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343 results found for “Mediator Complex”

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  • 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.

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    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:

    Methionine Adenosyltransferase II Alpha Human Recombinant

    MATA2, MATII, SAMS2, MAT-2A, S-adenosylmethionine synthetase isoform type-2, AdoMet synthetase 2, Methionine adenosyltransferase 2, Methionine adenosyltransferase II, MAT2A, AMS2.

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    ENZ-320

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    Description

    MAT2A Human Recombinant fused with His tag (20 a.a.) at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 415 amino acids and having a molecular mass of 45.8 kDa.The MAT2A is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The MAT2A solution (1mg/ml) contains 20mM Tris pH-8 & 10% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      MAT2A is an important enzyme in cellular metabolism and catalyzes the formation of S-adenosylmethionine (SAMe) from L-methionine and ATP. MAT2A is expressed in extrahepatic tissues. In liver, MAT2A expression associates with growth, dedifferentiation, and cancer. NF-kappa B and AP-1 are necessary for basal MAT2A expression in HepG2 cells and mediate the increase in MAT2A expression in response to TNF-alpha. Up-regulation of MAT2A provides growth improvement and s-adenosylmethionine and methylthioadenosine thus can block mitogenic signaling in colon cancer cells. Lower expression of both MAT2A and MAT2beta and interfere with leptin signaling in liver cancer cells.

    • Synonyms

      MATA2, MATII, SAMS2, MAT-2A, S-adenosylmethionine synthetase isoform type-2, AdoMet synthetase 2, Methionine adenosyltransferase 2, Methionine adenosyltransferase II, MAT2A, AMS2.

    • 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).Please prevent freeze-thaw cycles.

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MNGQLNGFHE AFIEEGTFLF TSESVGEGHP DKICDQISDA VLDAHLQQDP DAKVACETVA KTGMILLAGE ITSRAAVDYQ KVVREAVKHI GYDDSSKGFD YKTCNVLVAL EQQSPDIAQG VHLDRNEEDI GAGDQGLMFG YATDETEECM PLTIVLAHKL NAKLAELRRN GTLPWLRPDS KTQVTVQYMQ DRGAVLPIRV HTIVISVQHD EEVCLDEMRD ALKEKVIKAV VPAKYLDEDT IYHLQPSGRF VIGGPQGDAG LTGRKIIVDT YGGWGAHGGG AFSGKDYTKV DRSAAYAARW VAKSLVKGGL CRRVLVQVSY AIGVSHPLSI SIFHYGTSQK SERELLEIVK KNFDLRPGVI VRDLDLKKPI YQRTAAYGHF GRDSFPWEVP KKLKY.

    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.

    Mat2A Human
  • View Data Sheet

    Description:

    Osteoprotegerin Human Recombinant, His Tag

    TNFRSF11B, OPG, OCIF, Osteoclastogenesis inhibitory factor, TR1, MGC29565.

    Product # :

    CYT-290

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    Description

    Recombinant Human OCIF produced in E.coli cells is a single, non-glycosylated, polypeptide chain containing amino acids 201-401 and having a molecular mass of 31 kDa which includes a 4 kDa His tag.The OPG is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The protein was lyophilized from a concentrated (1mg/ml) solution with 1X PBS, 0.1% SDS and 1mM DTT.

    Purity

    Greater than 80.0% as determined by(a) Analysis by RP-HPLC.
    (b) Analysis by SDS-PAGE.

    More Info

    • Introduction

      Osteoprotegerin, which is a member of the tumor necrosis factor receptor superfamily and is involved in the regulation of bone metabolism. OPGand its ligand (OPGL) are cytokines regulating osteoclasto-genesis. OPGL binds to receptors on the surface of preosteoclasts and stimulates their differentiation into active osteoclasts. This leads to osteoresorption. OPG inhibits this osteoclasto-genesis (OPG is secreted by osteoblasts, and binds to OPGL, thus inhibiting maturation of osteoclasts and osteoresorption). The degree and activity of osteoresorption depend mainly on the balance between OPG and its ligand (OPGL); factors increasing OPGL expression mostly reduce OPG expression and vice versa.

    • Synonyms

      TNFRSF11B, OPG, OCIF, Osteoclastogenesis inhibitory factor, TR1, MGC29565.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Applications

      1. Positive control for Western blot.
      2. Antibody production.
      3. Protein assay.

    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.

    Osteoprotegerin Human His
  • View Data Sheet

    Description:

    Parkinson Disease Protein 7, Mouse Anti Human

    Protein DJ-1, Oncogene DJ1, Parkinson disease protein 7, PARK7, DJ1, DJ-1, FLJ27376.

    Product # :

    ANT-317

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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 PARK7 is a ubiquitously expressed protein involved in various cellular processes including spermatogenesis and fertilization, cancer, RNA-binding, androgen-receptor signaling and oxidative stress. Mutations in the PARK7 are the cause of autosomal recessive early-onset Parkinson’s disease 7 (Park7).

    • Synonyms

      Protein DJ-1, Oncogene DJ1, Parkinson disease protein 7, PARK7, DJ1, DJ-1, FLJ27376.

    • Immunogen

      Anti-human PARK7 mAb is derived from hybridization of mouse SP2/O myeloma cells with spleen cells from BALB/c mice immunized with recombinant human PARK7 amino acids 1-189 purified from E. coli.

    • Ig Subclass

      Mouse IgG1 heavy chain and κ light chain.

    • Clone

      P1B11AT.

    • Applications

      PARK7 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. Recommended dilution range for Western blot analysis is 1:500 ~ 2,000. Recommended starting dilution is 1:1,000.

    • 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

      PARK7 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.

    Park7 Antibody
  • View Data Sheet

    Description:

    Clusterin, Mouse Anti Human

    CLI, AAG4, KUB1, SGP2, SGP-2, SP-40, TRPM2, MGC24903, Complement-associated protein SP-40,40, Complement cytolysis inhibitor, NA1/NA2, Apolipoprotein J, Apo-J, Testosterone-repressed prostate message 2, TRPM-2.

