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  • View Data Sheet

    Description:

    Interleukin-27 Human Recombinant

    Interleukin-30, IL-30, IL-27/p28, p28, Interleukin-27, Interleukin-27/p28, IL-27, Interleukin-27 subunit alpha, IL-27 subunit alpha, IL27-A, Il27, Il27a, IL-27p28.

    Product # :

    CYT-048

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    Description

    IL-27 Human Recombinant produced in HEK cells is a glycosylated non-covalently heterodimer that consists of 2 chains, IL27A (IL27p28) having a Mw of 25kDa and IL27B (EBI3) having a Mw of 30kDa. Each chain migrates separately on SDS-PAGE. The IL-27 protein is purified by proprietary chromatographic techniques

    Source

    HEK.

    Formulation

    The IL-27 was lyophilized from 1mg/ml in 1xPBS.

    Purity

    Greater than 90% as obsereved by SDS-PAGE.

    Biological Activity

    The specific activity was determined by the dose dependent inhibition of HIV replication in human CD4+ T cells and in human monocyte-derived macrophages and is typically 4-12ng/ml.

    More Info

    • Introduction

      Interleukin-27 protein is related to IL-12A & is one of the subunits of a heterodimeric cytokine complex. IL-27 interacts with EBV induced gene 3 also called EBI3, and forms a complex that drives rapid expansion of CD4 (+) T cells. IL-27 complex is synergizes with IL-12 in order to trigger the cytokine production of IFN-Gamma of CD4 (+) T cells. The biological effect of IL-27 is mediated by class-I cytokine receptor (WSX1/TCRR). The pro-inflammatory activity of IL-27 is mediated through the growing expression of key molecules involved in the MHC class-I & MHC class-II pathways. Both MHC class-I and MHC-class-II expression are increased in endothelial cells after Interleukin-27 stimulation which suggests that it may play an important role in conferring the immune function on vascular endothelium IL-27p28 subunit can be induced by IFN-beta and during LPS-induced maturation of dendritic cells in type-I IFN-dependent manner through IFN regulatory factor-1 activation. Interleukin-27 regulates Interleukin-12 responsiveness of CD4+ T cells through Stat1-dependent and -independent mechanisms. IL-17 & IL-23 play an important IL-17 role in inflammation. Interleukin-27 possesses potent anti-angiogenic activity that plays an important role in its antitumor and antimetastatic activities. EBV induced gene 3 plays a role, independently from IL-27, in regulating anti-viral or anti-tumoral immune responses. Interleukin-27 is a potent inhibitor of HIV-1 replication in macrophages, CD4+ T cells, peripheral blood mononuclear cells. Interleukin-27 triggers STAT activation and gene transcription.

    • Synonyms

      Interleukin-30, IL-30, IL-27/p28, p28, Interleukin-27, Interleukin-27/p28, IL-27, Interleukin-27 subunit alpha, IL-27 subunit alpha, IL27-A, Il27, Il27a, IL-27p28.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized IL-27 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IL27 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-27 in sterile PBS containing 0.1% endotoxin-free recombinant HSA.

    • Amino Acid Sequence

      IL-27A (215aa):
      FPRPPGRPQL SLQELRREFT VSLHLARKLL AEVRGQAHRF AESHLPGVNL YLLPLGEQLP DVSLTFQAWR RLSDPERLCF ISTTLQPFHA LLGGLGTQGR WTNMERMQLW AMRLDLRDLQ RHLRFQVLAA GFNLPEEEEE EEEEEEEERK GLLPGALGSA LQGPAQVSWP QLLSTYRLLH SLELVLSRAV RELLLLSKAG HSVWPLGFPT LSPQP.

      IL-27B (209aa):
      RKGPPAALTL PRVQCRASRY PIAVDCSWTL PPAPNSTSPV SFIATYRLGM AARGHSWPCL QQTPTSTSCT ITDVQLFSMA PYVLNVTAVH PWGSSSSFVP FITEHIIKPD PPEGVRLSPL AERQLQVQWE PPGSWPFPEI FSLKYWIRYK RQGAARFHRV GPIEATSFIL RAVRPRARYY VQVAAQDLTD YGELSDWSLP ATATMSLGK.

    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 27 Human
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    Description:

    HIV-1 p31 Integrase Recombinant

    Product # :

    HIV-145

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    Description

    The E.coli derived recombinant protein is a non-glycosylated polypeptide chain, containing the HIV-1 immunodominant regions from the p31 protein (integrase) 9-289 amino acids, fused with six histidines at N-terminus.

    Source

    Escherichia Coli.

    Formulation

    1.5M urea, 25mM Tris-HCl pH 8.0, 0.2% Triton-X & 50% Glycerol.

    Purity

    Greater than 95.0% as determined by HPLC analysis and SDS-PAGE.

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    • Introduction

      Integrase is an enzyme produced by the HIV which enables its genetic material to be integrated into the DNA of the infected cell and is a key component in the pre-integration complex. HIV integrase contains 3 domains, an N-terminal HH-CC zinc fingerdomainwhich is partially responsible for multimerization, a central catalytic domain and a C-terminal domain. Both Central catalytic domain and C-terminal domains have been shown to bind both viral and cellular DNA. No crystal structure data exists with Integrase bound to its DNA substrates. HIV-1 integrase functions as a dimeror a tetramer. Additionally, several host cellular proteins interact with integrase and may facilitate the integration process.

    • Physical Appearance

      Sterile filtered colorless clear solution.

    • Stability

      HIV-1 Integrase p31 although stable at 4°C for 1 week, should be stored below -18°C. Please prevent freeze thaw cycles.

    • Applications

      HIV-1 Integrase p31 antigen is suitable for ELISA and Western blots, excellent antigen for early detection of HIV seroconvertors with minimal specificity problems.

    • Specificity

      Immunoreactive with all sera of HIV-1 infected individuals.

    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.

    Hiv 1 Integrase P31
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    Description:

    Interleukin-12 p35 Human Recombinant

    NKSF1, CTL maturation factor (TCMF), Cytotoxic lymphocyte maturation factor 35 kDa subunit (CLMF p35), TSF, Edodekin-alpha, IL-12 p35, IL-12A, IL-12 subunit p35, NK cell stimulatory factor chain 1, SGT2, FLJ39002.

    Product # :

    CYT-487

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    Description

    Interleukin-12 p35 His Human Recombinant produced in E.Coli is single, a non-glycosylated, polypeptide chain containing 197 amino acids fragment (57-253) with an amino-terminal hexahistidine tag. The IL-12 p35 His is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Interleukin-12 p35 His-Tag is supplied in 1xPBS and 50% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

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

    • Synonyms

      NKSF1, CTL maturation factor (TCMF), Cytotoxic lymphocyte maturation factor 35 kDa subunit (CLMF p35), TSF, Edodekin-alpha, IL-12 p35, IL-12A, IL-12 subunit p35, NK cell stimulatory factor chain 1, SGT2, FLJ39002.

    • Physical Appearance

      Sterile Filtered clear solution.

    • Stability

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

    • Background

      What is the source or expression system of IL12P35 HUMAN Protein?
      Escherichia Coli.

      What is the Purity of IL12P35 HUMAN Protein?
      IL12P35 HUMAN Protein is >95% pure as determined by SDS-PAGE.

      What is the Biological Activity of IL12P35 HUMAN Protein?
      The biological functionality of IL12P35 HUMAN Protein will be determined in the future.

      What is the amino acid sequence of IL12P35 HUMAN Protein?
      IL12P35 HUMAN Protein is composed from 197 amino acids.

      What applications can IL12P35 HUMAN Protein be used in?
      IL12P35 HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for IL12P35 HUMAN Protein?
      The endotoxin level is minimal, IL12P35 HUMAN Protein was purified using conventional chromatography techniques.

