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1000 results found for “other cytokines”

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  • View Data Sheet

    Description:

    Serum Amyloid A4 Human Recombinant

    Serum amyloid A-4 protein, Constitutively expressed serum amyloid A protein, C-SAA, SAA4, CSAA.

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    CYT-002

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    Description

    SAA4 Human Recombinant fused with a 21 amino acid His tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 131 amino acids (21-130 a.a.) and having a molecular mass of 14.9kDa. The SAA4 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The SAA4 solution (0.5 mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 20% glycerol, 5mM DTT, 0.2M NaCl and 0.5mM EDTA.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

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    • Introduction

      SAA4 is a constitutively expressed protein which is a member of the SAA family. SAA4 is a major acute phase reactant and an apolipoprotein of the HDL complex. SAA4 is constitutively expressed only in humans and mice; it is connected almost completely with lipoproteins of the high density range. The physiological function of SAA4 is unknown, and its serum concentration has no association with those of other major apolipoproteins. SAA4 mRNA and protein occurrence in macrophage derived foam cells of coronary and carotid arteries implied a specific role of human SAA4 during inflammation including atherosclerosis.

    • Synonyms

      Serum amyloid A-4 protein, Constitutively expressed serum amyloid A protein, C-SAA, SAA4, CSAA.

    • 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 MWRSFFKEAL QGVGDMGRAY WDIMISNHQN SNRYLYARGN YDAAQRGPGG VWAAKLISRS RVYLQGLIDY YLFGNSSTVL EDSKSNEKAE EWGRSGKDPD RFRPDGLPKK Y.

    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.

    Saa4 Human
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    Description:

    Interleukin-13 Mouse Recombinant

    Interleukin-13, NC300, ALRH, BHR1, P600, IL-13, IL13.

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    CYT-375

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    Description

    Interleukin-13 Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 111 amino acids and having a molecular mass of 12.3 kDa. The IL-13 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The protein (1mg/ml) was lyophilized in PBS, pH 7.2 and 5% trehalose.

    Purity

    Greater than 95% as determined by SDS-PAGE.

    Biological Activity

    The ED50 range=4 ng/ml, corresponding to a specific activity of 250,000IU/mg as determined by the dose dependent proliferation of TF-1 cells.

    More Info

    • Introduction

      IL13 is an immunoregulatory cytokine produced primarily by activated Th2 cells. IL-13 is involved in several stages of B-cell maturation and differentiation. It up-regulates CD23 and MHC class II expression, and promotes IgE isotype switching of B cells. This cytokine down-regulates macrophage activity, thereby inhibits the production of pro-inflammatory cytokines and chemokines. This cytokine is found to be critical to the pathogenesis of allergen-induced asthma but operates through mechanisms independent of IgE and eosinophils. This gene, IL3, IL5, IL4, and CSF2 form a cytokine gene cluster on chromosome 5q, with this gene particularly close to IL4.

    • Synonyms

      Interleukin-13, NC300, ALRH, BHR1, P600, IL-13, IL13.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized Interleukin-13 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IL13 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 13 in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      MPVPRSVSLP LTLKELIEEL SNITQDQTPL CNGSMVWSVD LAAGGFCVAL DSLTNISNCN AIYRTQRILH GLCNRKAPTT VSSLPDTKIE VAHFITKLLS YTKQLFRHGP F.

    • Protein content

      Protein quantitation was carried out by two independent methods:1. UV spectroscopy at 280 nm using the absorbency value of 0.69 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 calibrated solution of IL-13 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 13 Mouse
  • View Data Sheet

    Description:

    Interleukin-1 beta Human Recombinant, His Tag

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

    Product # :

    CYT-480

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    Description

    Interleukin-1 beta His-Tag Human Recombinant produced in E.Coli is a single, non-glycosylated, Polypeptide chain containing 153 amino acids fragment (117-269) and having a total molecular mass of 21.88 kDa fused with an amino-terminal hexahistidine tag. The IL-1b His is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    IL-1b His tag protein solution is supplied in 20mM Tris-HCl pH 8.0 and 50% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Interleukin-1b is a potent pro-inflammatory cytokine produced by a wide variety of cell types including monocytes and macrophages. It displays a broad range of biological activity including activation of B and T cells in response to inflammation and the activation of endothelial 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 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.

    • Amino Acid Sequence

      APVRSLNCTLRDSQQKSLVMSGPYELKALHLQGQDMEQQVVFSMSFV

      QGEESNDKIPVALGLKEKNLYLSCVLKDDKPTLQLESVDPKNYPKKKME

      KRFVFNKIEINNKLEFESAQFPNWYISTSQAENMPVFLGGTKGGQDITDFTMQFVSS

    • Background

      What is the molecular weight/Mw of IL1B HUMAN, HIS Protein?
      IL1B HUMAN, HIS Protein has a total Mw of 21.88kDa.

      What is the source or expression system of IL1B HUMAN, HIS Protein?
      Escherichia Coli.

      What is the Purity of IL1B HUMAN, HIS Protein?
      IL1B HUMAN, HIS Protein is >95% pure as determined by SDS-PAGE.

      What is the Biological Activity of IL1B HUMAN, HIS Protein?
      The biological functionality of IL1B HUMAN, HIS Protein will be determined in the future.

      What is the amino acid sequence of IL1B HUMAN, HIS Protein?
      APVRSLNCTLRDSQQKSLVMSGPYELKALHLQGQDMEQQVVFSMSFV
      QGEESNDKIPVALGLKEKNLYLSCVLKDDKPTLQLESVDPKNYPKKKME
      KRFVFNKIEINNKLEFESAQFPNWYISTSQAENMPVFLGGTKGGQDITDFTMQFVSS.

      What applications can IL1B HUMAN, HIS Protein be used in?
      IL1B HUMAN, HIS Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for IL1B HUMAN, HIS Protein?
      The endotoxin level is minimal, IL1B HUMAN, HIS Protein was purified using conventional chromatography techniques.


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

    Il 1 Beta Human His
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    Description:

    Interleukin-33 Mouse Recombinant

    Interleukin 33, DVS27, NF-HEV, NKHEV, C9orf26, Interleukin-1 family member 11, IL- 1F11, Nuclear factor from high endothelial venules, Il-33, Il1f11, 9230117N10Rik, Il33.

    Product # :

    CYT-655

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    Description

    Interleukin33 Mouse recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 159 amino acids and having a molecular mass of 17.7 kDa.

    Source

    Escherichia Coli.

    Formulation

    The Mouse IL-33 was lyophilized from a sterile 0.2 micron filtered aqueous solution containing 10mM sodium phosphate, pH 7.5.

    Purity

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

    Biological Activity

    The ED50 as determined by the dose-dependent stimulation of the proliferation of murine D10S cells is 0.04ng/ml, corresponding to a specific activity of 2.5x107units/mg.