    Product # :

    ANT-314

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    Formulation

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

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    • Introduction

      Clusterin also named Apolipoprotein J (APO-J) is a 75-80 kD disulfide-linked heterodimeric protein containing about 30% of N-linked carbohydrate rich in sialic acid but truncated forms targeted to the nucleus have also been identified. The precursor polypeptide chain is cleaved proteolytically to remove the 22-mer secretory signal peptide and subsequently between residues 227/228 to generate the ? and ? chains. These are assembled in anti-parallel to give a heterodimeric molecule in which the cysteine-rich centers are linked by five disulfide bridges and are flanked by two predicted coiled-coil ? -helices and three predicted amphipathic a-helices. Across a broad range of species clusterin shows a high degree of sequence homology ranging from 70% to 80%. It is nearly ubiquitously expressed in most mammalian tissues and can be found in plasma, milk, urine, cerebrospinal fluid and semen. It is able to bind and form complexes with numerous partners such as immunoglobulins, lipids, heparin, b

    • Synonyms

      CLI, AAG4, KUB1, SGP2, SGP-2, SP-40, TRPM2, MGC24903, Complement-associated protein SP-40,40, Complement cytolysis inhibitor, NA1/NA2, Apolipoprotein J, Apo-J, Testosterone-repressed prostate message 2, TRPM-2.

    • Physical Appearance

      Sterile Filtered clear solution.

    • Immunogen

      Anti-human Clusterin mAb, is derived from hybridization of mouse SP2/O myeloma cells with spleen cells from BALB/c mice immunized with Recombinant human Clusterin amino acids 1-333 purified from E. coli.

    • Ig Subclass

      Mouse IgG1 heavy chain and κ light chain.

    • Clone

      P1A11AT.

    • Applications

      Clusterin antibody has been tested by ELISA, Western blot, ICC/IF, IHC and FACS 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

      Clusterin 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.

    Clusterin Antibody
  • View Data Sheet

    Description:

    Interleukin-6 Human Recombinant, Sf9

    BSF2, HGF, HSF, IFNB2, IL-6.

    Product # :

    CYT-1150

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    • SDS-PAGE

    Description

    IL6 Human Recombinant produced in Baculovirus is a single glycosylated polypeptide chain containing 189 amino acids (30-212aa) and having a molecular mass of 21.6kDa.(Migrates at 18-28kDa on SDS-PAGE under reducing conditions).IL6 is fused to a 6 amino acid His-Tag at C-terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    IL6 protein (0.5mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 10% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Biological Activity

    The ED50, determined by cell proliferation assay using TF-1 human erythroleukemic cell, is 0.2 - 0.8 ng/ml . 

    SDS-PAGE

    More Info

    • Introduction

      Interleukin-6 or Il-6 is a cytokine with a large assortment of biological functions. IL-6 it has a crucial part in the last differentiation of b-cells into ig-secreting cells. This cytokine also induces myeloma and plasmacytoma growth. Interleukin-6 induces nerve cells differentiation, among hepatocytes it induces acute phase reactants.

    • Synonyms

      BSF2, HGF, HSF, IFNB2, IL-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

      VPPGEDSKDV AAPHRQPLTS SERIDKQIRY ILDGISALRK ETCNKSNMCE SSKEALAENN
      LNLPKMAEKD GCFQSGFNEE TCLVKIITGL LEFEVYLEYL QNRFESSEEQ ARAVQMSTKV
      LIQFLQKKAK NLDAITTPDP TTNASLLTKL QAQNQWLQDM TTHLILRSFK EFLQSSLRAL RQMHHHHHH.

    • Background

      Production and Applications of Human Recombinant Interleukin-6 in Sf9 Cells

      Abstract:

      Interleukin-6 (IL-6) holds a central role in immune regulation, inflammation, and hematopoiesis. The production of Human Recombinant IL-6 using the Sf9 insect cell system presents a versatile approach for investigating its biological functions and potential therapeutic applications. This paper outlines the methodology of producing Human Recombinant IL-6 in Sf9 cells and explores its significance in immunological research and clinical studies.

      Introduction:

      IL-6 is a multifunctional cytokine pivotal in various physiological processes, making it a target of intensive research. The expression of Human Recombinant IL-6 facilitates investigations into its intricate mechanisms and offers potential avenues for therapeutic development. The Sf9 cell system, harnessed from Spodoptera frugiperda, enables efficient recombinant protein expression through baculovirus vectors.

      Methods:

      Production of Human Recombinant IL-6 involves cloning the human IL-6 gene into a baculovirus transfer vector, which is co-transfected with linearized baculovirus DNA into Sf9 cells. The resultant recombinant baculovirus generates and secretes IL-6 into the culture medium. Purification methods, such as chromatography, ensure the protein's quality and functionality.

      Applications:

      Human Recombinant IL-6 from Sf9 cells has broad applications. It serves as a critical tool for investigating IL-6's roles in immune responses, inflammation, and hematopoiesis. Additionally, it plays a crucial role in the development of therapies targeting IL-6-associated disorders like autoimmune diseases, chronic inflammatory conditions, and cancer.

      Sf9 Expression Advantages:

      The Sf9 system offers notable advantages, including post-translational modifications and protein folding, necessary for IL-6's biological activity. Sf9 cells provide a platform for generating properly folded and functional recombinant IL-6, reflecting its native structure and function.

      Challenges and Future Prospects:

      While Sf9-based expression of Human Recombinant IL-6 offers significant advantages, optimization of expression conditions and scale-up strategies remain challenges. Furthermore, the therapeutic potential of Human Recombinant IL-6 requires in-depth preclinical and clinical investigations.

      Conclusion:

      The production of Human Recombinant IL-6 in Sf9 cells through baculovirus expression offers a powerful tool to comprehend IL-6's multifaceted roles in health and disease. This technology is poised to expand our knowledge of IL-6-related conditions and catalyze the development of precision therapeutic interventions.

      What is the molecular weight/Mw of IL 6 HUMAN, SF9 Protein?
      IL 6 HUMAN, SF9 Protein has a total Mw of 21.6kDa.

      What is the source or expression system of IL 6 HUMAN, SF9 Protein?
      Sf9, Baculovirus cells.

      What is the Purity of IL 6 HUMAN, SF9 Protein?
      IL 6 HUMAN, SF9 Protein is >95% pure as determined by SDS-PAGE.

      What is the Biological Activity of IL 6 HUMAN, SF9 Protein?
      The ED50, determined by cell proliferation assay using TF-1 human erythroleukemic cell, is 0.2 - 0.8 ng/ml .

      What is the amino acid sequence of IL 6 HUMAN, SF9 Protein?
      VPPGEDSKDV AAPHRQPLTS SERIDKQIRY ILDGISALRK ETCNKSNMCE SSKEALAENN
      LNLPKMAEKD GCFQSGFNEE TCLVKIITGL LEFEVYLEYL QNRFESSEEQ ARAVQMSTKV
      LIQFLQKKAK NLDAITTPDP TTNASLLTKL QAQNQWLQDM TTHLILRSFK EFLQSSLRAL RQMHHHHHH.

