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  • View Data Sheet

    Description:

    Cytotoxic T-Lymphocyte Associated Antigen-4 Human Recombinant, igG-His Tag

    CTLA4, ALPS5, CD, CD152, CELIAC3, CTLA-4, GRD4, GSE, IDDM12, CD152, Cytotoxic T-Lymphocyte Associated Antigen-4, igG-His Tag.

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    CYT-985

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    Description

    CTLA4 produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 368 amino acids (36-161a.a.) and having a molecular mass of 40.8kDa (Molecular size on SDS-PAGE will appear at approximately 40-57kDa). CTLA4 is expressed with a 239 amino acid hIgG-His-tag at C-Terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    CTLA4 protein solution (0.5mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 10% glycerol.

    Purity

    Greater than 95% as determined by SDS-PAGE.

    More Info

    • Introduction

      CTLA-4 is a member of the immunoglobulin superfamily and encodes a protein which transmits an inhibitory signal to T cells. The protein contains a V domain, a transmembrane domain, and a cytoplasmic tail. Alternate transcriptional splice variants, encoding different isoforms, have been characterized. The membrane-bound isoform functions as a homodimer interconnected by a disulfide bond, while the soluble isoform functions as a monomer. Mutations in this gene have been associated with insulin-dependent diabetes mellitus, Graves disease, Hashimoto thyroiditis, celiac disease, systemic lupus erythematosus, thyroid-associated orbitopathy, and other autoimmune diseases.

    • Synonyms

      CTLA4, ALPS5, CD, CD152, CELIAC3, CTLA-4, GRD4, GSE, IDDM12, CD152, Cytotoxic T-Lymphocyte Associated Antigen-4, igG-His Tag.

    • 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

      ADLKAMHVAQ PAVVLASSRG IASFVCEYAS PGKATEVRVT VLRQADSQVT EVCAATYMMG NELTFLDDSI CTGTSSGNQV NLTIQGLRAM DTGLYICKVE LMYPPPYYLG IGNGTQIYVI DPEPCPDSDL EPKSCDKTHT CPPCPAPELL GGPSVFLFPP KPKDTLMISR TPEVTCVVVD VSHEDPEVKF NWYVDGVEVH NAKTKPREEQ YNSTYRVVSV LTVLHQDWLN GKEYKCKVSN KALPAPIEKT ISKAKGQPRE PQVYTLPPSR DELTKNQVSL TCLVKGFYPS DIAVEWESNG QPENNYKTTP PVLDSDGSFF LYSKLTVDKS RWQQGNVFSC SVMHEALHNH YTQKSLSLSP GKHHHHHH.

    • Background

      What is the molecular weight/Mw of CTLA4 Protein?
      CTLA4 Protein has a total Mw of 40.8kDa.

      What is the source or expression system of CTLA4 Protein?
      Sf9, Baculovirus cells.

      What is the Purity of CTLA4 Protein?
      CTLA4 Protein is >95% pure as determined by SDS-PAGE.

      What is the Biological Activity of CTLA4 Protein?
      The biological functionality of CTLA4 Protein will be determined in the future.

      What is the amino acid sequence of CTLA4 Protein?
      ADLKAMHVAQ PAVVLASSRG IASFVCEYAS PGKATEVRVT VLRQADSQVT EVCAATYMMG NELTFLDDSI CTGTSSGNQV NLTIQGLRAM DTGLYICKVE LMYPPPYYLG IGNGTQIYVI DPEPCPDSDL EPKSCDKTHT CPPCPAPELL GGPSVFLFPP KPKDTLMISR TPEVTCVVVD VSHEDPEVKF NWYVDGVEVH NAKTKPREEQ YNSTYRVVSV LTVLHQDWLN GKEYKCKVSN KALPAPIEKT ISKAKGQPRE PQVYTLPPSR DELTKNQVSL TCLVKGFYPS DIAVEWESNG QPENNYKTTP PVLDSDGSFF LYSKLTVDKS RWQQGNVFSC SVMHEALHNH YTQKSLSLSP GKHHHHHH.

      What applications can CTLA4 Protein be used in?
      CTLA4 Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for CTLA4 Protein?
      The endotoxin level is minimal, CTLA4 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.

    Ctla4 Human Igg His
  • View Data Sheet

    Description:

    Brain-Derived Neurotrophic Factor Human Recombinant

    Brain-Derived Neurotrophic Factor, BDNF, MGC34632.

    Product # :

    CYT-207

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    • Activity

    Description

    BDNF Human Recombinant produced in E.Coli is a homodimer, non-glycosylated, polypeptide chain containing 2 x 119 amino acids (and an N-terminal Met) and having a total molecular mass of 28kDa. BDNF Human Recombinant is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The protein was lyophilized with 20mM PB and 400mM NaCl, pH 7.2.

    Purity

    BDNF is greater than 950% as determined SDS-PAGE.

