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Search results

1000 results found for “Influenza”

Name

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  • View Data Sheet

    Name :

    ITGB3BP Human

    Description:

    Integrin Beta 3 Binding Protein Human Recombinant

    CENP-R, CENPR, HSU37139, NRIF3, TAP20, Centromere protein R, Beta-3-endonexin, Integrin beta-3-binding protein, Nuclear receptor-interacting factor 3, ITGB3BP.

    Product # :

    PRO-1435

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    Description

    ITGB3BP Human Recombinant produced in E. coli is a single polypeptide chain containing 239 amino acids (1-216) and having a molecular mass of 27.1kDa. ITGB3BP is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    The ITGB3BP solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.4M Urea and 10% glycerol.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      Integrin Beta 3 Binding Protein (ITGB3BP1) is a broadly expressed protein which contains a DD1 or RepD1 domain and an LXXLL motif. ITGB3BP1 functions as a nuclear receptor coactivator while induced by estrogen. ITGB3BP1 is also relates with the CENP-A-CAD complex that is engaged in mitotic progression, the assembly of kinetochore proteins and chromosome segregation. ITGB3BP1 behave s as a transcriptional corepressor via its interaction with the NFKB1 NF-kappa-B subunit by interfering with the transactivation domain of NFKB1.

    • Synonyms

      CENP-R, CENPR, HSU37139, NRIF3, TAP20, Centromere protein R, Beta-3-endonexin, Integrin beta-3-binding protein, Nuclear receptor-interacting factor 3, ITGB3BP.

    • 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 MGSMPFAPVA QARVQWHDFR SLQHLLPAFK RFSCLSLGSS WDYSVKRSLK LDGLLEENSF DPSKITRKKS VITYSPTTGT CQMSLFASPT SSEEQKHRNG LSNEKRKKLN HPSLTESKES TTKDNDEFMM LLSKVEKLSE EIMEIMQNLS SIQALEGSRE LENLIGISCA SHFLKREMQK TKELMTKVNK QKLFEKSTGL PHKASRHLDS YEFLKAILN.

    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.

    Itgb3Bp Human
  • View Data Sheet

    Name :

    PVR Human

    Description:

    Poliovirus Receptor Human Recombinant

    Poliovirus receptor, Nectin-like protein 5, NECL-5, CD155, PVR, PVS.

    Product # :

    PRO-2463

    Price :

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    Description

    PVR Human Recombinant produced in Sf9 Insect cells is a single, glycosylated polypeptide chain containing 331 amino acids (21-343 a.a.) and having a molecular mass of 36.1kDa (Molecular size on SDS-PAGE will appear at approximately 40-57kDa). PVR is expressed with an 8 amino acids His tag at C-Terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

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

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      Poliovirus receptor, also known as PVR, is a Type I transmembrane glycoprotein which belongs to the immunoglobulin superfamily. PVR catalyzes a big structural modification in the virus which exposes membrane-binding protein chains. PVR regulates helper T cell differentiation as well as allergic diseases. PVR is expressed in many kinds of human cells and has various functions. PVR is potentially functional as a biomarker for cancer development as well as progression. PVR takes a vital part through both immunological & non-immunological mechanisms in pancreatic cancer.

    • Synonyms

      Poliovirus receptor, Nectin-like protein 5, NECL-5, CD155, PVR, PVS.

    • 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

      WPPPGTGDVV VQAPTQVPGF LGDSVTLPCY LQVPNMEVTH VSQLTWARHG ESGSMAVFHQ TQGPSYSESK RLEFVAARLG AELRNASLRM FGLRVEDEGN YTCLFVTFPQ GSRSVDIWLR VLAKPQNTAE VQKVQLTGEP VPMARCVSTG GRPPAQITWH SDLGGMPNTS QVPGFLSGTV TVTSLWILVP SSQVDGKNVT CKVEHESFEK PQLLTVNLTV YYPPEVSISG YDNNWYLGQN EATLTCDARS NPEPTGYNWS TTMGPLPPFA VAQGAQLLIR PVDKPINTTL ICNVTNALGA RQAELTVQVK EGPPSEHSGM SRNLEHHHHH H

    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.

    Pvr Human
  • View Data Sheet

    Name :

    CXCL12 Feline beta

    Description:

    Stromal Cell-Derived Factor-1 beta Feline Recombinant (CXCL12)

    SDF-1, CXCL12, Pre-B cell growth-stimulating factor, PBSF, hIRH, chemokine (C-X-C motif) ligand 12, SDF1, SDF1B, TPAR1, SCYB12, SDF-1b, TLSF-b, 12-O-tetradecanoylphorbol 13-acetate repressed protein 1, Thymic lymphoma cell-stimulating factor, TLSF.

    Product # :

    CHM-247

    Price :

    Quantity :

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    Description

    Stromal Cell-Derived Factor-1 beta Feline Recombinant produced in E.Coli is a non-glycosylated, Polypeptide chain containing 72 amino acids and having a molecular mass of 8526 Dalton. The SDF-1b is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

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

    Purity

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

    Biological Activity

    The specific activity as determined by its ability to chemoattract human peripheral T cells stimulated with IL-2 and PHA in a concentration range from 10-75 ng/ml corresponding to a Specific Activity of 13,334-100,000IU/mg.

    Citations

    More Info

    • Introduction

      SDF-1 (stromal cell-derived factor-1) is small cytokine belonging to the chemokine family that is officially designated Chemokine (C-X-C motif) ligand 12 (CXCL12). It is produced in two forms, SDF-1?/CXCL12a and SDF-1?/CXCL12b, by alternate splicing of the same gene. Chemokines are characterized by the presence of four conserved cysteines, which form two disulfide bonds. The CXCL12 proteins belong to the group of CXC chemokines, whose initial pair of cysteines are separated by one intervening amino acid. CXCL12 is strongly chemotactic for lymphocytes and has been implicated as an important cell co-ordinator during development. During embryogenesis it directs the migration of hematopoietic cells from foetal liver to bone marrow. Mice which were knocked-out for CXCL12 gene were lethal before the birth or within just 1 hour of life. As another role, CXCL12a alters also the electrophysiology of neurons. CXCL12 was shown to be expressend in many tissues in mice (including brain, thymus, heart, lung, liver, kidney, spleen and bone marrow).
      The receptor for this chemokine is CXCR4, which was previously called fusin. This CXCL12-CXCR4 interaction used to be considered exclusive (unlike for other chemokines and their receptors), but recently it was suggested that CXCL12 is also bound by CXCR7 receptor.
      The gene for CXCL12 is located on human chromosome 10. In human and mouse both CXCL12 and CXCR4 show high identity of sequence: 99% and 90%, respectively.