    More Info

    • Introduction

      Interleukin 33 (IL-33) is a 32kDa proinflammatory cytokine that may also regulate gene transcription in producer cells. IL-33 is structurally related to IL-1, which induces helper T cells to produce type 2 cytokines and acts through the receptor IL1RL-1 (IL1 receptor-like-1), which is known also as ST2. Binding of IL-33 to this receptor activates NF-kappa-B and MAP kinases and induces in vitro Th2 cells to produce cytokines. In vivo, IL-33 induces expression of IL-4, IL-5, IL-13 and leads to severe pathological changes in mucosal organs and in vitro, it can be divided to N-terminal fragment of 12kDa and C-terminal fragment of 18kDa by cleavage of caspase-1.

    • Synonyms

      Interleukin 33, DVS27, NF-HEV, NKHEV, C9orf26, Interleukin-1 family member 11, IL- 1F11, Nuclear factor from high endothelial venules, Il-33, Il1f11, 9230117N10Rik, Il33.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized IL-33 Recombinant although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IL-33 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 IL-33 in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      MSIQGTSLLT QSPASLSTYN DQSVSFVLEN GCYVINVDDS GKDQEQDQVL LRYYESPCPA SQSGDGVDGK KLMVNMSPIK DTDIWLHAND KDYSVELQRG DVSPPEQAFF VLHKKSSDFV SFECKNLPGT YIGVKDNQLA LVEEKDESCN NIMFKLSKI.

    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 33 Mouse
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    Description:

    Interleukin-31 Human Recombinant

    Interleukin 31, IL31, IL-31.

    Product # :

    CYT-625

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    Description

    IL-31 human recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 141 amino acids (24-164 a.a.) and having a molecular mass of 15.8 kDa.

    Source

    Escherichia Coli.

    Formulation

    The IL-31 (1mg/ml) was lyophilized with 20mM Phosphate buffer, 150mM NaCl pH-7.4.

    Purity

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

    Biological Activity

    The ED50 was determined by its ability to activate STAT following receptor ligand interaction and found to be <5ng/ml, corresponding to a specific activity of 200,000 units.

    More Info

    • Introduction

      IL-31 produced by activated Th2-type T cells, cooperates with a heterodimeric receptor consisting of IL-31 Receptor Anatagonist and Onconstatin-M Receptor that is continuesly expressed on epithelial cells and keratinocytes. IL-31 plays a role in the promotion of allergic skin disorders and in regulating other allergic diseases, such as asthma. IL-31 is involved in the itching sensation and endorses the scratching behavior in NC/Nga mice with atopic dermatitis. IL-31 expression is connectd with CLA(+) T cells and contributes to the development of atopic dermatitis-induced skin inflammation and pruritus. IL-31 is a powerful inducer of proinflammatory mediators in human colonic SEMFs. IL-31 takes part as a proinflammatory cytokine derived from Th2 cells.
      Serum IL-31 level is higher in patients with atopic dermatitis. IL-31 is involved in a broad range of immune- & non-immune cells & possesses potential pleiotropic physiological functions, including regulating hematopoiesis & immune response, causing inflammatory bowel disease, airway hypersensitivity & dermatitis.

    • Synonyms

      Interleukin 31, IL31, IL-31.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized IL-31 Recombinant although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IL-31 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 IL-31 in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      SHTLPVRLLR PSDDVQKIVE ELQSLSKMLL KDVEEEKGVL VSQNYTLPCL SPDAQPPNNI HSPAIRAYLK TIRQLDNKSV IDEIIEHLDK LIFQDAPETN ISVPTDTHEC KRFILTISQQ FSECMDLALK SLTSGAQQAT 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.

    Il 31 Human
  • View Data Sheet

    Description:

    Interleukin-17 Receptor Beta Human Recombinant

    Interleukin 17 Receptor B, IL17RH1, IL17BR, Interleukin 17B Receptor, Cytokine, Receptor-Like 4, Interleukin-17B Receptor, IL-17 Receptor Homolog 1, IL-17 Receptor B, IL-17B Receptor, IL-17Rh1, IL-17RB, EVI27, CRL4, Interleukin 17 Receptor Homolog 1, Interleukin-17 Receptor B, Cytokine Receptor CRL4.

    Product # :

    CYT-901

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    Description

    IL17RB Human Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 514 amino acids (18-292a.a) and having a molecular mass of 57.2kDa (Migrates at 50-70kDa on SDS-PAGE under reducing conditions).IL17RB is fused to a 239 amino acid hIgG-His-tag at C-terminus & purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    IL17RB protein solution (0.25mg/ml) containing phosphate buffered saline (pH 7.4) and 10% glycerol.

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      IL17 is a proinflammatory cytokine produced by activated T cells. IL-17 regulates the activities of NF-kappaB and mitogen-activated protein kinases. Interleukin-17 can stimulate the expression of IL6 and cyclooxygenase-2 (PTGS2/COX-2), as well as enhance the production of nitric oxide (NO). High levels of IL-17 are associated with several chronic inflammatory diseases including rheumatoid arthritis, psoriasis and multiple sclerosis.

    • Synonyms

      Interleukin 17 Receptor B, IL17RH1, IL17BR, Interleukin 17B Receptor, Cytokine, Receptor-Like 4, Interleukin-17B Receptor, IL-17 Receptor Homolog 1, IL-17 Receptor B, IL-17B Receptor, IL-17Rh1, IL-17RB, EVI27, CRL4, Interleukin 17 Receptor Homolog 1, Interleukin-17 Receptor B, Cytokine Receptor CRL4.

    • 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

      REPTVQCGSE TGPSPEWMLQ HDLIPGDLRD LRVEPVTTSV ATGDYSILMN VSWVLRADAS IRLLKATKIC VTGKSNFQSY SCVRCNYTEA FQTQTRPSGG KWTFSYIGFP VELNTVYFIG AHNIPNANMN EDGPSMSVNF TSPGCLDHIM KYKKKCVKAG SLWDPNITAC KKNEETVEVN FTTTPLGNRY MALIQHSTII GFSQVFEPHQ KKQTRASVVI PVTGDSEGAT VQLTPYFPTC GSDCIRHKGT VVLCPQTGVP FPLDNNKSKP GGWLPVEPKS CDKTHTCPPC PAPELLGGPS VFLFPPKPKD TLMISRTPEV TCVVVDVSHE DPEVKFNWYV DGVEVHNAKT KPREEQYNST YRVVSVLTVL HQDWLNGKEY KCKVSNKALP APIEKTISKA KGQPREPQVY TLPPSRDELT KNQVSLTCLV KGFYPSDIAV EWESNGQPEN NYKTTPPVLD SDGSFFLYSK LTVDKSRWQQ GNVFSCSVMH EALHNHYTQK SLSLSPGKHH 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.

