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1000 results found for “other cytokines”

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  • View Data Sheet

    Description:

    Interleukin-36 Receptor Antagonist Mouse Recombinant

    Product # :

    CYT-154

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    Description

    IL36RN Mouse Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 154 amino acids and having a molecular mass of 17.0kDa.The IL36RN 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 95.0% as determined by SDS-PAGE.

    Biological Activity

    Fully biologically active when compared to standard. Measured by its ability to inhibit IL-36a, IL-36b or IL-36g induced IL-6 secretion by NIH-3T3 mouse embryonic fibroblast cells. The ED50 for this effect is typically 0.8-4ug/ml (corresponding to a specific activity of 250-125units/mg) in the presence of 15ng/ml of recombinant mouse IL-36b.

    More Info

    • Introduction

      IL36RA belongs to the IL-1 family of proteins. IL36RA is produced as a 156 aa protein which holds no signal sequence, no prosegment and no potential N-linked glycosylation site but, IL36RA is secreted as a 17 kDa monomer. Cells known to express IL36Ra/IL1F5 include monocytes, B cells, keratinocytes, dendritic cells/Langerhans cells and gastric fundus Parietal and Chief cells.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized IL 36RN although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IL 36RN 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 IL36RN in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      VLSGALCFRM KDSALKVLYL HNNQLLAGGL HAEKVIKGEE ISVVPNRALD ASLSPVILGV QGGSQCLSCG TEKGPILKLE PVNIMELYLG AKESKSFTFY RRDMGLTSSF ESAAYPGWFL CTSPEADQPV RLTQIPEDPA WDAPITDFYF QQCD

    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.

    Il36Ra Mouse
  • View Data Sheet

    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.

    • Background

      What is the molecular weight/Mw of IL 5 RHESUS MACAQUE Protein?
      IL 5 RHESUS MACAQUE Protein has a total Mw of 26.1kDa.

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

      What is the Purity of IL 5 RHESUS MACAQUE Protein?
      IL 5 RHESUS MACAQUE Protein is >98% pure as determined by SDS-PAGE.

      What is the Biological Activity of IL 5 RHESUS MACAQUE Protein?
      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.

      What is the amino acid sequence of IL 5 RHESUS MACAQUE Protein?
      IPTEIPASAL VKETLALLST HRTLLIANET LRIPVPVHKN HQLCTEEIFQ GIGTLESQTV QGGTVERLFK NLSLIKKYIG GQKKKCGEER RRVNQFLDYL QEFLGVMNTE WIIES.

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

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

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

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

    Il 5 Rhesus Macaque
  • View Data Sheet

    Description:

    Interleukin 12 His Tag Human Recombinant

    23-219aa (IL12A) / 23-328aa (IL12B), Interleukin 12 (subunit beta/alpha), IL12 His, NKSF1, NKSF, CTL maturation factor (TCMF), Cytotoxic lymphocyte maturation factor (CLMF), TSF, Edodekin-alpha, IL-12.

    Product # :

    CYT-846

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    • SDS-PAGE

    Description

    IL12 Human Recombinant produced in a baculovirus expression system is a glycosylated disulfide linked (through cysteines in bold) heterodimer comprised of IL12A (23-219aa, total of 203 aa, MW 23.3kDa) and IL12B (23-328aa, total of 306 aa, MW 34.6kDa), having a total predicted molecular mass of 57.9kDa (Molecular weight on SDS-PAGE will appear higher).IL12A is fused to a 6 amino acid His-Tag at C-terminus and purified by proprietary chromatographic techniques.

    Source

    Baculovirus.

    Formulation

    IL12 protein solution (0.5mg/ml) containing Phosphate buffered saline (pH7.4) and 10% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    Biological Activity

    The activity is determined by the IFN-g ELISA in a using NK-92 cell. The ED50 for this effect is less than or equal to 0.03 ng/ml.

    SDS-PAGE

    More Info

    • Introduction

      IL-12 is a heterodimeric cytokine that stimulates the production of interferon gamma 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

      23-219aa (IL12A) / 23-328aa (IL12B), Interleukin 12 (subunit beta/alpha), IL12 His, NKSF1, NKSF, CTL maturation factor (TCMF), Cytotoxic lymphocyte maturation factor (CLMF), TSF, Edodekin-alpha, IL-12.

    • 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

      IL12A(p35):
      RNLPVATPDP GMFPCLHHSQ NLLRAVSNML QKARQTLEFY PCTSEEIDHE DITKDKTSTV EACLPLELTK NESCLNSRET SFITNGSCLA SRKTSFMMAL CLSSIYEDLK MYQVEFKTMN AKLLMDPKRQ IFLDQNMLAV IDELMQALNF NSETVPQKSS LEEPDFYKTK IKLCILLHAF RIRAVTIDRV MSYLNASHHH HHH.

      IL12B(p40):
      IWELKKDVYV VELDWYPDAP GEMVVLTCDT PEEDGITWTL DQSSEVLGSG KTLTIQVKEF GDAGQYTCHK GGEVLSHSLL LLHKKEDGIW STDILKDQKE PKNKTFLRCE AKNYSGRFTC WWLTTISTDL TFSVKSSRGS SDPQGVTCGA ATLSAERVRG DNKEYEYSVE CQEDSACPAA EESLPIEVMV DAVHKLKYEN YTSSFFIRDI IKPDPPKNLQ LKPLKNSRQV EVSWEYPDTW STPHSYFSLT FCVQVQGKSK REKKDRVFTD KTSATVICRK NASISVRAQD RYYSSSWSEW ASVPCS.

    • Background

      What is the molecular weight/Mw of IL12 HUMAN, HIS Protein?
      IL12 HUMAN, HIS Protein has a total Mw of 57.9kDa.

      What is the source or expression system of IL12 HUMAN, HIS Protein?
      Baculovirus.
      What is the Purity of IL12 HUMAN, HIS Protein?
      IL12 HUMAN, HIS Protein is >90% pure as determined by SDS-PAGE.

      What is the Biological Activity of IL12 HUMAN, HIS Protein?
      The activity is determined by the IFN-g ELISA in a using NK-92 cell. The ED50 for this effect is less than or equal to 0.03 ng/ml.

      What is the amino acid sequence of IL12 HUMAN, HIS Protein?
      IL12A(p35):
      RNLPVATPDP GMFPCLHHSQ NLLRAVSNML QKARQTLEFY PCTSEEIDHE DITKDKTSTV EACLPLELTK NESCLNSRET SFITNGSCLA SRKTSFMMAL CLSSIYEDLK MYQVEFKTMN AKLLMDPKRQ IFLDQNMLAV IDELMQALNF NSETVPQKSS LEEPDFYKTK IKLCILLHAF RIRAVTIDRV MSYLNASHHH HHH.
      IL12B(p40):
      IWELKKDVYV VELDWYPDAP GEMVVLTCDT PEEDGITWTL DQSSEVLGSG KTLTIQVKEF GDAGQYTCHK GGEVLSHSLL LLHKKEDGIW STDILKDQKE PKNKTFLRCE AKNYSGRFTC WWLTTISTDL TFSVKSSRGS SDPQGVTCGA ATLSAERVRG DNKEYEYSVE CQEDSACPAA EESLPIEVMV DAVHKLKYEN YTSSFFIRDI IKPDPPKNLQ LKPLKNSRQV EVSWEYPDTW STPHSYFSLT FCVQVQGKSK REKKDRVFTD KTSATVICRK NASISVRAQD RYYSSSWSEW ASVPCS.