    • Synonyms

      SDF-1, CXCL12, Pre-B cell growth-stimulating factor, PBSF, hIRH, chemokine (C-X-C motif) ligand 12, SDF1, SDF1B, TPAR1, SCYB12, SDF-1b, TLSF-b, 12-O-tetradecanoylphorbol 13-acetate repressed protein 1, Thymic lymphoma cell-stimulating factor, TLSF.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized SDF-1b although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution CXCL12 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 SDF-1b in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      KPVSLSYRCP CRFFESHVAR ANVKHLKILN TPNCALQIVA RLKNNNRQVC IDPKLKWIQE YLEKALNKRF KM.

    • Background

      What is the molecular weight/Mw of CXCL12 FELINE BETA Protein?
      CXCL12 FELINE BETA Protein has a total Mw of 8.5kDa.

      What is the source or expression system of CXCL12 FELINE BETA Protein?
      Escherichia Coli.

      What is the Purity of CXCL12 FELINE BETA Protein?
      CXCL12 FELINE BETA Protein is > 97% pure as determined by SDS-PAGE.

      What is the Biological Activity of CXCL12 FELINE BETA Protein?
      The specific activity as determined by its ability to chemoattract human peripheral T cells stimulated with IL-2 and PHA in a concentration range from 10-75 ng/ml corresponding to a Specific Activity of 13,334-100,000IU/mg.

      What is the amino acid sequence of CXCL12 FELINE BETA Protein?
      KPVSLSYRCP CRFFESHVAR ANVKHLKILN TPNCALQIVA RLKNNNRQVC IDPKLKWIQE YLEKALNKRF KM.

      What applications can CXCL12 FELINE BETA Protein be used in?
      CXCL12 FELINE BETA Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for CXCL12 FELINE BETA Protein?
      The endotoxin level is minimal, CXCL12 FELINE BETA Protein was purified using conventional chromatography techniques.

      Who supplies recombinant CXCL12 FELINE BETA 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 CXCL12 FELINE BETA?
      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.

    Cxcl12 Feline
  • View Data Sheet

    Name :

    IL1A Rat, His

    Description:

    Interleukin-1 alpha Rat Recombinant, His Tag

    Interleukin-1 alpha, IL-1 alpha.

    Product # :

    CYT-913

    Price :

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    Description

    IL 1 alpha Rat Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 179 amino acids (115-270 a.a) and having a molecular mass of 20.2kDa. IL 1 alpha is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    IL 1 alpha protein solution (1mg/ml) containing Phosphate Buffered Saline (pH 7.4) and 10% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Biological Activity

    The biological activity was Rat IL1 alpha was measured in a cell proliferation assay using D10.G4.1 mouse helper T cell. The ED50 for this effect is less or equal to 20 pg/ml.

    Citations

    More Info

    • Introduction

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

    • Synonyms

      Interleukin-1 alpha, IL-1 alpha.

    • Physical Appearance

      Sterile Filtered colorless solution.

    • Stability

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

    • Amino Acid Sequence

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

    • Background

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

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

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

      What is the Biological Activity of IL1A RAT, HIS Protein?
      The biological activity was Rat IL1 alpha was measured in a cell proliferation assay using D10.G4.1 mouse helper T cell. The ED50 for this effect is less or equal to 20 pg/ml.

      What is the amino acid sequence of IL1A RAT, HIS Protein?
      MGSSHHHHHH SSGLVPRGSH MGSSAPHSFQ NNLRYKLIRI VKQEFIMNDS LNQNIYVDMD RIHLKAASLN DLQLEVKFDM YAYSSGGDDS KYPVTLKVSN TQLFVSAQGE DKPVLLKEIP ETPKLITGSE TDLIFFWEKI NSKNYFTSAA FPELLIATKE QSQVHLARGL PSMIDFQIS.

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

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

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

    Il 1 Alpha Rat His
  • View Data Sheet

    Name :

    IL17 Human

    Description:

    Interleukin-17 Human Recombinant

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

    Product # :

    CYT-250

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    • Citations

    Description

    Interleukin-17A Human Recombinant produced in E.Coli is a homodimeric, non-glycosylated polypeptide chain containing a total of 264 amino acids (2 chains of 132 aa) and having a molecular mass of 31kDa. The IL-17 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Sterile filtered lyophilized (freeze-dried) powder, with 20mM Citrate, 0.1M NaCl, pH4.5.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Biological Activity

    The ED50 as determined by the dose-dependent induction of IL-6 in Hs68 cell line was found to be approximately 2ng/ml corresponding to a Specific Activity of 500,000IU/mg.

    sds-page

    IL17A Human SDS-PAGE - Product image 1

    Citations

    More Info

    • Introduction

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

    • Synonyms

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

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized Interleukin 17A although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IL17 should be stored at 4°C between 2-7 days and for future use below -18°C.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.

    • Solubility

      It is recommended to reconstitute the lyophilized Interleukin 17 in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Background

      What is the molecular weight/Mw of IL17 HUMAN Protein?
      IL17 HUMAN Protein has a total Mw of 31kDa.

      What is the source or expression system of IL17 HUMAN Protein?
      Escherichia Coli.

      What is the Purity of IL17 HUMAN Protein?
      IL17 HUMAN Protein is >95% pure as determined by SDS-PAGE.

      What is the Biological Activity of IL17 HUMAN Protein?
      The ED50 as determined by the dose-dependent induction of IL-6 in Hs68 cell line was found to be approximately 2ng/ml corresponding to a Specific Activity of 500,000IU/mg.

      What is the amino acid sequence of IL17 HUMAN Protein?
      IL17 HUMAN Protein is composed from 264 amino acids.

      What applications can IL17 HUMAN Protein be used in?
      IL17 HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for IL17 HUMAN Protein?
      The endotoxin level is minimal, IL17 HUMAN Protein was purified using conventional chromatography techniques.