    Il17Rb Human
  • View Data Sheet

    Description:

    Interleukin-17D Human Recombinant

    Interleukin 17D, Interleukin 27, IL-17D, IL-27, IL27, Interleukin-17D, Interleukin-27, IL17D.

    Product # :

    CYT-876

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    Description

    Interleukin-17D Human Recombinant (18-202) produced in E.Coli is a non-glycosylated disulfide-linked homodimer containing 2 polypeptide chains of 185 amino acids each and having a molecular mass of 40kDa.The IL-17D is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

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

    Purity

    Greater than 97.0% as determined by SDS-PAGE.

    Biological Activity

    Immobilized rHuIL-17D binds to rHuIL-17BR with EC50 less than 2µg/ml.

    More Info

    • Introduction

      IL17D modulates immune responses indirectly by stimulating the production of myeloid growth factors and chemokines, as well as suppressing the proliferation of myeloid progenitors. IL17D is expressed in the skeletal muscle, heart, adipose tissue, lung, pancreas, and nervous system. Among IL-17 family members, IL17D is most closely related to IL17B, sharing 27% aa sequence identity. The treatment of endothelial cells with IL17D cytokine stimulates the production of other cytokines including IL6, IL8 and CSF2/ GM-CSF. The increased expression of IL8 induced by IL17D cytokine is NF-kappa B-dependent.

    • Synonyms

      Interleukin 17D, Interleukin 27, IL-17D, IL-27, IL27, Interleukin-17D, Interleukin-27, IL17D.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized IL17D although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IL-17D 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-17D in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      APRAGRRPAR PRGCADRPEE LLEQLYGRLA AGVLSAFHHT LQLGPREQAR NASCPAGGRP ADRRFRPPTN LRSVSPWAYR ISYDPARYPR YLPEAYCLCR GCLTGLFGEE DVRFRSAPVY MPTVVLRRTP ACAGGRSVYT EAYVTIPVGC TCVPEPEKDA DSINSSIDKQ GAKLLLGPND APAGP.

    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.

    Il17D Human
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    Description:

    Interleukin-6 Rat Recombinant, sf9

    IL6, Ifnb2, ILg6.

    Product # :

    CYT-1048

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    Description

    IL6 produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 196 amino acids (25-211 a.a.) and having a molecular mass of 22.8kDa (Molecular size on SDS-PAGE will appear at approximately 18-28 kDa).IL6 is expressed with a 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    IL6 protein solution (0.5mg/ml) contains 20% glycerol & Phosphate Buffered Saline (pH 7.4).

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Biological Activity

    Measured in a cell proliferation assay using M-NFS-60 mouse B cell. The ED50 for this effects is less or equal to 0.1 ng/ml.

    More Info

    • Introduction

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

    • Synonyms

      IL6, Ifnb2, ILg6.

    • 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

      ADPFPTSQVR RGDFTEDTTH NRPVYTTSQV GGLITYVLRE ILEMRKELCN GNSDCMNSDDALSENNLKLP EIQRNDGCFQ TGYNQEICLL KICSGLLEFR FYLEFVKNNL QDNKKDKARVIQSNTETLVH IFKQEIKDSY KIVLPTPTSN ALLMEKLESQ KEWLRTKTIQ LILKALEEFL KVTMRSTRQT HHHHHH

    • Background

      Production and Applications of Rat Recombinant Interleukin-6 in sf9 Cells

      Abstract:

      Interleukin-6 (IL-6) is a critical cytokine involved in various physiological processes, including inflammation, immune responses, and hematopoiesis. The production of recombinant IL-6 has paved the way for numerous applications in research and therapeutic development. This paper elucidates the production of Rat Recombinant IL-6 in sf9 cells using baculovirus expression system and explores its potential applications in immunology and disease research.

      Introduction:

      Interleukin-6 is a pleiotropic cytokine with diverse functions in immune regulation, acute phase responses, and tissue homeostasis. The ability to produce recombinant IL-6 allows researchers to investigate its role in various biological contexts and develop potential therapies. The sf9 cell line, derived from Spodoptera frugiperda insect cells, offers an efficient platform for recombinant protein expression through the baculovirus system.

      Methods:

      The production of Rat Recombinant IL-6 involves inserting the rat IL-6 gene into a baculovirus transfer vector. This vector is then co-transfected with a linearized baculovirus DNA into sf9 cells. The resulting recombinant baculovirus expresses the IL-6 protein, which is secreted into the culture medium. The expressed protein is subsequently purified using chromatographic techniques to ensure its quality and activity.

      Applications:

      Rat Recombinant IL-6 produced in sf9 cells has widespread applications. It serves as a valuable tool for investigating the mechanisms underlying IL-6-mediated immune responses, inflammation, and hematopoiesis. Furthermore, it enables the development of potential therapies targeting IL-6-related disorders, including autoimmune diseases, inflammatory conditions, and certain types of cancer.

      Advantages of sf9 Expression:

      The sf9 expression system offers several advantages, including high protein yields, post-translational modifications, and proper protein folding. This system is especially suitable for complex cytokines like IL-6, which require correct tertiary structure for optimal biological activity.

      Challenges and Future Prospects:

      While sf9-based expression of Rat Recombinant IL-6 offers numerous benefits, challenges such as optimization of expression conditions, scale-up, and quality control remain. Additionally, further research is needed to explore the therapeutic potential of Rat Recombinant IL-6 in preclinical and clinical settings.

      Conclusion:

      The production of Rat Recombinant IL-6 in sf9 cells using the baculovirus expression system provides a powerful tool for unraveling the roles of IL-6 in various biological processes. This platform holds promise for advancing our understanding of IL-6-related diseases and facilitating the development of targeted therapeutic interventions.

      What is the molecular weight/Mw of IL6 RAT, SF9 Protein?
      IL6 RAT, SF9 Protein has a total Mw of 22.8kDa.

      What is the source or expression system of IL6 RAT, SF9 Protein?
      Sf9, Baculovirus cells.

      What is the Purity of IL6 RAT, SF9 Protein?
      IL6 RAT, SF9 Protein is >95% pure as determined by SDS-PAGE.

      What is the Biological Activity of IL6 RAT, SF9 Protein?
      Measured in a cell proliferation assay using M-NFS-60 mouse B cell. The ED50 for this effects is less or equal to 0.1 ng/ml.

      What is the amino acid sequence of IL6 RAT, SF9 Protein?
      ADPFPTSQVR RGDFTEDTTH NRPVYTTSQV GGLITYVLRE ILEMRKELCN GNSDCMNSDDALSENNLKLP EIQRNDGCFQ TGYNQEICLL KICSGLLEFR FYLEFVKNNL QDNKKDKARVIQSNTETLVH IFKQEIKDSY KIVLPTPTSN ALLMEKLESQ KEWLRTKTIQ LILKALEEFL KVTMRSTRQT HHHHHH.