      What applications can IL12 HUMAN, HIS Protein be used in?
      IL12 HUMAN, HIS Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for IL12 HUMAN, HIS Protein?
      The endotoxin level is minimal, IL12 HUMAN, HIS Protein was purified using conventional chromatography techniques.

      Who supplies recombinant IL12 HUMAN, HIS that is in stock and available to order?
      ProSpec has the protein in stock and available for immediate delivery.

      Where can I order bulk mg quantities of IL12 HUMAN, HIS?
      ProSpec supplies bulk mg quantities at affordable prices that meets research and academic budgets.

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

    Il12 Human His
  • View Data Sheet

    Description:

    Interleukin 17A Canine Recombinant

    IL17A, IL17, IL-17A, CTLA8, CTLA8, Interleukin 17A, Interleukin-17A, cytotoxic T-lymphocyte-associated serine esterase 8.

    Product # :

    CYT-1207

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    Description

    IL17A Canine Recombinant produced in HEK293 cells is a single, glycosylated polypeptide chain (29-155a.a) containing 133 amino acids and having a molecular mass of 15.6kDa.IL17A is expressed with a 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

    Source

    HEK293 cells.

    Formulation

    IL17A protein (0.5mg/ml) contains 10% glycerol and Phosphate-Buffered Saline (pH 7.4).

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    Biological Activity

    The activity is determined by the IL-6 ELISA in a using NIH/3T3 mouse embryonic fibroblast cells. The ED50 range ≤ 10 ng/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

      IL17A, IL17, IL-17A, CTLA8, CTLA8, Interleukin 17A, Interleukin-17A, cytotoxic T-lymphocyte-associated serine esterase 8.

    • 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

      FPQNPGCRNT EDKNFPQHVK VNLNILNRNT NSRRPSDYYN RSTSPWNLHR NEDPERYPSV IWEAKCRHLG CVNNEGNINY HMNSVPIQQE ILVLRRESQH CPHSFRLEKM LVAVGCTCVT PIVRHVAHHH 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.

    Il17A Canine
  • View Data Sheet

    Name :

    IL9 Rat

    Description:

    Interleukin-9 Rat Recombinant

    Interleukin 9, Protein Il9, Il9.

    Product # :

    CYT-748

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    Description

    Interleukin-9 Rat Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 127 amino acids and having a molecular mass of 14.3kDa.The IL-9 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    IL9 protein 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 TS1 cells is less than 10 ng/ml, corresponding to a specific activity of > 1.0 × 105 IU/mg.

    More Info

    • Introduction

      Factor that is thought to be a regulator of hematopoiesis. It has been shown to enhance the growth of human mast cells and megakaryoblastic leukemic cells as well as murine helper t-cell clones. IL-9 is a glycoprotein with a molecular weight of 32-39 that is derived from T-cells, and maps to human chromosome 5.

    • Synonyms

      Interleukin 9, Protein Il9, Il9.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized Interleukin-9 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IL9 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 9 in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      MQRCSTSWGI QHTSYLIENL KDDPSSKCSC SANVTSCLCL PIPSDDCTTP CFQEGMSQVT NATQQSKFSP FFFRVKRIVE TLKSNKCQFF SCEKPCNQTT AGNTVSFLKS LLKTFQKTEV QVQRSRA.

    • Background

      What is the molecular weight/Mw of IL9 RAT Protein?
      IL9 RAT Protein has a total Mw of 14.3kDa.

      What is the source or expression system of IL9 RAT Protein?
      Escherichia Coli.

      What is the Purity of IL9 RAT Protein?
      IL9 RAT Protein is >97% pure as determined by SDS-PAGE.

      What is the Biological Activity of IL9 RAT Protein?
      The ED50 as determined by a cell proliferation assay using murine TS1 cells is less than 10 ng/ml, corresponding to a specific activity of > 1.0 × 105 IU/mg.

      What is the amino acid sequence of IL9 RAT Protein?
      MQRCSTSWGI QHTSYLIENL KDDPSSKCSC SANVTSCLCL PIPSDDCTTP CFQEGMSQVT NATQQSKFSP FFFRVKRIVE TLKSNKCQFF SCEKPCNQTT AGNTVSFLKS LLKTFQKTEV QVQRSRA.

      What applications can IL9 RAT Protein be used in?
      IL9 RAT Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for IL9 RAT Protein?
      The endotoxin level is minimal, IL9 RAT Protein was purified using conventional chromatography techniques.

      Who supplies recombinant IL9 RAT that is in stock and available to order?
      ProSpec has the protein in stock and available for immediate delivery.

      Where can I order bulk mg quantities of IL9 RAT?
      ProSpec supplies bulk mg quantities at affordable prices that meets research and academic budgets.

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

    Il 9 Rat
  • View Data Sheet

    Description:

    Recombinant Anti Human Tumor Necrosis Factor-Alpha

    Product # :

    ANT-599

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    Description

    Recombinant TNF-a Antibody is a recombinant human IgG1 monoclonal antibody specific for human tumor necrosis factor (TNF). Recombinant TNF-a Antibody is produced by recombinant DNA technology in a Chinese Hamster Ovary mammalian cell expression system in a serum-free medium and has a molecular weight of approximately 148 kDa.

    Source

    CHO.

    Formulation

    The Recombinant TNF-a Antibody 53mg/ml solution contains 6.16 mg/ml of sodium chloride, 0.86 mg/ml of monobasic sodium phosphate dihydrate, 1.53 mg/ml of dibasic sodium phosphate dihydrate, 0.3 mg/ml of sodium citrate, 1.30 mg/ml of citric acidmonohydrate, 12 mg/ml of mannitol, 1mg/ml of polysorbate 80, pH-5.

    Purity

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

    Biological Activity

    The EC50 as determined by L929 cell proliferation assay for neutralization reaction between TNF-a Antibody and TNFA, Perform a comparison of a dilution series of the Sample solution with a dilution series of the Standard solution, measured potency was found to be 1.2 X 104EU/mg.

    More Info

    • Introduction

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

    • Physical Appearance

      Clear and colorless solution.

    • Stability

      Recombinant TNF-a Antibody should be stored between 2-8°C and should be protected from light. DO NOT FREEZE. DO NOT SHAKE.

    • Amino Acid Sequence

      LIGHT CHAIN
      DIQMTQSPSSLSASVGDRVTITCRASQGIRNYLAWYQQKPGKAPKLLIYAASTLQSGVPSRFSGSGSGTDF
      TLTISSLQPEDVATYYCQRYNRAPYTFGQGTKVEIKRTVAAPSVFIFPPSDEQLKSGTASVVCLLNNFYPR
      EAKVQWKVDNALQSGNSQESVTEQDSKDSTYSLSSTLTLSKADYEKHKVYACEVTHQGLSSPVTKSFNRGEC

      HEAVY CHAIN
      EVQLVESGGGLVQPGRSLRLSCAASGFTFDDYAMHWVRQAPGKGLEWVSAITWNSGHIDYADSVEGRFTISR
      DNAKNSLYLQMNSLRAEDTAVYYCAKVSYLSTASSLDYWGQGTLVTVSSASTKGPSVFPLAPSSKSTSGGTA
      ALGCLVKDYFPEPVTVSWNSGALTSGVHTFPAVLQSSGLYSLSSVVTVPSSSLGTQTYICNVNHKPSNTKVD
      KKVEPKSCDKTHTCPPCPAPELLGGPSVFLFPPKPKDTLMISRTPEVTCVVVDVSHEDPEVKFNWYVDGVEV
      HNAKTKPREEQYNSTYRVVSVLTVLHQDWLNGKEYKCKVSNKALPAPIEKTISKAKGQPREPQVYTLPPSRD
      ELTKNQVSLTCLVKGFYPSDIAVEWESNGQPENNYKTTPPVLDSDGSFFLYSKLTVDKSRWQQGNVFSCSVM
      HEALHNHYTQKSLSLSPGK.