      Who supplies recombinant IL12P35 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 IL12P35 HUMAN?
      ProSpec supplies bulk mg quantities at affordable prices that meets research and academic budgets.

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

    Il 12 P35 Human His
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    Description:

    Interleukin-31 Canine Recombinant, His Tag

    IL-31, Interleukin 31, IL31.

    Product # :

    CYT-1016

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    Description

    IL31 Canine Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 142 amino acids (24-159a.a.) and having a molecular mass of 16.1kDa (Molecular size on SDS-PAGE will appear at approximately 18-28kDa).IL31 is fused to a 6 amino acid His-Tag at C-terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    IL31 Canine protein solution (1mg/ml) containing Phosphate buffered saline (pH7.4) and 10% glycerol.

    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 response, causing inflammatory bowel disease, airway hypersensitivity & dermatitis.

    • Synonyms

      IL-31, Interleukin 31, IL31.

    • 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. Please avoid freeze thaw cycles.

    • Amino Acid Sequence

      SHMAPTHQLP PSDVRKIILE LQPLSRGLLE DYQKKETGVP ESNRTLLLCL TSDSQPPRLN SSAILPYFRA IRPLSDKNII DKIIEQLDKL KFQHEPETEI SVPADTFECK SFILTILQQF SACLESVFKS LNSGPQHHHH HH.

    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 Canine
  • View Data Sheet

    Description:

    Interleukin-36 Beta 153 a.a Human Recombinant

    Interleukin 36 beta, interleukin 1 family member 8 (eta), Interleukin-1 homolog 2, IL1F8 (Canonical product IL-1F8a), IL-1F8 (FIL1-eta), Interleukin-1 Superfamily e, IL1H2, MGC126880, MGC126882.

    Product # :

    CYT-180

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    Description

    IL36B 153 a.a. Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 153 amino acids (5-157a.a.) and having a molecular mass of 17.2kDa.The IL36B 153 a.a. Human is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Lyophilized from a 0.2µm filtered concentrated solution in 1xPBS, pH 7.4.

    Purity

    Greater than 97.0% as determined by SDS-PAGE and HPLC analyses.

    Biological Activity

    Fully biologically active when compared to standard. The ED50 as measured by its ability to induce IL-8 secretion in human preadipocytes is less than 10ng/ml, corresponding to a specific activity of 10IU/mg.

    More Info

    • Introduction

      Human IL-36b belongs to the IL-1 family that 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-36 beta is known to be actively secreted. Cells expressing IL-36 beta include resting and activated monocytes and B cells. The receptor for IL-36 beta is a blend of IL-1 Rrp2 and IL-1 RAcP. Recombinant IL-36 beta stimulates processes involving NF-kB and MAPK in an IL-1 Rrp2-dependent manner.

    • Synonyms

      Interleukin 36 beta, interleukin 1 family member 8 (eta), Interleukin-1 homolog 2, IL1F8 (Canonical product IL-1F8a), IL-1F8 (FIL1-eta), Interleukin-1 Superfamily e, IL1H2, MGC126880, MGC126882.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized IL36B 153 a.a. Human although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IL36B 153 a.a. Human 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 IL36B 153 a.a. Human in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      REAAPKSYAI RDSRQMVWVL SGNSLIAAPL SRSIKPVTLH LIACRDTEFS DKEKGNMVYL GIKGKDLCLF CAEIQGKPTL QLKEKNIMDL YVEKKAQKPF LFFHNKEGST SVFQSVSYPG WFIATSTTSG QPIFLTKERG ITNNTNFYLD SVE

    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.

    Il36B 153 Aa Human
  • View Data Sheet

    Description:

    Canine IL-6 Recombinant

    IL6, IL-6, Interleukin-6.

    Product # :

    CYT-1006

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    • SDS-PAGE

    Description

    IL6 Canine Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 195 amino acids (21-207a.a.) and having a molecular mass of 22.0kDa (Molecular size on SDS-PAGE will appear at approximately 18-28kDa).IL6 is expressed with an 8 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 Phosphate Buffered Saline (pH 7.4) and 10% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    SDS-PAGE

    More Info

    • Introduction

      Il-6 is a cytokine with a wide variety of biological functions: it plays an essential role in the final differentiation of b-cells into ig-secreting cells, it induces myeloma and plasmacytoma growth, it induces nerve cells differentiation, in hepatocytes it induces acute phase reactants.

    • Synonyms

      IL6, IL-6, Interleukin-6.

    • 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

      FPTPGPLAGD SKDDATSNSL PLTSANKVEE LIKYILGKIS ALRKEMCDKF NKCEDSKEAL AENNLHLPKL EGKDGCFQSG FNQETCLTRI TTGLVEFQLH LNILQNNYEG DKENVKSVHM STKILVQMLK SKVKNQDEVT TPDPTTDASL QAILQSQDEC VKHTTIHLIL RSLEDFLQFS LRAVRIMLEH HHHHH.

    • Background

      Canine IL-6 Recombinant: Implications for Immunotherapy and Veterinary Medicine

      Abstract:

      Interleukin-6 (IL-6) plays a pivotal role in the immune response and inflammation regulation in various species, including canines. The advent of recombinant DNA technology has enabled the production of Canine IL-6 Recombinant (cIL-6r), opening new avenues for research in immunotherapy and veterinary medicine. This paper delves into the significance of cIL-6r, its production methods, and its potential applications in the treatment of inflammatory and autoimmune diseases in dogs.

      Introduction:

      Interleukin-6 is a multifunctional cytokine that exerts its effects on a wide range of physiological processes, including immune responses, hematopoiesis, and inflammation. In the canine immune system, IL-6 plays a crucial role in coordinating immune cell activation, antibody production, and acute phase responses. Recombinant IL-6 production has emerged as a promising strategy to harness its therapeutic potential.

      Methods:

      The production of cIL-6r involves recombinant DNA technology, where the canine IL-6 gene is inserted into an expression vector and transfected into a suitable host cell line, typically bacterial or mammalian cells. The recombinant protein is then purified using various chromatographic techniques to ensure high purity and biological activity.

      Applications:

      Canine IL-6 Recombinant holds immense promise in various applications within veterinary medicine. Its immunomodulatory properties make it a potential candidate for treating conditions such as immune-mediated diseases, inflammatory disorders, and certain types of cancer in dogs. Additionally, cIL-6r can be utilized to stimulate immune responses in vaccines, thereby enhancing their efficacy.

      Challenges and Future Directions:

      While cIL-6r shows great potential, its therapeutic use requires comprehensive studies to establish optimal dosages, safety profiles, and potential side effects. Long-term effects and potential interactions with existing treatments must also be explored.

      Conclusion:

      The advent of Canine IL-6 Recombinant marks a significant advancement in veterinary medicine, offering new avenues for immunotherapy and disease management in dogs. With further research and development, cIL-6r could become an invaluable tool in treating various conditions, ultimately enhancing the health and well-being of our canine companions.

      What is the molecular weight/Mw of IL6 CANINE Protein?
      IL6 CANINE Protein has a total Mw of 22kDa.

      What is the source or expression system of IL6 CANINE Protein?
      Sf9, Baculovirus cells.
      What is the Purity of IL6 CANINE Protein?
      IL6 CANINE Protein is >95% pure as determined by SDS-PAGE.

      What is the Biological Activity of IL6 CANINE Protein?
      The biological functionality of IL6 CANINE Protein will be determined in the future.