      What applications can IL6 RAT, SF9 Protein be used in?
      IL6 RAT, SF9 Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for IL6 RAT, SF9 Protein?
      The endotoxin level is minimal, IL6 RAT, SF9 Protein was purified using conventional chromatography techniques.

      Who supplies recombinant IL6 RAT, SF9 that is in stock and available to order?
      ProSpec has the protein in stock and available for immediate delivery.

      Where can I order bulk mg quantities of IL6 RAT, SF9?
      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.

    Rat Il 6
  • View Data Sheet

    Description:

    Interleukin-1 Alpha Porcine Recombinant

    Hematopoietin-1, Lymphocyte-activating factor (LAF), Endogenous Pyrogen (EP), Leukocyte Endogenous Mediator (LEM), Mononuclear Cell Factor (MCF), IL-1 alpha, IL1, IL-1A, IL1F1.

    Product # :

    CYT-396

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    Description

    Interleukin-1A Porice Recombinant produced in E.Coli is single, a non-glycosylated, Polypeptide chain containing 158 amino acids and having a molecular mass of 18076 Dalton. The IL-1A is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The protein was lyophilized from a concentrated (1mg/ml) sterile 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 ED50 as determined by the dose-dependant stimulation of D10S cells is < 0.03 ng/ml.

    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

      Hematopoietin-1, Lymphocyte-activating factor (LAF), Endogenous Pyrogen (EP), Leukocyte Endogenous Mediator (LEM), Mononuclear Cell Factor (MCF), IL-1 alpha, IL1, IL-1A, IL1F1.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized Interleukin-1 alpha although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IL1A 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-1 alpha 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 Ser-Ala-Thr-Tyr-Ser.

    • Background

      What is the molecular weight/Mw of IL1A PORCINE Protein?
      IL1A PORCINE Protein has a total Mw of 18kDa.

      What is the source or expression system of IL1A PORCINE Protein?
      Escherichia Coli.

      What is the Purity of IL1A PORCINE Protein?
      IL1A PORCINE Protein is >95% pure as determined by SDS-PAGE.

      What is the Biological Activity of IL1A PORCINE Protein?
      The ED50 as determined by the dose-dependant stimulation of D10S cells is < 0.03 ng/ml.

      What is the amino acid sequence of IL1A PORCINE Protein?
      The sequence of the first five N-terminal amino acids was determined and was found to be Ser-Ala-Thr-Tyr-Ser.

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

      What is the endotoxin level for IL1A PORCINE Protein?
      The endotoxin level is minimal, IL1A PORCINE Protein was purified using conventional chromatography techniques.


    • Protein content

      Protein quantitation was carried out by two independent methods:1. UV spectroscopy at 280 nm using the absorbency value of 0.669 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 IL-1 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 1 Alpha Porcine
  • View Data Sheet

    Description:

    Interleukin-5 Mouse Recombinant

    EDF, BCDFII, TRF, T-cell replacing factor, Eosinophil differentiation factor, B cell differentiation factor II, IL-5, BCGF-II, Cytotoxic T-lymphocyte inducer, Il5.

    Product # :

    CYT-689

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    Description

    Interleukin-5 Mouse Recombinant produced in E.Coli is a dimeric, non-glycosylated polypeptide chain containing 2 x 113 amino acids forming a disulfide linked homodimer and having a molecular mass of 26.2 kDa.The Mouse IL-5 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Lyophilized from a concentrated (1mg/ml) solution containing 20mM Sodium Phosphate and 50mM NaCl pH-7.5.

    Purity

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

    Biological Activity

    The ED50 as determined by the dose-dependant stimulation of the proliferation of TF-1 cells was found to be 1.7ng/ml, corresponding to a specific activity of 588,235.3IU/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 II, IL-5, BCGF-II, Cytotoxic T-lymphocyte inducer, Il5.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized Mouse Interleukin-5 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Mouse 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 Mouse Interleikin-5 in sterile 18MΩ-cm H2O at a concentration of 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      MEIPMSTVVK ETLTQLSAHR ALLTSNETMR LPVPTHKNHQ LCIGEIFQGL DILKNQTVRG GTVEMLFQNL SLIKKYIDRQ KEKCGEERRR TRQFLDYLQE FLGVMSTEWA MEG.

    • Background

      What is the molecular weight/Mw of IL 5 MOUSE Protein?
      IL 5 MOUSE Protein has a total Mw of 26.2kDa.

      What is the source or expression system of IL 5 MOUSE Protein?
      Escherichia Coli.

      What is the Purity of IL 5 MOUSE Protein?
      IL 5 MOUSE Protein is >97% pure as determined by SDS-PAGE.

      What is the Biological Activity of IL 5 MOUSE Protein?
      The ED50 as determined by the dose-dependant stimulation of the proliferation of TF-1 cells was found to be 1.7ng/ml, corresponding to a specific activity of 588,235.3IU/mg.

      What is the amino acid sequence of IL 5 MOUSE Protein?
      MEIPMSTVVK ETLTQLSAHR ALLTSNETMR LPVPTHKNHQ LCIGEIFQGL DILKNQTVRG GTVEMLFQNL SLIKKYIDRQ KEKCGEERRR TRQFLDYLQE FLGVMSTEWA MEG.

      What applications can IL 5 MOUSE Protein be used in?
      IL 5 MOUSE Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for IL 5 MOUSE Protein?
      The endotoxin level is minimal, IL 5 MOUSE Protein was purified using conventional chromatography techniques.

      Who supplies recombinant IL 5 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 IL 5 MOUSE?
      ProSpec supplies bulk mg quantities at affordable prices that meets research and academic budgets.

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

    Interleukin 5 Mouse
  • View Data Sheet

    Description:

    Interleukin-21 Receptor Mouse Recombinant

    Interleukin-21 receptor, IL-21 receptor, IL-21R, Il21r, Lymphocyte receptor beta, LR-beta, Novel interleukin receptor, Novel cytokine receptor 8, NR8, Novel interleukin receptor, CD360, CD360 antigen, NILR, Nilr.

    Product # :

    CYT-1204

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    Description

    IL21R Mouse Recombinant produced in HEK293 Cells is a single, glycosylated polypeptide chain containing 457amino acids (20-237 a.a) and having a molecular mass of 52 kDa.IL21R is expressed with a 239 amino acid hIgG-His-Tag at C-Terminus and purified by proprietary chromatographic techniques.

    Source

    HEK293 Cells.

    Formulation

    The IL21R solution (0.25mg/1ml) contains PBS (pH7.4) and 10% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Biological Activity

    Measured by its ability to inhibit IFN-g secretion using NK-92 human natural killer cells. The ED50 range ≤ 4 ug/ml with mouse IL-2.

