema pallidum is a gram-negative spirochaete bacterium and is considered to be metabolically crippled. There are at least four known subspecies: T. pallidum pallidum, T. pallidum pertenue, T. pallidum carateum and T. pallidum endemicum. The helical structure of T. pallidum pallidum allows it to move in a corkscrew motion through viscous mediums such as mucus. Treponema pallidum subsp. pallidum has one of the smallest bacterial genomes at 1.14 million base pairs (Mb) and has limited metabolic capabilities, reflecting its adaptation through genome reduction to the rich environment of mammalian tissue.

    • Stability

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

    • Applications

      Treponema Pallidum protein is suitable for ELISA and Western blots, excellent antigen for detection of T.Pallidum with minimal specificity problems.

    • Specificity

      Immunoreactive with sera of T.Pallidum infected individuals.

    • Purification Method

      Treponema Pallidum proteinwas purified by proprietary chromatographic technique.

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

    Tpallidum P47
  • View Data Sheet

    Name :

    SSR2 Antibody

    Description:

    Signal Sequence Receptor Beta, Mouse Anti Human

    HSD25, TLAP, TRAP-BETA, TRAPB, Translocon-associated protein subunit beta, Signal sequence receptor subunit beta, SSR-beta.

    Product # :

    ANT-501

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    Formulation

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

    Citations

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    • Introduction

      The signal sequence receptor (SSR) is a glycosylated endoplasmic reticulum membrane receptor related with protein translocation across the ER membrane. The SSR consists of 2 subunits, a 34-kD glycoprotein (alpha-SSR or SSR1) and a 22-kD glycoprotein (beta-SSR or SSR2). The human beta-signal sequence receptor gene (SSR2) maps to chromosome bands 1q21-q23. Diseases correlated with SSR2 include calcaneonavicular coalition, and osteosarcoma, and among its related super-pathways are Viral mRNA Translation and Generic Transcription Pathway.

    • Synonyms

      HSD25, TLAP, TRAP-BETA, TRAPB, Translocon-associated protein subunit beta, Signal sequence receptor subunit beta, SSR-beta.

    • Physical Appearance

      Sterile filtered colorless solution.

    • Immunogen

      Anti-human SSR2 mAb, clone PAT31G6AT, is derived from hybridization of mouse F0 myeloma cells with spleen cells from BALB/c mice immunized with a recombinant human SSR2 protein 18-149 amino acids purified from E. coli.

    • Ig Subclass

      Mouse IgG1 heavy chain and k light chain.

    • Clone

      PAT31G6AT.

    • 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 1:500.

    • 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

      SSR2 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.

    Ssr2 Antibody
  • View Data Sheet

    Name :

    GHRH Human

    Description:

    Growth Hormone Releasing Hormone Human

    Somatoliberin, Growth hormone-releasing factor, GRF, Growth hormone-releasing hormone, GHRH, Somatocrinin, Somatorelin, Sermorelin, GHRF, MGC119781.

    Product # :

    HOR-235

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    Description

    Growth Hormone Releasing Hormone Human Synthetic is a single, non-glycosylated, polypeptide chain containing 29 amino acids and having a molecular mass of 3358.9 Dalton.Corresponds to the amino-terminal segment of the naturally occurring human growth hormone-releasing hormone consisting of 44 amino acid residues.The GHRH is purified by proprietary chromatographic techniques.

    Formulation

    The GHRH peptide (1mg/ml) was lyophilized after extensive dialyses against 1.7 mg sodium phosphate buffer (0.1 mg sodium phosphate monobasic & 1.6 mg sodium phosphate dibasic).

    Purity

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

    Biological Activity

    GHRH increases plasma growth hormone concentrations by directly stimulating the anterior pituitary gland to release natural human growth hormone.

    Citations

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    • Introduction

      Growth-hormone-releasing hormone (GHRH), also known as growth-hormone-releasing factor (GRF or GHRF) or somatocrinin, is a 44-amino acidpeptide hormoneproduced in the arcuate nucleusof the hypothalamus.
      GHRH is released from neurosecretory nerve terminals of these arcuate neurons, and is carried by the hypothalamo-hypophysial portal circulation to the anterior pituitary glandwhere it stimulates growth hormone(GH) secretion. GHRH also stimulates the production of GH. GHRH is released in a pulsatile manner, stimulating similar pulsatile release of GH. In addition, GHRH also promotes slow-wave sleepdirectly.