      What applications can IL 6 HUMAN, SF9 Protein be used in?
      IL 6 HUMAN, SF9 Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for IL 6 HUMAN, SF9 Protein?
      The endotoxin level is minimal, IL 6 HUMAN, SF9 Protein was purified using conventional chromatography techniques.

      Who supplies recombinant IL 6 HUMAN, 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 IL 6 HUMAN, 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.

    Il6 Human
  • View Data Sheet

    Description:

    Interleukin-12 Human Recombinant

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

    Product # :

    CYT-101

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    Description

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

    Source

    HEK.

    Formulation

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

    Purity

    Greater than 95% as obsereved by SDS-PAGE.

    Biological Activity

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

    More Info

    • Introduction

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

    • Synonyms

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

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized IL-12 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IL12 should be stored at 4°C between 2-7 days and for future use below -18°C.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.

    • Solubility

      It is recommended to reconstitute the lyophilized IL12 in sterile PBS containing 0.1% endotoxin-free recombinant HSA.

    • Amino Acid Sequence

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

    • Background

      What is the molecular weight/Mw of IL12 HUMAN Protein?
      IL12 HUMAN Protein has a total Mw of 57kDa.

      What is the source or expression system of IL12 HUMAN Protein?
      HEK.

      What is the Purity of IL12 HUMAN Protein?
      IL12 HUMAN Protein is >95% pure as determined by SDS-PAGE.

      What is the Biological Activity of IL12 HUMAN Protein?
      The specific activity was determined by the dose-dependent release of IFN-gamma from the human NK92 cell line in presence of 20ng/mL rIL-2.
      The EC50 is 0.5ng/ml.
      What is the amino acid sequence of IL12 HUMAN Protein?
      IL-12 is a heterodimer of IL-12A and IL-12B linked through a disulfide-bond between cysteines in red in sequences below.
      >IL-12 A
      RNLPVATPDPGMFPCLHHSQNLLRAVSNMLQKARQTLEFYPCTSEEIDHEDITKDKTSTVEACLP
      LELTKNESCLNSRETSFITNGSCLASRKTSFMMALCLSSIYEDLKMYQVEFKTMNAKLLMDPKRQ
      IFLDQNMLAVIDELMQALNFNSETVPQKSSLEEPDFYKTKIKLCILLHAFRIRAVTIDRVMSYLNAS.
      >IL-12B
      IWELKKDVYVVELDWYPDAPGEMVVLTCDTPEEDGITWTLDQSSEVLGSGKTLTIQVKEFGDAG
      QYTCHKGGEVLSHSLLLLHKKEDGIWSTDILKDQKEPKNKTFLRCEAKNYSGRFTCWWLTTISTD
      LTFSVKSSRGSSDPQGVTCGAATLSAERVRGDNKEYEYSVECQEDSACPAAEESLPIEVMVDAV
      HKLKYENYTSSFFIRDIIKPDPPKNLQLKPLKNSRQVEVSWEYPDTWSTPHSYFSLTFCVQVQGK
      SKREKKDRVFTDKTSATVICRKNASISVRAQDRYYSSSWSEWASVPCS.

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

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

      Who supplies recombinant IL12 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 IL12 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 Human Hek
  • View Data Sheet

    Description:

    Interleukin-7, Mouse Anti-Human

    Lymphopoietin 1 (LP-1), pre-B cell factor, IL-7 TypeMouse Anti Human Monoclonal.

    Product # :

    ANT-110

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    Formulation

    1mg/ml in PBS (after reconstitution).

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    • Introduction

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

    • Synonyms

      Lymphopoietin 1 (LP-1), pre-B cell factor, IL-7 TypeMouse Anti Human Monoclonal.

    • Solubility

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

    • Immunogen

      r.Human IL-7.

    • Ig Subclass

      Mouse IgG1.

    • Clone

      NYRhIL7.

    • Applications

      Direct ELISA, Western Blot, Immuneprecipitation, Immunohistochemistry, Intracellular staining.

    • Titer

      By direct ELISA, 1:10,000 dilution will yield 0.3 O.D using alkaline phosphatase conjugated rabbit anti-mouse Ig (Jackson Laboratories).

    • Shipping Conditions

      Antibody is shipped lyophilized at ambient temperature.

    • Storage Procedures

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

    • 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 7 Antibody
  • View Data Sheet

    Description:

    Tumor Necrosis Factor-Alpha Mutant Human Recombinant

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

    Product # :

    CYT-384

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    Description

    Tumor Necrosis Factor-a Variant Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 151 amino acids and having a molecular mass of 16598 Dalton. The TNF-alpha Variant is purified by standard chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The protein was lyophilized after extensive dialysis against 0.5x PBS pH -7.

    Purity

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

    Biological Activity

    The ED50 as determined by the cytolysis of murine L929 cells in the presence of Actinomycin D is < 0.05ng/ml, corresponding to a Specific Activity of 20,000,000 units/mg.

    More Info

    • Introduction

      The clinical use of the potent anti-tumor activity of TNF-a has been limited by the proinflammatory side effects including fever, dose-limiting hypotension, hepatotoxicity, intravascular thrombosis, and hemorrhage. Designing clinically applicable TNF-a mutants with low systemic toxicity has been an intense pharmacological interest. Human TNF-a, which binds to the murine TNF-R55 but not to the mouse TNF-R75, exhibits retained anti-tumor activity and reduced systemic toxicity in mice compared with murine TNF-a, which binds to both murine TNF receptors. Based on these results, many TNF-? mutants that selectively bind to TNF-R55 have been designed. These mutants displayed cytotoxic activities on tumor cell lines in vitro, and exhibited lower systemic toxicity in vivo.
      Recombinant Human TNF-a Variant/Mutant compared with the wild-type, has an amino acid sequence deletion from a.a. 1-7, and the following a.a. substitutes Arg8, Lys9, Arg10 and Phe157 which is proven tohave more activity and with less inflammatory side effect in vivo.

    • Synonyms

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

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Solubility

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

    • Amino Acid Sequence

      MRKRKPVAHV VANPQAEGQL QWLNRRANAL LANGVELRDN
      QLVVPSEGLY LIYSQVLFKG QGCPSTHVLL THTISRIAVS YQTKVNLLSA IKSPCQRETP EGAEAKPWYE PIYLGGVFQL EKGDRLSAEI NRPDYLDFAE SGQVYFGIIAF.

    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.