    More Info

    • Introduction

      IL-21 is produced by CD4+ T cells in response to antigenic stimulation. Its action enhances antigen-specific responses of immune cells. The biological effects of IL-21 include induction of differentiation of T-cells-stimulated B-cells into plasma cells and memory B-cells, stimulation (in conjuction) with IL-4 of IgG production, and induction of apoptotic effects in na?ve B-cells and stimulated B-cells in the absence of T-cell signaling. Additionally, IL-21 promotes the anti-tumor activity of CD8+ T-cells and NK cells. IL-21 exerts its effect through binding to a specific type I cytokine receptor, IL-21R, which also contains the gamma chain (?c) found in other cytokine receptors including IL-2, IL-4, IL-7, IL-9 and IL-15. The IL-21/IL-21R interaction triggers a cascade of events which includes activation of the tyrosine kinases JAK1 and JAK3, followed by activation of the transcription factors STAT1 and STAT3.

    • Synonyms

      Interleukin-21 receptor, IL-21 receptor, IL-21R, Il21r, Lymphocyte receptor beta, LR-beta, Novel interleukin receptor, Novel cytokine receptor 8, NR8, Novel interleukin receptor, CD360, CD360 antigen, NILR, Nilr.

    • 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

      CLDLTCYTDY LWTITCVLET RSPNPSILSL TWQDEYEELQ DQETFCSLHR SGHNTTHIWY TCHMRLSQFL SDEVFIVNVT DQSGNNSQEC GSFVLAESIK PAPPLNVTVA FSGRYDISWD SAYDEPSNYV LRGKLQYELQ YRNLRDPYAV RPVTKLISVD SRNVSLLPEE FHKDSSYQLQ VRAAPQPGTS FRGTWSEWSD PVIFQTQAGE PEAGWDPHLE PKSCDKTHTC PPCPAPELLG GPSVFLFPPK PKDTLMISRT PEVTCVVVDV SHEDPEVKFN WYVDGVEVHN AKTKPREEQY NSTYRVVSVL TVLHQDWLNG KEYKCKVSNK ALPAPIEKTI SKAKGQPREP QVYTLPPSRD ELTKNQVSLT CLVKGFYPSD IAVEWESNGQ PENNYKTTPP VLDSDGSFFL YSKLTVDKSR WQQGNVFSCS VMHEALHNHY TQKSLSLSPG KHHHHHH

    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.

    Il21R Mouse
  • View Data Sheet

    Description:

    Flt3 Ligand Porcine Recombinant

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

    Product # :

    CYT-1041

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    Description

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

    Source

    Escherichia Coli.

    Formulation

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

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

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

    • Synonyms

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

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Solubility

      It is recommended to reconstitute the lyophilized Flt3-L in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

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

    • Background

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

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

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

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

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

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

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

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

    Flt3 Ligand Porcine
  • View Data Sheet

    Description:

    APRIL Mouse Recombinant

    Tumor necrosis factor ligand superfamily member 13, A proliferation-inducing ligand, APRIL, CD256, Tnfsf13, April.

    Product # :

    CYT-803

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    Description

    APRIL Mouse Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 146 amino acids and having a molecular mass of 16.4 kDa. The APRIL is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Lyophilized from a 0.2µm filtered concentrated solution in PBS, pH 7.4, with 0.02 % Tween-20.

    Purity

    Greater than 97.0% as determined by Analysis by SDS-PAGE.

    Biological Activity

    Determined by a cell proliferation assay using activated T cells.

    More Info

    • Introduction

      APRIL which is a part of the TNF ligand superfamily (TNFSF13) is a type II transmembrane protein. Normally, APRIL expression is low in tissues, but is elevated in numerous types of tumors and transformed cell lines. APRIL stimulates proliferation of tumor cell lines and intensifies tumorigenicity in nude mice.

    • Synonyms

      Tumor necrosis factor ligand superfamily member 13, A proliferation-inducing ligand, APRIL, CD256, Tnfsf13, April.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Amino Acid Sequence

      AVLTQKHKKK HSVLHLVPVN ITSKADSDVT EVMWQPVLRR GRGLEAQGDI VRVWDTGIYL LYSQVLFHDV TFTMGQVVSR EGQGRRETLF RCIRSMPSDP DRAYNSCYSA GVFHLHQGDI ITVKIPRANA KLSLSPHGTF LGFVKL.

    • Background

      What is the molecular weight/Mw of APRIL Protein?
      APRIL Protein has a total Mw of 16.4kDa.

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

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

      What is the Biological Activity of APRIL Protein?
      Determined by a cell proliferation assay using activated T cells.

      What is the amino acid sequence of APRIL Protein?
      AVLTQKHKKK HSVLHLVPVN ITSKADSDVT EVMWQPVLRR GRGLEAQGDI VRVWDTGIYL LYSQVLFHDV TFTMGQVVSR EGQGRRETLF RCIRSMPSDP DRAYNSCYSA GVFHLHQGDI ITVKIPRANA KLSLSPHGTF LGFVKL.

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

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

    April Mouse
  • View Data Sheet

    Description:

    Interleukin-17 Rat Recombinant

    CTLA-8, IL-17, IL-17A, Cytotoxic T-lymphocyte-associated antigen 8, Interleukin-17A.

    Product # :

    CYT-542

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    Description

    Interleukin-17A Rat Recombinant produced in E.Coli is a homodimeric, non-glycosylated polypeptide chain having a molecular mass of 30 kDa. The IL-17A Rat is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Lyophilized from a concentrated (1mg/ml) solution containing 10mM NaCitrate, pH-3.0.

    Purity

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

    Biological Activity

    The ED50 as determined by dose-dependent induction of IL-6 by mouse NIH 3T3 fibroblasts is 0.44-0.66ng/ml.

    More Info

    • Introduction

      IL17 is a proinflammatory cytokine produced by activated T cells. IL-17 regulates the activities of NF-kappaB and mitogen-activated protein kinases. Interleukin-17 can stimulate the expression of IL6 and cyclooxygenase-2 (PTGS2/COX-2), as well as enhance the production of nitric oxide (NO). High levels of IL-17 are associated with several chronic inflammatory diseases including rheumatoid arthritis, psoriasis and multiple sclerosis.

    • Synonyms

      CTLA-8, IL-17, IL-17A, Cytotoxic T-lymphocyte-associated antigen 8, Interleukin-17A.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized Interleukin Rat 17A although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Rat IL17 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 Rat 17A in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      MAVLIPQSSV CPNAEANNFL QNVKVNLKVL NSLSSKASSR RPSDYLNRST SPWTLSRNED PDRYPSVIWE AQCRHQRCVN AEGKLDHHMN SVLIQQEILV LKREPEKCPF TFRVEKMLVG VGCTCVSSIV RHAS.

    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 17 Rat
  • View Data Sheet

    Description:

    Interleukin-13 Rat Recombinant

    NC300, ALRH, BHR1, P600, IL-13.

    Product # :

    CYT-391

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    Description

    Interleukin-13 Rat Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 113 amino acids and having a molecular mass of 12.7 kDa.The IL-13 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The protein (1mg/ml) was lyophilized with no additives.