    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.

    Recombinant Tnf A Antibody
  • View Data Sheet

    Description:

    Interleukin-21 Human Recombinant

    Za11, IL-21.

    Product # :

    CYT-408

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    Description

    IL21 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 132 amino acids and having a total molecular mass of 15.4kDa. The IL-21 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Lyophilized from PBS, pH 7.4.

    Purity

    Greater than 97.0% as determined by SDS-PAGE.

    Biological Activity

    Measured by its ability to proliferate activated B cells.

    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 naive 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

      Za11, IL-21.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized Interleukin-21 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IL21 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 -21 in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      MQDRHMIRMR QLIDIVDQLK NYVNDLVPEF LPAPEDVETN CEWSAFSCFQ KAQLKSANTG NNERIINVSI KKLKRKPPST NAGRRQKHRL TCPSCDSYEK KPPKEFLERF KSLLQKMIHQ HLSSRTHGSE DS.

    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 21 Human
  • View Data Sheet

    Description:

    Neurotrophic Receptor Tyrosine Kinase 2, HEK Human Recombinant

    GP145-TrkB, trk-B, TRKB, NTRK2.

    Product # :

    CYT-1230

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    Description

    NTRK2 Human Recombinant is a single, glycosylated, polypeptide chain (32-430 a.a) containing a total of 632 amino acids and having a molecular mass of 70.3 kDa. NTRK2 is fused to a 233 a.a hIgG-His-Tag at C-terminus and is purified by proprietary chromatographic techniques.

    Source

    HEK293 Cells.

    Formulation

    The NTRK2 solution (1mg/ml) contains 10% Glycerol and Phosphate-Buffered Saline (pH 7.4).

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Synonyms

      GP145-TrkB, trk-B, TRKB, NTRK2.

    • 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

      CPTSCKCSAS RIWCSDPSPG IVAFPRLEPN SVDPENITEI FIANQKRLEI INEDDVEAYV GLRNLTIVDS GLKFVAHKAF LKNSNLQHIN FTRNKLTSLS RKHFRHLDLS ELILVGNPFT CSCDIMWIKT LQEAKSSPDT QDLYCLNESS KNIPLANLQI PNCGLPSANL AAPNLTVEEG KSITLSCSVA GDPVPNMYWD VGNLVSKHMN ETSHTQGSLR ITNISSDDSG KQISCVAENL VGEDQDSVNL TVHFAPTITF LESPTSDHHW CIPFTVKGNP KPALQWFYNG AILNESKYIC TKIHVTNHTE YHGCLQLDNP THMNNGDYTL IAKNEYGKDE KQISAHFMGW PGIDDGANPN YPDVIYEDYG TAANDIGDTT NRSNEIPSTD VTDKTGREH LEPKSCDKTHT CPPCPAPELL GGPSVFLFPP KPKDTLMISR TPEVTCVVVD VSHEDPEVKF NWYVDGVEVH NAKTKPREEQ YNSTYRVVSV LTVLHQDWLN GKEYKCKVSN KALPAPIEKT ISKAKGQPRE PQVYTLPPSR DELTKNQVSL TCLVKGFYPS DIAVEWESNG QPENNYKTTP PVLDSDGSFF LYSKLTVDKS RWQQGNVFSC SVMHEALHNH YTQKSLSLSP GK.

    • Background

      NTRK2, also known as TrkB, is a high-affinity receptor for BDNF and other neurotrophins such as neurotrophin-4 (NT-4) and neurotrophin-3 (NT-3). It plays a crucial role in the development, function, and plasticity of the nervous system. Dysregulation of NTRK2 signaling is associated with various neurological disorders, including neurodegenerative diseases, psychiatric disorders, and cancers. NTRK2 has been developed to facilitate research into its biological functions and potential therapeutic applications. This paper provides a comprehensive overview of the scientific research on recombinant human NTRK2, focusing on its biological functionality, detailed description, and physical properties.

      NTRK2 is critical for synaptic plasticity, which underlies learning and memory. Research with rhNTRK2 has demonstrated that BDNF-NTRK2 signaling enhances synaptic strength and facilitates long-term potentiation (LTP) in hippocampal neuron.

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    Ntrk2 Protein
  • View Data Sheet

    Description:

    Interleukin 18 Receptor Accessory Protein Human Recombinant

    Interleukin-18 receptor accessory protein, IL-18 receptor accessory protein, IL-18RAcP, Accessory protein-like, AcPL, CD218 antigen-like family member B, CDw218b, IL-1R accessory protein-like, IL-1RAcPL, Interleukin-1 receptor 7, IL-1R-7, IL-1R7, Interleukin-18 receptor accessory protein-like, Interleukin-18 receptor beta, IL-18R-beta, IL-18Rbeta, CD218b, IL1R7.

    Product # :

    CYT-1050

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    Description

    IL18RAP produced in Sf9 Insect cells is a single, glycosylated polypeptide chain containing 576 amino acids (20-356 a.a.) and having a molecular mass of 65.4kDa.IL18RAP is expressed with an 239 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Insect cells.

    Formulation

    IL18RAP protein solution (0.25mg/ml) contains Phosphate Buffered Saline (pH 7.4) AND 10% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Interleukin-18 receptor accessory protein (IL18RAP), belongs to the IL-1 family of cytokines which holds multiple immunoregulatory functions. It has been found that IL18RAP does not mediate IL18-binding, however, IL18RAP is involved in IL18-dependent signal transduction, which leads to NF-kappa-B and JNK activation. IL18R1 as well as IL18RAP polymorphisms have been linked with the following diseases: schizophrenia, HSV1 seropositivity and atopic asthma.

    • Synonyms

      Interleukin-18 receptor accessory protein, IL-18 receptor accessory protein,
      IL-18RAcP, Accessory protein-like, AcPL, CD218 antigen-like family member B, CDw218b, IL-1R accessory protein-like, IL-1RAcPL, Interleukin-1 receptor 7, IL-1R-7, IL-1R7, Interleukin-18 receptor accessory protein-like, Interleukin-18 receptor beta, IL-18R-beta, IL-18Rbeta, CD218b, IL1R7.