      Who supplies recombinant IL17 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 IL17 HUMAN?
      ProSpec supplies bulk mg quantities at affordable prices that meets research and academic budgets.

    • Protein content

      Protein quantitation was carried out by two independent methods1. UV spectroscopy at 280 nm using the absorbency value of 1.13 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-17 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 17 Human
  • View Data Sheet

    Name :

    IL3 Human

    Description:

    Interleukin-3 Human Recombinant

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

    Product # :

    CYT-210

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    Description

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

    Source

    Escherichia Coli.

    Formulation

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

    Purity

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

    Biological Activity

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

    Citations

    More Info

    • Introduction

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

    • Synonyms

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

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized Interleukin-3 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IL3 should be stored at 4°C between 2-7 days and for future use below -18°C.Please prevent freeze-thaw cycles.

    • Solubility

      It is recommended to reconstitute the lyophilized Interleukin-3 in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

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

    • Background

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

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

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

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

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

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

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

      Who supplies recombinant IL3 HUMAN that is in stock and available to order?
      ProSpec has the protein in stock and available for immediate delivery.

      Where can I order bulk mg quantities of IL3 HUMAN?
      ProSpec supplies bulk mg quantities at affordable prices that meets research and academic budgets.

    • Protein content

      Protein quantitation was carried out by two independent methods:1. UV spectroscopy at 280 nm using the absorbency value of 0.84 as the extinction coefficient for a 0.1% (1mg/ml) solution. This value is calculated by the PC GENE computer analysis program of protein sequences (IntelliGenetics). 2. Analysis by RP-HPLC, using a standard solution of IL-3 as a Reference Standard.

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

    Il 3 Human
  • View Data Sheet

    Name :

    Interleukin 2r Antibody

    Description:

    Interleukin-2 Receptor (CD25), Rat Anti-Mouse

    CD25, IL2R, TCGFR, IL-2RA, sIL-2RA, TAC antigen, sIL-2R, IDDM10, p55.

    Product # :

    ANT-103

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    Formulation

    1mg/ml in PBS (after reconstitution).

    Citations

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    • Introduction

      IL2-Ra is one of the three constituent subunits of the IL2 receptor. IL-2Ra is released into the serum after increased cellular expression such as increased activation of B and T cells. Clinical manifestations of IL2-Ra elevation include autoimmune conditions and some leukemias and lymphomas.

    • Synonyms

      CD25, IL2R, TCGFR, IL-2RA, sIL-2RA, TAC antigen, sIL-2R, IDDM10, p55.

    • Solubility

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

    • Immunogen

      Con A-activated T cells.

    • Ig Subclass

      Rat IgG1.

    • Clone

      NYRmIL-2R.

    • Titer

      1:1,000 dilution will block T cell proliferation induced by specific Ag or concanavaline A. 10µl will stain 106 IL-R positive cells for FACS analysis.

    • Shipping Conditions

      Antibody is shipped lyophilized at ambient temperature.

    • Type

      Rat Anti Mouse 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 2R Mouse Antibody
  • View Data Sheet

    Name :

    ADSL Antibody

    Description:

    Adenylosuccinate Lyase, Mouse Anti Human

    Adenylosuccinate lyase, ASL, Adenylosuccinase, ASase, ADSL, AMPS.

    Product # :

    ANT-623

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    Formulation

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

    Citations

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    • Introduction

      Adenylosuccinate lyase (ADSL) is an enzyme which converts adenylosuccinate to AMP and fumarate as part of the purine nucleotide cycle. ADSL is involved in both de novo synthesis of purines and formation of adenosine monophosphate from inosine monophosphate. ADSL catalyzes 2 reactions in AMP biosynthesis: the removal of a fumarate from succinylaminoimidazole carboxamide (SAICA) ribotide to yield aminoimidazole carboxamide ribotide (AICA) and removal of fumarate from adenylosuccinate to yield AMP. Defects in the ADSL are the cause of adenylosuccinase deficiency (ADSL deficiency). ADSL deficiency is an autosomal recessive disorder distinguished by the accumulation in the body fluids of succinylaminoimidazole-carboxamide riboside (SAICA-riboside) and succinyladenosine (S-Ado). Adenylosuccinase deficiency results in succinylpurinemic autism, psychomotor retardation, and in some cases, growth retardation associated with muscle wasting and epilepsy.

    • Synonyms

      Adenylosuccinate lyase, ASL, Adenylosuccinase, ASase, ADSL, AMPS.

    • Physical Appearance

      Sterile filtered colorless solution.

    • Immunogen

      Anti-human ADSL mAb, is derived from hybridization of mouse F0 myeloma cells with spleen cells from BALB/c mice immunized with a recombinant human ADSL protein 1-484 amino acids purified from E. coli.

    • Ig Subclass

      Mouse IgG1 heavy chain and k light chain.

    • Clone

      PAT16C10AT.

    • Applications

      The antibody has been tested by ELISA, Western blot analysis, Flow cytometry and ICC/IF 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

      ADSL antibody was purified from mouse ascitic fluids 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.

    Adsl Antibody
  • View Data Sheet

    Name :

    LTA Antibody

    Description:

    Lymphotoxin-alpha, Mouse Anti Human

    Lymphotoxin-alpha, LT-alpha, TNF-beta, Tumor necrosis factor ligand superfamily member 1, LTA, TNFB, TNFSF1, LT.

    Product # :

    ANT-014

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    Formulation

    1mg/ml containing PBS, pH-7.4, & 0.1% Sodium Azide.

    Citations

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    • Introduction

      Lymphotoxin-alpha (LT-alpha or LTA) belongs to the TNF ligand superfamily, which bind the same TNF receptor and mediate similar pleiotropic effect. LTA is a proinflammatory cytokine with important biological activity and immunomodulatory function and is known to influence a variety of cellular response. Furthermore, LTA mediates a large variety of inflammatory, immunostimulatory, and antiviral responses, is involved in the formation of secondary lymphoid organs during development and has a role in apoptosis. LTA is highly inducible, secreted, and forms heterotrimers with lymphotoxin-beta which anchors lymphotoxin-alpha to the cell surface. LTA, which is located within the MHC III region of chromosome 6, shows close relation to the HLA class I (HLA-B) and class II (HLA-DR) genes. Polymorphism in the LTA gene appears to contribute to infectious disease susceptibility and infection. Genetic variations in the LTA gene are linked to susceptibility to leprosy type 4 and psoriatic arthritis.

