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Search results

569 results found for “Leukocyte Cell Derived Chemotaxin”

Name

Description

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  • View Data Sheet

    Name :

    FTCD Human

    Description:

    Formiminotransferase Cyclodeaminase Human Recombinant

    Formiminotransferase-cyclodeaminase, FTCD, LCHC1, LC-1.

    Product # :

    ENZ-302

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    • More Info

    Description

    Formiminotransferase Cyclodeaminase Human Recombinant (also called liver cytosol type 1) produced in SF9, is a glycosylated, polypeptide chain having a molecular mass of 59,749 Dalton.The FTCD is expressed with a -6xHis tag and purified by proprietary chromatographic techniques.

    Source

    Sf9 insect cells.

    Formulation

    FTCD is supplied in 16mM HEPES buffer pH-7.6, 240mM sodium chloride, and 20% glycerol.

    Purity

    Greater than 95% as determined by SDS-PAGE.

    More Info

    • Introduction

      Formiminotransferase cyclodeaminase is an enzyme which catalyzes the conversion of formiminoglutamateand tetrahydrofolateinto formiminotetrahydrofolateand glutamate.
      Formiminotransferase cyclodeaminase, a bifunctional enzyme of tetrahydrofolate synthesis, is the target antigen of anti-LC1 (liver cytosol antigen type 1) autoantibodies. Presence of LC1 autoantibodies is a marker for type 2 autoimmune hepatitis (for which anti-LKM 1/cytochrome P450 2D6 autoantibodies are a further marker).
      Serum LC1 autoantibody concentrations appear to fluctuate in parallel with aminotransferase levels, a particularly intriguing observation that suggests a possible role of LC1 autoreactivity in the pathogenic mechanism leading to hepatocyte injury.

    • Synonyms

      Formiminotransferase-cyclodeaminase, FTCD, LCHC1, LC-1.

    • Stability

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

    • Immunological Functions

      1. Binds IgG-type human auto-antibodies.2. Standard ELISA test (checker-board analysis of positive/negative sera panels, immuno-dot test).

    • coating concentration

      0.35-0.7 µg/ml (depending on the type of ELISA plate and coating buffer).Suitable for biotinylation and iodination.

    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.

    Ftcd Hunan
  • View Data Sheet

    Name :

    Betacellulin His Human

    Description:

    Betacellulin Human Recombinant, His Tag

    Betacellulin, Probetacellulin. 

    Product # :

    CYT-077

    Price :

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    • sds-page

    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

    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 :

    CoV-2 S1 (16-685), Fc

    Description:

    Coronavirus 2019 Spike Glycoprotein-S1 (16-685 a.a.), Fc Recombinant

    Product # :

    SARS-027

    Price :

    Quantity :

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    Description

    The HEK293 derived recombinant protein contains the Coronavirus 2019 CoV-2 Spike Glycoprotein S1, Wuhan-Hu-1 strain, amino acids 16-685 fused to Fc tag at C-terminal.

    Source

    HEK293 Cells.

    Formulation

    CoV-2 S1 protein is supplied in sodium chloride, glycine, arginine pH-7.5 & 5% trehalose.

    Purity

    Protein is >95% pure as determined SDS-PAGE.

    More Info

    • Introduction

      A human infecting coronavirus (viral pneumonia) called 2019 novel coronavirus, 2019-nCoV was found in the fish market at the city of Wuhan, Hubei province of China on December 2019.

      The 2019-nCoV shares an 87% identity to the 2 bat-derived severe acute respiratory syndrome 2018 SARS-CoV-2 located in Zhoushan of eastern China. 2019-nCoV has an analogous receptor-BD-structure to that of 2018 SARS-CoV, even though there is a.a. diversity so thus the 2019-nCoV might bind to ACE2 receptor protein (angiotensin-converting enzyme 2) in humans.

      While bats are possibly the host of 2019-nCoV, researchers suspect that animal from the ocean sold at the seafood market was an intermediate host. RSCU analysis proposes that the 2019-nCoV is a recombinant within the viral spike glycoprotein between the bat coronavirus and an unknown coronavirus.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized Cov-2 Spike S1 Glycoprotein although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution CoV2 Spike protein 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.

    • Purification Method

      Purified by Protein-G 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.

    product_image.jpg
  • View Data Sheet

    Name :

    BCL7A Human

    Description:

    B-cell CLL/lymphoma 7A Human Recombinant

    B-cell CLL/lymphoma 7 protein family member A, BCL7A, BCL7.

    Product # :

    PRO-1318

    Price :

    Quantity :

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    • description
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    Description

    BCL7A Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 233 amino acids (1-210 a.a.) and having a molecular mass of 25.2kDa (Molecular size on SDS-PAGE will appear higher).BCL7A is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    BCL7A protein solution (0.25mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 10% glycerol, 1mM DTT and 2mM EDTA.

    Purity

    Greater than 85% as determined by SDS-PAGE.

    More Info

    • Introduction

      B-cell CLL/lymphoma 7A (BCL7A) is a member of the BCL7 family. BCL7A is directly involved, with Myc and IgH, in a three-way gene translocation in a Burkitt lymphoma cell line. Thru gene translocation, the N-terminal region of the BCL7A gene is disrupted, which is assumed to be connected to the pathogenesis of a subset of high-grade B cell non-Hodgkin lymphoma. The N-terminal portion involved in the translocation includes the region which shares a compelling sequence similarity with those of BCL7B and BCL7C. Chromosomal anomalies involving BCL7A may be a cause of B-cell non-Hodgkin lymphoma.

    • Synonyms

      B-cell CLL/lymphoma 7 protein family member A, BCL7A, BCL7.

    • 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 MGSMSGRSVR AETRSRAKDD IKRVMAAIEK VRKWEKKWVT VGDTSLRIYK WVPVTEPKVD DKNKNKKKGK DEKCGSEVTT PENSSSPGMM DMHDDNSNQS SIADASPIKQ ENSSNSSPAP EPNSAVPSDG TEAKVDEAQA DGKEHPGAED ASDEQNSQSS MEHSMNSSEK VDRQPSGDSG LAAETSAISQ DLEGVPPSKK MKLEASQQNS EEM.

    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.

    Bcl7A Human
  • View Data Sheet

    Name :

    Flt3 Ligand Mouse

    Description:

    Flt3 Ligand Mouse Recombinant

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

    Product # :

    CYT-340

    Price :

    Quantity :

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    • More Info

    Description

    Flt3-Ligand Mouse Recombinant produced in E.Coli is a non-glycosylated, polypeptide chain containing 163 amino acids and having a molecular mass of 18.6kDa. Flt3-Ligand is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The FLT3L Mouse protein was lyophilized from sterile filtered solution containing 10mM sodium phosphate, pH 7.5.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Biological Activity

    The ED50, calculated by the dose-dependent proliferation of mouse AML5 cells is 4.96ng/ml, corresponding to a specific activity of 2.0x105 units/mg.