    Purity

    Greater than 95% as determined by SDS-PAGE.

    Biological Activity

    ED50 range = 2-6 ng/mL as determined by the dose dependent proliferation of human TF-1 cells. Optimal concentration for individual application should be determined by a dose response assay.

    More Info

    • Introduction

      IL13 is an immunoregulatory cytokine produced primarily by activated Th2 cells. IL-13 is involved in several stages of B-cell maturation and differentiation. It up-regulates CD23 and MHC class II expression, and promotes IgE isotype switching of B cells. This cytokine down-regulates macrophage activity, thereby inhibits the production of pro-inflammatory cytokines and chemokines. This cytokine is found to be critical to the pathogenesis of allergen-induced asthma but operates through mechanisms independent of IgE and eosinophils. This gene, IL3, IL5, IL4, and CSF2 form a cytokine gene cluster on chromosome 5q, with this gene particularly close to IL4.

    • Synonyms

      NC300, ALRH, BHR1, P600, IL-13.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized Interleukin-13 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IL13 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 13 in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Protein content

      Protein quantitation was carried out by two independent methods:1. UV spectroscopy at 280 nm using the absorbency value of 0.69 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 calibrated solution of IL-13 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 13 Rat
  • View Data Sheet

    Description:

    Interleukin-1 Alpha Rhesus Macaque Recombinant

    Hematopoietin-1, Lymphocyte-activating factor (LAF), Endogenous Pyrogen (EP), Leukocyte Endogenous Mediator (LEM), Mononuclear Cell Factor (MCF), IL-1 alpha,IL1, IL-1A, IL1F1.

    Product # :

    CYT-790

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    Description

    Recombinant IL 1 alpha Rhesus Macaque produced in E.coli cells is a non-glycosylated, homodimeric protein containing 159 amino acid chain and having a molecular mass of 18.1kDa. The IL 1 alpha is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The IL 1 alpha was 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 as determined by a cell proliferation assay using murine D10S cells is less than 10 pg/ml, corresponding to a specific activity of > 1.0×108IU/mg.

    More Info

    • Introduction

      IL-1 alpha is produced by activated macrophages, stimulates thymocyte proliferation by inducing il-2 release, b-cell maturation and proliferation, and fibroblast growth factor activity. IL1A 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

      Hematopoietin-1, Lymphocyte-activating factor (LAF), Endogenous Pyrogen (EP), Leukocyte Endogenous Mediator (LEM), Mononuclear Cell Factor (MCF), IL-1 alpha,IL1, IL-1A, IL1F1.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Amino Acid Sequence

      SAPFSFLSNM TYHFIRIIKH EFILNDTLNQ TIIRANDQHL TAAAIHNLDE AVKFDMGAYT SSKDDTKVPV ILRISKTQLY VSAQDEDQPV LLKEMPEINK TITGSETNFL FFWETHGTKN YFISVAHPNL FIATKHDNWV CLAKGLPSIT DFQILENQA

    • Background

      What is the molecular weight/Mw of IL1A RHESUS MACAQUE Protein?
      IL1A RHESUS MACAQUE Protein has a total Mw of 18.1kDa.

      What is the source or expression system of IL1A RHESUS MACAQUE Protein?
      Escherichia Coli.

      What is the Purity of IL1A RHESUS MACAQUE Protein?
      IL1A RHESUS MACAQUE Protein is >97% pure as determined by SDS-PAGE.

      What is the Biological Activity of IL1A RHESUS MACAQUE Protein?
      The ED50 as determined by a cell proliferation assay using murine D10S cells is less than 10 pg/ml, corresponding to a specific activity of > 1.0×108IU/mg.

      What is the amino acid sequence of IL1A RHESUS MACAQUE Protein?
      SAPFSFLSNM TYHFIRIIKH EFILNDTLNQ TIIRANDQHL TAAAIHNLDE AVKFDMGAYT SSKDDTKVPV ILRISKTQLY VSAQDEDQPV LLKEMPEINK TITGSETNFL FFWETHGTKN YFISVAHPNL FIATKHDNWV CLAKGLPSIT DFQILENQA

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

      What is the endotoxin level for IL1A RHESUS MACAQUE Protein?
      The endotoxin level is minimal, IL1A RHESUS MACAQUE 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 Rhesus Macaque
  • View Data Sheet

    Description:

    Interleukin-13 Variant Human Recombinant

    Interleukin-13, NC30, ALRH, BHR1, P600, IL-13, MGC116786, MGC116788, MGC116789.

    Product # :

    CYT-682

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    Description

    Interleukin-13 Variant Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 114 amino acids, with a substitution of Q for R at position 112 compared with the wild type IL-13, having a molecular mass of 12.5 kDa. The IL-13 Variant is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Lyophilized from a 0.2µm filtered concentrated solution in 1xPBS, pH 7.2, containing 5% trehalose.

    Purity

    Greater than 95% as determined by(a) Analysis by RP-HPLC.
    (b) Analysis by SDS-PAGE.

    Biological Activity

    The ED50 was determined by the dose dependent prolifiration of TF-1 cells and was found to be < 1ng/ml, corresponding to a specific activity of >1,000,000 units/mg. This analog has also been shown to exhibit increased in vivo activity compared to wild type IL-13.

    More Info

    • Introduction

      IL13 is an immunoregulatory cytokine produced primarily by activated Th2 cells. IL-13 is involved in several stages of B-cell maturation and differentiation. It up-regulates CD23 and MHC class II expression, and promotes IgE isotype switching of B cells. This cytokine down-regulates macrophage activity, thereby inhibits the production of pro-inflammatory cytokines and chemokines. This cytokine is found to be critical to the pathogenesis of allergen-induced asthma but operates through mechanisms independent of IgE and eosinophils. This gene, IL3, IL5, IL4, and CSF2 form a cytokine gene cluster on chromosome 5q, with this gene particularly close to IL4.

    • Synonyms

      Interleukin-13, NC30, ALRH, BHR1, P600, IL-13, MGC116786, MGC116788, MGC116789.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized Interleukin-13 Variant although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IL13 Variant 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 13 Variant in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      SPGPVPPSTA LRELIEELVN ITQNQKAPLC NGSMVWSINL TAGMYCAALE SLINVSGCSA IEKTQRMLSG FCPHKVSAGQ FSSLHVRDTK IEVAQFVKDL LLHLKKLFRE GQFN.

    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 13 Variant Human
  • View Data Sheet

    Description:

    Interleukin-18 Human Recombinant, His Tag

    Interferon-gamma-inducing factor, IGIF, IL-1g, IL-18, IL1F4, MGC12320, IFN-gamma-inducing factor, Interleukin-1 gamma, IL-1 gamma, Iboctadekin, IL18.