    • Synonyms

      Lymphotoxin-alpha, LT-alpha, TNF-beta, Tumor necrosis factor ligand superfamily member 1, LTA, TNFB, TNFSF1, LT.

    • Physical Appearance

      Sterile Filtered clear solution.

    • Immunogen

      Anti-human LTA mAb, is derived from hybridization of mouse F0 myeloma cells with spleen cells from BALB/c mice immunized with recombinant human LTA amino acids 35-205 purified from E. coli.

    • Ig Subclass

      Mouse IgG2b heavy chain and ? light chain.

    • Clone

      PAT15A3AT.

    • Applications

      LTA antibody has been tested by ELISA, Western blot and Immunofluorescence 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 and Immunofluorescence is 1:250 ~ 500.
      Recommended starting dilution is 1:250.

    • 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

      LTA 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.

    Lta Antibody
  • View Data Sheet

    Name :

    ASF1A Human

    Description:

    ASF1 Anti-Silencing Function 1 Homolog A Human Recombinant

    CGI-98, HSPC146, DKFZp547E2110, ASF1A, Histone chaperone ASF1A, Anti-silencing function protein 1 homolog A, hAsf1, hAsf1a, CCG1-interacting factor A, CIA, hCIA.

    Product # :

    PRO-682

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    Description

    ASF1A Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 240 amino acids (1-204 a.a.) and having a molecular mass of 27kDa.ASF1A is fused to a 36 amino acid His Tag and purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The ASF1A protein solution contains 20mM Tris-HCl, pH-8, 1mM DTT and 10% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      ASF1A is part of the H3/H4 family of histone chaperone proteins corresponding to the anti-silencing function-1 gene in yeast. ASF1A is an important element of the histone donor complex that functions in nucleosome assembly. ASF1A interacts with histones H3 and H4, and functions together with a chromatin assembly factor during DNA replication and repair. Deletion of ASF1A in yeast and Drosophila confers sensitivity to various DNA damaging agents and inhibitors of DNA replication, increases genomic instability and sister chromatid exchange, and activates the DNA damage checkpoint.

    • Synonyms

      CGI-98, HSPC146, DKFZp547E2110, ASF1A, Histone chaperone ASF1A, Anti-silencing function protein 1 homolog A, hAsf1, hAsf1a, CCG1-interacting factor A, CIA, hCIA.

    • Physical Appearance

      Sterile filtered colorless solution.

    • Stability

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

    • Amino Acid Sequence

      MRGSHHHHHH GMASMTGGQQ MGRDLYDDDD KDRWGSMAKV QVNNVVVLDN PSPFYNPFQF EITFECIEDL SEDLEWKIIY VGSAESEEYD QVLDSVLVGP VPAGRHMFVF QADAPNPGLI PDADAVGVTV VLITCTYRGQ EFIRVGYYVN NEYTETELRE NPPVKPDFSK LQRNILASNPRVTRFHINWE DNTEKLEDAE SSNPNLQSLL STDALPSASK GWSTSENSLN VMLESHMDCM.

    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.

    Asf1A Human
  • View Data Sheet

    Name :

    PhI p 2

    Description:

    Pollen allergen Phl p 2 Recombinant

    Pollen allergen Phl p 2, Allergen Phl p II, Phl p 2, PHLPII.

    Product # :

    PRO-2306

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    Description

    Recombinant Pollen allergen Phl p 2 produced in SF9 is a glycosylated, polypeptide chain having a calculated molecular mass of 14,734 Dalton. PhI p 2 is expressed with a 10xHis tag at N-terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9 insect cells.

    Formulation

    PhI p 2 is supplied in 20mM HEPES buffer pH-7.9 and 6M Urea.

    Purity

    Greater than 80.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      Pollen allergen Phl p 2 (PhI p 2) causes an allergic reaction in humans.

    • Synonyms

      Pollen allergen Phl p 2, Allergen Phl p II, Phl p 2, PHLPII.

    • Physical Appearance

      Sterile Filtered clear solution.

    • Stability

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

    • Immunological Functions

      1. Binds IgE type human antibodies. 2. Immunodot test with positive/negative sera panels.

    • Molar extinction coefficient

      15470; A280(1mg/ml)=1.269

    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.

    Phi P 2
  • View Data Sheet

    Name :

    PhI p 5

    Description:

    Group V allergen Phl p 5.0203 Recombinant

    Group V allergen Phl p 5.0203, PhI p 5.

    Product # :

    PRO-2307

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    Description

    Recombinant Group V allergen Phl p 5.0203 produced in SF9 is a glycosylated, polypeptide chain having a calculated molecular mass of 27,582 Dalton. PhI p 5 is expressed with a 10xHis tag at N-terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9 insect cells.

    Formulation

    PhI p 5 is supplied in 20mM HEPES buffer pH-7.9 and 6M Urea.

    Purity

    Greater than 80.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      Group V allergen Phl p 5.0203 (PhI p 5) causes an allergic reaction in humans.

    • Synonyms

      Group V allergen Phl p 5.0203, PhI p 5.

    • Physical Appearance

      Sterile Filtered clear solution.

    • Stability

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

    • Immunological Functions

      1. Binds IgE type human antibodies. 2. Immunodot test with positive/negative sera panels.

    • Molar extinction coefficient

      11920; A280(1mg/ml)=0.432

    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.

    Phi P 5
  • View Data Sheet

    Name :

    Pen a 1.0101

    Description:

    Tropomyosin Pen a 1.0101 Recombinant

    Product # :

    ALR-024

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    Description

    Recombinant Tropomyosin Pen a 1.0101 produced in SF9 is a glycosylated, polypeptide chain having a calculated molecular mass of 38kDa.Pen a 1.0101 is expressed with a 10xHis tag and purified by proprietary chromatographic techniques.

    Source

    Sf9 insect cells.

    Formulation

    Pen a 1.0101 is supplied in 20mM HEPES buffer pH-7.9 200mM NaCl and 6M Urea.