    Tnf Alpha Mutant Human
  • View Data Sheet

    Description:

    Cytohesin 3 Human Recombinant

    Cytohesin 3, PSCD3, ARNO3, GRP1, PH SEC7 and Coiled-Coil Domain-Containing Protein 3 , Pleckstrin Homology Sec7 and Coiled-Coil Domains 3, General Receptor of Phosphoinositides 1 , ARF Nucleotide-Binding Site Opener 3 , Protein ARNO3 , Cytohesin-3, CYTH3.

    Product # :

    PRO-1951

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    Description

    CYTH3 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 422 amino acids (1-399) and having a molecular mass of 48.7 kDa.CYTH3 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    The CYTH3 solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 20% glycerol and 1mM DTT.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    More Info

    • Introduction

      Cytohesin 3 (CYTH3) belongs to the PSCD family, whose members have identical structural organization which consists of an N-terminal coiled-coil motif, a central Sec7 domain, and a C-terminal pleckstrin homology (PH) domain, and seem to mediate the regulation of protein sorting and membrane trafficking. CYTH3 is involved in the regulation of Golgi structure and function, and it might have a physiological role in regulating ADP-ribosylation factor protein 6 (ARF) functions, in addition to acting on ARF1.

    • Synonyms

      Cytohesin 3, PSCD3, ARNO3, GRP1, PH SEC7 and Coiled-Coil Domain-Containing Protein 3 , Pleckstrin Homology Sec7 and Coiled-Coil Domains 3, General Receptor of Phosphoinositides 1 , ARF Nucleotide-Binding Site Opener 3 , Protein ARNO3 , Cytohesin-3, CYTH3.

    • 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 MGSMDEDGGG EGGGVPEDLS LEEREELLDI RRRKKELIDD IERLKYEIAE VMTEIDNLTS VEESKTTQRN KQIAMGRKKF NMDPKKGIQF LIENDLLQSS PEDVAQFLYK GEGLNKTVIG DYLGERDEFN IKVLQAFVEL HEFADLNLVQ ALRQFLWSFR LPGEAQKIDR MMEAFASRYC LCNPGVFQST DTCYVLSFAI IMLNTSLHNH NVRDKPTAER FIAMNRGINE GGDLPEELLR NLYESIKNEP FKIPEDDGND LTHTFFNPDR EGWLLKLGGR VKTWKRRWFI LTDNCLYYFE YTTDKEPRGI IPLENLSIRE VEDPRKPNCF ELYNPSHKGQ VIKACKTEAD GRVVEGNHVV YRISAPSPEE KEEWMKSIKA SISRDPFYDM LATRKRRIAN KK.

    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.

    Cyth3 Human
  • View Data Sheet

    Description:

    Interleukin-4 Mouse Recombinant

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

    Product # :

    CYT-282

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    Description

    Interleukin-4 Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 120 amino acids and having a molecular mass of 13500 Dalton. The IL-4 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Lyophilized from a 0.2µm concentrated (1mg/ml) solution in PBS pH 7.4.

    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 the dose-dependant induction of HT-2 cell proliferation is less than 2 ng/ml corresponding to a Specific Activity of 500,000IU/mg.

    More Info

    • Introduction

      Interleukin-4 is a pleiotropic cytokine produced primarily by activated T lymphocytes, basophils and mast cells. Multiple immune response-modulating functions are performed by IL-4 on a variety of cell types and it has an important role in the regulator of isotype switching, induction of IgE production in B lymphocytes and differentiation of precursor T helper cells. IL-4 binds to both membrane-bound and secreted soluble IL-4 receptors.

    • 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 10mM HAc not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      MHIHGCDKNH LREIIGILNE VTGEGTPCTE MDVPNVLTAT KNTTESELVC RASKVLRIFY LKHGKTPCLK KNSSVLMELQ RLFRAFRCLD SSISCTMNES KSTSLKDFLE SLKSIMQMDY S.

    • Background

      What is the molecular weight/Mw of IL 4 MOUSE Protein?
      IL 4 MOUSE Protein has a total Mw of 13.5kDa.

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

      What is the Purity of IL 4 MOUSE Protein?
      IL 4 MOUSE Protein is >96% pure as determined by SDS-PAGE.

      What is the Biological Activity of IL 4 MOUSE Protein?
      The ED50 as determined by the dose-dependant induction of HT-2 cell proliferation is less than 2 ng/ml corresponding to a Specific Activity of 500,000IU/mg.

      What is the amino acid sequence of IL 4 MOUSE Protein?
      MHIHGCDKNH LREIIGILNE VTGEGTPCTE MDVPNVLTAT KNTTESELVC RASKVLRIFY LKHGKTPCLK KNSSVLMELQ RLFRAFRCLD SSISCTMNES KSTSLKDFLE SLKSIMQMDY S.

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

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

      Who supplies recombinant IL 4 MOUSE that is in stock and available to order?
      ProSpec has the protein in stock and available for immediate delivery.

      Where can I order bulk mg quantities of IL 4 MOUSE?
      ProSpec supplies bulk mg quantities at affordable prices that meets research and academic budgets.

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

    Il 4 Mouse
  • View Data Sheet

    Description:

    Sequestosome 1 Human Recombinant

    A170, OSIL, p60, p62, p62B, PDB3, ZIP3, EBIAP, ORCA, OSIL, SQSTM1.

    Product # :

    PRO-806

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    Description

    SQSTM1 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 364 amino acids (1-356 a.a.) and having a molecular mass of 39.7 kDa. SQSTM1 protein is fused to an 8 amino acid His-Tag at C-terminus and purified by standard chromatography.

    Source

    Escherichia Coli.

    Formulation

    SQSTM1 Human 0.5mg/ml solution containing 20mM Tris-HCl pH-8, 1mM DTT and 10% glycerol.

    Purity

    Greater than 85% as determined by SDS-PAGE.

    More Info

    • Introduction

      SQSTM1 is an adapter protein which binds ubiquitin and mediates the activation of NFKB1 by TNF-a, NGF and IL-1. SQSTM1 is involved in titin/TTN downstream signaling in muscle cells. SQSTM1 controls signaling cascades through ubiquitination. SQSTM1 participates in cell differentiation, apoptosis, immune response and regulation of K(+) channels. Mutations in UBA domain of the SQSTM1 protein cause Paget’s disease because the UBA is essential for aggregate sequestration and cell survival.

    • Synonyms

      A170, OSIL, p60, p62, p62B, PDB3, ZIP3, EBIAP, ORCA, OSIL, SQSTM1.