    • 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

      FNISGCSTKK LLWTYSTRSE EEFVLFCDLP EPQKSHFCHR NRLSPKQVPE HLPFMGSNDL SDVQWYQQPS NGDPLEDIRK SYPHIIQDKC TLHFLTPGVN NSGSYICRPK MIKSPYDVAC CVKMILEVKP QTNASCEYSA SHKQDLLLGS TGSISCPSLS CQSDAQSPAV TWYKNGKLLS VERSNRIVVD EVYDYHQGTY VCDYTQSDTV SSWTVRAVVQ VRTIVGDTKL KPDILDPVED TLEVELGKPL TISCKARFGF ERVFNPVIKW YIKDSDLEWE VSVPEAKSIK STLKDEIIER NIILEKVTQR DLRRKFVCFV QNSIGNTTQS VQLKEKRLEP KSCDKTHTCP PCPAPELLGG PSVFLFPPKP KDTLMISRTP EVTCVVVDVS HEDPEVKFNW YVDGVEVHNA KTKPREEQYN STYRVVSVLT VLHQDWLNGK EYKCKVSNKA LPAPIEKTIS KAKGQPREPQ VYTLPPSRDE LTKNQVSLTC LVKGFYPSDI AVEWESNGQP ENNYKTTPPV LDSDGSFFLY SKLTVDKSRW QQGNVFSCSV MHEALHNHYT QKSLSLSPGK HHHHHH.

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

    Il18Rap Human
  • View Data Sheet

    Description:

    Interleukin-1 alpha Mouse 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-523

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    Description

    Interleukin-1A Mouse Recombinant produced in E.Coli is single, a non-glycosylated, Polypeptide chain containing 156 amino acids and having a molecular mass of 17.9 kDa. 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 1xPBS, 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 D10S cells is < 0.002 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-1a 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 1a in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      SAPYTYQSDL RYKLMKLVRQ KFVMNDSLNQ TIYQDVDKHY LSTTWLNDLQ QEVKFDMYAY SSGGDDSKYP VTLKISDSQL FVSAQGEDQP VLLKELPETP KLITGSETDL IFFWKSINSK NYFTSAAYPE LFIATKEQSR VHLARGLPSM TDFQIS.

    • Background

      What is the molecular weight/Mw of IL1A MOUSE Protein?
      IL1A MOUSE Protein has a total Mw of 17.9kDa.

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

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

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

      What is the amino acid sequence of IL1A MOUSE Protein?
      SAPYTYQSDL RYKLMKLVRQ KFVMNDSLNQ TIYQDVDKHY LSTTWLNDLQ QEVKFDMYAY SSGGDDSKYP VTLKISDSQL FVSAQGEDQP VLLKELPETP KLITGSETDL IFFWKSINSK NYFTSAAYPE LFIATKEQSR VHLARGLPSM TDFQIS.
      What applications can IL1A MOUSE Protein be used in?
      IL1A MOUSE Protein can probably be used in western blot, ELISA and Lateral Flow.

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

    Il 1 Alpha Mouse
  • View Data Sheet

    Description:

    Interleukin-1 Receptor Antagonist Rat Recombinant, His Tag

    Interleukin-1 receptor antagonist protein, IL-1RN, IL-1ra, IRAP, IL1 inhibitor, Il1rn, Il-1ra, Interleukin-1 Receptor Antagonist, IL-1ra, IL 1RA.

    Product # :

    CYT-899

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    Description

    IL 1RA Rat Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 175 amino acids (27-178a.a.) and having a molecular mass of 19.8kDa.IL 1RA is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    IL 1RA protein solution (1mg/ml) containing Phosphate Buffer Saline (pH7.4), 10% glycerol and 1mM DTT.

    Purity

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

    More Info

    • Introduction

      Interleukin-1 ra is a member of the interleukin 1 cytokine family. This protein inhibits the activities of interleukin 1, alpha (IL1A) and interleukin 1, beta (IL1B), and modulates a variety of interleukin 1 related immune and inflammatory responses. This gene and five other closely related cytokine genes form a gene cluster spanning approximately 400 kb on chromosome 2. A polymorphism of this gene is reported to be associated with increased risk of osteoporotic fractures and gastric cancer. Four alternatively spliced transcript variants encoding distinct isoforms have been reported.

    • Synonyms

      Interleukin-1 receptor antagonist protein, IL-1RN, IL-1ra, IRAP, IL1 inhibitor, Il1rn, Il-1ra, Interleukin-1 Receptor Antagonist, IL-1ra, IL 1RA.

    • Physical Appearance

      Sterile Filtered clear solution.

    • Stability

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

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MGSHPAGKRP CKMQAFRIWD TNQKTFYLRN NQLIAGYLQG PNTKLEEKID MVPIDFRNVF LGIHGGKLCL SCVKSGDDTK LQLEEVNITD LNKNKEEDKR FTFIRSETGP TTSFESLACP GWFLCTTLEA DHPVSLTNTP KEPCTVTKFY FQEDQ.

    • Background

      What is the molecular weight/Mw of IL1RA RAT, HIS Protein?
      IL1RA RAT, HIS Protein has a total Mw of 19.8kDa.

      What is the source or expression system of IL1RA RAT, HIS Protein?
      Escherichia Coli.

      What is the Purity of IL1RA RAT, HIS Protein?
      IL1RA RAT, HIS Protein is >90% pure as determined by SDS-PAGE.

      What is the Biological Activity of IL1RA RAT, HIS Protein?
      The biological functionality of IL1RA RAT, HIS Protein will be determined in the future.

      What is the amino acid sequence of IL1RA RAT, HIS Protein?
      MGSSHHHHHH SSGLVPRGSH MGSHPAGKRP CKMQAFRIWD TNQKTFYLRN NQLIAGYLQG PNTKLEEKID MVPIDFRNVF LGIHGGKLCL SCVKSGDDTK LQLEEVNITD LNKNKEEDKR FTFIRSETGP TTSFESLACP GWFLCTTLEA DHPVSLTNTP KEPCTVTKFY FQEDQ.

      What applications can IL1RA RAT, HIS Protein be used in?
      IL1RA RAT, HIS Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for IL1RA RAT, HIS Protein?
      The endotoxin level is minimal, IL1RA RAT, HIS Protein was purified using conventional chromatography techniques.

      Who supplies recombinant IL1RA RAT, HIS that is in stock and available to order?
      ProSpec has the protein in stock and available for immediate delivery.

      Where can I order bulk mg quantities of IL1RA RAT, HIS?
      ProSpec supplies bulk mg quantities at affordable prices that meets research and academic budgets.

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

    Il 1Ra Rat His
  • View Data Sheet

    Description:

    LIGHT Mouse Recombinant

    Tumor necrosis factor ligand superfamily member 14, CD258, Tnfsf14, Light.

    Product # :

    CYT-826

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    Description

    TNFSF14 Mouse Recombinant produced in E. Coli is a single, non-glycosylated, polypeptide chain containing 168 amino acids and having a molecular mass of 18.4kDa.

    Source

    Escherichia Coli.

    Formulation

    TNFSF14 protein was lyophilized from a 0.2µm filtered concentrated solution in PBS pH7.4.

    Purity

    Greater than 96.0% as determined by: (a) Analysis by RP-HPLC.(b) Analysis by SDS-PAGE.

    Biological Activity

    The ED50 as determined by a cytotoxicity assay using human HT-29 cells is less than 2µg/ml, corresponding to a specific activity of > 500 IU/mg in the presence of murine anti-polyHistidine monoclonal antibody and rHuIFN-g.

    More Info

    • Introduction

      TNFRSF14, a member of the TNF receptor superfamily, is a type I transmembrane protein. TNFRSF14 is expressed in peripheral blood T cells, B cells, monocytes and in various tissues enriched in lymphoid cells. TNFRSF14 operates as a co-stimulatory factor for the activation of lymphoid cells and as a deterrent to infection by herpesvirus. Additionally, TNFRSF14 encourages the proliferation of T cells, and triggers apoptosis of various tumor cells.