    More Info

    • Introduction

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

    • Synonyms

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

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized Flt3-Ligand although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Flt-3 Ligand should be stored at 4°C between 2-7 days and for future use below -18°C. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA). Please prevent freeze-thaw cycles.

    • Solubility

      It is recommended to reconstitute the lyophilized Flt3l Mouse recombinant in sterile 18MΩ-cm H2O at a concentration of 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      MTPDCYFSHS PISSNFKVKF RELTDHLLKD YPVTVAVNLQ DEKHCKALWS LFLAQRWIEQ LKTVAGSKMQ TLLEDVNTEI HFVTSCTFQP LPECLRFVQT NISHLLKDTC TQLLALKPCI GKACQNFSRC LEVQCQPDSS TLLPPRSPIA LEATELPEPR PRQ.

    • Background

      What is the molecular weight/Mw of FLT3 LIGAND MOUSE Protein?
      FLT3 LIGAND MOUSE Protein has a total Mw of 18.6kDa.

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

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

      What is the Biological Activity of FLT3 LIGAND MOUSE Protein?
      The ED50, calculated by the dose-dependent proliferation of mouse AML5 cells is 4.96ng/ml, corresponding to a specific activity of 2.0x105 units/mg.

      What is the amino acid sequence of FLT3 LIGAND MOUSE Protein?
      MTPDCYFSHS PISSNFKVKF RELTDHLLKD YPVTVAVNLQ DEKHCKALWS LFLAQRWIEQ LKTVAGSKMQ TLLEDVNTEI HFVTSCTFQP LPECLRFVQT NISHLLKDTC TQLLALKPCI GKACQNFSRC LEVQCQPDSS TLLPPRSPIA LEATELPEPR PRQ.

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

      What is the endotoxin level for FLT3 LIGAND MOUSE Protein?
      The endotoxin level is minimal, FLT3 LIGAND MOUSE Protein was purified using conventional chromatography techniques.

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

    Flt3 Mouse
  • View Data Sheet

    Name :

    IL 10 Human, His

    Description:

    Interleukin-10 Human Recombinant, His

    B-TCGF, CSIF, TGIF, IL-10, IL10A, MGC126450, MGC126451, Cytokine synthesis inhibitory factor.

    Product # :

    CYT-486

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    Description

    Interleukin-10 Human Recombinant produced in E.Coli is single, a non-glycosylated, Polypeptide chain containing 181 amino acids fragment (19-178) and having a total molecular mass of 20.94kDa with a 20 amino acids N-Terminal His tag. The IL-10 His-Tag protein is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Interleukin-10 His is supplied in 20mM Tris-HCl pH-8 and 20% glycerol.

    Purity

    Greater than 95.0% by SDS-PAGE.

    More Info

    • Introduction

      Interleukin-10 is a multifunctional cytokine produced by a variety of cell types including T helper cells activated B cells and activated macrophages. Interleukin-10 regulates immune-mediated inflammation and modulates the function of cells such as lymphocytes, monocytes, natural killer cells and dendritic cells.

    • Synonyms

      B-TCGF, CSIF, TGIF, IL-10, IL10A, MGC126450, MGC126451, Cytokine synthesis inhibitory factor.

    • Physical Appearance

      Sterile Filtered clear solution.

    • Stability

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

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MSPGQGTQSE NSCTHFPGNL PNMLRDLRDA FSRVKTFFQM KDQLDNLLLK ESLLEDFKGY LGCQALSEMI QFYLEEVMPQ AENQDPDIKA HVNSLGENLK TLRLRLRRCH RFLPCENKSK AVEQVKNAFN KLQEKGIYKA MSEFDIFINY IEAYMTMKIR 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.

    Il 10 Human His
  • View Data Sheet

    Name :

    IL 5 Rhesus Macaque

    Description:

    Interleukin-5 Rhesus Macaque Recombinant

    Interleukin-5, IL-5, Eosinophil differentiation factor, T-cell replacing factor, TRF, IL5.

    Product # :

    CYT-772

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    Description

    IL5 Rhesus Macaque Recombinant produced in E.Coli is a disulfide-linked homodimeric, non-glycosylated, polypeptide protein containing 2x115 amino acids chains and having a total molecular mass of 26.1kDa.The IL-5 Rhesus Macaque is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Lyophilized from a 0.2µm filtered concentrated solution in 1xPBS, pH 7.4 and 5% Trehalose.

    Purity

    Greater than 98.0% as determined by HPLC and SDS-PAGE.

    Biological Activity

    The ED50 as determined by a cell proliferation assay using human TF-1 cells is less than 5ng/ml, corresponding to a specific activity of > 2.0 × 105 IU/mg.

    More Info

    • Introduction

      The protein encoded by this gene is a cytokine that acts as a growth and differentiation factor for both B cells and eosinophils. This cytokine is a main regulator of eosinopoiesis, eosinophil maturation and activation. The elevated production of this cytokine is reported to be related to asthma or hypereosinophilic syndromes. The receptor of this cytokine is a heterodimer, whose beta subunit is shared with the receptors for interleukine 3 (IL3) and colony stimulating factor 2 (CSF2/GM-CSF). This gene, together with those for interleukin 4 (IL4), interleukin 13 (IL13), and CSF2, form a cytokine gene cluster on chromosome 5. This cytokine, IL4, and IL13 are found to be regulated coordinately by long-range regulatory elements spread over 120 kilobases on chromosome 5q31.

    • Synonyms

      Interleukin-5, IL-5, Eosinophil differentiation factor, T-cell replacing factor, TRF, IL5.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized IL-5 Rhesus Macaque although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IL5 Rhesus Macaque 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 Interleikin-5 in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      IPTEIPASAL VKETLALLST HRTLLIANET LRIPVPVHKN HQLCTEEIFQ GIGTLESQTV QGGTVERLFK NLSLIKKYIG GQKKKCGEER RRVNQFLDYL QEFLGVMNTE WIIES.

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    Il 5 Rhesus Macaque
  • View Data Sheet

    Name :

    IL 7 Human, HEK

    Description:

    Interleukin-7 Human Recombinant, HEK

    Lymphopoietin 1 (LP-1), pre-B cell factor, IL-7.