    Purity

    Greater than 95% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      Pen a 1.0101 is a Tropomyosin and the only major allergen in brown shrimp Penaeus aztecus. The panallergen is highly conserved and soluble muscle protein. Pen a 1.0101 is has an alpha-helical homodimeric, coiled-coil structure.

    • 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.Avoid multiple freeze-thaw cycles.

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

    Pen A 10101
  • View Data Sheet

    Name :

    HSA, Sf9

    Description:

    Serum Albumin Human, Sf9

    Albumin, Cell Growth Inhibiting Protein 42, Growth-Inhibiting Protein 20, Albumin (32 AA), Albumin (AA 34), Serum Albumin, PRO0883, PRO0903, PRO1341, ANALBA, FDAH, HAS, ALB.

    Product # :

    PRO-2195

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    Description

    HSA produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain (19-609 a.a.) and fused to a 6 aa His Tag at C-terminus containing a total of 597 amino acids and having a molecular mass of 68kDa.HSA shows multiple bands between 50-70kDa on SDS-PAGE, reducing conditions and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

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

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    Citations

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    • Introduction

      Albumin is synthesized in the liver as preproalbumin which has an N-terminal peptide that is removed before the nascent protein is released from the rough endoplasmic reticulum. The product, proalbumin, is in turn cleaved in the Golgi vesicles to produce the secreted albumin. Albumin is a soluble, monomeric protein which comprises about one-half of the blood serum protein. Albumin functions primarily as a carrier protein for steroids, fatty acids, and thyroid hormones and plays a role in stabilizing extracellular fluid volume. Mutations in this gene on chromosome 4 result in various anomalous proteins. Albumin is a globular unglycosylated serum protein of molecular weight 65,000. The human albumin gene is 16,961 nucleotides long from the putative 'cap' site to the first poly (A) addition site. It is split into 15 exons which are symmetrically placed within the 3 domains that are thought to have arisen by triplication of a single primordial domain.
      HSA is widely used to stabilize blood volume generally from donors but the fear of contamination such as HIV & Hepatitis has enticed great interest in the recombinant form which is identical to the natural blood.

    • Synonyms

      Albumin, Cell Growth Inhibiting Protein 42, Growth-Inhibiting Protein 20, Albumin (32 AA), Albumin (AA 34), Serum Albumin, PRO0883, PRO0903, PRO1341, ANALBA, FDAH, HAS, ALB.

    • 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

      RGVFRRDAHK SEVAHRFKDL GEENFKALVL IAFAQYLQQC PFEDHVKLVN EVTEFAKTCV ADESAENCDK SLHTLFGDKL CTVATLRETY GEMADCCAKQ EPERNECFLQ HKDDNPNLPR LVRPEVDVMC TAFHDNEETF LKKYLYEIAR RHPYFYAPEL LFFAKRYKAA FTECCQAADK AACLLPKLDE LRDEGKASSA KQRLKCASLQ KFGERAFKAW AVARLSQRFP KAEFAEVSKL VTDLTKVHTE CCHGDLLECA DDRADLAKYI CENQDSISSK LKECCEKPLL EKSHCIAEVE NDEMPADLPS LAADFVESKD VCKNYAEAKD VFLGMFLYEY ARRHPDYSVV LLLRLAKTYE TTLEKCCAAA DPHECYAKVF DEFKPLVEEP QNLIKQNCEL FEQLGEYKFQ NALLVRYTKK VPQVSTPTLV EVSRNLGKVG SKCCKHPEAK RMPCAEDYLS VVLNQLCVLH EKTPVSDRVT KCCTESLVNR RPCFSALEVD ETYVPKEFNA ETFTFHADIC TLSEKERQIK KQTALVELVK HKPKATKEQL KAVMDDFAAF VEKCCKADDK ETCFAEEGKK LVAASQAALG LHHHHHH

    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.

    Hsa Sf9
  • View Data Sheet

    Name :

    CX3CL1 Human, His

    Description:

    Fractalkine Human Recombinant (CX3CL1), His Tag

    Fractalkine, CX3CL1, Neurotactin, CX3C membrane-anchored chemokine, Small inducible cytokine D1, NTN, NTT, CXC3, CXC3C, SCYD1, ABCD-3, C3Xkine.

    Product # :

    CHM-360

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    Description

    Fractalkine Human Recombinant fused with a 20 amino acid His tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 97 amino acids (25-100 a.a.) and having a molecular mass of 10.9kDa. The Fractalkine is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The Fractalkine solution (0.5 mg/ml) contains Phosphate Buffered Saline pH7.4 and 10% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    SDS-PAGE

    CX3CL1 Human, His-SDS-PAGE - Product image 1

    Citations

    More Info

    • Introduction

      Fractalkine soluble form is chemotactic for t-cells and monocytes, but not for neutrophils. Fractalkine membrane-bound form promotes adhesion of those leukocytes to endothelial cells. Fractalkine regulates leukocyte adhesion and migration processes at the endothelium and binds to CX3CR1. Natural Human Fractalkine is produced as a long protein (373-amino acid) with an extended mucin-like stalk and a chemokine domain on top. The mucin-like stalk permits it to bind to the cell surface. Fractalkine gene is located on human chromosome 16 along with some CC chemokines known as CCL17 and CCL22.

    • Synonyms

      Fractalkine, CX3CL1, Neurotactin, CX3C membrane-anchored chemokine, Small inducible cytokine D1, NTN, NTT, CXC3, CXC3C, SCYD1, ABCD-3, C3Xkine.

    • 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 MQHHGVTKCN ITCSKMTSKI PVALLIHYQQ NQASCGKRAI ILETRQHRLF CADPKEQWVK DAMQHLDRQA AALTRNG.

    • Background

      What is the molecular weight/Mw of CX3CL1 HUMAN, HIS Protein?
      CX3CL1 HUMAN, HIS Protein has a total Mw of 10.9kDa.

      What is the source or expression system of CX3CL1 HUMAN, HIS Protein?
      Escherichia Coli.

      What is the Purity of CX3CL1 HUMAN, HIS Protein?
      CX3CL1 HUMAN, HIS Protein is >90% pure as determined by SDS-PAGE.