    • 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

      MAMSYVKDDI FRIYIKEKKE CRRDHRPPCA QEAPRNMVHP NVICDGCNGP VVGTRYKCSV CPDYDLCSVC EGKGLHRGHT KLAFPSPFGH LSEGFSHSRW LRKVKHGHFG WPGWEMGPPG NWSPRPPRAG EARPGPTAES ASGPSEDPSV NFLKNVGESV AAALSPLGIE VDIDVEHGGK RSRLTPVSPE SSSTEEKSSS QPSSCCSDPS KPGGNVEGAT QSLAEQMRKI ALESEGRPEE QMESDNCSGG DDDWTHLSSK EVDPSTGELQ SLQMPESEGP SSLDPSQEGP TGLKEAALYP HLPPEADPRL IESLSQMLSM GFSDEGGWLT RLLQTKNYDI GAALDTIQYS KHPPPLLEHH 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.

    Sqstm1 Human
  • View Data Sheet

    Description:

    Interleukin-1 beta Mouse Recombinant

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

    Product # :

    CYT-273

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    Description

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

    Source

    Escherichia Coli.

    Formulation

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

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Biological Activity

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

    More Info

    • Introduction

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

    • Synonyms

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

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized Interleukin-1b although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IL1b should be stored at 4°C between 2-7 days and for future use below -18°C.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.

    • Solubility

      It is recommended to reconstitute the lyophilized Interleukin-1b in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

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

    • Background

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

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

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

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

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

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

    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 Mouse
  • View Data Sheet

    Description:

    sFas Receptor Human Recombinant

    Tumor necrosis factor receptor superfamily member 6, Apo-1 antigen, Apoptosis-mediating surface antigen FAS, FASLG receptor, CD95, FAS, APT1, FAS1, APO-1, FASTM, ALPS1A, TNFRSF6.

    Product # :

    CYT-125

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    Description

    sFas Receptor Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 157 amino acids and having a molecular mass of 17.6kDa.The FAS is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    FAS protein was lyophilized from a 0.2µm filtered concentrated solution in 1×PBS, pH 7.4.

    Purity

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

    Biological Activity

    The ED50 was determined by its ability to inhibit the cytotoxicity of Jurkat cells is between 10-15 µg/ml in the presence of 2ng/ml of hFasL.

    More Info

    • Introduction

      Fas and Fas Ligand (FasL) are members of the TNF superfamily and are type I and type II transmembrane proteins, respectively. Binding of FasL to Fas initiates apoptosis in Fas-bearing cells. The apoptosis mechanism involves the recruitment of pro-caspase 8 through an adaptor molecule named FADD followed by processing of the pro-enzyme to active forms. These active caspases subsequently cleave a variety of cellular substrates leading to the eventual cell death. sFasR is able to inhibit FasL-induced apoptosis by acting as a decoy receptor whicht serves as a sink for FasL. The full length Fas Receptor is a 319 a.a type I transmembrane protein, which contains a 157 a.a extracellular domain, a 17 a.a transmembrane domain, and 145 a.a cytoplasmic domain. The mature human Fas ECD shares 55%, 58%, a.a sequence identity with the mouse, rat, Fas, respectively.

    • Synonyms

      Tumor necrosis factor receptor superfamily member 6, Apo-1 antigen, Apoptosis-mediating surface antigen FAS, FASLG receptor, CD95, FAS, APT1, FAS1, APO-1, FASTM, ALPS1A, TNFRSF6.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Amino Acid Sequence

      MRLSSKSVNA QVTDINSKGL ELRKTVTTVE TQNLEGLHHD GQFCHKPCPP GERKARDCTV NGDEPDCVPC QEGKEYTDKA HFSSKCRRCR LCDEGHGLEV EINCTRTQNT KCRCKPNFFC NSTVCEHCDP CTKCEHGIIK ECTLTSNTKC KEEGSRS.

    • Background

      What is the molecular weight/Mw of FAS Protein?
      FAS Protein has a total Mw of 17.6kDa.

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

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

      What is the Biological Activity of FAS Protein?
      The ED50 was determined by its ability to inhibit the cytotoxicity of Jurkat cells is between 10-15 µg/ml in the presence of 2ng/ml of hFasL.

      What is the amino acid sequence of FAS Protein?
      MRLSSKSVNA QVTDINSKGL ELRKTVTTVE TQNLEGLHHD GQFCHKPCPP GERKARDCTV NGDEPDCVPC QEGKEYTDKA HFSSKCRRCR LCDEGHGLEV EINCTRTQNT KCRCKPNFFC NSTVCEHCDP CTKCEHGIIK ECTLTSNTKC KEEGSRS.

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

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

    Fas Human
  • View Data Sheet

    Description:

    Marginal Zone B And B1 Cell-Specific Protein Human Recombinant

    Marginal Zone B and B1 Cell-Specific Protein, MZB1, PACAP, Mesenteric Oestrogen-Dependent Adipose Gene- 7, Plasma Cell-Induced ER Protein 1, Proapoptotic Caspase Adaptor Protein, Mesenteric Estrogen-Dependent Adipose 7, Plasma Cell-Induced Resident Endoplasmic Reticulum Protein, Plasma Cell-Induced Resident ER Protein, Proapoptotic Caspase Adapter Protein, MEDA-7, pERp1, HSPC190, Caspase-2 Binding Protein, Marginal Zone B- And B1-Cell-Specific Protein, MEDA7, MGC29506.

    Product # :

    PRO-608

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    Description

    MZB1 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 120 amino acids (1-97) and having a molecular mass of 12.9 kDa.MZB1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The MZB1 solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 10% glycerol and 1mM DTT.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Marginal zone B- and B1-cell-specific protein (MZB1) functions as a hormone-regulated adipokine/proinflammatory cytokine which is implicated in causing chronic inflammation and affecting cellular expansion. MZB1 links with immunoglobulin M (IgM) heavy and light chains and stimulate s IgM assembly and secretion. MZB1 exerts its effect by acting as a molecular chaperone or as an oxidoreductase as it exhibits a low level of oxidoreductase activity. MZB1 helps to diversify peripheral B-cell functions by regulating Ca(2+) stores, antibody secretion and integrin activation.

    • Synonyms

      Marginal Zone B and B1 Cell-Specific Protein, MZB1, PACAP, Mesenteric Oestrogen-Dependent Adipose Gene- 7, Plasma Cell-Induced ER Protein 1, Proapoptotic Caspase Adaptor Protein, Mesenteric Estrogen-Dependent Adipose 7, Plasma Cell-Induced Resident Endoplasmic Reticulum Protein, Plasma Cell-Induced Resident ER Protein, Proapoptotic Caspase Adapter Protein, MEDA-7, pERp1, HSPC190, Caspase-2 Binding Protein, Marginal Zone B- And B1-Cell-Specific Protein, MEDA7, MGC29506.