      What is the amino acid sequence of IL6 CANINE Protein?
      FPTPGPLAGD SKDDATSNSL PLTSANKVEE LIKYILGKIS ALRKEMCDKF NKCEDSKEAL AENNLHLPKL EGKDGCFQSG FNQETCLTRI TTGLVEFQLH LNILQNNYEG DKENVKSVHM STKILVQMLK SKVKNQDEVT TPDPTTDASL QAILQSQDEC VKHTTIHLIL RSLEDFLQFS LRAVRIMLEH HHHHH.

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

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

      Who supplies recombinant IL6 CANINE 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 CANINE?
      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.

    Il6 Canine
  • View Data Sheet

    Name :

    IL4 Rat

    Description:

    Interleukin-4 Rat Recombinant

    BCGF, BCDF, B cell stimulating factor, BSF-1, Lymphocyte stimulatory factor 1, IL-4, MGC79402, Binetrakin, Pitrakinra.

    Product # :

    CYT-385

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    Description

    Interleukin-4 Rat Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 125 amino acids and having a molecular mass of 14kDa. The IL-4 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Lyophilized from a 0.2µm filtered concentrated solution in PBS pH 7.4 and 5% trehalose.

    Purity

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

    Biological Activity

    The ED50 as determined in a cell proliferation assay using rat splenocytes is less than 2ng/ml corresponding to a specific activity of 500,000IU/mg. 

    More Info

    • Introduction

      IL4 is a pleiotropic cytokine produced by activated T cells. IL4 is a ligand for interleukin 4 receptor. The interleukin 4 receptor also binds to IL13, which may contribute to many overlapping functions of this cytokine and IL13. STAT6, a signal transducer and activator of transcription, has been shown to play a central role in mediating the immune regulatory signal of this cytokine. This gene, IL3, IL5, IL13, and CSF2 form a cytokine gene cluster on chromosome 5q, with this gene particularly close to IL13. IL4, IL13 and IL5 are found to be regulated coordinately by several long-range regulatory elements in an over 120 kilobase range on the chromosome. Two alternatively spliced transcript variants of this gene encoding distinct isoforms have been reported.

    • Synonyms

      BCGF, BCDF, B cell stimulating factor, BSF-1, Lymphocyte stimulatory factor 1, IL-4, MGC79402, Binetrakin, Pitrakinra.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized Interleukin-4 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IL4 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 4 in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      HGCNDSPLR EIINTLNQVT EKGTPCTEMF VPDVLTATRN TTENELICRA SRVLRKFYFP RDVPPCLKNK SGVLGELRKL CRGVSGLNSL RSCTVNESTL TTLKDFLESL KSILRGKYLQ SCTSMS.

    • Background

      What is the molecular weight/Mw of IL 4 RAT Protein?
      IL 4 RAT Protein has a total Mw of 14kDa.

      What is the source or expression system of IL 4 RAT Protein?
      Escherichia Coli.

      What is the Purity of IL 4 RAT Protein?
      IL 4 RAT Protein is >95% pure as determined by SDS-PAGE.

      What is the Biological Activity of IL 4 RAT Protein?
      The ED50 as determined in a cell proliferation assay using rat splenocytes is less than 2ng/ml corresponding to a specific activity of 500,000IU/mg.

      What is the amino acid sequence of IL 4 RAT Protein?
      HGCNDSPLR EIINTLNQVT EKGTPCTEMF VPDVLTATRN TTENELICRA SRVLRKFYFP RDVPPCLKNK SGVLGELRKL CRGVSGLNSL RSCTVNESTL TTLKDFLESL KSILRGKYLQ SCTSMS.

      What applications can IL 4 RAT Protein be used in?
      IL 4 RAT Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for IL 4 RAT Protein?
      The endotoxin level is minimal, IL 4 RAT Protein was purified using conventional chromatography techniques.

      Who supplies recombinant IL 4 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 IL 4 RAT?
      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 0.2 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-4 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 4 Rat
  • View Data Sheet

    Description:

    Interleukin-6 Soluble Receptor Human Recombinant

    IL6R-alpha, CD126, IL-6R 1, CD126 antigen, IL6RA, Interleukin 6 receptor, Interleukin 6 receptor alpha subunit, Interleukin-6 receptor alpha chain precursor, B cell stimulatory factor-2,Membrane glycoprotein 80, gp80, IL-6R, MGC104991.

    Product # :

    CYT-286

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    Description

    sIL-6R Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 338 amino acids (20-357) corresponding to the mature IL-6R protein, having a molecular weight of 42.25 kDa, with an aminoterminal hexahistidine tag.The sIL6R is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    CD126 His-Tag protein is supplied in 20mM Tris-HCl, pH 8.0, 0.8M Urea & 50% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      The IL-6 receptor complex is composed of two membrane glycoproteins: the low affinity receptor and the signaltransducing component. The soluble form of IL6R is found in the urine of healthy adult humans and the serum of HIV positive individuals, as well as in the cell culture supernatants of stimulated PBMC’s. This soluble form of IL6R results from either proteolytic cleavage from the membrane, or an isoform derived splice variant.

    • Synonyms

      IL6R-alpha, CD126, IL-6R 1, CD126 antigen, IL6RA, Interleukin 6 receptor, Interleukin 6 receptor alpha subunit, Interleukin-6 receptor alpha chain precursor, B cell stimulatory factor-2,Membrane glycoprotein 80, gp80, IL-6R, MGC104991.

    • 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

      Research Paper on Interleukin-6 Soluble Receptor Human Recombinant

      Abstract:

      Interleukin-6 (IL-6) Soluble Receptor Human Recombinant holds a critical place in immunological research, offering a unique lens into the intricate world of immune signaling. This research paper explores the molecular intricacies and the profound implications of IL-6 Soluble Receptor Human Recombinant in the context of immune responses. As we unravel its functions, synonyms, including DIF, TNFA, and TNFSF2, and potential applications, we gain valuable insights into the multifaceted role of immune regulation.

      Introduction:

      IL-6 Soluble Receptor Human Recombinant has emerged as a focal point of interest in the field of immunology. This paper aims to provide a comprehensive overview of its molecular characteristics and its role in shaping immune responses.

      Molecular Insights and Receptor Specificity:

      Delving into the molecular structure of IL-6 Soluble Receptor Human Recombinant, we uncover its pivotal role in binding IL-6. Its high affinity and specificity contribute to precise modulation of IL-6-mediated signaling pathways.

      Mediating Immune Responses:

      IL-6 exerts profound effects on immune cell activation, inflammation, and homeostasis. IL-6 Soluble Receptor Human Recombinant acts as a strategic player in fine-tuning these responses by sequestering IL-6, thereby influencing immune balance.

      Synonyms and Complex Interactions:

      Understanding the synonyms linked to IL-6, such as DIF, TNFA, and TNFSF2, enriches our comprehension of immune signaling networks. The interplay between IL-6 Soluble Receptor Human Recombinant and these molecules intricately shapes immune outcomes.

      Potential Therapeutic and Diagnostic Applications:

      The implications of IL-6 Soluble Receptor Human Recombinant extend beyond research settings. Its potential as a therapeutic candidate for immune-related disorders and its diagnostic utility in disease monitoring highlight its translational significance.

      Clinical Relevance and Future Prospects:

      IL-6 Soluble Receptor Human Recombinant's clinical potential is underscored by its role in diseases characterized by dysregulated IL-6 signaling. Investigating its role as a therapeutic intervention paves the way for innovative treatment strategies.

      Conclusion:

      In the realm of immunology, IL-6 Soluble Receptor Human Recombinant emerges as a key regulator of immune equilibrium. Its molecular intricacies, vital functions, and potential therapeutic implications position it as a cornerstone in unraveling immune responses and disease pathogenesis.

      What is the molecular weight/Mw of SIL 6R HUMAN Protein?
      SIL 6R HUMAN Protein has a total Mw of 42.25kDa.

      What is the source or expression system of SIL 6R HUMAN Protein?
      Escherichia Coli.