    Product # :

    CYT-663

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    Description

    Interleukin-18 Human Recombinant produced in E.Coli is a single, non-glycosylated, Polypeptide chain containing 157 amino acids fragment (37-193) having a molecular weight of 20kDa and fused with a 4.5kDa amino-terminal hexahistidine tag. The IL-18 His is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Interleukin -18 His-Tag protein is supplied in 20mM Tris-HCl pH-8 and 50% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      IL-18 is a proinflammatory cytokine. This cytokine can induce the IFN-gamma production of T cells. The combination of this cytokine and IL12 has been shown to inhibit IL4 dependent IgE and IgG1 production, and enhance IgG2a production of B cells. IL-18 binding protein (IL18BP) can specifically interact with this cytokine, and thus negatively regulate its biological activity.

    • Synonyms

      Interferon-gamma-inducing factor, IGIF, IL-1g, IL-18, IL1F4, MGC12320, IFN-gamma-inducing factor, Interleukin-1 gamma, IL-1 gamma, Iboctadekin, IL18.

    • 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.

    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 18 Human His
  • View Data Sheet

    Description:

    Interleukin-31 Mouse Recombinant

    Interleukin 31, IL31, IL-31.

    Product # :

    CYT-604

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    Description

    IL31 mouse recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 141 amino acids and having a molecular mass of 15.7 kDa.

    Source

    Escherichia Coli.

    Formulation

    The IL31 (1mg/ml) was lyophilized from 10mM sodium Phosphate pH-7.5.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      IL-31 produced by activated Th2-type T cells, cooperates with a heterodimeric receptor consisting of IL-31 Receptor Anatagonist and Onconstatin-M Receptor that is continuesly expressed on epithelial cells and keratinocytes. IL-31 plays a role in the promotion of allergic skin disorders and in regulating other allergic diseases, such as asthma. IL-31 is involved in the itching sensation and endorses the scratching behavior in NC/Nga mice with atopic dermatitis. IL-31 expression is connectd with CLA(+) T cells and contributes to the development of atopic dermatitis-induced skin inflammation and pruritus. IL-31 is a powerful inducer of proinflammatory mediators in human colonic SEMFs. IL-31 takes part as a proinflammatory cytokine derived from Th2 cells.
      Serum IL-31 level is higher in patients with atopic dermatitis. IL-31 is involved in a broad range of immune- & non-immune cells & possesses potential pleiotropic physiological functions, including regulating hematopoiesis & immune re

    • Synonyms

      Interleukin 31, IL31, IL-31.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized IL31 Recombinant although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IL31 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 IL31 in sterile 18MΩ -cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      MTCSLSFGAP ISKEDLRTTI DLLKQESQDL YNNYSIKQAS GMSADESIQL PCFSLDREAL TNISVIIAHL EKVKVLSENT VDTSWVIRWL TNISCFNPLN LNISVPGNTD ESYDCKVFVL TVLKQFSNCM AELQAKDNTT C.

    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.

    Il31 Mouse
  • View Data Sheet

    Description:

    Interleukin-15 Rat Recombinant

    IL-15, MGC9721.

    Product # :

    CYT-345

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    Description

    Interleukin-15 Rat Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 115 amino acids and having a molecular mass of 13533 Dalton. The IL-15 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The protein was lyophilized from 10mM Tris, pH-8.5.

    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 CTLL-2 was found to be < 10 ng/ml, corresponding to a Specific Activity of 100,000IU/mg.

    More Info

    • Introduction

      The protein encoded by this gene is a cytokine that regulates T and natural killer cell activation and proliferation. This cytokine and interleukine 2 share many biological activities. They are found to bind common hematopoietin receptor subunits, and may compete for the same receptor, and thus negatively regulate each other's activity. The number of CD8+ memory cells is shown to be controlled by a balance between this cytokine and IL2. This cytokine induces the activation of JAK kinases, as well as the phosphorylation and activation of transcription activators STAT3, STAT5, and STAT6. Studies of the mouse counterpart suggested that this cytokine may increase the expression of apoptosis inhibitor BCL2L1/BCL-x(L), possibly through the transcription activation activity of STAT6, and thus prevent apoptosis. Two alternatively spliced transcript variants of this gene encoding the same protein have been reported.

    • Synonyms

      IL-15, MGC9721.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized Interleukin-15 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IL15 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-15 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-Asn-Trp-Ile-Asp.

    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 15 Rat
  • View Data Sheet

    Description:

    Interleukin-2 Mouse Recombinant

    Interleukin-2, T-cell growth factor (TCGF),  Lymphokine, IL-2.

    Product # :

    CYT-370

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    Description

    Interleukin-2 Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 148 amino acids and having a molecular mass of 17.2kDa. The IL-2 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Lyophilized from a 0.2µm filtered concentrated solution (1mg/ml) in 20mM 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 as determined by the dose-dependant stimulation of murine CTLL-2 cells is less than 0.2ng/ml corresponding to a Specific Activity of 5x106IU/mg.

    More Info

    • Introduction

      IL2 is a secreted cytokine that is important for the proliferation of T and B lymphocytes. The receptor of this cytokine is a heterotrimeric protein complex whose gamma chain is also shared by interleukin 4 (IL4) and interleukin 7 (IL7). The expression of this gene in mature thymocytes is monoallelic, which represents an unusual regulatory mode for controlling the precise expression of a single gene. The targeted disruption of a similar gene in mice leads to ulcerative colitis-like disease, which suggests an essential role of this gene in the immune response to antigenic stimuli.

    • Synonyms

      Interleukin-2, T-cell growth factor (TCGF), Lymphokine, IL-2.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized Interleukin-2 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IL2 should be stored at 4°C between 2-7 days and for future use below -18°C.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.

    • Solubility

      It is recommended to reconstitute the lyophilized Mouse IL-2 in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      PTSSSTSSST AEAQQQQQQQ QQQQQHLEQL LMDLQELLSR MENYRNLKLP RMLTFKFYLP KQATELKDLQ CLEDELGPLR HVLDLTQSKS FQLEDAENFI SNIRVTVVKL KGSDNTFECQ FDDESATVVD FLRRWIAFCQ SIISTSPQ.

    • Background

      What is the molecular weight/Mw of IL 2 MOUSE Protein?
      IL 2 MOUSE Protein has a total Mw of 17.2kDa.

      What is the source or expression system of IL 2 MOUSE Protein?
      Escherichia Coli.

      What is the Purity of IL 2 MOUSE Protein?
      IL 2 MOUSE Protein is >97% pure as determined by SDS-PAGE.

      What is the Biological Activity of IL 2 MOUSE Protein?
      The ED50 as determined by the dose-dependant stimulation of murine CTLL-2 cells is less than 0.2ng/ml corresponding to a Specific Activity of 5x106IU/mg.

      What is the amino acid sequence of IL 2 MOUSE Protein?
      PTSSSTSSST AEAQQQQQQQ QQQQQHLEQL LMDLQELLSR MENYRNLKLP RMLTFKFYLP KQATELKDLQ CLEDELGPLR HVLDLTQSKS FQLEDAENFI SNIRVTVVKL KGSDNTFECQ FDDESATVVD FLRRWIAFCQ SIISTSPQ.