    • Synonyms

      Tumor necrosis factor ligand superfamily member 14, CD258, Tnfsf14, Light.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized TNFSF14 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution TNFSF14 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 TNFSF14 in sterile 100mM HAc not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      DGGKGSWEKL IQDQRSHQAN PAAHLTGANA SLIGIGGPLL WETRLGLAFL RGLTYHDGAL VTMEPGYYYV YSKVQLSGVG CPQGLANGLP ITHGLYKRTS RYPKELELLV SRRSPCGRAN SSRVWWDSSF LGGVVHLEAG EEVVVRVPGN RLVRPRDGTR SYFGAFMV.

    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.

    Tnfsf14 Mouse
  • View Data Sheet

    Description:

    Betacellulin Bovine Recombinant

    Product # :

    CYT-406

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    Description

    Betacellulin Bovine Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 80 amino acids and having a molecular mass of 9003 Dalton. Betacellulin Bovine Recombinant is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The Betacellulin Bovine Recombinant was lyophilized after extensive dialysis against 50mM acetic acid.

    Purity

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

    Biological Activity

    The ED50, calculated by the dose-dependent proliferation of murine BALB\C 3T3 cells (measured by 3H-thymidine uptake) is < 10.0 ng/ml, corresponding to a Specific Activity 100,000 units/mg.

    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.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized Betacellulin Bovine Recombinant although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution BTC Bovine 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 BTC Bovine 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 Asp-Gly-Asn-Ser-Thr.

    • Background

      What is the molecular weight/Mw of BETACELLULIN Protein?
      BETACELLULIN Protein has a total Mw of 9kDa.

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

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

      What is the Biological Activity of BETACELLULIN Protein?
      The ED50, calculated by the dose-dependent proliferation of murine BALB\C 3T3 cells (measured by 3H-thymidine uptake) is < 10.0 ng/ml, corresponding to a Specific Activity 100,000 units/mg.

      What is the amino acid sequence of BETACELLULIN Protein?
      BETACELLULIN Protein is composed from 80 amino acids.

      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.

    • Protein content

      Protein quantitation was carried out by two independent methods:1. UV spectroscopy at 280 nm using the absorbency value of 0.59 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 BTC as a Reference Standard.

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    Betacellulin Bovine
  • View Data Sheet

    Description:

    IFN-Beta 1a Human Recombinant

    Leukocyte IFN, B cell IFN, Type I IFN, IFNB1, IFB, IFF, IFNB, IFN-b 1a ,MGC96956.

    Product # :

    CYT-236

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    Description

    IFN-beta 1a Human Recombinant produced in CHO (Chinese Hamster Ovarian) cells is a single, glycosylated polypeptide chain containing 166 amino acids and having a molecular mass of 22500 Dalton.IFN-beta1a is purified by proprietary chromatographic techniques.

    Source

    CHO (Chinese Hamster Ovarian) cells.

    Formulation

    Lyophilized from a solution containing 91 mg Human Albumin, and 620 mg mannitol and 50mM Acetate acid pH 3.8.

    Purity

    Greater than 99.0% as determined by:
    (a) Analysis by RP-HPLC.
    (b) Analysis by SDS-PAGE.

    Biological Activity

    The specific activity as determined in a viral resistance assay (human "Wish" cell line and VSV virus or the monkey VERO cell line with EMCV virus) was found to be 270 x 106 IU/mg.

    More Info

    • Introduction

      IFN-beta has antiviral, antibacterial and anticancer activities.

    • Synonyms

      Leukocyte IFN, B cell IFN, Type I IFN, IFNB1, IFB, IFF, IFNB, IFN-b 1a ,MGC96956.

    • Stability

      Lyophilized IFN-beta 1a although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IFN-Beta1a 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 IFN beta 1a in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Background

      What is the molecular weight/Mw of IFN BETA 1A HUMAN Protein?
      IFN BETA 1A HUMAN Protein has a total Mw of 22.5kDa.

      What is the source or expression system of IFN BETA 1A HUMAN Protein?
      CHO (Chinese Hamster Ovarian) cells.

      What is the Purity of IFN BETA 1A HUMAN Protein?
      IFN BETA 1A HUMAN Protein is >99% pure as determined by SDS-PAGE.

      What is the Biological Activity of IFN BETA 1A HUMAN Protein?
      The specific activity as determined in a viral resistance assay (human "Wish" cell line and VSV virus or the monkey VERO cell line with EMCV virus) was found to be 270 x 106 IU/mg.

      What is the amino acid sequence of IFN BETA 1A HUMAN Protein?
      IFN BETA 1A HUMAN Protein is composed from 166 amino acids.

      What applications can IFN BETA 1A HUMAN Protein be used in?
      IFN BETA 1A HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for IFN BETA 1A HUMAN Protein?
      The endotoxin level is minimal, IFN BETA 1A HUMAN Protein was purified using conventional chromatography techniques.

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

    Interferon Beta 1A Human
  • View Data Sheet

    Description:

    Interleukin-1 Receptor Antagonist Mouse Recombinant

    IRAP, IL1F3, IL1RA, IL-1ra3, ICIL-1RA, IL1RN, IL1 inhibitor, IL-1ra, F630041P17Rik.

    Product # :

    CYT-658

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    Description

    IL1 ra Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 153 amino acids and having a molecular mass of 17.4kDa. The IL1ra is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The protein was lyophilized from a concentrated (1mg/ml) solution in water containing NaHCO3.

    Purity

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

    Biological Activity

    The mouse IL-1Ra is capable of inhibiting IL-1-alpha activity in helper T cell line D10.G4.1.

    More Info

    • Introduction

      Interleukin-1 ra is a member of the interleukin 1 cytokine family. This protein inhibits the activities of interleukin 1, alpha (IL1A) and interleukin 1, beta (IL1B), and modulates a variety of interleukin 1 related immune and inflammatory responses. This gene and five other closely related cytokine genes form a gene cluster spanning approximately 400 kb on chromosome 2. A polymorphism of this gene is reported to be associated with increased risk of osteoporotic fractures and gastric cancer. Four alternatively spliced transcript variants encoding distinct isoforms have been reported.

    • Synonyms

      IRAP, IL1F3, IL1RA, IL-1ra3, ICIL-1RA, IL1RN, IL1 inhibitor, IL-1ra, F630041P17Rik.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized Interleukin 1ra although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IL-1ra 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-1ra 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 six N-terminal amino acids was determined and was found to be Ala-Cys-Arg-Pro-Ser-Gly.

    • Background

      What is the molecular weight/Mw of IL1RA MOUSE Protein?
      IL1RA MOUSE Protein has a total Mw of 17.4kDa.

      What is the source or expression system of IL1RA MOUSE Protein?
      Escherichia Coli.

      What is the Purity of IL1RA MOUSE Protein?
      IL1RA MOUSE Protein is >98% pure as determined by SDS-PAGE.

      What is the Biological Activity of IL1RA MOUSE Protein?
      The mouse IL-1Ra is capable of inhibiting IL-1-alpha activity in helper T cell line D10.G4.1.

      What is the amino acid sequence of IL1RA MOUSE Protein?
      The sequence of the first six N-terminal amino acids was determined and was found to be Ala-Cys-Arg-Pro-Ser-Gly.

      What applications can IL1RA MOUSE Protein be used in?
      IL1RA MOUSE Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for IL1RA MOUSE Protein?
      The endotoxin level is minimal, IL1RA MOUSE Protein was purified using conventional chromatography techniques.