      What is the Purity of SIL 6R HUMAN Protein?
      SIL 6R HUMAN Protein is >90% pure as determined by SDS-PAGE.

      What is the Biological Activity of SIL 6R HUMAN Protein?
      The biological functionality of SIL 6R HUMAN Protein will be determined in the future.

      What is the amino acid sequence of SIL 6R HUMAN Protein?
      SIL 6R HUMAN Protein is composed from 338 amino acids.

      What applications can SIL 6R HUMAN Protein be used in?
      SIL 6R HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for SIL 6R HUMAN Protein?
      The endotoxin level is minimal, SIL 6R HUMAN Protein was purified using conventional chromatography techniques.

      Who supplies recombinant SIL 6R 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 SIL 6R HUMAN?
      ProSpec supplies bulk mg quantities at affordable prices that meets research and academic budgets.

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

    Il 6R Human
  • View Data Sheet

    Description:

    Interleukin-1b, Mouse Anti-Human FITC

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

    Product # :

    ANT-250

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    Formulation

    1 mg/ml in PBS (after reconstitution).

    More Info

    • Introduction

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

    • Synonyms

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

    • Solubility

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

    • Immunogen

      r.Human IL-1b.

    • Ig Subclass

      Mouse IgG2b.

    • Clone

      NYR-hIL1b.

    • Titer

      For intra-cellular staining, 10µl per 1,000,000 cells. By direct ELISA, 1:10,000 dilution will yield >1.0 O.D using alkaline phosphatase conjugated rabbit anti-mouse Ig (Jackson Laboratories).

    • Shipping Conditions

      Antibody is shipped lyophilized at ambient temperature.

    • Type

      Mouse Anti Human Monoclonal.

    • Storage Procedures

      In lyophilized form, for long periods, store at 4°C in a dry environment. After reconstitution, if not intended for use within a month, aliquot and store at -20°C.

    • Purification Method

      Ion Exchange.

    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 Antibody Fitc
  • View Data Sheet

    Description:

    Interleukin-3 Mouse Recombinant, sf9

    Interleukin-3, Interleukin-3, sf9, IL3 sf9, L-3, Hematopoietic growth factor, Mast cell growth factor, MCGF, Multipotential colony-stimulating factor, P-cell-stimulating factor, Il3, Csfmu, Il-3, BPA, Csfmu, HCGF, Il-3, MCGF, PSF.

    Product # :

    CYT-922

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    • SDS-PAGE

    Description

    IL3 Mouse Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 148 amino acids (27-166 a.a.) and having a molecular mass of 16.7kDa (Migrates at 18-28kDa on SDS-PAGE under reducing conditions).IL3 is expressed with a 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    IL3 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.

    Biological Activity

    The ED50 is Measured in a cell proliferation assay using TF-1 human erythroleukemic and is ≤ 0.1 ng/ml.

    SDS-PAGE

    More Info

    • Introduction

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

    • Synonyms

      Interleukin-3, Interleukin-3, sf9, IL3 sf9, L-3, Hematopoietic growth factor, Mast cell growth factor, MCGF, Multipotential colony-stimulating factor, P-cell-stimulating factor, Il3, Csfmu, Il-3, BPA, Csfmu, HCGF, Il-3, MCGF, PSF.

    • 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

      ASISGRDTHR LTRTLNCSSI VKEIIGKLPE PELKTDDEGP SLRNKSFRRV NLSKFVESQG EVDPEDRYVI KSNLQKLNCC LPTSANDSAL PGVFIRDLDD FRKKLRFYMV HLNDLETVLT SRPPQPASGS VSPNRGTVEC LEHHHHHH.

    • Background

      What is the molecular weight/Mw of IL3 MOUSE, SF9 Protein?
      IL3 MOUSE, SF9 Protein has a total Mw of 16.7kDa.

      What is the source or expression system of IL3 MOUSE, SF9 Protein?
      Sf9, Baculovirus cells.

      What is the Purity of IL3 MOUSE, SF9 Protein?
      IL3 MOUSE, SF9 Protein is >90% pure as determined by SDS-PAGE.

      What is the Biological Activity of IL3 MOUSE, SF9 Protein?
      The ED50 is Measured in a cell proliferation assay using TF-1 human erythroleukemic and is ≤ 0.1 ng/ml.

      What is the amino acid sequence of IL3 MOUSE, SF9 Protein?
      ASISGRDTHR LTRTLNCSSI VKEIIGKLPE PELKTDDEGP SLRNKSFRRV NLSKFVESQG EVDPEDRYVI KSNLQKLNCC LPTSANDSAL PGVFIRDLDD FRKKLRFYMV HLNDLETVLT SRPPQPASGS VSPNRGTVEC LEHHHHHH.

      What applications can IL3 MOUSE, SF9 Protein be used in?
      IL3 MOUSE, SF9 Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for IL3 MOUSE, SF9 Protein?
      The endotoxin level is minimal, IL3 MOUSE, SF9 Protein was purified using conventional chromatography techniques.

      Who supplies recombinant IL3 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 IL3 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.

    Il3 Mouse Sf9
  • View Data Sheet

    Description:

    Interleukin-37 Human Recombinant

    Interleukin-37, FIL1 zeta, IL-1X, Interleukin-1 family member 7, IL-1F7, Interleukin-1 homolog 4, IL-1H, IL-1H4, Interleukin-1 zeta, IL-1 zeta, Interleukin-1-related protein, IL-1RP1, Interleukin-23, IL-37, IL37, FIL1Z, IL1F7, IL1H4, IL1RP1, FIL1, FIL1(ZETA).

    Product # :

    CYT-011

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    Description

    Interleukin-37 Human Recombinant produced in E.Coli is a single, non-glycosylated, Polypeptide chain containing 167 amino acids (Lys27-Asp192) and having a molecular mass of 18.6kDa.The IL37 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    IL37 was lyophilized from a 0.2μM filtered solution of 20mM PB, 150mM NaCl and 2mM DTT pH 7.4.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Biological Activity

    As measured by its binding ability in a functional ELISA, immobilized IL1F7 at 1 µg/ml (100 µl/well) can bind rhIL-18 R/Fc Chimera with a linear range of 0.015-1µg/ml.

    More Info

    • Introduction

      Human interleukin family 1, member 7 (IL1F7) belongs to the interleukin 1 cytokine family. There are 5 alternatively spliced transcript variants encoding distinct isoforms with distinct expression profiles. The longest IL-1F7 transcript, named IL1F7b or IL1F7 isoform 1, encodes a 218 aa residues proprotein and containing a 45 aa propeptide which is cleaved to produce a mature protein. IL1F7b binds to IL18 Rb with low affinity however it doesn’t exert any IL18 agonistic or antagonistic effects. IL1F7b also binds IL18BP (interleukin 18 binding protein), which is an inhibitory binding protein of interleukin 18 (IL18), and afterward forms a complex with IL18 receptor beta subunit, and through which it inhibits the activity of IL18.

    • Synonyms

      Interleukin-37, FIL1 zeta, IL-1X, Interleukin-1 family member 7, IL-1F7, Interleukin-1 homolog 4, IL-1H, IL-1H4, Interleukin-1 zeta, IL-1 zeta, Interleukin-1-related protein, IL-1RP1, Interleukin-23, IL-37, IL37, FIL1Z, IL1F7, IL1H4, IL1RP1, FIL1, FIL1(ZETA).

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized IL37 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IL-37 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 quick spin followed by reconstitution of IL37 in PBS to a concentration no less than 100 µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      MKNLNPKKFSIHDQDHKVLVLDSGNLIAVPDKNYIRPEIFFALASSLSSASAEKGSPILLGVSKGEFCLYCDKDKGQSHPSLQLKKEKLMKLAAQKESARRPFIFYRAQVGSWNMLESAAHPGWFICTSCNCNEPVGVTDKFENRKHIEFSFQPVCKAEMSPSEVSD.