    Product # :

    CYT-197

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    Description

    IL-7 Human Recombinant produced in HEK cells is a glycosylated monomer, having a molecular weight range of 19-30kDa due to glycosylation.The IL-7 is purified by proprietary chromatographic techniques.

    Source

    HEK.

    Formulation

    The IL7 was lyophilized from 1mg/ml in 1xPBS.

    Purity

    Greater than 95% as obsereved by SDS-PAGE.

    Biological Activity

    The activity was determined by the dose dependent stimulation of the proliferation of murine 2E8 cells and is typically 0.3ng/ml corresponding to a specific activity of 3,333,334units/mg.

    More Info

    • Introduction

      IL-7 is a cytokine important for B and T cell development. This cytokine and the hepatocyte growth factor (HGF) form a heterodimer that functions as a pre-pro-B cell growth-stimulating factor. This cytokine is found to be a cofactor for V(D)J rearrangement of the T cell receptor beta (TCRB) during early T cell development. This cytokine can be produced locally by intestinal epithelial and epithelial goblet cells, and may serve as a regulatory factor for intestinal mucosal lymphocytes. Knockout studies in mice suggested that this cytokine plays an essential role in lymphoid cell survival.

    • Synonyms

      Lymphopoietin 1 (LP-1), pre-B cell factor, IL-7.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized IL-7 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IL7 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 IL-7 in sterile PBS containing 0.1% endotoxin-free recombinant HSA.

    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 7 Human Hek
  • View Data Sheet

    Name :

    IL 1 beta Equine

    Description:

    Interleukin-1 beta Equine Recombinant

    Catabolin, Lymphocyte-activating factor (LAF), Endogenous Pyrogen (EP), Leukocyte Endogenous Mediator (LEM), Mononuclear Cell Factor (MCF), IL1F2, IL-1 beta.

    Product # :

    CYT-411

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    Description

    Recombinant IL 1 beta Equine produced in E.coli cells is a non-glycosylated, homodimeric protein containing 153 amino acid chain and having a molecular mass of 17.3kDa. The IL 1 beta is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The IL 1 beta was lyophilized from a 0.2µm filtered concentrated solution in PBS pH 7.4, containing 0.1 % Tween-80.

    Purity

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

    Biological Activity

    The ED50 as determined by a cell proliferation assay using murine D10S cells is less than 20 pg/ml, corresponding to a specific activity of > 5.0 × 107 IU/mg.

    More Info

    • Introduction

      Interleukin-1b is produced by activated macrophages, IL-1B stimulates thymocyte proliferation by inducing il-2 release, b-cell maturation and proliferation, and fibroblast growth factor activity. IL1B proteins are involved in the inflammatory response, being identified as endogenous pyrogens, and are reported to stimulate the release of prostaglandin and collagenase from synovial cells.

    • Synonyms

      Catabolin, Lymphocyte-activating factor (LAF), Endogenous Pyrogen (EP), Leukocyte Endogenous Mediator (LEM), Mononuclear Cell Factor (MCF), IL1F2, IL-1 beta.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized IL 1 beta although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IL 1 beta 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 IL 1 beta in sterile distilled H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      AAMHSVNCRL RDIYHKSLVL SGACELQAVH LNGENTNQQV VFCMSFVQGE EETDKIPVAL GLKEKNLYLS CGMKDGKPTL QLETVDPNTY PKRKMEKRFV FNKMEIKGNV EFESAMYPNW YISTSQAEKS PVFLGNTRGG RDITDFIMEI TSA

    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 Beta Equine
  • View Data Sheet

    Name :

    GM- CSF Human, Sf9

    Description:

    Granulocyte Macrophage-Colony Stimulating Factor Human Recombinant, Sf9

    CSF-2, MGI-1GM, GMCSF, Pluripoietin-alpha, Molgramostin, Sargramostim.

    Product # :

    CYT-416

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    Description

    GM-CSF Human Recombinant produced in insect cells is a single, glycosylated, polypeptide chain containing 127 amino acids (18-144) and having a molecular mass of 14.6kDa. GM-CSF is fused to a C-terminal His -tag (6x His) and purified by proprietary chromatographic techniques.

    Source

    Insect Cells.

    Formulation

    The protein was lyophilized with PBS.

    Purity

    Greater than 98.0% as determined by SDS-PAGE.

    Biological Activity

    The ED50 as determined by the dose-dependant stimulation of the proliferation of human TF-1 cells (human erythroleukemic indicator cell line) is < 0.1 ng/ml, corresponding to a Specific Activity of 10,000,000IU/mg.

    More Info

    • Introduction

      GMCSF is a cytokine that controls the production, differentiation, and function of granulocytes and macrophages. The active form of the protein is found extracellularly as a homodimer. This gene has been localized to a cluster of related genes at chromosome region 5q31, which is known to be associated with interstitial deletions in the 5q- syndrome and acute myelogenous leukemia. Other genes in the cluster include those encoding interleukins 4, 5, and 13.
      GM-CSF stimulates the growth and differentiation of hematopoietic precursor cells from various lineages, including granulocytes, macrophages, eosinophils and erythrocytes.

    • Synonyms

      CSF-2, MGI-1GM, GMCSF, Pluripoietin-alpha, Molgramostin, Sargramostim.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Amino Acid Sequence

      The sequence of the first five N-terminal amino acids was determined and was found to be Ala-Pro-Ala-Arg-Ser.

    • Background

      Recombinant Granulocyte-Macrophage Colony-Stimulating Factor (GMCSF) is a protein that plays a crucial role in the production and differentiation of white blood cells, including granulocytes and macrophages. It is a potent stimulator of hematopoietic stem cells, which are responsible for the production of all blood cells in the body. Recombinant GMCSF is a synthetic version of the protein that is produced using recombinant DNA technology.

      Recombinant GMCSF has been extensively studied for its potential therapeutic applications in a variety of medical conditions, including cancer, autoimmune diseases, and infectious diseases. In cancer, GMCSF is used as an immunostimulatory agent to enhance the immune response against cancer cells. By stimulating the production and differentiation of white blood cells, GM-CSF can increase the number of immune cells that can recognize and attack cancer cells. This approach has been successfully used in the treatment of several types of cancer, including melanoma and leukemia.

      In autoimmune diseases, recombinant GMCSF has been investigated as a potential treatment for conditions such as rheumatoid arthritis and multiple sclerosis. These diseases are characterized by an overactive immune response that attacks healthy tissues in the body. By modulating the immune response, GMCSF may be able to reduce inflammation and prevent further damage to affected tissues.