      Who supplies recombinant IL1RA 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 IL1RA MOUSE?
      ProSpec supplies bulk mg quantities at affordable prices that meets research and academic budgets.

    • Protein content

      Protein quantitation was carried out by UV spectroscopy at 280 nm using the absorbency value of 0.91 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).

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

    Il 1Ra Mouse
  • View Data Sheet

    Description:

    CD30 Ligand Receptor Mouse Recombinant

    Tumor Necrosis Factor Receptor Superfamily, Member 8, Lymphocyte Activation Antigen CD30, CD30L Receptor, Ki-1 Antigen, D1S166E, CD30, Cytokine Receptor CD30, CD30 Antigen, Ki-1

    Product # :

    CYT-1165

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    Description

    TNFRSF8 Mouse Recombinant produced in Baculovirus is a single glycosylated polypeptide chain containing 479 amino acids (19-258 aa) and having a molecular mass of 52.2kDa.TNFRSF8 is fused to a 239 amino acid hIgG-His tag at C-terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    TNFRSF8 protein (1mg/ml) contains 10% glycerol and Phosphate-Buffered Saline (pH 7.4).

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Tumor necrosis factor receptor superfamily member 8 (TNFRSF8) is a receptor for TNFSF8/CD30L. TNFRSF8 has a role in the regulation of cellular growth and transformation of activated lymphoblasts. In addition, the TNFRSF8 protein regulates gene expression via activation of NF-kappa-B. TNFRSF8 being a regulator of apoptosis, induces cell death or proliferation, depending on the cell type.

    • Synonyms

      Tumor Necrosis Factor Receptor Superfamily, Member 8, Lymphocyte Activation Antigen CD30, CD30L Receptor, Ki-1 Antigen, D1S166E, CD30, Cytokine Receptor CD30, CD30 Antigen, Ki-1

    • Physical Appearance

      Sterile Filtered colorless solution.

    • Stability

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

    • Amino Acid Sequence

      FPTDRPLKTT CAGDLSHYPG EAARNCCYQC PSGLSPTQPC PRGPAHCRKQ CAPDYYVNED GKCTACVTCL PGLVEKAPCS GNSPRICECQ PGMHCCTPAV NSCARCKLHC SGEEVVKSPG TAKKDTICEL PSSGSGPNCS NPGDRKTLTS HATPQAMPTL ESPANDSARS LLPMRVTNLV QEDATELVKV PESSSSKARE PSPDPGNAEK NMTLELPSPG TLPDISTSEN SKEPASTAST LEPKSCDKTH TCPPCPAPEL LGGPSVFLFP PKPKDTLMIS RTPEVTCVVV DVSHEDPEVK FNWYVDGVEV HNAKTKPREE QYNSTYRVVS VLTVLHQDWL NGKEYKCKVS NKALPAPIEK TISKAKGQPR EPQVYTLPPS RDELTKNQVS LTCLVKGFYP SDIAVEWESN GQPENNYKTT PPVLDSDGSF FLYSKLTVDK SRWQQGNVFS CSVMHEALHN HYTQKSLSLS PGKHHHHHH

    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.

    Cd30 Mouse
  • View Data Sheet

    Description:

    Interleukin-36 Alpha Mouse Recombinant, His Tag

    Interleukin-36 alpha, FIL1 epsilon, Interleukin-1 epsilon, IL-1 epsilon, Interleukin-1 family member 6, IL-1F6, Interleukin-1 homolog 1, IL-1H1, Il36a, Fil1e, Il1e, Il1f6, Il1h1.

    Product # :

    CYT-905

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    Description

    IL36A Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 183 amino acids (1-160 a.a) and having a molecular mass of 20.4kDa. IL36A is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    IL36A protein solution (1mg/ml) containing Phosphate Buffered Saline (pH7.4) and 10% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Human IL-36a belongs to the IL-1 family which includes IL-1b, IL-1a, IL-1ra, IL-18, IL-36ra (IL1F5), IL-36b (IL1F8), IL-36g (IL1F9), IL-37 (IL1F7) and IL-38 (IL-1F10). The IL-1 family members display a 12 b-strand, b-trefoil configuration, and are thought to have ascended from a mutual ancestral gene. IL-36a is an 18-22kDa, 158aa intracellular and secreted protein which holds no signal sequence, no prosegment and no potential from N-linked glycosylation sites. IL-36a is released as a reaction to LPS and the cell ATP-induced activation of the P2X7 receptor.
      Human IL-36a (aa 6-158) shares 57-68% aa sequence homology with mouse, rabbit, equine and bovine IL-36a and 27-57% aa sequence homology with other new IL-1 family members. IL-36a is mostly found in skin and lymphoid tissues, but also in fetal brain, trachea, stomach and intestine.

    • Synonyms

      Interleukin-36 alpha, FIL1 epsilon, Interleukin-1 epsilon, IL-1 epsilon, Interleukin-1 family member 6, IL-1F6, Interleukin-1 homolog 1, IL-1H1, Il36a, Fil1e, Il1e, Il1f6, Il1h1.

    • 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 MGSMNKEKEL RAASPSLRHV QDLSSRVWIL QNNILTAVPR KEQTVPVTIT LLPCQYLDTL ETNRGDPTYM GVQRPMSCLF CTKDGEQPVL QLGEGNIMEM YNKKEPVKAS LFYHKKSGTT STFESAAFPG WFIAVCSKGS CPLILTQELG EIFITDFEMI VVH.

    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.

    Il36A Mouse His
  • View Data Sheet

    Description:

    Tumor Necrosis Factor-alpha Bovine Recombinant

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

    Product # :

    CYT-1104

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    Description

    TNFA Bovine produced in E.Coli is a single, non-glycosylated polypeptide chain containing 158 amino acids (78-234 a.a.) and having a molecular mass of 17.5kDa. TNFA is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The TNFA (1mg/ml) contains Phosphate buffer saline(pH7.4) and 10% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    Biological Activity

    The ED50 Is < 15 ng/ml and is measured in a cytotoxicity assay using L929 mouse fibrosarcoma cells in the presence of the metabolic inhibitor actinomycin D.

    More Info

    • Introduction

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

    • Synonyms

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

    • 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

      MLRSSSQASS NKPVAHVVAD INSPGQLRWW DSYANALMAN GVKLEDNQLV VPADGLYLIY SQVLFRGQGC PSTPLFLTHT ISRIAVSYQT KVNILSAIKS PCHRETPEWA EAKPWYEPIY QGGVFQLEKG DRLSAEINLP DYLDYAESGQ VYFGIIAL.

    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.

    Tnfa Bovine
  • View Data Sheet

    Description:

    Interleukin-11 Human Recombinant, Pichia

    Interleukin-11, IL-11, Adipogenesis inhibitory factor, AGIF, Oprelvekin, IL11.

    Product # :

    CYT-013

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    Description

    IL11 Human Recombinant produced in Pichia Pastoris is a single, non-glycosylated, Polypeptide chain containing 177 amino acids (it differs from the 178 amino acid length of the native IL11 only in lack of the N-terminal praline residue) and having a molecular mass of 19kDa.The IL11 is purified by proprietary chromatographic techniques.

    Source

    Pichia Pastoris.

    Formulation

    IL11 was Lyophilized from a 0.2 µm filtered concentrated solution of 20mM PB, pH7.2 and 2% Glycine buffer.

    Purity

    Greater than 95% as determined by SDS-PAGE.