      What is the Biological Activity of CX3CL1 HUMAN, HIS Protein?
      The biological functionality of CX3CL1 HUMAN, HIS Protein will be determined in the future.

      What is the amino acid sequence of CX3CL1 HUMAN, HIS Protein?
      MGSSHHHHHH SSGLVPRGSH MQHHGVTKCN ITCSKMTSKI PVALLIHYQQ NQASCGKRAI ILETRQHRLF CADPKEQWVK DAMQHLDRQA AALTRNG.

      What applications can CX3CL1 HUMAN, HIS Protein be used in?
      CX3CL1 HUMAN, HIS Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for CX3CL1 HUMAN, HIS Protein?
      The endotoxin level is minimal, CX3CL1 HUMAN, HIS Protein was purified using conventional chromatography techniques.

      Who supplies recombinant CX3CL1 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 CX3CL1 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.

    Fractalkine Human His
  • View Data Sheet

    Name :

    CIDEC Human

    Description:

    Cell Death-Inducing DFFA-Like Effector C Human Recombinant

    Cell Death-Inducing DFFA-Like Effector C, FSP27, CIDE3, FPLD5, Cell Death-Inducing DFFA-Like Effector Protein C, Fat-Specific Protein FSP27 Homolog, Cell Death Activator CIDE-3, Fat Specific Protein 27, CIDE-3, CIDEC.

    Product # :

    PRO-2026

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    Description

    CIDEC Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain (Glu2-Gln238) containing 247 amino acids including a 10 aa His tag at N-terminus. The total calculated molecular mass is 28kDa.

    Source

    Escherichia Coli.

    Formulation

    CIDEC filtered (0.4µm) solution at a concentration of 0.4mg/ml in 30mM acetate buffer and 10mM dithiothreitol, pH 4.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      Cell Death-Inducing DFFA-Like Effector C (CIDEC) belongs to the cell death-inducing DNA fragmentation factor-like effector family, whose members have significant roles in apoptosis. CIDEC is expressed mainly in adipocytes, intestine, heart, stomach, and weakly in the brain, kidney and liver. CIDEC overexpression in preadipocytes induces apoptosis. CIDEC regulates enlargement of lipid droplets.

    • Synonyms

      Cell Death-Inducing DFFA-Like Effector C, FSP27, CIDE3, FPLD5, Cell Death-Inducing DFFA-Like Effector Protein C, Fat-Specific Protein FSP27 Homolog, Cell Death Activator CIDE-3, Fat Specific Protein 27, CIDE-3, CIDEC.

    • Physical Appearance

      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

      MKHHHHHHASEYAMKSLSLL YPKSLSRHVS VRTSVVTQQL LSEPSPKAPR ARPCRVSTAD RSVRKGIMAY SLEDLLLKVR DTLMLADKPF FLVLEEDGTT VETEEYFQAL AGDTVFMVLQ KGQKWQPPSE QGTRHPLSLS HKPAKKIDVA RVTFDLYKLN PQDFIGCLNV KATFYDTYSL SYDLHCCGAK RIMKEAFRWA LFSMQATGHV LLGTSCYLQQ LLDATEEGQP PKGKASSLIP TCLKILQ.

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    Cidec Human
  • View Data Sheet

    Name :

    HIV-1 Polyvalent

    Description:

    HIV-1 Polyvalent Recombinant

    Product # :

    HIV-017

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    Description

    Polyvalent HIV1 antigens contain HIV1 gp41 (long sequence) and new discovered HIV1 protein P30 from HIV1 genome.

    Source

    Escherichia Coli.

    Formulation

    HIV-1 Polyvalent solution contains 25mM K2₂CO₃ & PBS.

    Purity

    Protein is >95% pure as determined by 10% PAGE (coomassie staining).

    Citations

    More Info

    • 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.

    • Applications

      Immunoassay.

    • Background

      The Human Immunodeficiency Virus type 1 (HIV-1) continues to pose a global health challenge, with millions of individuals affected by the virus. The development of an effective HIV vaccine has been a long-standing goal in the field of virology and immunology. One promising approach is the use of polyvalent HIV-1 recombinant vaccines, which aim to target multiple viral strains and epitopes simultaneously. This research delves into the concept of polyvalent HIV-1 vaccines, shedding light on their potential to provide broad and robust protection against HIV-1 infection.

      The primary objective of this research is to explore the rationale behind polyvalent HIV-1 vaccines. HIV-1 exhibits extensive genetic diversity, with multiple subtypes and circulating recombinant forms (CRFs) worldwide. Polyvalent vaccines are designed to encompass a range of viral strains, ensuring coverage against various subtypes and epitope variants. Understanding the genetic diversity of HIV-1 and the importance of polyvalent approaches is fundamental for vaccine design.

      The second objective is to investigate the immunological mechanisms underlying polyvalent HIV-1 vaccines. In vitro and in vivo studies will be conducted to assess the ability of polyvalent vaccines to induce broad and cross-reactive immune responses. This includes investigations into the generation of neutralizing antibodies, cytotoxic T lymphocyte (CTL) responses, and mucosal immunity. These studies aim to elucidate the key immune correlates of protection conferred by polyvalent vaccines.

      The third objective is to assess the clinical potential of polyvalent HIV-1 recombinant vaccines. Clinical trials involving diverse populations at risk of HIV-1 infection will be conducted to evaluate the safety, immunogenicity, and efficacy of polyvalent vaccine candidates. These trials may provide crucial insights into the feasibility and effectiveness of polyvalent vaccine strategies in real-world settings.

      By delving into the concept of polyvalent HIV-1 recombinant vaccines, this research aims to contribute to the ongoing efforts to develop a successful HIV vaccine. The findings may provide a pathway towards a vaccine that can offer comprehensive protection against the diverse array of HIV-1 strains, bringing us closer to ending the HIV/AIDS pandemic.

    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 Polyvalent
  • View Data Sheet

    Name :

    HSV-1 gD (84-175)

    Description:

    Herpes Simplex Virus-1 gD (84-175 a.a.) Recombinant

    Product # :

    HSV-231

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    Description

    The E.Coli derived recombinant protein contains the HSV-1 gD (84-175) immunodominant region.

    Source

    Escherichia Coli.

    Formulation

    0.1 % SDS, 50% glycerol and 100 mM NaCl.