      In infectious diseases, recombinant GMCSF has been studied as a potential treatment for conditions such as sepsis and HIV/AIDS. In sepsis, a severe bacterial infection, GMCSF may be able to stimulate the production of white blood cells and improve the immune response against the infection. In HIV/AIDS, GMCSF may be able to enhance the immune response against the virus and reduce the risk of opportunistic infections.

      Recombinant GMCSF is typically administered by injection, either directly into the affected tissue or into the bloodstream. It is generally well-tolerated, although some patients may experience side effects such as fever, fatigue, and muscle pain.

      In conclusion, recombinant GMCSF is a promising therapeutic agent with potential applications in a variety of medical conditions. Its ability to stimulate the production and differentiation of white blood cells makes it a valuable tool in the treatment of cancer, autoimmune diseases, and infectious diseases. Ongoing research is likely to uncover new uses for this protein and further refine its therapeutic potential.

      What is the molecular weight/Mw of GM- CSF HUMAN, SF9 Protein?
      GM- CSF HUMAN, SF9 Protein has a total Mw of 14.6kDa.

      What is the source or expression system of GM- CSF HUMAN, SF9 Protein?
      Insect Cells.
      What is the Purity of GM- CSF HUMAN, SF9 Protein?
      GM- CSF HUMAN, SF9 Protein is >98% pure as determined by SDS-PAGE.

      What is the Biological Activity of GM- CSF HUMAN, SF9 Protein?
      The ED50 as determined by the dose-dependant stimulation of the proliferation of human TF-1 cells (human erythroleukemic indicator cell line) is < 0.1 ng/ml, corresponding to a Specific Activity of 10,000,000IU/mg.

      What is the amino acid sequence of GM- CSF HUMAN, SF9 Protein?
      The sequence of the first five N-terminal amino acids was determined and was found to be Ala-Pro-Ala-Arg-Ser.

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

      What is the endotoxin level for GM- CSF HUMAN, SF9 Protein?
      The endotoxin level is minimal, GM- CSF HUMAN, SF9 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.

    Gm Csf Human Sf9
  • View Data Sheet

    Name :

    PRDX2 Human

    Description:

    Peroxiredoxin-2 Human Recombinant

    PRP, TSA, PRX2, NKEFB, PRXII, TDPX1, MGC4104, PRDX2, Peroxiredoxin-2, Thioredoxin peroxidase 1, Thioredoxin-dependent peroxide reductase 1, Thiol-specific antioxidant protein, Natural killer cell-enhancing factor B, NKEF-B.

    Product # :

    ENZ-414

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    Description

    PRDX2 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 198 amino acids and having a molecular mass of 21.8 kDa.The PRDX2 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The Peroxiredoxin solution contains 20mM Tris-HCl pH-8, & 10% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    Biological Activity

    The specific activity is > 2000 pmole/min/µg. Enzymatic activity is defined as the amount of hydroperoxide that 1ug of enzyme can reduce at 25°C for 1 minute.

    More Info

    • Introduction

      PRDX2 is part of the peroxiredoxin family of antioxidant enzymes, which reduce hydrogen peroxide and alkyl hydroperoxides. PRDX2 takes part as an antioxidant protective role in cells, and contributes to the antiviral activity of CD8(+) T-cells. PRDX2 has proliferative effect in cancer development or progression.
      If PRDX2 protection is insufficient against peroxidases, the DNA damage results in neurological disease such as Alzheimer's or DNA damage leading to cancer.

    • Synonyms

      PRP, TSA, PRX2, NKEFB, PRXII, TDPX1, MGC4104, PRDX2, Peroxiredoxin-2, Thioredoxin peroxidase 1, Thioredoxin-dependent peroxide reductase 1, Thiol-specific antioxidant protein, Natural killer cell-enhancing factor B, NKEF-B.

    • Physical Appearance

      Sterile Filtered colorless solution.

    • Stability

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

    • Amino Acid Sequence

      MASGNARIGK PAPDFKATAV VDGAFKEVKL SDYKGKYVVL FFYPLDFTFV CPTEIIAFSN RAEDFRKLGC EVLGVSVDSQ FTHLAWINTP RKEGGLGPLN IPLLADVTRR LSEDYGVLKT DEGIAYRGLF IIDGKGVLRQ ITVNDLPVGR SVDEALRLVQ AFQYTDEHGE VCPAGWKPGS DTIKPNVDDS KEYFSKHN.

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    Prdx2 Human
  • View Data Sheet

    Name :

    BSG Human

    Description:

    Basigin Human Recombinant

    Basigin isoform 2, 5F7, CD147, EMMPRIN, OK, TCSF, Leukocyte activation antigen M6, OK blood group antigen.

    Product # :

    PRO-2516

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    Description

    BSG produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 428 amino acids (22-207a.a.) and having a molecular mass of 47.5kDa. (Molecular size on SDS-PAGE will appear at approximately 40-57kDa).BSG is expressed with a 242 amino acid hIgG-His tag at C-Terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

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

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Basigin Isoform 2 or BSG is a part of the immunoglobulin superfamily, it is a type 1 transmembrane protein which has a variety of Nand O- glycosylation. BSG has several ligands, such as integrins, cyclophilin proteins Cyp-A & CyP-B. The protein has a crucial role in intercellular recognition, it takes part in many immunologic processes, differentiation and cell development. Also, it regulates numerus cell processes such as production and release of expression of the mono-carboxylate transporter, spermatogenesis, etc. Basigin Isoform 2 promotes invasion, metastasis, growth and survival of malignant cells by producing and releasing matrix metalloproteinases nearby mesenchymal cells and tumor cells.

    • Synonyms

      Basigin isoform 2, 5F7, CD147, EMMPRIN, OK, TCSF, Leukocyte activation antigen M6, OK blood group 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

      ADPAAGTVFT TVEDLGSKIL LTCSLNDSAT EVTGHRWLKG GVVLKEDALP GQKTEFKVDS DDQWGEYSCV FLPEPMGTAN IQLHGPPRVK AVKSSEHINE GETAMLVCKS ESVPPVTDWA WYKITDSEDK ALMNGSESRF FVSSSQGRSE LHIENLNMEA DPGQYRCNGT SSKGSDQAII
      TLRVRSHLAL EPKSCDKTHT CPPCPAPELL GGPSVFLFPP KPKDTLMISR TPEVTCVVVD VSHEDPEVKF NWYVDGVEVH NAKTKPREEQ YNSTYRVVSV LTVLHQDWLN GKEYKCKVSN KALPAPIEKT ISKAKGQPRE PQVYTLPPSR DELTKNQVSL TCLVKGFYPS DIAVEWESNG
      QPENNYKTTP PVLDSDGSFF LYSKLTVDKS RWQQGNVFSC SVMHEALHNH YTQKSLSLSP GKHHHHHH.