    • Synonyms

      Somatoliberin, Growth hormone-releasing factor, GRF, Growth hormone-releasing hormone, GHRH, Somatocrinin, Somatorelin, Sermorelin, GHRF, MGC119781.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized Growth Hormone Releasing Hormone although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution GHRF 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 GHRH in sterile 18MΩ-cm H2O not less than 100 µg/ml, which can then be further diluted to other aqueous solutions. The GHRH is also soluble in 1% Acetic acid at a concentration of >1mg/ml to give a clear, colorless solution.

    • Amino Acid Sequence

      The free base of sermorelin has the empirical formula C149H246N 44O42S.
      Tyr-Ala-Asp-Ala-Ile-Phe-Thr-Asn-Ser-Tyr-Arg-Lys-Val-Leu-Gly-Gln-Leu-Ser-Ala-Arg-Lys-Leu-Leu-Gln-Asp-Ile-Met-Ser-Arg-NH2.

    • Background

      What is the molecular weight/Mw of GHRH Protein?
      GHRH Protein has a total Mw of 3.35kDa.


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

      What is the Biological Activity of GHRH Protein?
      GHRH increases plasma growth hormone concentrations by directly stimulating the anterior pituitary gland to release natural human growth hormone.
      What is the amino acid sequence of GHRH Protein?
      The free base of sermorelin has the empirical formula C149H246N 44O42S.
      Tyr-Ala-Asp-Ala-Ile-Phe-Thr-Asn-Ser-Tyr-Arg-Lys-Val-Leu-Gly-Gln-Leu-Ser-Ala-Arg-Lys-Leu-Leu-Gln-Asp-Ile-Met-Ser-Arg-NH2.
      What applications can GHRH Protein be used in?
      GHRH Protein can probably be used in western blot, ELISA and Lateral Flow.

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

    Ghrh Human
  • View Data Sheet

    Name :

    IL12p40 Human

    Description:

    Interleukin-12 p40 Human Recombinant

    NKSF2, CTL maturation factor (TCMF), Cytotoxic lymphocyte maturation factor 40 kDa subunit (CLMF p40), TSF, Edodekin-alpha, IL-12 p40, IL-12B, IL-12 subunit p40, NK cell stimulatory factor chain 2.

    Product # :

    CYT-488

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    Description

    Interleukin-12 p40 His Human Recombinant produced in E.Coli is single, a non-glycosylated, polypeptide chain containing 306 amino acids fragment (23-328) with an amino-terminal hexahistidine tag. The IL-12 p40 His is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Interleukin-12 p40 His is supplied in 1xPBS and 50% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      Active IL-12 is a p70 disulphide-linked dimer composed of p35 and p40 subunits. The protein is a pleiotropic cytokine produced primarily by antigen presenting cells and has multiple effects on T lymphocytes and natural killer cells in terms of stimulating cytotoxicity, proliferation, production of other cytokines and Th1 subset differentiation.

    • Synonyms

      NKSF2, CTL maturation factor (TCMF), Cytotoxic lymphocyte maturation factor 40 kDa subunit (CLMF p40), TSF, Edodekin-alpha, IL-12 p40, IL-12B, IL-12 subunit p40, NK cell stimulatory factor chain 2.

    • 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. Please avoid freeze thaw cycles.

    • Background

      What is the source or expression system of IL12P40 HUMAN Protein?
      Escherichia Coli.

      What is the Purity of IL12P40 HUMAN Protein?
      IL12P40 HUMAN Protein is >95% pure as determined by SDS-PAGE.

      What is the Biological Activity of IL12P40 HUMAN Protein?
      The biological functionality of IL12P40 HUMAN Protein will be determined in the future.

      What applications can IL12P40 HUMAN Protein be used in?
      IL12P40 HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for IL12P40 HUMAN Protein?
      The endotoxin level is minimal, IL12P40 HUMAN Protein was purified using conventional chromatography techniques.