    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.

    Il1F7 Human
  • View Data Sheet

    Description:

    Interleukin-15 PAT7G9AT Mouse Anti-Human

    IL-15, MGC9721, Interleukin-15.

    Product # :

    ANT-776

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    Formulation

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

    More Info

    • Synonyms

      IL-15, MGC9721, Interleukin-15.

    • Physical Appearance

      Sterile filtered colorless solution.

    • Immunogen

      Anti-human IL15 mAb, is derived from hybridization of mouse F0 myeloma cells with spleen cells from BALB/c mice immunized with a recombinant human IL15 protein 49-162 amino acids purified from E. coli.

    • Ig Subclass

      Mouse IgG2a heavy chain and Kappa light chain.

    • Clone

      PAT7G9T.

    • Applications

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

    • Background

      Interleukin-15 which is produced by a wide variety of cells and tissues is a pleiotropic cytokine which takes part in innate and adaptive immunity. IL- 15 is well known due to its involvement in a trans-signaling mechanism where IL-15 receptor alpha from 1 subset of cells presents IL-15 to close cells that express IL-2Rβ/γc. IL-15 like IL-2, stimulates the proliferation of Tlymphocytes and induces the generation of cytotoxic T-lymphocytes (CTLs) and lymphokine-activated killer (LAK) cells. IL-15 and IL-2 may also compete for the same receptor, and thus negatively regulate each other's activity.

    • Type

      Mouse Anti Human Monoclonal.

    • Storage Procedures

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

    • Purification Method

      IL15 antibody was purified by protein-A affinity chromatography.

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

    Il15 Antibody
  • View Data Sheet

    Description:

    Interleukin-8 (1-77 a.a) Human Recombinant (CXCL8), His Tag

    IL-8, CXCL8, Monocyte-derived neutrophil chemotactic factor, MDNCF, T-cell chemotactic factor, Neutrophil-activating protein 1, NAP-1, Protein 3-10C, Granulocyte chemotactic protein 1, GCP-1, Monocyte-derived neutrophil-activating peptide, MONAP, Emoctakin, K60, NAF, LECT, LUCT, 3-10C, LYNAP, SCYB8, TSG-1, AMCF-I, b-ENAP.

    Product # :

    CHM-345

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    Description

    Interleukin-8 Human Recombinant produced in E.Coli is single, a non-glycosylated, Polypeptide chain containing 77 amino acids fragment (23-99) and having a total molecular mass of 13.7kDa with an amino-terminal hexahistidine tag. The IL-8 His is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    IL8 His is supplied in 10mM Tris-HCl pH 8, 250mM NaCl and 50% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Interleukin-8 (IL-8) is a chemokine produced by macrophages and other cell types such as epithelial cells. It is also synthesized by endothelial cells, which store IL-8 in their storage vesicles, the Weibel-Palade bodies. When first encountering an antigen, the primary cells to encounter it are the macrophages who phagocytose the particle. Upon processing, they release chemokines to signal other immune cells to come in to the site of inflammation. IL-8 is one such chemokine. It serves as a chemical signal that attracts neutrophils at the site of inflammation, and therefore is also known as Neutrophil Chemotactic Factor.

    • Synonyms

      IL-8, CXCL8, Monocyte-derived neutrophil chemotactic factor, MDNCF, T-cell chemotactic factor, Neutrophil-activating protein 1, NAP-1, Protein 3-10C, Granulocyte chemotactic protein 1, GCP-1, Monocyte-derived neutrophil-activating peptide, MONAP, Emoctakin, K60, NAF, LECT, LUCT, 3-10C, LYNAP, SCYB8, TSG-1, AMCF-I, b-ENAP.

    • 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 CXCL8 HUMAN, HIS Protein?
      CXCL8 HUMAN, HIS Protein has a total Mw of 13.7kDa.

      What is the source or expression system of CXCL8 HUMAN, HIS Protein?
      Escherichia Coli.

      What is the Purity of CXCL8 HUMAN, HIS Protein?
      CXCL8 HUMAN, HIS Protein is >95% pure as determined by SDS-PAGE.

      What is the Biological Activity of CXCL8 HUMAN, HIS Protein?
      The biological functionality of CXCL8 HUMAN, HIS Protein will be determined in the future.

      What is the amino acid sequence of CXCL8 HUMAN, HIS Protein?
      CXCL8 HUMAN, HIS Protein is composed from 77 amino acids.

      What applications can CXCL8 HUMAN, HIS Protein be used in?
      CXCL8 HUMAN, HIS Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for CXCL8 HUMAN, HIS Protein?
      The endotoxin level is minimal, CXCL8 HUMAN, HIS Protein was purified using conventional chromatography techniques.

      Who supplies recombinant CXCL8 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 CXCL8 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 8 77 Human His
  • View Data Sheet

    Description:

    Interleukin-1 Receptor Antagonist Mouse Recombinant, Active His Tag

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

    Product # :

    CYT-1136

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    Description

    IL1RA Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 177 amino acids (27-178 aa) and having a molecular mass of 20kDa.IL1RA is fused to a 25 amino acid His tag at N-terminus and purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The IL1RA solution (1 mg/ml) contains 10% Glycerol, 20mM Tris-HCl buffer (pH 8.0) and 0.1M NaCl

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Biological Activity

    Measured by the ability to inhibit proliferation using D10.G4.1 mouse helper T cells. ED50 for this effect is ≤ 60 ng/ml with Mouse IL-1 alpha.

    More Info

    • Introduction

      Interleukin-1 ra is a member of the interleukin 1 cytokine family. IL1RAinhibits the activities of interleukin 1, alpha (IL1A) and interleukin 1, beta (IL1B), and modulates a variety of interleukin 1 related immune and inflammatory responses. IL1RAand 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.

    • Synonyms

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

    • 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 MGSHMRPSGK RPCKMQAFRI WDTNQKTFYL RNNQLIAGYL
      QGPNIKLEEK IDMVPIDLHS VFLGIHGGKL CLSCAKSGDD IKLQLEEVNI TDLSKNKEED
      KRFTFIRSEK GPTTSFESAA CPGWFLCTTL EADRPVSLTN TPEEPLIVTK FYFQEDQ

    • Background

      What is the molecular weight/Mw of IL1RA MOUSE, HIS ACTIVE Protein?
      IL1RA MOUSE, HIS ACTIVE Protein has a total Mw of 20kDa.

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

      What is the Purity of IL1RA MOUSE, HIS ACTIVE Protein?
      IL1RA MOUSE, HIS ACTIVE Protein is >95% pure as determined by SDS-PAGE.

      What is the Biological Activity of IL1RA MOUSE, HIS ACTIVE Protein?
      Measured by the ability to inhibit proliferation using D10.G4.1 mouse helper T cells. ED50 for this effect is ≤ 60 ng/ml with Mouse IL-1 alpha.

      What is the amino acid sequence of IL1RA MOUSE, HIS ACTIVE Protein?
      MGSSHHHHHH SSGLVPRGSH MGSHMRPSGK RPCKMQAFRI WDTNQKTFYL RNNQLIAGYL
      QGPNIKLEEK IDMVPIDLHS VFLGIHGGKL CLSCAKSGDD IKLQLEEVNI TDLSKNKEED
      KRFTFIRSEK GPTTSFESAA CPGWFLCTTL EADRPVSLTN TPEEPLIVTK FYFQEDQ

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

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

      Who supplies recombinant IL1RA MOUSE, HIS ACTIVE 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, HIS ACTIVE?
      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.