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    Basigin Human
  • View Data Sheet

    Name :

    IL 5 Human

    Description:

    Interleukin-5 Human Recombinant

    EDF, BCDFII, TRF, T-cell replacing factor, Eosinophil differentiation factor, B cell differentiation factor I, IL-5.

    Product # :

    CYT-212

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    Description

    Interleukin-5 Human Recombinant produced in E.Coli is a dimeric, non-glycosylated polypeptide chain containing two 113 amino acids chains, and having a molecular mass of 26522.84 Dalton. The IL-5 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 98.0% as determined by:
    (a) Analysis by RP-HPLC.
    (b) Analysis by SDS-PAGE.

    Biological Activity

    The ED50 as determined by the dose-dependant stimulation of the proliferation of TF-1 cells was found to be < 0.15ng/ml, corresponding to a Specific Activity of 6 x 106 IU/mg.

    More Info

    • Introduction

      The protein encoded by this gene is a cytokine that acts as a growth and differentiation factor for both B cells and eosinophils. This cytokine is a main regulator of eosinopoiesis, eosinophil maturation and activation. The elevated production of this cytokine is reported to be related to asthma or hypereosinophilic syndromes. The receptor of this cytokine is a heterodimer, whose beta subunit is shared with the receptors for interleukine 3 (IL3) and colony stimulating factor 2 (CSF2/GM-CSF). This gene, together with those for interleukin 4 (IL4), interleukin 13 (IL13), and CSF2, form a cytokine gene cluster on chromosome 5. This cytokine, IL4, and IL13 are found to be regulated coordinately by long-range regulatory elements spread over 120 kilobases on chromosome 5q31.

    • Synonyms

      EDF, BCDFII, TRF, T-cell replacing factor, Eosinophil differentiation factor, B cell differentiation factor I, IL-5.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized Interleukin-5 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IL5 should be stored at 4°C between 2-7 days and for future use below -18°C.Please avoid freeze thaw cycles.

    • Solubility

      It is recommended to reconstitute the lyophilized Interleikin-5 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-Ile-Pro-Thr-Glu.

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

    Il 5 Human
  • View Data Sheet

    Name :

    CLEC7A Human

    Description:

    C-Type Lectin Domain Family 7, Member A Human Recombinant

    BGR, Dendritic Cell-Associated C-Type Lectin-1, Dendritic Cell-Associated C-Type Lectin 1, C-Type Lectin Domain Family 7, Member A, Lectin-Like Receptor 1, CD369 Antigen, CANDF4, SCARE2, CD369, C-Type Lectin Domain Containing 7A, C-Type Lectin Domain Family 7 Member A, C-Type (Calcium Dependent, Carbohydrate-Recognition Domain) Lectin, Superfamily Member 12, C-Type Lectin Superfamily Member 12, DC-Associated C-Type Lectin 1, Beta-Glucan Receptor, Dectin-1, CLECSF12, DECTIN1.

    Product # :

    PRO-2634

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    Description

    CLEC7A Human Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 183 amino acids (71-244 a.a) and having a molecular mass of 21kDa. CLEC7A is fused to a 9 amino acid His-tag at C-terminus & purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    The CLEC7A solution (0.5mg/1ml) contains phosphate buffered saline (pH7.4) and 10% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      C-type lectin domain family 7 member A 1 or CLEC7A is a protein, that in the innate immune system, acts against fungal pathogens. CLEC7A can be found in the immune system response cells such as monocytes, macrophages & neutrophils, or in dendritic and T cells. The protein is enhanced by macrophages by using GM-CSF, IL-4, or IL-13, or diminishes by dexamethasone, IL-10 and LPS.

    • Synonyms

      BGR, Dendritic Cell-Associated C-Type Lectin-1, Dendritic Cell-Associated C-Type Lectin 1, C-Type Lectin Domain Family 7, Member A, Lectin-Like Receptor 1, CD369 Antigen, CANDF4, SCARE2, CD369, C-Type Lectin Domain Containing 7A, C-Type Lectin Domain Family 7 Member A, C-Type (Calcium Dependent, Carbohydrate-Recognition Domain) Lectin, Superfamily Member 12, C-Type Lectin Superfamily Member 12, DC-Associated C-Type Lectin 1, Beta-Glucan Receptor, Dectin-1, CLECSF12, DECTIN1.

    • 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

      ADPRHNSGRN PEEKDNFLSR NKENHKPTES SLDEKVAPSK ASQTTGGFSQ SCLPNWIMHG KSCYLFSFSG NSWYGSKRHC SQLGAHLLKI DNSKEFEFIE SQTSSHRINA FWIGLSRNQS EGPWFWEDGS AFFPNSFQVR NTVPQESLLH NCVWIHGSEV YNQICNTSSY SICEKELHHH HHH.

    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.

    Clec7A Human
  • View Data Sheet

    Name :

    IL-12 Human

    Description:

    Interleukin-12 Human Recombinant

    NKSF, CTL maturation factor (TCMF), Cytotoxic lymphocyte maturation factor (CLMF), TSF, Edodekin-alpha, IL-12.

    Product # :

    CYT-101

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    Description

    Interleukin-12 Human Recombinant produced in HEK cells is a glycosylated heterodimer, having a total molecular weight of 57kDa.The IL12 is purified by proprietary chromatographic techniques.

    Source

    HEK.

    Formulation

    IL12 was lyophilized from a 0.2µm filtered solution containing 1xPBS.

    Purity

    Greater than 95% as obsereved by SDS-PAGE.

    Biological Activity

    The specific activity was determined by the dose-dependent release of IFN-gamma from the human NK92 cell line in presence of 20ng/mL rIL-2.
    The EC50 is 0.5ng/ml.

    More Info

    • Introduction

      IL-12 is a heterodimeric cytokine that stimulates the production of IFNgamma from T-cells and natural killer cells, and also induces differentiation of Th1 helper cells. IL-12 is an initiator of cell-mediated immunity.

    • Synonyms

      NKSF, CTL maturation factor (TCMF), Cytotoxic lymphocyte maturation factor (CLMF), TSF, Edodekin-alpha, IL-12.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized IL-12 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IL12 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 IL12 in sterile PBS containing 0.1% endotoxin-free recombinant HSA.