    • 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 MGSMPAELWL TSYGVREVDQ VKRLTGPGLS EGPEPSISVM VTGGPWPTRL SRTCLHYLGE FGEDQIYEAH QQGRGALEAL LCGGPQGACS EKVSATREEL.

    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.

    Mzb1 Human
  • View Data Sheet

    Description:

    Desert Hedgehog (C23II) Human Recombinant

    HHG-3, Desert Hedgehog homolog, MGC35145, Desert hedgehog protein, DHH.

    Product # :

    CYT-362

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    Description

    DHH (C23II) Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 177 amino acids and having a molecular mass of 19.9kDa. The DHH (C23II) is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

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

    Purity

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

    Biological Activity

    The Biological Activity was determined by its ability to induce alkaline phosphatase production by C3H/10T1/2 (CCL-226) cells. The expected ED50 for this effect is 15-45 μg/ml.

    More Info

    • Introduction

      DHH is part of the Hedgehog family which encodes signaling molecules that are involved in regulating morphogenesis. DHH protein is a precursor that is autocatalytically cleaved, the N-terminal portion is soluble and contains the signalling activity while the C-terminal portion is involved in precursor processing. Additionally, the C-terminal product covalently attaches a cholesterol moiety to the N-terminal product, restricting the N-terminal product to the cell surface and preventing it from freely diffusing throughout the organism. Defects in DHH protein have been associated with partial gonadal dysgenesis (PGD) accompanied by minifascicular polyneuropathy. DHH plays a role both male gonadal differentiation and perineurial development.
      DHH plays a role in intercellular signaling which is essential for a variety of patterning events during development. DHH functions as a spermatocyte survival factor in the testes & is essential for testes development.

    • Synonyms

      HHG-3, Desert Hedgehog homolog, MGC35145, Desert hedgehog protein, DHH.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized DHH (C23II) although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution DHH (C23II) 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 DHH (C23II) in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      IIGPGRGPVG RRRYARKQLV PLLYKQFVPG VPERTLGASG PAEGRVARGS ERFRDLVPNY NPDIIFKDEE NSGADRLMTE RCKERVNALA IAVMNMWPGV RLRVTEGWDE DGHHAQDSLH YEGRALDITT SDRDRNKYGL LARLAVEAGF DWVYYESRNH VHVSVKADNS LAVRAGG.

    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.

    Dhh C23Ii Human
  • View Data Sheet

    Description:

    Glia Maturation Factor Gamma Human Recombinant

    Glia maturation factor gamma, GMF-gamma, GMFG, MGC126867.

    Product # :

    CYT-632

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    • SDS-PAGE

    Description

    Glia Maturation Factor-Gamma (GMF-Gamma) Human Recombinant produced in E.Coli is a signle, non-glycosylated, polypeptide chain containing 142 amino acids and having a total molecular mass of 16.8 kDa. Glia Maturation Factor-Gamma, GMF-Gamma, Human Recombinant is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The GMF-gamma protein contains 20mM Tris-HCl pH-8, 1mM DTT, 1mM EDTA and 10% Glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    SDS-PAGE

    More Info

    • Introduction

      GMFG is a hematopoietic-specific protein that mediates the pluripotentiality and lineage commitment of human hematopoietic stem cells. Glia maturation factor gamma is a cytokine-responsive protein in EPO-induced and G-CSF-induced hematopoietic lineage development. Glia maturation factor also acts as a Nerve Growth Factor in nervous system development, angiogenesis and immune function. GMFG possesses hematopoietic tissue-specific gene expression, a promoter concentrated with high-score hematopoiesis-specific transcription factors, and molecular coevolution with a rudimentary blood/immune system.

    • Synonyms

      Glia maturation factor gamma, GMF-gamma, GMFG, MGC126867.

    • Physical Appearance

      Sterile Filtered colorless 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

      MSDSLVVCEV DPELTEKLRK FRFRKETDNA AIIMKVDKDR QMVVLEEEFQ NISPEELKME LPERQPRFVV YSYKYVHDDG RVSYPLCFIF SSPVGCKPEQ
      QMMYAGSKNR LVQTAELTKV FEIRTTDDLT EAWLQEKLSF FR.

    • Background

      What is the molecular weight/Mw of GMFG HUMAN Protein?
      GMFG HUMAN Protein has a total Mw of 16.8kDa.

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

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

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

      What is the amino acid sequence of GMFG HUMAN Protein?
      MSDSLVVCEV DPELTEKLRK FRFRKETDNA AIIMKVDKDR QMVVLEEEFQ NISPEELKME LPERQPRFVV YSYKYVHDDG RVSYPLCFIF SSPVGCKPEQ
      QMMYAGSKNR LVQTAELTKV FEIRTTDDLT EAWLQEKLSF FR.

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

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

    Gmfg Human
  • View Data Sheet

    Description:

    TNF Ligand Receptor Superfamily Member 25 Recombinant Human

    Tumor necrosis factor receptor superfamily member 25, TNFRSF25, TNF Ligand Receptor Superfamily Member 25, APO-3, DDR3, DR3, LARD, TNFRSF12, TR3, TRAMP, WSL-1, WSL-LR, Apo-3, Apoptosis-inducing receptor AIR, Protein WSL, Apoptosis-mediating receptor DR3, Apoptosis-mediating receptor TRAMP, Death receptor 3, Lymphocyte-associated receptor of death.

    Product # :

    CYT-980

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    Description

    TNFRSF25 Human Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 417 amino acids (25-199) and having a molecular mass of 46.1kDa (Molecular size on SDS-PAGE will appear at approximately 40-57kDa). TNFRSF25 is fused to a 242 amino acid IgG His-Tag at C-terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    TNFRSF25 protein solution (0.25mg/ml) containing Phosphate Buffered Saline (pH 7.4) and 10% glycerol.

    Purity

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

    Biological Activity

    Determined by the binding ability in a functional ELISA with Human VEGI (CAT# cyt-589). The ED50 range ≤ 5ug/ml.

    More Info

    • Introduction

      TNF Ligand Receptor Superfamily Member 25 (TNFRSF25) belongs to the TNF receptor superfamily that binds to the TNF-like protein TL1A. TNFRSF25 interacts directly with the adapter TRADD and regulates lymphocyte homeostasis. TNFRSF25 is also mediates activation of NF-kappa-B and induces apoptosis. TNFRSF25 signals are vital to exert T helper cell 2 effector activity in Th2-polarized CD4 cells and co-stimulate interleukin-13 production by glycosphingolipid-activated NKT cells.