    Il1Ra Mouse
  • View Data Sheet

    Description:

    Inducible T Cell Costimulator 4 Human Recombinant

    Inducible T Cell Costimulator, Activation-Inducible Lymphocyte Immunomediatory Molecule, Inducible T-Cell Costimulator, AILIM, Inducible T-Cell Co-Stimulator, Inducible Costimulator, CD278 Antigen, CD278, CVID1.   

    Product # :

    PRO-2534

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    Description

    ICOS produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 362 amino acids (21-140a.a.) and having a molecular mass of 40.8kDa. (Molecular size on SDS-PAGE will appear at approximately 40-57kDa). ICOS is expressed with an 242 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    ICOS protein solution (0.25mg/ml) contains 20mM MES buffer (pH 5.5), 40% glycerol, 2mM DTT and 1mM EDTA 0.1M NaCl.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      ICOS (inducible T-cell costimulatory) belongs to the CD28 family of immune-assisted stimulatory receptors. ICOS forms homodimers and takes a significant part in immune responses, cell-cell signaling, as well as regulation of cell proliferation. The interaction of B7-H2 / ICOS takes a vital role in T-cell differentiation, T-B cell interaction in addition to humoral immune response is essential for the formation of reproductive centers as well as the production of cytokine IL-4. Moreover, ICOS is more effective in inducing IL-10 production, a cytokine which is important for the inhibitory function of T regulatory cells. The ICOS-B7RP-1 and B7-1 / B7-2-CD28 / CTLA-4 pathways offer a significant second signal which can regulate the inhibition, activation and fine regulation of T-lymphocyte responses. ICOS stimulates the production of Th1 and Th2 cytokines, however it can also participate in the generation of Th2 cells.

    • Synonyms

      Inducible T Cell Costimulator, Activation-Inducible Lymphocyte Immunomediatory Molecule, Inducible T-Cell Costimulator, AILIM, Inducible T-Cell Co-Stimulator, Inducible Costimulator, CD278 Antigen, CD278, CVID1.

    • 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

      ADPEINGSAN YEMFIFHNGG VQILCKYPDI VQQFKMQLLK GGQILCDLTK TKGSGNTVSI KSLKFCHSQL SNNSVSFFLY NLDHSHANYY FCNLSIFDPP PFKVTLTGGY LHIYESQLCC QLKLEPKSCD KTHTCPPCPA PELLGGPSVF LFPPKPKDTL MISRTPEVTC VVVDVSHEDP EVKFNWYVDG VEVHNAKTKP REEQYNSTYR VVSVLTVLHQ DWLNGKEYKC KVSNKALPAP IEKTISKAKG QPREPQVYTL PPSRDELTKN QVSLTCLVKG FYPSDIAVEW ESNGQPENNY KTTPPVLDSD GSFFLYSKLT VDKSRWQQGN VFSCSVMHEA LHNHYTQKSL SLSPGKHHHH
      HH

    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.

    Icos Human
  • View Data Sheet

    Description:

    Interleukin-22 Receptor Antagonist (Y51A), PEG Mouse Recombinant

    Product # :

    CYT-1248

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    Description

    Interleukin 22 Y51A mutan Mouse Recombinant is a single non-glycosilated polypeptide chain containing 147 amino acids and additional Ala at N-terminus. The iL22RA is bound to 20 kDa PEG molecule at N-terminus, resulting in 36.0 kDa. The Mouse iL22RA (Y51A) Pegylated runs as a 50 kDa due to enlarged hydrodymanic volume. iL22RA Mutant Mouse Recombinant was purified by proprietary chromatographic techniques.

    Source

    Escherichia coli.

    Formulation

    The Mouse iL22RA (Y51A) was lyophilized from a concentrated (1mg/ml) solution with 0.003mM NaHCO3.

    Purity

    Greater than 98.0% as determined by:

    (a) Gel filtration analysis.

    (b) Analysis by SDS-PAGE.

    Biological Activity

    Pegylated Mouse iL22RA inhibits mouse IL-22 induced STAT3 phosphorylation in HepG cells. Its inhibitory acrtivity in vitro is ~ 10-20% compared to the non-pegylated mIL22 (Y51A) mutant.

    More Info

    • Physical Appearance

      White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized iL22RA (Y51A) Mutant Mouse Recombinant although stable at room temperature for several weeks, should be stored desiccated below -18°C. Upon reconstitution at > 0.1 mg/ml and up to 2mM and filter sterilization iL22RA mutant can be stored at 4°C or even room temperature for several weeks making it suitable for long term infusion studies using osmotic pumps. At lower concentration addition of a carrier protein (0.1% HSA or BSA) is suggested. Please prevent freeze-thaw cycles.

    • Solubility

      It is recommended to reconstitute the lyophilized iL22RA (Y51A) Mutant Mouse Recombinant in sterile water or sterile 0.4% NaHCO3 adjusted to pH 8-9, not less than 100µg/ml, which can then be further diluted with other aqueous solutions.

    • Background

      IL-22 is a part of the IL-10 family of regulatory cytokines and produced by several populations of immune cells at a site of inflammation. Members of this family share partial homology in their amino acid sequences, but varies in their biological functions. IL-22 takes effect on non-hematopoietic cells. IL-22 takes part in wound healing and in protection against microbs. Produced by T lymphocytes, IL-22 inhibits IL-4 production by Th2 cells, and induces acute phase reactants in the pancreas and liver.

    • Protein content

      Protein quantization was carried out by UV spectroscopy at 280 nm using the absorbency value of 0.18 as the extinction coefficient for a 0.1% (1mg/ml) solution at pH 8.0. This value is calculated by the DNAman computer analysis program of protein sequences.

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

    Il22Ra Mouse Peg
  • View Data Sheet

    Description:

    Interleukin-27 Mouse Recombinant

    Interleukin-30, IL-30, IL-27/p28, p28, Interleukin-27, Interleukin-27/p28, IL-27, Interleukin-27 subunit alpha, IL-27 subunit alpha, IL27-A, Il27, Il27a, IL-27p28.

    Product # :

    CYT-570

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    Description

    Interleukin-27 Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 207 amino acids and having a molecular mass of 23.7 kDa. The Murine IL-27 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Lyophilized from 10mM NaHCO₃ buffer pH-8.5.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Biological Activity

    Mouse p28 biological activity was measured via dose-dependent inhibition of TGF-beta and IL-6-induced IL-17A expression in mouse CD4 splenocytes. 50ng/ml of mouse p28 is capable of inhibiting >25% of IL-17A expression in this assay. 

    More Info

    • Introduction

      Interleukin-27 protein is related to IL-12A & is one of the subunits of a heterodimeric cytokine complex. IL-27 interacts with EBV induced gene 3 also called EBI3, and forms a complex that drives rapid expansion of CD4 (+) T cells.
      IL-27 complex is synergizes with IL-12 in order to trigger the cytokine production of IFN-Gamma of CD4 (+) T cells. The biological effect of IL-27 is mediated by class-I cytokine receptor (WSX1/TCRR).
      The pro-inflammatory activity of IL-27 is mediated through the growing expression of key molecules involved in the MHC class-I & MHC class-II pathways. Both MHC class-I and MHC-class-II expression are increased in endothelial cells after Interleukin-27 stimulation which suggests that it may play an important role in conferring the immune function on vascular endothelium IL-27p28 subunit can be induced by IFN-beta and during LPS-induced maturation of dendritic cells in type-I IFN-dependent manner through IFN regulatory factor-1 activation. Interleukin-27 regulates Interleukin-12 responsiveness of CD4+ T cells through Stat1-dependent and -independent mechanisms. IL-17 & IL-23 play an important IL-17 role in inflammation. Interleukin-27 possesses potent anti-angiogenic activity that plays an important role in its antitumor and antimetastatic activities.
      EBV induced gene 3 plays a role, independently from IL-27, in regulating anti-viral or anti-tumoral immune responses. Interleukin-27 is a potent inhibitor of HIV-1 replication in macrophages, CD4+ T cells, peripheral blood mononuclear cells.
      Interleukin-27 triggers STAT activation and gene transcription.