    • Amino Acid Sequence

      IL-12 is a heterodimer of IL-12A and IL-12B linked through a disulfide-bond between cysteines in red in sequences below.
      >IL-12 A
      RNLPVATPDPGMFPCLHHSQNLLRAVSNMLQKARQTLEFYPCTSEEIDHEDITKDKTSTVEACLP
      LELTKNESCLNSRETSFITNGSCLASRKTSFMMALCLSSIYEDLKMYQVEFKTMNAKLLMDPKRQ
      IFLDQNMLAVIDELMQALNFNSETVPQKSSLEEPDFYKTKIKLCILLHAFRIRAVTIDRVMSYLNAS.
      >IL-12B
      IWELKKDVYVVELDWYPDAPGEMVVLTCDTPEEDGITWTLDQSSEVLGSGKTLTIQVKEFGDAG
      QYTCHKGGEVLSHSLLLLHKKEDGIWSTDILKDQKEPKNKTFLRCEAKNYSGRFTCWWLTTISTD
      LTFSVKSSRGSSDPQGVTCGAATLSAERVRGDNKEYEYSVECQEDSACPAAEESLPIEVMVDAV
      HKLKYENYTSSFFIRDIIKPDPPKNLQLKPLKNSRQVEVSWEYPDTWSTPHSYFSLTFCVQVQGK
      SKREKKDRVFTDKTSATVICRKNASISVRAQDRYYSSSWSEWASVPCS.

    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 Human Hek
  • View Data Sheet

    Name :

    IL 3 Dog

    Description:

    Interleukin-3 Canine Recombinant

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

    Product # :

    CYT-722

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    Description

    Interleukin-3 Canine Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 120 amino acids and having a molecular mass of 14 kDa. The IL-3 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Lyophilized from a concentrated (1mg/ml) solution in water containing 1X PBS pH7.4.

    Purity

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

    Biological Activity

    The ED50 as determined by the dose-dependant stimulation of TF-1 cells is < 0.2 ng/ml, corresponding to a Specific Activity of 5,000,000 IU/mg.

    More Info

    • Introduction

      IL3 is a potent growth promoting cytokine. This cytokine is capable of supporting the proliferation of a broad range of hematopoietic cell types. It is involved in a variety of cell activities such as cell growth, differentiation and apoptosis. This cytokine has been shown to also possess neurotrophic activity, and it may be associated with neurologic disorders.

    • 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 IL3 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IL3 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 IL3 in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      RPFSTDLPKQ YFTMINEIME MLNKSPSPSE EPLDSNEKET LLEDTLLRPN LDVFLNASSK FHKNGLLIWN NLKEFLPLLP TPTPRGEPIS IMENNWGDFQ RKLKKYLEAL DNFLNFKNKP.

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    Il 3 Dog
  • View Data Sheet

    Name :

    IL5 Mouse, Sf9

    Description:

    Interleukin-5 Mouse Recombinant, Sf9

    interleukin 5, Il, Il-5, B-cell growth factor II, BCGF-II, Cytotoxic T-lymphocyte inducer, Eosinophil differentiation factor, T-cell replacing factor, EDF, TRF, B cell differentiation factor I, IL5.

    Product # :

    CYT-1195

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    Description

    IL5 Mouse produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 119 amino acids (21-133 a.a) and having a molecular mass of 13.9kDa.IL5 is expressed with a 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    The IL5 solution (0.25mg/1ml) contains phosphate buffered saline (pH7.4) and 10% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    Biological Activity

    Measured in a cell proliferation assay using TF-1 human erythroleukemic cells. The ED50 range ≤ 1 ng/ml.

    More Info

    • Introduction

      The protein encoded by this gene is a cytokine that acts as a growth and differentiation factor for both B cells and eosinophils. IL5is a main regulator of eosinopoiesis, eosinophil maturation and activation. The elevated production of IL5is reported to be related to asthma or hypereosinophilic syndromes. The receptor of IL5is a heterodimer, whose beta subunit is shared with the receptors for interleukine 3 (IL3) and colony stimulating factor 2 (CSF2/GM-CSF). IL5, together with those for interleukin 4 (IL4), interleukin 13 (IL13), and CSF2, form a cytokine gene cluster on chromosome 5. IL5, IL4, and IL13 are found to be regulated coordinately by long-range regulatory elements spread over 120 kilobases on chromosome 5q31.

    • Synonyms

      interleukin 5, Il, Il-5, B-cell growth factor II, BCGF-II, Cytotoxic T-lymphocyte inducer, Eosinophil differentiation factor, T-cell replacing factor, EDF, TRF, B cell differentiation factor I, IL5.

    • 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

      MEIPMSTVVK ETLTQLSAHR ALLTSNETMR LPVPTHKNHQ LCIGEIFQGL DILKNQTVRG GTVEMLFQNL SLIKKYIDRQ KEKCGEERRR TRQFLDYLQE FLGVMSTEWA MEGHHHHHH

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    Il 5 Mouse
  • View Data Sheet

    Name :

    HAVCR2 Human

    Description:

    Hepatitis A Virus Cellular Receptor 2 Human Recombinant

    Hepatitis A virus cellular receptor 2, HAVcr-2, T-cell immunoglobulin and mucin domain-containing protein 3, TIMD-3, T-cell membrane protein 3, TIM-3, HAVCR2, TIM3, TIMD3, TIM3, KIM-3.

    Product # :

    HAV-224

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    Description

    Recombinant Human HAVCR2 produced in E. coli is a single polypeptide chain containing 206 amino acids (aa 22-202) and having a molecular mass of 22.7kDa.HAVCR2 is fused to a 25 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The HAVCR2 solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.4M urea and 10% glycerol.

    Purity

    Greater than 90% as determined by SDS-PAGE.

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    • Introduction

      Hepatitis A Virus Cellular Receptor 2 (HAVCR2) is a member of the immunoglobulin superfamily. HACVR2 controls macrophage activation. HACVR2 inhibits T-helper type 1 lymphocyte (Th1)-mediated auto- and alloimmune responses and stimulates immunological tolerance.

    • Synonyms

      Hepatitis A virus cellular receptor 2, HAVcr-2, T-cell immunoglobulin and mucin domain-containing protein 3, TIMD-3, T-cell membrane protein 3, TIM-3, HAVCR2, TIM3, TIMD3, TIM3, KIM-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 MGSHMSEVEY RAEVGQNAYL PCFYTPAAPG NLVPVCWGKG ACPVFECGNV VLRTDERDVN YWTSRYWLNG DFRKGDVSLT IENVTLADSG IYCCRIQIPG IMNDEKFNLK LVIKPAKVTP APTLQRDFTA AFPRMLTTRG HGPAETQTLG SLPDINLTQI STLANELRDS RLANDLRDSG ATIRIG.