    Purity

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

    Citations

    More Info

    • Introduction

      Receptors across the cell membrane interact with some viral glycoproteins therefor enabling HSV to enter the host cell. The HSV enter through pores created by the binding of particular receptors across the cell membrane with the virus's coating envelope, following by a fusion of the HSV and the host cell. HSV enters the host cell through the same mechanism and stages as other viruses do. Initially, matching receptors across the virus's envelope and host cell's membrane interacts and bring the two together. During the transitional stage, begins fusion between the host cell and virus (hemifusion state). The closing stage happens when a steady pore was made; through these pores the virus's particles enter the cell.

    • Physical Appearance

      Sterile Filtered clear solution.

    • Stability

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

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

    Hsv1 Gd
  • View Data Sheet

    Name :

    IL1B Mouse, His

    Description:

    Interleukin-1 beta Mouse Recombinant, His Tag

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

    Product # :

    CYT-578

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    Description

    Interleukin-1 beta Mouse Recombinant produced in E.Coli is a non-glycosylated, Polypeptide chain containing 189 amino acids and having a molecular mass of 21 kDa. The IL-1b is fused to His-Tag and purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The IL-1B protein contains 20mM Tris pH-8 and 10% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    Citations

    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. IL-1b is an inflammatory cytokine which modulates angiogenesis by interacting directly with vascular endothelial cells & increasing the production of proangiogenic factors through paracrine control. IL-1 beta stimulates endothelial cell migration and proliferation, adhesion-molecule expression, inflammatory mediator production, and leukocyte recruitment. IL1B is essential for tumor growth, metastasis, and angiogenesis in quite a few animal models.

    • Synonyms

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

    • Physical Appearance

      Sterile Filtered colorless solution.

    • Stability

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

    • Amino Acid Sequence

      MRGSHHHHHH GMASMTGGQQ MGRDLYDDDD KDRWGSMVPI RQLHYRLRDE QQKSLVLSDP YELKALHLNG QNINQQVIFS MSFVQGEPSN DKIPVALGLK GKNLYLSCVM KDGTPTLQLE SVDPKQYPKK KMEKRFVFNK IEVKSKVEFE SAEFPNWYIS TSQAEHKPVF LGNNSGQDII DFTMESVSS.

    • Background

      What is the molecular weight/Mw of IL1B MOUSE, HIS Protein?
      IL1B MOUSE, HIS Protein has a total Mw of 21kDa.

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

      What is the Purity of IL1B MOUSE, HIS Protein?
      IL1B MOUSE, HIS Protein is >90% pure as determined by SDS-PAGE.

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

      What is the amino acid sequence of IL1B MOUSE, HIS Protein?
      MRGSHHHHHH GMASMTGGQQ MGRDLYDDDD KDRWGSMVPI RQLHYRLRDE QQKSLVLSDP YELKALHLNG QNINQQVIFS MSFVQGEPSN DKIPVALGLK GKNLYLSCVM KDGTPTLQLE SVDPKQYPKK KMEKRFVFNK IEVKSKVEFE SAEFPNWYIS TSQAEHKPVF LGNNSGQDII DFTMESVSS.

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

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


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

    Il 1 Beta Mouse His
  • View Data Sheet

    Name :

    IL3 Mouse

    Description:

    Interleukin-3 Mouse Recombinant

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

    Product # :

    CYT-371

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    Description

    Interleukin-3 mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 135 amino acids and having a molecular mass of 15100 Dalton. The IL-3 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

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

    Purity

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

    Biological Activity

    The ED50 as determined by the dose-dependant stimulation of murine M-NFS-60 cells is < 0.05 ng/ml, corresponding to a Specific Activity of 20,000,000IU/mg.

    Citations

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    • 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

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

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Amino Acid Sequence

      The sequence of the first five N-terminal amino acids was determined and was found to be Met-Asp-Thr-His-Arg.

    • Background

      What is the molecular weight/Mw of IL3 MOUSE Protein?
      IL3 MOUSE Protein has a total Mw of 15.1kDa.

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

      What is the Purity of IL3 MOUSE Protein?
      IL3 MOUSE Protein is >97% pure as determined by SDS-PAGE.

      What is the Biological Activity of IL3 MOUSE Protein?
      The ED50 as determined by the dose-dependant stimulation of murine M-NFS-60 cells is < 0.05 ng/ml, corresponding to a Specific Activity of 20,000,000IU/mg.

      What is the amino acid sequence of IL3 MOUSE Protein?
      The sequence of the first five N-terminal amino acids was determined and was found to be Met-Asp-Thr-His-Arg.

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

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

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

    • Protein content

      Protein quantitation was carried out by two independent methods1. UV spectroscopy at 280 nm using the absorbency value of 0.154 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 IL3 as a Reference Standard.

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

    Il 3 Mouse
  • View Data Sheet

    Name :

    Malaria Pf. MSP1

    Description:

    Malaria Falciparum MSP1 Recombinant

    Product # :

    MAL-004

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    Description

    Merozoite surface antigen is a protein located on the outside of the merozoite, playing an imperative role in immune reaction. About 55% cases of malaria are infected by Plasmodium falciparum (Pf). Pf MSP1 has to be used with Plasmodium vivax (Pv) together for ELISA and rapid diagnostic test, Plasmodium falciparum and vivax infection takes about 95% of Plasmodium caused infection. Recombinant Malaria Falciparum MSP1 produced in E.coli, is a 62kDa protein fused to a GST tag at N-terminus and purified by proprietary chromatographic technique.

    Formulation

    Sterile Filtered solution containing PBS and 25mM K2CO3.

    Purity

    Protein is >90% pure as determined by 10% PAGE (coomassie staining).

    Citations

    More Info

    • Introduction

      Plasmodium falciparum is a protozoan parasite, one of the species of Plasmodium that cause malaria. Malaria parasites are members of the Apicomplexa. Apicomplexa are characterized by a set of organelles found in some stages of the parasite's life cycle. These organelles, collectively known as apical organelles because of their localization at one end of the parasite, are involved in interactions between the parasite and host. In particular, the apical organelles have been implicated in the process of host cell invasion. In the case of Plasmodium, three distinct invasive forms have been identified: sporozoite, merozoite, and ookinete.