      What applications can IL 2 MOUSE Protein be used in?
      IL 2 MOUSE Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for IL 2 MOUSE Protein?
      The endotoxin level is minimal, IL 2 MOUSE Protein was purified using conventional chromatography techniques.

      Who supplies recombinant IL 2 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 IL 2 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 methods:1. UV spectroscopy at 280 nm using the absorbency value of 0.482 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 calibrated solution of IL-2 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 2 Mouse
  • View Data Sheet

    Description:

    Interleukin-3 Human Recombinant

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

    Product # :

    CYT-210

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    Description

    Interleukin-3 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 133 amino acids and having a molecular mass of 15000 Dalton. The IL-3 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Lyophilized from a concentrated (1mg/ml) solution in water containing 0.3 mg/ml of NaHCO3.

    Purity

    Greater than 98.0% 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 TF-1 cells is < 0.1 ng/ml, corresponding to a Specific Activity of 10,000,000 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 Interleukin-3 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 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 Ala-Pro-Met-Thr-Gln.

    • Background

      What is the molecular weight/Mw of IL3 HUMAN Protein?
      IL3 HUMAN Protein has a total Mw of 15kDa.

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

      What is the Purity of IL3 HUMAN Protein?
      IL3 HUMAN Protein is >98% pure as determined by SDS-PAGE.

      What is the Biological Activity of IL3 HUMAN Protein?
      The ED50 as determined by the dose-dependant stimulation of TF-1 cells is < 0.1 ng/ml, corresponding to a Specific Activity of 10,000,000 IU/mg.

      What is the amino acid sequence of IL3 HUMAN Protein?
      The sequence of the first five N-terminal amino acids was determined and was found to be Ala-Pro-Met-Thr-Gln.

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

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

      Who supplies recombinant IL3 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 IL3 HUMAN?
      ProSpec supplies bulk mg quantities at affordable prices that meets research and academic budgets.

    • Protein content

      Protein quantitation was carried out by two independent methods:1. UV spectroscopy at 280 nm using the absorbency value of 0.84 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 IL-3 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 Human
  • View Data Sheet

    Description:

    LIF Human Recombinant, Yeast

    CDF, HILDA, D-FACTOR, Differentiation- stimulating factor, Melanoma-derived LPL inhibitor, MLPLI, Emfilermin, Leukemia inhibitory factor, LIF, DIA.

    Product # :

    CYT-191

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    Description

    LIF Human Recombinant produced in yeast is a single, glycosylated polypeptide chain containing 180 amino acids and having a molecular mass of 58.5 kDa. The LIF is purified by proprietary chromatographic techniques.

    Source

    Pichia pastoris.

    Formulation

    The protein was lyophilized from a 0.2 µm filtered PBS.

    Purity

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

    Biological Activity

    The biological activity of recombinant human LIF was measured by the ability to induce differentiation of murine M1 myeloid leukemic cells. The minimal detectable concentration of human LIF in this assay is <0.05 ng/mL. The specific activity is > 1 x 108 units/mg.

    More Info

    • Introduction

      Leukemia Inhibitory Factor also called LIF is a lymphoid factor that promotes long-term maintenance of embryonic stem cells by suppressing spontaneous differentiation. Leukemia Inhibitory Factor has several functions such as cholinergic neuron differentiation, control of stem cell pluripotency, bone & fat metabolism, mitogenesis of factor dependent cell lines & promotion of megakaryocyte production in vivo. Human and mouse LIF exhibit a 78% identity in its amino acid sequence.

    • Synonyms

      CDF, HILDA, D-FACTOR, Differentiation- stimulating factor, Melanoma-derived LPL inhibitor, MLPLI, Emfilermin, Leukemia inhibitory factor, LIF, DIA.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Amino Acid Sequence

      S P L P I T P V N A T C A I R H P C H N N L M N Q I R S Q L A Q L N G S A N A L F I L Y Y T A Q G E P F P N N L D K L C G P N V T D F P P F H A N G T E K A K L V E L Y R I V V Y L G T S L G N I T R D Q K I L N P S A L S L H S K L N A T A D I L R G L L S N V L C R L C S K Y H V G H V D V T Y G P D T S G K D V F Q K K K L G C Q L L G K Y K Q I I A V L A Q A F.

    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.

    Lif Human Yeast
  • View Data Sheet

    Description:

    Interleukin-1 beta Mouse Recombinant

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

    Product # :

    CYT-273

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    Description

    Interleukin-1 beta Mouse Recombinant produced in E.Coli is a non-glycosylated, Polypeptide chain containing 153 amino acids and having a molecular mass of 17500 Dalton. The IL-1b is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Mouse IL-1b was lyophilized from a sterile filtered aqueous solution in 10mM sodium phosphate, pH 7.5.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Biological Activity

    The activity as determined by the dose-dependent proliferation of mouse D10S cells is 0.9-1.3pg/ml, corresponding to a Specific Activity of 1.1 x 106 Units/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 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 Interleukin-1b although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IL1b 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-1b in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      MVPIRQLHYR LRDEQQKSLV LSDPYELKAL HLNGQNINQQ VIFSMSFVQGEPSNDKIPVA LGLKGKNLYL SCVMKDGTPT LQLESVDPKQ YPKKKMEKRFVFNKIEVKSK VEFESAEFPN WYISTSQAEH KPVFLGNNSG QDIIDFTMES VSS.

    • Background

      What is the molecular weight/Mw of IL1B MOUSE Protein?
      IL1B MOUSE Protein has a total Mw of 17.5kDa.

      What is the source or expression system of IL1B MOUSE Protein?
      Escherichia Coli.

      What is the Purity of IL1B MOUSE Protein?
      IL1B MOUSE Protein is >95% pure as determined by SDS-PAGE.

      What is the Biological Activity of IL1B MOUSE Protein?
      The activity as determined by the dose-dependent proliferation of mouse D10S cells is 0.9-1.3pg/ml, corresponding to a Specific Activity of 1.1 x 106 Units/mg.

      What is the amino acid sequence of IL1B MOUSE Protein?
      MVPIRQLHYR LRDEQQKSLV LSDPYELKAL HLNGQNINQQ VIFSMSFVQGEPSNDKIPVA LGLKGKNLYL SCVMKDGTPT LQLESVDPKQ YPKKKMEKRFVFNKIEVKSK VEFESAEFPN WYISTSQAEH KPVFLGNNSG QDIIDFTMES VSS.
      What applications can IL1B MOUSE Protein be used in?
      IL1B MOUSE Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for IL1B MOUSE Protein?
      The endotoxin level is minimal, IL1B MOUSE Protein was purified using conventional chromatography techniques.

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    Il 1 Beta Mouse