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    Havcr2 Human
  • View Data Sheet

    Name :

    CD48 Human

    Description:

    CD48 Human Recombinant

    CD48 antigen, B-lymphocyte activation marker BLAST-1, BCM1 surface antigen, Leukocyte antigen MEM-102, SLAM family member 2, SLAMF2, Signaling lymphocytic activation molecule 2, TCT.1.

    Product # :

    PRO-2462

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    Description

    CD48 Human Recombinant produced in Sf9 Insect cells is a single, glycosylated polypeptide chain containing 203 amino acids (27-220a.a.) and having a molecular mass of 23.4kDa (Molecular size on SDS-PAGE will appear at approximately 28-40kDa).CD48 is expressed with a 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Insect cells.

    Formulation

    NECTIN2 protein solution (1.0mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 10% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

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    • Introduction

      CD48, is a GPI-linked protein which belongs to the CD2 family of immunoglobulin superfamily molecules. CD48 is capable to transduce signals and can likewise trigger signaling through CD2 or 2B4. CD48 to CD2 interactions advocate T cell activation and class replacing to IgG2a in B cells. In addition, high affinity of CD48 to 2B4, interactions may either promote or inhibit NK cell as well as cytotoxic T cell (CTL) activation. CD48 does not contain a transmembrane domain, though it is held at the cell surface by a GPI anchor through a C-terminal domain which possibly split to produce a soluble form of the receptor.

    • Synonyms

      CD48 antigen, B-lymphocyte activation marker BLAST-1, BCM1 surface antigen, Leukocyte antigen MEM-102, SLAM family member 2, SLAMF2, Signaling lymphocytic activation molecule 2, TCT.1.

    • 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

      ADPQGHLVHM TVVSGSNVTL NISESLPENY KQLTWFYTFD QKIVEWDSRK SKYFESKFKG RVRLDPQSGA LYISKVQKED NSTYIMRVLK KTGNEQEWKI KLQVLDPVPK PVIKIEKIED MDDNCYLKLS CVIPGESVNY TWYGDKRPFP KELQNSVLET TLMPHNYSRC YTCQVSNSVS
      SKNGTVCLSP PCTLARSHHH HHH.

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    Cd48 Human
  • View Data Sheet

    Name :

    Borrelia p100

    Description:

    Borrelia Burgdorferi p100 Recombinant

    Product # :

    BOR-003

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    Description

    Recombinant Borrelia Burgdorferi p100 (p100/p83) produced in SF9 is a glycosylated, polypeptide chain having a calculated molecular mass of 77,813 Dalton. Borrelia p100 is expressed with a -6x His tag at N-terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9 insect cells.

    Formulation

    Borrelia p100 is supplied in 20mM HEPES buffer pH-8.0, 200mM NaCl and 20% glycerol.

    Purity

    Greater than 95% as determined by SDS-PAGE.

    More Info

    • Introduction

      Borrelia belongs to a genus of bacteria of the spirochete phylum. Borrelia causes borreliosis, which is a zoonotic, vector-borne disease transmitted mainly by ticks and some by lice, depending on the species. Of the 36 known species of Borrelia, 12 are distinguished to cause Lyme disease or borreliosis and are transmitted by ticks. The main Borrelia species causing Lyme disease are Borrelia burgdorferi, Borrelia afzelii, and Borrelia garinii. The Borrelia genus members have a linear chromosome which is about 900 kbp in length as well as an excess of both linear and circular plasmids in the 5-220 kbp size range. The plasmids are atypical, as compared to most bacterial plasmids, since they contain many paralogous sequences, a large number of pseudogenes and, in some cases, essential genes. Moreover, a number of the plasmids have features suggesting that they are prophages.

    • 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. Avoid multiple freeze-thaw cycles.

    • Applications

      Western blot with Lyme positive plasma.

    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.

    Borrelia P100
  • View Data Sheet

    Name :

    IL 32A Human, His

    Description:

    Interleukin-32 alpha Human Recombinant , His Tag

    NK4, TAIF, TAIFa, TAIFb, TAIFc, TAIFd, IL-32beta, IL-32alpha, IL-32delta, IL-32gamma, Interleukin-32, IL-32, Natural killer cells protein 4, Tumor necrosis factor alpha-inducing factor, IL-32a, IL32a, IL32, Interleukin-32 alpha.

    Product # :

    CYT-648

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    Description

    Interleukin-32 human recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 168 amino acids (1-131 a.a.) and having a molecular mass of 19.1 kDa. The IL-32 is fused to a 37 amino acid His Tag at N-terminus and purified by conventional chromatography.

    Source

    Escherichia Coli.

    Formulation

    The IL-32 His Tag protein solution contains 20mM Tris-HCl, pH-8, 1mM DTT and 10% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      IL-32 is part of the cytokine family and contains a tyrosine sulfation site, 3 potential N-myristoylation sites, multiple putative phosphorylation sites, and an RGD cell-attachment sequence. IL-32 expression is elevated after the activation of T-cells by mitogens or the activation of NK cells by IL-2. IL-32 induces the production of TNF-a from macrophage cells. IL-32 pro-inflammatory pathway is activated in response to influenza A virus infection. Dysregulation of IL-32 in myelodysplastic syndrome and chronic myelomonocytic leukemia modulates apoptosis and impairs NK function.
      Induction of TNF, IL-1beta, and IL-6 by IL-32 is intervened by p38-MAPK. IL-32 induced monocyte-to-macrophage differentiation is mediated through nonapoptotic, caspase-3-dependent mechanisms. IL32 plays an important role in the pathogenesis of rheumatoid arthritis. IL-32 is involved in activation-induced cell death in T cells, through its intracellular actions. IL-32 is a cell-associated proinflammatory cytokine, which is particularly stimulated by mycobacteria through a caspase-1- and IL-18-dependent production of interferon gamma.
      IL-32 is associated with TNF-a, IL-1beta, and IL-18. IL32 is involved in human rheumatoid arthritis and is a novel target in autoimmune diseases.

    • Synonyms

      NK4, TAIF, TAIFa, TAIFb, TAIFc, TAIFd, IL-32beta, IL-32alpha, IL-32delta, IL-32gamma, Interleukin-32, IL-32, Natural killer cells protein 4, Tumor necrosis factor alpha-inducing factor, IL-32a, IL32a, IL32, Interleukin-32 alpha.

    • Physical Appearance

      Sterile filtered colorless solution.

    • Stability

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

    • Amino Acid Sequence

      MRGSHHHHHH GMASMTGGQQ MGRDLYDDDD KDRWGSHMCF PKVLSDDMKK LKARMHQAIE RFYDKMQNAE SGRGQVMSSL AELEDDFKEGYLETVAAYYE EQHPELTPLL EKERDGLRCR GNRSPVPDVE DPATEEPGES FCDKSYGAPR GDKEELTPQK CSEPQSSK.