    • Synonyms

      Tumor necrosis factor receptor superfamily member 25, TNFRSF25, TNF Ligand Receptor Superfamily Member 25, APO-3, DDR3, DR3, LARD, TNFRSF12, TR3, TRAMP, WSL-1, WSL-LR, Apo-3, Apoptosis-inducing receptor AIR, Protein WSL, Apoptosis-mediating receptor DR3, Apoptosis-mediating receptor TRAMP, Death receptor 3, Lymphocyte-associated receptor of death.

    • 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

      ADPQGGTRSP RCDCAGDFHK KIGLFCCRGC PAGHYLKAPC TEPCGNSTCL VCPQDTFLAW ENHHNSECAR CQACDEQASQ VALENCSAVA DTRCGCKPGW FVECQVSQCV SSSPFYCQPC LDCGALHRHT RLLCSRRDTD CGTCLPGFYE HGDGCVSCPT STLGSCPERC AAVCGWRQLE PKSCDKTHTC PPCPAPELLG GPSVFLFPPK PKDTLMISRT PEVTCVVVDV SHEDPEVKFN WYVDGVEVHN AKTKPREEQY NSTYRVVSVL TVLHQDWLNG KEYKCKVSNK ALPAPIEKTI SKAKGQPREP QVYTLPPSRD ELTKNQVSLT CLVKGFYPSD IAVEWESNGQ PENNYKTTPP VLDSDGSFFL YSKLTVDKSR WQQGNVFSCS VMHEALHNHY TQKSLSLSPG KHHHHHH.

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

    Tnfrsf25 Human
  • View Data Sheet

    Description:

    Melanotan-II

    Melanotan-II, MT-II, Melanotan.

    Product # :

    HOR-289

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    Description

    The molecular formula of Melanotan-II is C50H69N15O9. It has the amino acid sequence of Ac-Nle-cyclo [Asp-His-D-Phe-Arg-Trp-Lys]-NH2 and a molecular weight of 1024.2 Dalton. The CAS Number is 121062-08-6.

    Formulation

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

    Purity

    Greater than 99% as determined by by RP-HPLC.

    More Info

    • Introduction

      Melanotan and Melanotan-II are both analogs of the peptide hormone alpha melanocyte stimulating hormone (a-MSH) that tend to induce skin tanning. Unlike Melanotan, Melanotan-II has the additional effect of increasing libido. Melanotan II has aphrodisiac properties.

    • Synonyms

      Melanotan-II, MT-II, Melanotan.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Amino Acid Sequence

      Ac-Nle-cyclo [Asp-His-D-Phe-Arg-Trp-Lys]-NH2

    • Background

      What is the molecular weight/Mw of MELANOTAN Protein?
      MELANOTAN Protein has a total Mw of 1.024kDa.

      What is the Purity of MELANOTAN Protein?
      MELANOTAN Protein is >99% pure as determined by SDS-PAGE.

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

      What is the amino acid sequence of MELANOTAN Protein?
      Ac-Nle-cyclo [Asp-His-D-Phe-Arg-Trp-Lys]-NH2

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

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

      Who supplies MELANOTAN 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 MELANOTAN?
      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.

    Melanotan Ii
  • View Data Sheet

    Description:

    Interleukin-1 beta Porcine Recombinant

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

    Product # :

    CYT-400

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    Description

    Recombinant IL 1 beta Porcine produced in E.coli cells is a non-glycosylated, homodimeric protein containing 153 amino acid chain and having a molecular mass of 17.6kDa. The IL 1 beta is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The IL 1 beta was lyophilized from a 0.2µm filtered concentrated solution in PBS pH 7.4, containing 3 % 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 by a cell proliferation assay using murine D10S cells is less than 5.0 ng/ml, corresponding to a specific activity of > 2.0 × 105 IU/mg.

    More Info

    • Introduction

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

    • Synonyms

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

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized IL 1 beta although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IL 1 beta should be stored at 4°C between 2-7 days and for future use below -18°C.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.

    • Solubility

      It is recommended to reconstitute the lyophilized IL 1 beta in sterile distilled H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      ANVQSMECKL QDKDHKSLVL AGPHMLKALH LLTGDLKREV VFCMSFVQGD DSNNKIPVTL GIKGKNLYLS CVMKDNTPTL QLEDIDPKRY PKRDMEKRFV FYKTEIKNRV EFESALYPNW YISTSQAEQK PVFLGNSKGR QDITDFTMEV LSP

    • Background

      What is the molecular weight/Mw of IL1B PORCINE Protein?
      IL1B PORCINE Protein has a total Mw of 17.6kDa.

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

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

      What is the Biological Activity of IL1B PORCINE Protein?
      The ED50 as determined by a cell proliferation assay using murine D10S cells is less than 5.0 ng/ml, corresponding to a specific activity of > 2.0 × 105 IU/mg.

      What is the amino acid sequence of IL1B PORCINE Protein?
      ANVQSMECKL QDKDHKSLVL AGPHMLKALH LLTGDLKREV VFCMSFVQGD DSNNKIPVTL GIKGKNLYLS CVMKDNTPTL QLEDIDPKRY PKRDMEKRFV FYKTEIKNRV EFESALYPNW YISTSQAEQK PVFLGNSKGR QDITDFTMEV LSP.

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

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


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

    Il 1 Beta Porcine
  • View Data Sheet

    Description:

    Interleukin-1b, Mouse Anti-Human Biotin

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

    Product # :

    ANT-249

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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 Biotin
  • View Data Sheet

    Description:

    Interleukin-17 Receptor Alpha Human Recombinant

    Interleukin 17 Receptor A, IL-17 Receptor A, IL-17RA, CDw217, IL17R, Interleukin-17 Receptor A, Interleukin 17 Receptor, CD217 Antigen, HIL-17R, CANDF5, CD217, IMD51.

    Product # :

    CYT-1023

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    Description

    IL17RA Human Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 527 amino acids (33-320) and having a molecular mass of 60.4kDa (Molecular size on SDS-PAGE will appear at approximately 70-100kDa). IL17RA is fused to a 239 amino acids hIgG-His-Tag at C-terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    IL17RA protein solution (0.5mg/ml) containing Phosphate Buffered Saline (pH 7.4) and 10% glycerol.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    More Info

    • Introduction

      Interleukin-17 receptor A isoform 1 (IL17RA) is a cytokine receptor which binds interleukin 17. IL17RA is a potent inducer of the maturation of CD34-positive hematopoietic precursors into neutrophils. IL17RA is a type 1 membrane glycoprotein which binds with low affinity to interleukin 17A. The IL17RA protein and Interleukin 17A has a pathogenic role in many inflammatory and autoimmune diseases such as rheumatoid arthritis.