    • Synonyms

      Interleukin-30, IL-30, IL-27/p28, p28, Interleukin-27, Interleukin-27/p28, IL-27, Interleukin-27 subunit alpha, IL-27 subunit alpha, IL27-A, Il27, Il27a, IL-27p28.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized IL-27 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IL27 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-27 in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      MFPTDPLSLQ ELRREFTVSL YLARKLLSEV QGYVHSFAES RLPGVNLDLL PLGYHLPNVS LTFQAWHHLS DSERLCFLAT TLRPFPAMLG GLGTQGTWTS SEREQLWAMR LDLRDLHRHL RFQVLAAGFK CSKEEEDKEE EEEEEEEEKK LPLGALGGPN QVSSQVSWPQ LLYTYQLLHS LELVLSRAVR DLLLLSLPRR PGSAWDS.

    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 27 Mouse
  • View Data Sheet

    Description:

    Interleukin-1 receptor-like 1 Human Recombinant

    Interleukin-1 receptor-like 1, Protein ST2, IL1RL1, DER4, ST2, T1, ST2L, ST2V, FIT-1, MGC32623.

    Product # :

    CYT-671

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    Description

    IL1RL1 Human Recombinant produced in E.Coli is a single, non-glycosylated, Polypeptide chain containing 310 amino acids fragment (19-328) corresponding to the soluble IL1RL1 coding sequence, having a molecular weight of 39.5kDa and fused with a 4.5kDa amino-terminal hexahistidine tag. The IL1RL1 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    IL1RL1 protein solution is supplied in 25mM Sodium Acetate pH 4.8 and 50% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      The IL1RL1 gene is a member of the IL-1 receptor family, encoding a transmembrane protein with a structure similar to IL-1R1. IL1RL1 is a receptor for interleukin-33, its stimulation recruits MYD88, IRAK1, IRAK4, and TRAF6, followed by phosphorylation of MAPK3/ERK1 and/or MAPK1/ERK2, MAPK14, and MAPK8. IL1RL1 may possibly be involved in helper T-cell function. IL1RL1 is highly expressed in kidney, lung, placenta, stomach, skeletal muscle, colon and small intestine.
      A soluble form of the IL1RL1 is produced from the same gene by alternative splicing and was shown to be expressed in several cell types including fibroblasts and mast cells. Soluble IL1RL1 also acts as a negative regulator of Th2 cytokine production and high levels have been reported in several disease states and conditions including asthma, sepsis and myocardial infarction.
      Analysis of the similar gene in mouse suggested that the IL1RL1 receptor can be induced by proinflammatory stimuli, and may be involved in the function of helper T cells.

    • Synonyms

      Interleukin-1 receptor-like 1, Protein ST2, IL1RL1, DER4, ST2, T1, ST2L, ST2V, FIT-1, MGC32623.

    • 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 IL1RL1 HUMAN Protein?
      IL1RL1 HUMAN Protein has a total Mw of 39.5kDa.

      What is the source or expression system of IL1RL1 HUMAN Protein?
      Escherichia Coli.

      What is the Purity of IL1RL1 HUMAN Protein?
      IL1RL1 HUMAN Protein is >95% pure as determined by SDS-PAGE.

      What is the Biological Activity of IL1RL1 HUMAN Protein?
      The biological functionality of IL1RL1 HUMAN Protein will be determined in the future.

      What is the amino acid sequence of IL1RL1 HUMAN Protein?
      IL1RL1 HUMAN Protein is composed from 310 amino acids.

      What applications can IL1RL1 HUMAN Protein be used in?
      IL1RL1 HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for IL1RL1 HUMAN Protein?
      The endotoxin level is minimal, IL1RL1 HUMAN Protein was purified using conventional chromatography techniques.

      Who supplies recombinant IL1RL1 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 IL1RL1 HUMAN ?
      ProSpec supplies bulk mg quantities at affordable prices that meets research and academic budgets.

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

    Il1Rl1 Human
  • View Data Sheet

    Description:

    Interleukin-2 Canine Recombinant, His Tag

    Interleukin-2, IL-2, T-cell growth factor, TCGF.

    Product # :

    CYT-1011

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    • SDS-PAGE

    Description

    IL2 Canine Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 160 amino acids (21-155 a.a) and having a molecular mass of 18.1 kDa.IL2 Canine is fused to a 25 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    IL2 Canine protein solution (0. 5mg/ml) contains Phosphate buffered saline (pH7.4).

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Biological Activity

    The ED50 measured in a cell proliferation assay using CTLL-2 mouse cytotoxic T cells. is < 0.3 ng/ml.

    SDS-PAGE

    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, IL-2, T-cell growth factor, TCGF.

    • 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. Please avoid freeze thaw cycles.

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MGSHMAPITS SSTKETEQQM EQLLLDLQLL LNGVNNYENP QLSRMLTFKF YTPKKATEFT HLQCLAEELK NLEEVLGLPQ SKNVHLTDTK ELISNMNVTL LKLKGSETSY NCEYDDETAT ITEFLNKWIT FSQSIFSTLT.

    • Background

      What is the molecular weight/Mw of IL 2 CANINE, IS Protein?
      IL 2 CANINE, HIS Protein has a total Mw of 18.1kDa.

      What is the source or expression system of IL 2 CANINE, HIS Protein?
      Escherichia Coli.

      What is the Purity of IL 2 CANINE, HIS Protein?
      IL 2 CANINE, HIS Protein is >95% pure as determined by SDS-PAGE.

      What is the Biological Activity of IL 2 CANINE, HIS Protein?
      The ED50 measured in a cell proliferation assay using CTLL-2 mouse cytotoxic T cells. is < 0.3 ng/ml.

      What is the amino acid sequence of IL 2 CANINE, HIS Protein?
      MGSSHHHHHH SSGLVPRGSH MGSHMAPITS SSTKETEQQM EQLLLDLQLL LNGVNNYENP QLSRMLTFKF YTPKKATEFT HLQCLAEELK NLEEVLGLPQ SKNVHLTDTK ELISNMNVTL LKLKGSETSY NCEYDDETAT ITEFLNKWIT FSQSIFSTLT.

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

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

      Who supplies recombinant IL 2 CANINE, HIS that is in stock and available to order?
      ProSpec has the protein in stock and available for immediate delivery.

      Where can I order bulk mg quantities of IL 2 CANINE, 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.

    Il2 Canine
  • View Data Sheet

    Description:

    Intein Bacillus Circulans Recombinant

    Intein-CBD

    Product # :

    PRO-958

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    Description

    Intein Bacillus Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 533 amino acids (3-518) and having a molecular mass of 59.4 kDa.Intein is fused to a 16 amino acid His-tag at C-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    The Intein solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 1mM DTT, 0.1M NaCl and 10% glycerol.

    Purity

    Greater than 95% as determined by SDS-PAGE.

    More Info

    • Introduction

      Intein is a section of a protein which can remove itself and return the remaining segment with a peptide bond. In addition, Inteins hold an endonuclease domain which takes part in Intein proliferation. Actually, various genes have unrelated intein-coding segments inserted at altered positions and they were found in all three domains of life (eukaryotes, bacteria, and archaea) and in viruses.