    Biological Activity

    The ED50 as determined by the dose-dependent stimulation of the proliferation of murine 7TD1 was found to be less then 0.2ng-0.8ng/ml, corresponding to a Specific Activity of greater than 1,000,000 IU/ mg.

    More Info

    • Introduction

      IL11 is a member of the gp130 family of cytokines. These cytokines drive the assembly of multisubunit receptor complexes, all of which contain at least one molecule of the transmembrane signaling receptor IL6ST (gp130). IL-11 is shown to stimulate the T-cell-dependent development of immunoglobulin-producing B cells. It is also found to support the proliferation of hematopoietic stem cells and megakaryocyte progenitor cells.

    • Synonyms

      Interleukin-11, IL-11, Adipogenesis inhibitory factor, AGIF, Oprelvekin, IL11.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized IL11 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IL11 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 -11 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 Gly-Pro-Pro-Pro-Gly.

    • Background

      What is the molecular weight/Mw of IL11 HUMAN, PICHIA Protein?
      IL11 HUMAN, PICHIA Protein has a total Mw of 19kDa.

      What is the source or expression system of IL11 HUMAN, PICHIA Protein?
      Pichia Pastoris.
      What is the Purity of IL11 HUMAN, PICHIA Protein?
      IL11 HUMAN, PICHIA Protein is >95% pure as determined by SDS-PAGE.

      What is the Biological Activity of IL11 HUMAN, PICHIA Protein?
      The ED50 as determined by the dose-dependent stimulation of the proliferation of murine 7TD1 was found to be less then 0.2ng-0.8ng/ml, corresponding to a Specific Activity of greater than 1,000,000 IU/ mg.

      What is the amino acid sequence of IL11 HUMAN, PICHIA Protein?
      The sequence of the first five N-terminal amino acids was determined and was found to be Gly-Pro-Pro-Pro-Gly.

      What applications can IL11 HUMAN, PICHIA Protein be used in?
      IL11 HUMAN, PICHIA Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for IL11 HUMAN, PICHIA Protein?
      The endotoxin level is minimal, IL11 HUMAN, PICHIA Protein was purified using conventional chromatography techniques.

      Who supplies recombinant IL11 HUMAN, PICHIA 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 IL11 HUMAN, PICHIA?
      ProSpec supplies bulk mg quantities at affordable prices that meets research and academic budgets.

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

    Il 11 Human Pichia
  • View Data Sheet

    Description:

    Interleukin-1 alpha Rat Recombinant, His Tag Active

    Interleukin-1 alpha, IL-1 alpha.

    Product # :

    CYT-1100

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    Description

    IL1A Rat Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 179 amino acids (115-270 a.a) and having a molecular mass of 20.2kDa.IL1A is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    IL1A protein solution (1mg/ml) contains 10% glycerol & Phosphate Buffered Saline (pH 7.4).

    Purity

    Greater than 95% as determined by SDS-PAGE.

    Biological Activity

    The ED50 that was measured in a cell proliferation assay using D10.G4.1 mouse helper T cell is <20 pg/ml.

    More Info

    • Introduction

      IL-1 alpha is produced by activated macrophages.IL-1 alpha stimulates thymocyte proliferation by inducing il-2 release, b-cell maturation and proliferation, and fibroblast growth factor activity. IL1A proteins take part in the inflammatory response, being identified as endogenous pyrogens, and stimulate the release of prostaglandin and collagenase from synovial cells.

    • Synonyms

      Interleukin-1 alpha, IL-1 alpha.

    • Physical Appearance

      Sterile Filtered colorless solution.

    • Stability

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

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MGSSAPHSFQ NNLRYKLIRI VKQEFIMNDS LNQNIYVDMD
      RIHLKAASLN DLQLEVKFDM YAYSSGGDDSKYPVTLKVSN TQLFVSAQGE DKPVLLKEIP
      ETPKLITGSE TDLIFFWEKI NSKNYFTSAA FPELLIATKE QSQVHLARGL PSMIDFQIS.

    • Background

      What is the molecular weight/Mw of IL1A RAT, HIS ACTIVE Protein?
      IL1A RAT, HIS ACTIVE Protein has a total Mw of 20.2kDa.

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

      What is the Purity of IL1A RAT, HIS ACTIVE Protein?
      IL1A RAT, HIS ACTIVE Protein is >95% pure as determined by SDS-PAGE.

      What is the Biological Activity of IL1A RAT, HIS ACTIVE Protein?
      The ED50 that was measured in a cell proliferation assay using D10.G4.1 mouse helper T cell is <20 pg/ml.

      What is the amino acid sequence of IL1A RAT, HIS ACTIVE Protein?
      MGSSHHHHHH SSGLVPRGSH MGSSAPHSFQ NNLRYKLIRI VKQEFIMNDS LNQNIYVDMD
      RIHLKAASLN DLQLEVKFDM YAYSSGGDDSKYPVTLKVSN TQLFVSAQGE DKPVLLKEIP
      ETPKLITGSE TDLIFFWEKI NSKNYFTSAA FPELLIATKE QSQVHLARGL PSMIDFQIS.
      .What applications can IL1A RAT, HIS ACTIVE Protein be used in?
      IL1A RAT, HIS ACTIVE Protein can probably be used in western blot, ELISA and Lateral Flow.

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

    Il1A Rat
  • View Data Sheet

    Description:

    Interleukin 12, Sf9 Human Recombinant

    Interleukin 12 (subunit beta/alpha), IL12b/IL12a, Il-12b/Il-12a, IL-12p40/Il-12p35, Il12p40/Il12p35, p40/p35, Sf9.

    Product # :

    CYT-1058

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    • SDS-PAGE

    Description

    IL12 Mouse Recombinant produced in a baculovirus expression system is a glycosylated disulfide linked (through cysteines in bold) heterodimer comprised of IL12A (23-335aa, total of 319 aa, MW 35.7kDa) and IL12B (23-215aa, total of 199 aa, MW 22.5kDa), having a total predicted molecular mass of 58.3kDa (Molecular weight on SDS-PAGE will appear higher). IL12A is fused to a 6 amino acid His-Tag at C-terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    IL12 protein solution (0.5mg/ml) contains phosphate buffered saline (pH7.4) and 10% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Biological Activity

    The activity is determined by the IFN-g ELISA in a using NK-92 human natural killer cells. The ED50 for this effect is less or equal to 10ng/ml.

    SDS-PAGE

    More Info

    • Introduction

      interleukin 12 subunit beta/alpha or IL12b/IL12a is a growth factor cytokine which increases the lytic activity of NK/lymphokine-activated killer cells, activated T and NK cells and prompt IFN-gamma production (through resting PBMC). IL12b/IL12a is a crucial part to the process of cellular-immunity and activates the differentiation of Th1 cells originates from the precursor T helper cells. The protein is linked to IL23A and creates the IL-23 interleukin, by that, the autoimmune inflammation is induced and autoimmune inflammatory diseases and tumorigenesis are being affected.

    • Synonyms

      Interleukin 12 (subunit beta/alpha), IL12b/IL12a, Il-12b/Il-12a, IL-12p40/Il-12p35, Il12p40/Il12p35, p40/p35, Sf9.