      Who supplies recombinant IL12P40 HUMAN 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 IL12P40 HUMAN?
      ProSpec supplies bulk mg quantities at affordable prices that meets research and academic budgets.

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

    Il 12 P40 Human His
  • View Data Sheet

    Name :

    CD90 Thy-1 Antibody

    Description:

    Thy-1 (CD90), Rat Anti-Mouse

    CD-90, CD90, THY-1, THY1, Theta Antigen.

    Product # :

    ANT-142

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    Formulation

    1mg/ml in PBS (after reconstitution).

    Citations

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    • Introduction

      CD-90 plays a role in cell-cell or cell-ligand interactions during synaptogenesis and other events in the brain.
      Thy-1 is the designation for a major cell surface glycoprotein characteristic to T cells,. The Thy-1 glycoproteins are constituents of thymocytes and neurons and probably are involved in cell-cell interactions. Human Thy-1 homolog maps to chromosome 11 because that is where T3D is found, in the mouse T3D and Thy-1 map to chromosome 9 along with certain other loci that are on human 11q.

    • Synonyms

      CD-90, CD90, THY-1, THY1, Theta Antigen.

    • Solubility

      Reconstitute with H20. Mix gently, wash the sides of the vial and wait 30-60 seconds before use.

    • Immunogen

      Purified mouse LN T cells.

    • Ig Subclass

      Rat IgG1.

    • Clone

      mThy-1.

    • Applications

      Cytotoxic and staining antibody. For staining, use 10µl/1,000,000 cells. This antibody is extremely efficient for killing in vivo. Exact titer for cytotoxicity should be determined by the investigator.

    • Available Conjugates

      This antibody is only available as purified antibody.

    • Type

      Rat Anti Mouse Monoclonal.

    • Storage Procedures

      Lyophilized: store at 4oC. After reconstitution, if not intended for use within a month, aliquot and store at -20oC.

    • Purification Method

      Ion exchange column.

    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.

    Cd90 Thy 1 Antibody
  • View Data Sheet

    Name :

    CD27 Human

    Description:

    CD27 Human Recombinant

    Tumor Necrosis Factor Receptor Superfamily Member 7,T-Cell Activation Antigen CD27, CD27 Molecule, CD27 Antigen,T Cell Activation Antigen S152, CD27L Receptor, TNFRSF7, S152, Tp55, T14.

    Product # :

    PRO-1213

    Price :

    Quantity :

    Shipping Method :

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    More Info

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

    Description

    CD27 Human Recombinant produced in E. coli is a single polypeptide chain containing 196 amino acids (21-191) and having a molecular mass of 21.8 kDa.CD27 is fused to a 25 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    The CD27 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.

    Citations

    More Info

    • Introduction

      CD27 belongs to the TNF-receptor superfamily. CD27 is necessary for initiation and long-term maintenance of T cell immunity. CD27 binds to ligand CD70, and has a crucial role in regulating B-cell activation and immunoglobulin synthesis. The CD27 receptor transduces signals which result in the activation of NF-kappaB and MAPK8/JNK. Adaptor proteins TRAF2 and TRAF5 mediate the signaling process of CD27. CD27-binding protein (SIVA), which is a proapoptotic protein, can bind to the CD27 receptor and is believed to have a significant role in the apoptosis induced by CD27.

    • Synonyms

      Tumor Necrosis Factor Receptor Superfamily Member 7,T-Cell Activation Antigen CD27, CD27 Molecule, CD27 Antigen,T Cell Activation Antigen S152, CD27L Receptor, TNFRSF7, S152, Tp55, T14.

    • 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 MGSHMTPAPK SCPERHYWAQ GKLCCQMCEP GTFLVKDCDQ HRKAAQCDPC IPGVSFSPDH HTRPHCESCR HCNSGLLVRN CTITANAECA CRNGWQCRDK ECTECDPLPN PSLTARSSQA LSPHPQPTHL PYVSEMLEAR TAGHMQTLAD FRQLPARTLS THWPPQRSLC SSDFIR.

    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.

    Cd27 Human
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