    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 32A Human His
  • View Data Sheet

    Name :

    IL17E Mouse

    Description:

    Interleukin-17E Mouse Recombinant

    IL-25, IL-17E, IL17E, IL25, Interleukin-25.

    Product # :

    CYT-641

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    Description

    Recombinant mouse IL-17E is a non-glycosylated, disulfide-linked homodimer, containing 2x145 amino acid chains, with a total molecular weight of 35.5 kDa. The Mouse IL-17E is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    IL17E was lyophilized from a concentrated (1mg/ml) solution containing no additives.

    Purity

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

    Biological Activity

    The activity is determined by the dose-dependent production of IL-8 by human PBMCs and is 322-488ng/ml.

    More Info

    • Introduction

      IL-25 also called IL-17E cytokine has a sequence similarity with IL17.
      IL-17E indluces NF-kappaB activation, and stimulates the production of IL-8. IL17E and IL17B are ligands for the cytokine receptor IL17BR. IL-25 is a proinflammatory cytokine favoring Th2-type immune response. The upregulation of costimulation-induced IL-17E receptors and release of cytokines and chemokines from IL-17E treated costimulated Th cells are differentially regulated by intracellular JNK, p38 MAPK and NF-kappaB activity. Blocking Iinterleukin-25 prevents airway hyperresponsiveness, a critical feature of clinical asthma. IL25 produced by innate effector eosinophils and basophils increase the allergic inflammation by enhancing the maintenance and functions of TSLP-DC activated adaptive Th2 memory cells. Over expression of IL-25 up-regulates gene expression of Th2 cytokines and induces growth retardation, jaundice, and multiorgan inflammation in a transgenic mouse model. IL-25 contributes to the induction and maintenance of eosinophilic inflammation by acting on lung fibroblasts which supports the fact that IL-17E is an important factor in asthma pathophysiology. IL-17E operates by amplifying TH2 cell-mediated allergic airway inflammation but doesn’t induce allergic inflammation in vivo.

    • Synonyms

      IL-25, IL-17E, IL17E, IL25, Interleukin-25.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized Murine IL17E although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IL17E should be stored at 4°C between 2-7 days and for future use below -18°C.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.

    • Solubility

      It is recommended to reconstitute the lyophilized Mouse IL17E in sterile 10mM HCl at a concentration not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      VSLRIQEGCSHLPSCCPSKEQEPPEEWLKWSSASVS
      PPEPLSHTHHAESCRASKDGPLNSRAISPWSYELDRD
      LNRVPQDLYHARCLCPHCVSLQTGSHMDPLGNSVPL
      YHNQTVFYRRPCHGEEGTHRRYCLERRLYRVSLACV
      CVRPRVMA.

    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.

    Il17E Mouse
  • View Data Sheet

    Name :

    CD7 Human, Sf9

    Description:

    CD7 Human Recombinant, Sf9

    T-cell antigen CD7, GP40, LEU-9, Tp40, TP41, CD7, T-cell leukemia antigen, T-cell surface antigen Leu-9.

    Product # :

    PRO-2420

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    • More Info

    Description

    CD7 Human Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 164 amino acids (26-180a.a.) and having a molecular mass of 17.5kDa (Molecular size on SDS-PAGE will appear at approximately 18-28kDa). CD7 is expressed with a 6 amino acids His tag at C-Terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    CD7 protein solution (1mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 10% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      T-cell antigen CD7 (CD7) is a type I transmembrane glycoprotein which is expressed on pluripotential hemapoietic cells, nearly all human thymocytes and some peripheral blood T cells. The CD7 molecule is missing in a subset of human T cells under some physiologic conditions. An increase in CD7 negative T cells can be observed in a number of inflammatory skin diseases.

    • Synonyms

      T-cell antigen CD7, GP40, LEU-9, Tp40, TP41, CD7, T-cell leukemia antigen, T-cell surface antigen Leu-9.

    • 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

      ADLAQEVQQS PHCTTVPVGA SVNITCSTSG GLRGIYLRQL GPQPQDIIYY EDGVVPTTDR RFRGRIDFSG SQDNLTITMH RLQLSDTGTY TCQAITEVNV YGSGTLVLVT EEQSQGWHRC SDAPPRASAL PAPPTGSALP DPQTASALPD PPAASALPHH HHHH.

    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.

    Cd7 Human Sf9
  • View Data Sheet

    Name :

    sCD23 Human

    Description:

    Soluble CD23 Human Recombinant

    Low affinity immunoglobulin epsilon Fc receptor, Lymphocyte IgE receptor, Fc-epsilon-RII, BLAST-2, Immunoglobulin E-binding factor, CD23 antigen, FCER2, CD23, FCE2, CD23A, IGEBF, CLEC4J.

    Product # :

    PRO-1789

    Price :

    Quantity :

    Shipping Method :

    Room Temp Icon

    Shipped at Room temp

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    More Info

    • description
    • source
    • formulation
    • purity
    • biological activity
    • More Info

    Description

    sCD23 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 172 amino acids and having a molecular mass of 19.2kDa.The sCD23 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

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

    Purity

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

    Biological Activity

    The ED50 is determined by its ability to induce TNF-alpha production by human PBMCs. 

    More Info

    • Introduction

      CD23 is a 45kDa glycoprotein, which is present on a subpopulation of freshly isolated peripheral blood and tonsil B cells and strongly expressed on EBV-transformed B lymphoblasts. The CD23 molecule is identical to the low affinity IgE receptor found on B cells. Expression of CD23 has been detected in neoplastic cells from cases of B cell chronic lymphocyctic leukaemia and some cases of centroblastic/centrocytic lymphoma.

    • Synonyms

      Low affinity immunoglobulin epsilon Fc receptor, Lymphocyte IgE receptor, Fc-epsilon-RII, BLAST-2, Immunoglobulin E-binding factor, CD23 antigen, FCER2, CD23, FCE2, CD23A, IGEBF, CLEC4J.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized sCD23 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution sCD23 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 sCD23 in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      MELQVSSGFV CNTCPEKWIN FQRKCYYFGK GTKQWVHARY ACDDMEGQLV SIHSPEEQDF LTKHASHTGS WIGLRNLDLK GEFIWVDGSH VDYSNWAPGE PTSRSQGEDC VMMRGSGRWN DAFCDRKLGA WVCDRLATCT PPASEGSAES MGPDSRPDPD GRLPTPSAPL HS

    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.

    Scd23 Human
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