    • 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

      IL12B(p40)
      MWELEKDVYV VEVDWTPDAP GETVNLTCDT PEEDDITWTS DQRHGVIGSG KTLTITVKEF LDAGQYTCHK GGETLSHSHL LLHKKENGIW STEILKNFKN KTFLKCEAPN YSGRFTCSWL VQRNMDLKFN IKSSSSSPDS RAVTCGMASL SAEKVTLDQR DYEKYSVSCQ EDVTCPTAEE
      TLPIELALEA RQQNKYENYS TSFFIRDIIK PDPPKNLQMK PLKNSQVEVS WEYPDSWSTP HSYFSLKFFV RIQRKKEKMK ETEEGCNQKG AFLVEKTSTE VQCKGGNVCV QAQDRYYNSS CSKWACVPCR VRS
      IL12A(p35)
      RVIPVSGPAR CLSQSRNLLK TTDDMVKTAR EKLKHYSCTA EDIDHEDITR DQTSTLKTCL PLELHKNESC LATRETSSTT RGSCLPPQKT SLMMTLCLGS IYEDLKMYQT EFQAINAALQ NHNHQQIILD KGMLVAIDEL MQSLNHNGET LRQKPPVGEA DPYRVKMKLC ILLHAFSTRV
      VTINRVMGYL SSAHHHHHH.

    • Background

      What is the molecular weight/Mw of IL12 MOUSE, SF9 Protein?
      IL12 MOUSE, SF9 Protein has a total Mw of 58.3kDa.

      What is the source or expression system of IL12 MOUSE, SF9 Protein?
      Sf9, Baculovirus cells.
      What is the Purity of IL12 MOUSE, SF9 Protein?
      IL12 MOUSE, SF9 Protein is >95% pure as determined by SDS-PAGE.

      What is the Biological Activity of IL12 MOUSE, SF9 Protein?
      The activity is determined by the IFN-g ELISA in a using NK-92 human natural killer cells. The ED50 for this effect is less or equal to 10ng/ml.

      What is the amino acid sequence of IL12 MOUSE, SF9 Protein?
      IL12B(p40)
      MWELEKDVYV VEVDWTPDAP GETVNLTCDT PEEDDITWTS DQRHGVIGSG KTLTITVKEF LDAGQYTCHK GGETLSHSHL LLHKKENGIW STEILKNFKN KTFLKCEAPN YSGRFTCSWL VQRNMDLKFN IKSSSSSPDS RAVTCGMASL SAEKVTLDQR DYEKYSVSCQ EDVTCPTAEE
      TLPIELALEA RQQNKYENYS TSFFIRDIIK PDPPKNLQMK PLKNSQVEVS WEYPDSWSTP HSYFSLKFFV RIQRKKEKMK ETEEGCNQKG AFLVEKTSTE VQCKGGNVCV QAQDRYYNSS CSKWACVPCR VRS
      IL12A(p35)
      RVIPVSGPAR CLSQSRNLLK TTDDMVKTAR EKLKHYSCTA EDIDHEDITR DQTSTLKTCL PLELHKNESC LATRETSSTT RGSCLPPQKT SLMMTLCLGS IYEDLKMYQT EFQAINAALQ NHNHQQIILD KGMLVAIDEL MQSLNHNGET LRQKPPVGEA DPYRVKMKLC ILLHAFSTRV
      VTINRVMGYL SSAHHHHHH.
      What applications can IL12 MOUSE, SF9 Protein be used in?
      IL12 MOUSE, SF9 Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for IL12 MOUSE, SF9 Protein?
      The endotoxin level is minimal, IL12 MOUSE, SF9 Protein was purified using conventional chromatography techniques.

      Who supplies recombinant IL12 MOUSE, 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 IL12 MOUSE, 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.

    Il 12 Mouse Protein
  • View Data Sheet

    Description:

    Growth and Differentiation Factor 15 Human Recombinant, His Tag

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

    Product # :

    CYT-691

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    Description

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

    Source

    Escherichia Coli.

    Formulation

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

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

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

    • Synonyms

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

    • Physical Appearance

      Sterile filtered colorless solution.

    • Stability

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

    • Amino Acid Sequence

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

    • Background

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

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

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

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

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

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

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

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

    Gdf15 Human
  • View Data Sheet

    Description:

    Interleukin-13 Human Recombinant, His Tag

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

    Product # :

    CYT-489

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    Description

    Interleukin-13 His Human Recombinant produced in E.Coli is a single, non-glycosylated, Polypeptide chain containing 112 amino acids fragment (21-132) having a molecular weight of 12.84kDa with a 4kDa amino-terminal hexahistidine tag (total weight of 16.84kDa). The IL-13 His is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Interleukin -13 His-Tag protein is supplied in 25mM Na-Acetate (pH 4.8) and 50% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

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    • Introduction

      Interleukin-13 is a pleiotropic regulatory cytokine, which shares many of the properties of Interleukin-4. IL-13 is produced primarily by activated T lymphocytes and acts via specific cell surface receptor complexes. Its biological activities include the stimulation of B-cell proliferation and differentiation and the regulation of inflammatory and immune responses.

    • Synonyms

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

    • Physical Appearance

      Sterile Filtered clear solution.

    • Stability

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

    • Background

      What is the molecular weight/Mw of IL13 HUMAN, HIS Protein?
      IL13 HUMAN, HIS Protein has a total Mw of 12.8kDa.

      What is the source or expression system of IL13 HUMAN, HIS Protein?
      Escherichia Coli.

      What is the Purity of IL13 HUMAN, HIS Protein?
      IL13 HUMAN, HIS Protein is >95% pure as determined by SDS-PAGE.

      What is the Biological Activity of IL13 HUMAN, HIS Protein?
      The biological functionality of IL13 HUMAN, HIS Protein will be determined in the future.

      What is the amino acid sequence of IL13 HUMAN, HIS Protein?
      IL13 HUMAN, HIS Protein is composed from 112 amino acids.

      What applications can IL13 HUMAN, HIS Protein be used in?
      IL13 HUMAN, HIS Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for IL13 HUMAN, HIS Protein?
      The endotoxin level is minimal, IL13 HUMAN, HIS Protein was purified using conventional chromatography techniques.

      Who supplies recombinant IL13 HUMAN, HIS that is in stock and available to order?
      ProSpec has the protein in stock and available for immediate delivery.

      Where can I order bulk mg quantities of IL13 HUMAN, HIS?
      ProSpec supplies bulk mg quantities at affordable prices that meets research and academic budgets.

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

    Il 13 Human His
  • View Data Sheet

    Description:

    Interleukin-17E Human Recombinant

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

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    CYT-583

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    Description

    Interleukin-17E Human Recombinant produced in E.Coli is a non-glycosylated disulfide-linked homodimer containing 2x145 amino acids (with an N-terminal Methionine for each chain total aa for each chain 146) and having a total predicted molecular mass of 33.7kDa. The IL-25 Human is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

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

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Biological Activity

    The ED50 as determined by the dose-dependent production of IL-8 by Human PBMCs is 26-40ng/ml, corresponding to a specific activity of 3.8x104 units/mg.

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    • 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, Interleukin-17E.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized Interleukin Human IL17E although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Human IL-25 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 Human IL25 in sterile 10mM HCl not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      MYSHWPSCCP SKGQDTSEEL LRWSTVPVPP LEPARPNRHP ESCRASEDGP LNSRAISPWR YELDRDLNRL PQDLYHARCL CPHCVSLQTG SHMDPRGNSE LLYHNQTVFY RRPCHGEKGT HKGYCLERRL YRVSLACVCV RPRVMG.

    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 17E Human