    • Synonyms

      Interleukin 17 Receptor A, IL-17 Receptor A, IL-17RA, CDw217, IL17R, Interleukin-17 Receptor A, Interleukin 17 Receptor, CD217 Antigen, HIL-17R, CANDF5, CD217, IMD51.

    • 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

      LRLLDHRALV CSQPGLNCTV KNSTCLDDSW IHPRNLTPSS PKDLQIQLHF AHTQQGDLFP VAHIEWTLQT DASILYLEGA ELSVLQLNTN ERLCVRFEFL SKLRHHHRRW RFTFSHFVVD PDQEYEVTVH HLPKPIPDGD PNHQSKNFLV PDCEHARMKV TTPCMSSGSL WDPNITVETL EAHQLRVSFT LWNESTHYQI LLTSFPHMEN HSCFEHMHHI PAPRPEEFHQ RSNVTLTLRN LKGCCRHQVQ IQPFFSSCLN DCLRHSATVS CPEMPDTPEP IPDYMPLWVE PKSCDKTHTC PPCPAPELLG GPSVFLFPPK PKDTLMISRT PEVTCVVVDV SHEDPEVKFN WYVDGVEVHN AKTKPREEQY NSTYRVVSVL TVLHQDWLNG KEYKCKVSNK ALPAPIEKTI SKAKGQPREP QVYTLPPSRD ELTKNQVSLT CLVKGFYPSD IAVEWESNGQ PENNYKTTPP VLDSDGSFFL YSKLTVDKSR WQQGNVFSCS VMHEALHNHY TQKSLSLSPG KHHHHHH.

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

    Il17Ra Human
  • View Data Sheet

    Description:

    Tumor Necrosis Factor-Alpha Human Recombinant

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

    Product # :

    CYT-223

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    Description

    Tumor Necrosis Factor-a Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 158 amino acids (157 a.a. of the mature human TNF-alpha and an N-terminal methionine) and having a molecular mass of 17.5kDa. The TNF-alpha is purified by standard chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    TNF-a Human was lyophilized from a concentrated 1mg/ml solution containing 20mM PB, pH-7.2, and 100mM NaCl.

    Purity

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

    Biological Activity

    The Specific Activity is >5.0×107 IU/mg as determined by the cytolysis of murine L929 cells in the presence of Actinomycin D.

    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, 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, INS resistance, and cancer.

    • Synonyms

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

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Amino Acid Sequence

      MVRSSSRTPS DKPVAHVVAN PQAEGQLQWL NRRANALLAN GVELRDNQLV VPSEGLYLIY SQVLFKGQGC PSTHVLLTHT ISRIAVSYQT KVNLLSAIKS PCQRETPEGA E AKPWYEPIY LGGVFQLEKG DRLSAEINRP DYLDFAESGQ VYFGIIAL.

    • Background

      TNF Alpha Human: An Overview of Its Role and Importance in Immunology

      TNF alpha human, also known as Tumor Necrosis Factor-alpha, is a critical cytokine in the immune system. Macrophages mainly produce this protein, and it plays a key role in inflammation and the acute phase reaction.

      This protein is involved in various cellular functions, including cell death, differentiation, proliferation, and immune regulation.

      Production and Properties

      Tumor Necrosis Factor-alpha is produced recombinantly in E. coli and consists of a single, non-glycosylated polypeptide chain. It includes 157 amino acids of the mature human TNF-alpha and an N-terminal methionine, resulting in a molecular mass of approximately 17.5 kDa.

      Furthermore, the protein is purified through standard chromatographic techniques to ensure high purity and biological activity.

      Solubility and Usage

      The lyophilized form of TNF appears as a sterile, white powder. It is recommended to reconstitute this powder in sterile water to achieve a solution of no less than 100µg/ml.

      This solution can then be further diluted for various experimental applications. TNF alpha is used extensively in research, particularly for studying its effects on cell signaling and immune response.

      Storage and Stability

      For long-term storage, TNF should be kept desiccated below -18°C. Once reconstituted, it should be used within a week if stored at 4°C or kept below -18°C for future use. Avoiding freeze-thaw cycles is crucial to maintain the protein's functionality.

      Biological Role and Implications

      TNF alpha human is involved in the regulation of immune cells and is known for its role in inflammatory processes.

      Dysregulation of TNF alpha production is linked to various diseases, such as autoimmune disorders, insulin resistance, and cancer. It is also a target for therapeutic interventions, particularly in conditions like rheumatoid arthritis and inflammatory bowel disease.

      Mechanism of Action

      TNF alpha can induce fever, apoptotic cell death, and can inhibit tumorigenesis and viral replication. Moreover, it is a potent mediator of the acute phase reaction, which influences the activity of various cells involved in systemic inflammation.

      Research and Clinical Importance

      Scientific research on TNF has provided insights into its complex role in disease mechanisms. Its interaction with receptors such as TNFRSF1A underscores its multifaceted effects across different organ systems, from liver function to brain activity.

      Ongoing studies continue to explore its therapeutic potential, especially how it can be modulated to treat diseases without harmful side effects.

      In essence, TNF alpha human is a versatile and powerful component of the immune system, important for both health and disease. Understanding its pathways and functions helps scientists develop better treatments for various inflammatory and autoimmune diseases.



    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.

    Tnf Alpha Human
  • View Data Sheet

    Description:

    CJC-1295 DAC

    Product # :

    HOR-065

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    Description

    CJC-1295 DAC is a synthetic single, non-glycosylated polypeptide chain containing 30 amino acids, having a molecular mass of 3647.18 Dalton and a Molecular formula of C165H269N47O46.

    Formulation

    The protein was lyophilized with no additives.

    Purity

    Greater than 97.0% as determined by analysis by RP-HPLC.

    More Info

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized CJC-1295 DAC although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution CJC-1295 DAC 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 CJC-1295 DAC in sterile 18MΩ-cm H2O not less than 100 µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      H-Tyr-D-Ala-Asp-Ala-Ile-PheThr-Gln-Ser-Tyr-Arg-Lys-Val-Leu-Ala-Gln-Leu-Ser-Ala-Arg-Lys-LeuLeu-Gln-Asp-Ile-Leu-Ser-Arg-Lys(Mal)-NH2.

    • Background

      CJC-1295 DAC owns a Drug Affinity Complex (DAC), which allows it to bind to serum albumin, extending its half-life to 6–8 days. CJC-1295 DAC normalizes growth and metabolism while maintaining natural hormone pulsatility.

    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.

    CJC-1295-DAC