    • Synonyms

      Intein-CBD

    • 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

      MKIEEGKLVI GSLEGCFAKG TNVLMADGSI ECIENIEVGN KVMGKDGRPR EVIKLPRGRE TMYSVVQKSQ HRAHKSDSSR EVPELLKFTC NATHELVVRT PRSVRRLSRT IKGVEYFEVI TFEMGQKKAP DGRIVELVKE VSKSYPISEG PERANELVES YRKASNKAYF EWTIEARDLS LLGSHVRKAT YQTYAPILYE NDHFFDYMQK SKFHLTIEGP KVLAYLLGLW IGDGLSDRAT FSVDSRDTSL MERVTEYAEK LNLCAEYKDR KEPQVAKTVN LYSKVVRGAS TNPGVSAWQV NTAYTAGQLV TYNGKTYKCL QPHTSLAGWE PSNVPALWQL QGGHGGIRNN LNTENPLWDA IVGLGFLKDG VKNIPSFLST DNIGTRETFL AGLIDSDGYV TDEHGIKATI KTIHTSVRDG LVSLARSLGL VVSVNAEPAK VDMNVTKHKI SYAIYMSGGD VLLNVLSKCA GSKKFRPAPA AAFARECRGF YFELQELKED DYYGITLSDD SDHQFLLGSQ VVVQNLEHHH 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.

    Intein Bacillus Circulans
  • View Data Sheet

    Description:

    Vaspin Human Recombinant, His Tag

    Serpin A12 precursor, Visceral adipose-specific serpin, Visceral adipose tissue- derived serine protease inhibitor, Vaspin, OL-64, SERPINA12, Serine (or cysteine) proteinase inhibitor, clade A, antitrypsin, alpha-1 antiproteinase.

    Product # :

    CYT-459

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    Description

    Vaspin Human Recombinant produced in E.Coli is a single, non-glycosylated, His Tag, polypeptide chain containing 415 amino acids and having a molecular mass of 47 kDa.The Vaspin is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Vaspin in 20mM Tris pH-8, 0.2mM PMSF and 10% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Vaspin (visceral adipose-specific SERPIN), a newly identified adipokine, which is a member of serine protease inhibitor family. Vaspin is also a unique insulin sensitizing adipocytokine in obesity. A recent publication indicates that induction of human vaspin mRNA expression in adipose tissue is regulated in a fat depot-specific manner and could be associated with parameters of obesity, insulin resistance, and glucose metabolism.

    • Synonyms

      Serpin A12 precursor, Visceral adipose-specific serpin, Visceral adipose tissue- derived serine protease inhibitor, Vaspin, OL-64, SERPINA12, Serine (or cysteine) proteinase inhibitor, clade A, antitrypsin, alpha-1 antiproteinase.

    • Physical Appearance

      Sterile Filtered colorless solution.

    • Stability

      Liquid Vaspin although stable at 10°C for 1 week, should be stored 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.

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MLKPSFSPRN YKALSEVQGW KQRMAAKELA RQNMDLGFKL LKKLAFYNPG RNIFLSPLSI STAFSMLCLG AQDSTLDEIK QGFNFRKMPE KDLHEGFHYI IHELTQKTQD LKLSIGNTLF IDQRLQPQRK FLEDAKNFYS AETILTNFQN LEMAQKQIND FISQKTHGKI NNLIENIDPG TVMLLANYIF FRARWKHEFD PNVTKEEDFF LEKNSSVKVP MMFRSGIYQV GYDDKLSCTI LEIPYQKNIT AIFILPDEGK LKHLEKGLQV DTFSRWKTLL SRRVVDVSVP RLHMTGTFDL KKTLSYIGVS KIFEEHGDLT KIAPHRSLKV GEAVHKAELK MDERGTEGAA GTGAQTLPME TPLVVKIDKP YLLLIYSEKI PSVLFLGKIV NPIGK.

    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.

    Vaspin Human
  • View Data Sheet

    Description:

    FAS Blocking Antibody (CD95), Mouse anti Human

    FASLG receptor, Apoptosis-mediating surface antigen FAS, Apo-1 antigen, CD95, Tumor necrosis factor receptor superfamily member 6 TNR6, APT1, FAS1, TNFRSF6.

    Product # :

    ANT-205

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    More Info

    • Introduction

      The Fas receptor (CD95) mediates apoptotic signaling by Fas-ligand expressed on the surface of other cells. The Fas-FasL interaction plays an important role in the immune system and lack of this system leads to autoimmunity, indicating that Fas-mediated apoptosis removes self-reactive lymphocytes. Fas signaling is also involved in immune surveillance to remove transformed cells and virus infected cells. Binding of FAS to oligimerized FasL on another cell activates apoptotic signaling through a cytoplasmic domain termed the death domain that interacts with signaling adaptors including FAF, FADD and DAX to activate the caspase proteolytic cascade. Caspase-8 and caspase-10 are first activated, to then cleave and activate downstream caspases, and a variety of cellular substrates that lead to cell death. Caspases cleave nuclear lamins, causing the nucleus to break down and lose its normal structure and another caspase substrate is DFF, inducing cleavage and degradation of the genome. Other caspase substrates are involved in cytoskeletal structure, cell cycle regulation and signaling pathways. Activation of JNK kinase, activation of Jun, and production of ceramide may also play roles in Fas-mediated apoptosis. Activation of fas-mediated apoptosis is opposed by I-FLICE and FAP. Viruses and tumors may escape immune surveillance in part through suppression of fas-mediated apoptosis using similar mechanisms.

    • Synonyms

      FASLG receptor, Apoptosis-mediating surface antigen FAS, Apo-1 antigen, CD95, Tumor necrosis factor receptor superfamily member 6 TNR6, APT1, FAS1, TNFRSF6.

    • Solubility

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

    • Immunogen

      Recombinant Human FAS.

    • Ig Subclass

      mouse IgG1.

    • Clone

      NYRhFAS.

    • Note

      This is a BLOCKING antibody and will block FAS-mediated apoptosis.

    • Titer

      By direct ELISA, 1:10,000 dilution will yield 0.5 O.D using alkaline phosphatase conjugated rabbit anti-mouse Ig (Jackson Laboratories).

    • Shipping Conditions

      Antibody is shipped lyophilized at ambient temperature.

    • Type

      Mouse Anti Human Monoclonal.

    • Storage Procedures

      In lyophilized form, for long periods, store at 4°C in a dry environment. After reconstitution, if not intended for use within a month, aliquot and store at -20°C.

    • Purification Method

      Ion exchange column Protein concentration1 mg/ml in PBS (after reconstitution).

    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.

    Fas B Antibody
  • View Data Sheet

    Description:

    Macrophage Migration Inhibitory Factor, Mouse Anti Human

    Phenylpyruvate tautomerase, Glycosylation- inhibiting factor, GIF, MMIF, MIF.

    Product # :

    ANT-311

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    Formulation

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

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    • Introduction

      The cytokine Macrophage migration inhibitory factor (MIF) has been identified to be secreted by the pituitary gland and the monocyte/macrophage and to play an important role in endotoxic shock. MIF has the unique property of being released from macrophages and T cells in response to physiological concentrations of glucocorticoids. The secretion of MIF is tightly regulated and decreases at high, anti-inflammatory steroid concentration.

    • Synonyms

      Phenylpyruvate tautomerase, Glycosylation- inhibiting factor, GIF, MMIF, MIF.

    • Immunogen

      Anti-human MIF mAb, is derived from hybridization of mouse SP2/0 myeloma cells with spleen cells from BALB/c mice immunized with Recombinant human MIF amino acids 1-114 purified from E. coli.

    • Ig Subclass

      Mouse IgG1 heavy chain and κ light chain.

    • Clone

      P4E4AT.

    • Applications

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

    • Type

      Mouse Anti Human Monoclonal.

    • Storage Procedures

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

    • Purification Method

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

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

    Mif Antibody
  • 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