    • Physical Appearance

      Sterile Filtered clear solution.

    • Stability

      Pf. MSP1 although stable at 4°C for 1 week, should be stored below -18°C. Please prevent freeze thaw cycles.

    • Applications

      Rapid test and Immunoassay.

    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.

    Malaria Pf Msp1
  • View Data Sheet

    Name :

    IL 21 Rat

    Description:

    Interleukin-21 Rat Recombinant

    Interleukin-21, IL-21, Il21.

    Product # :

    CYT-033

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    Description

    Interleukin-21 Rat Recombinant produced in E.Coli is a single, non-glycosilated polypeptide chain containing 129 amino acids and having a total molecular mass of 15.2kDa. The Rat IL-21 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Rat IL-21 was lyophilized from a 0.2µm filtered concentrated solution in 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 is measured by its ability to proliferate activated B cells.

    Citations

    More Info

    • Introduction

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

    • Synonyms

      Interleukin-21, IL-21, Il21.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized Rat IL-21 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Rat IL21 should be stored at 4°C between 2-7 days and for future use below -18°C. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.

    • Solubility

      It is recommended to reconstitute the lyophilized Rat IL21 in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      HKSSPQRPDH LLIRLRHLMD IVEQLKIYEN DLDPELLTAP QDVKGQCEHE AFACFQKAKL KPSNTGNNKT FINDLLAQLR RRLPAKRTGN KQRHMAKCPS CDLYEKKTPK EFLERLKWLL QKMIHQHLS.

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    Il 21 Rat
  • View Data Sheet

    Name :

    IL36G 152 a.a. Human

    Description:

    Interleukin-36 Gamma (152 a.a) Human Recombinant

    Interleukin 36 gamma, IL1F9, interleukin 1 family member 9, Interleukin-1 epsilon, IL-1RP2, IL-1H1, IL1E, interleukin 1-related protein 2, Interleukin-1 homolog 1.

    Product # :

    CYT-161

    Price :

    Quantity :

    Shipping Method :

    Room Temp Icon

    Shipped at Room temp

    Add To Cart

    More Info

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

    Description

    IL36G (152 a.a.) Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 152 amino acids and having a molecular mass of 17.0kDa.The IL36G (152 a.a.) is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Lyophilized from a 0.2µm filtered concentrated solution in 1×PBS, pH 7.4, containing 5% trehalose.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    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 15ng/ml, corresponding to a Specific Activity of 67,000 IU/mg.

    Citations

    More Info

    • Introduction

      IL-36gamma belongs to the IL-1 family which includes IL-1b, IL-1a, IL-1ra, IL-18, IL-36 Ra (IL-1F5), IL-36a (IL-1F6), IL-36b (IL-1F8), IL-37 (IL-1F7) and 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-36g is an 18-22 kDa, 169aa intracellular and secreted protein which holds no signal sequence, no prosegment and no potential N-linked glycosylation sites. Human IL-36g shares 58%- 69% aa sequence homology with mouse, rat, bovine and equine IL-36g, and 23 - 57% aa sequence homology with other family members. The IL-36g receptor is a mixture of IL-1 Rrp2, mostly located in epithelia and keratinocytes, and the extensively expressed IL-1 RAcP. All IL-36 (a, b and g) activate N F-?B and MAPK pathways in an IL-1 Rrp2 dependent reaction. Additionally, IL-36g induces production of inflammatory cytokines and chemokines like CXCL8/IL-8.

    • Synonyms

      Interleukin 36 gamma, IL1F9, interleukin 1 family member 9, Interleukin-1 epsilon, IL-1RP2, IL-1H1, IL1E, interleukin 1-related protein 2, Interleukin-1 homolog 1.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized IL36g Human although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IL36g 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 IL36g in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      SMCKPITGTI NDLNQQVWTL QGQNLVAVPR SDSVTPVTVA VITCKYPEAL EQGRGDPIYL GIQNPEMCLY CEKVGEQPTL QLKEQKIMDL YGQPEPVKPF LFYRAKTGRT STLESVAFPD WFIASSKRDQ PIILTSELGK SYNTAFELNI ND

    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.

    Il36G 152 Aa Human
  • View Data Sheet

    Name :

    IL4 Human, Yeast

    Description:

    Interleukin 4 Human Recombinant, Yeast

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

    Product # :

    CYT-712

    Price :

    Quantity :

    Shipping Method :

    Room Temp Icon

    Shipped at Room temp

    Add To Cart

    More Info

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

    Description

    Interleukin-4 Human Recombinant produced in yeast is a single, glycosylated polypeptide chain containing 129 amino acids.The IL-4 is purified by proprietary chromatographic techniques.

    Source

    Pichia pastoris.

    Formulation

    The protein was lyophilized from 0.2µm filtered solution in 20mM sodium phosphate buffer pH 6.0 in absence of any carrier protein.

    Purity

    Greater than 98% as determined by SDS-PAGE.

    Biological Activity

    The biological activity is determined by measuring the dose-dependent proliferation of human TF–1 cells and CD23 expression. A concentration range of 0.1–10.0 ng/ml is effective for most in vitro applications. ED50 = 0.05–0.4ng/ml.

    Citations

    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 Interleukin-4 should be stored at 4°C between 2-7 days and for future use below -18°C. Please prevent freeze-thaw cycles.

    • Solubility

      It is recommended to reconstitute the lyophilized Interleukin-4 in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Background

      What is the source or expression system of IL 4 HUMAN, YEAST Protein?
      Pichia pastoris.

      What is the Purity of IL 4 HUMAN, YEAST Protein?
      IL 4 HUMAN, YEAST Protein is >98% pure as determined by SDS-PAGE.

      What is the Biological Activity of IL 4 HUMAN, YEAST Protein?
      The biological activity is determined by measuring the dose-dependent proliferation of human TF–1 cells and CD23 expression. A concentration range of 0.1–10.0 ng/ml is effective for most in vitro applications. ED50 = 0.05–0.4ng/ml.

      What is the amino acid sequence of IL 4 HUMAN, YEAST Protein?
      IL 4 HUMAN, YEAST Protein is composed from 129 amino acids.

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

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

      Who supplies recombinant IL 4 HUMAN, YEAST 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 HUMAN, YEAST?
      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 Human Yeast
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