    Biological Activity

    The activity was determined using Immobilized Human TrkB-His tag protein 2ug/ml (100 μl/well) for its binding to NHS-Biotin BDNF. The ED50 of was found to be ≤20ng/mL

    Activity

    More Info

    • Introduction

      BDNF promotes the survival of neuronal populations that are all located either in the central nervous system or directly connected to it. BDNF is a major regulator of synaptic transmission and plasticity at adult synapses in many regions of the cns. The versatility of BDNF is emphasized by its contribution to a range of adaptive neuronal responses including long-term potentiation (ltp), long-term depression (ltd), certain forms of short-term synaptic plasticity, as well as homeostatic regulation of intrinsic neuronal excitability.

    • Synonyms

      Brain-Derived Neurotrophic Factor, BDNF, MGC34632.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Amino Acid Sequence

      HSDPARRGE LSVCDSISEW VTAADKKTAV DMSGGTVTVL EKVPVSKGQL KQYFYETKCN PMGYTKEGCR GIDKRHWNSQ CRTTQSYVRA LTMDSKKRIG WRFIRIDTSC VCTLTIKRGR.

    • Background

      Final Thoughts

      Although more research is needed on the safety and effectiveness of BDNF human recombinant, trials suggest that this laboratory-produced protein may be effective in managing and treating several neurological and psychiatric disorders. It's important for experts to stay up to date on the latest developments and research to learn more about potential risks and benefits.

      What is the molecular weight/Mw of BDNF Protein?
      BDNF Protein has a total Mw of 27kDa.

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

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

      What is the Biological Activity of BDNF Protein?
      The ED50, as determined by the dose-dependent induction of C6 cells proliferation, is 1.3-2µg/ml.

      What is the amino acid sequence of BDNF Protein?
      MHSDPARRGE LSVCDSISEW VTAADKKTAV DMSGGTVTVL EKVPVSKGQL KQYFYETKCN PMGYTKEGCR GIDKRHWNSQ CRTTQSYVRA LTMDSKKRIG WRFIRIDTSC VCTLTIKRGR.

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

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

    • Protein content

      BDNF quantitation was carried out by two independent methods:1. UV spectroscopy at 280 nm using the absorbency value of 1.6 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 Brain-derived Neurotrophic Factor 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.

    Bdnf Human
  • View Data Sheet

    Description:

    Alpha Synuclein NACP112 Human Recombinant

    Alpha-synuclein, Non-A beta component of AD amyloid, Non-A4 component of amyloid precursor, NACP, PD1, PARK1, PARK4, MGC110988, a-Synuclein, SNCA.

    Product # :

    PRO-162

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    Description

    A-Synuclein NACP112 Human Recombinant which is an alternatively spliced (103-129) form of a-Synuclein, produced in E.Coli is a single, non-glycosylated polypeptide chain of 112 amino acids having a molecular mass of 11.3kDa. The Recombinant Human a-Synuclein NACP112 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The SNCA NACP112 protein solution (1mg/ml) contains 20mM Tris-HCl buffer pH 7.5 and 100mM NaCl.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      a-Synuclein (amino acids 1-140), an acidic neuronal protein of 140 amino acids, is extremely heat-resistant and is natively unfolded with an extended structure primarily composed of random coils. a-synuclein has been suggested to be implicated in the pathogenesis of Parkinson’s disease and related neurodegenerative disorders, and more recently, to be an important regulatory component of vesicular transport in neuronal cells. Moreover, recent studies have shown that a-synuclein has chaperone activity and that this activity is lost upon removing its C-terminal acidic tail (amino acids 96-140).

    • Synonyms

      Alpha-synuclein, Non-A beta component of AD amyloid, Non-A4 component of amyloid precursor, NACP, PD1, PARK1, PARK4, MGC110988, a-Synuclein, SNCA.

    • 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

      MDVFMKGLSK AKEGVVAAAE KTKQGVAEAA GKTKEGVLYV GSKTKEGVVH GVATVAEKTK EQVTNVGGAV VTGVTAVAQK TVEGAGSIAA ATGFVKKDQL GKEGYQDYEP EA.

    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.

    Snca Nacp112 Human
  • View Data Sheet

    Description:

    Interleukin-1 Receptor Antagonist Porcine Recombinant

    IRAP, IL1F3, IL1RA, IL-1ra3, ICIL-1RA, IL1RN, IL1 inhibitor, IL-1ra, MGC10430.

    Product # :

    CYT-376

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    Description

    Recombinant IL 1RA Porcine produced in E.coli cells is a non-glycosylated, homodimeric protein containing 152 amino acid chain and having a molecular mass of 17.1kDa. The IL 1RA is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The IL 1RA was lyophilized from a 0.2µm filtered concentrated solution in 1×PBS, pH 7.4, containing 1mM DTT.

    Purity

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

    Biological Activity

    The ED50 as determined by inhibiting IL-1a-dependent proliferation of murine D10S cells is less than 50 ng/ml, corresponding to a specific activity of > 2.0 × 104 IU/mg in the presence of 75 pg/ml rPoIL-1a.

    More Info

    • Introduction

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

    • Synonyms

      IRAP, IL1F3, IL1RA, IL-1ra3, ICIL-1RA, IL1RN, IL1 inhibitor, IL-1ra, MGC10430.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Solubility

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

    • Amino Acid Sequence

      HPLGKRPCRM QAFRIWDVNQ KTFYLRNNQL VAGYLQGPNT KLEEKIDVVP VEPHFVFLGI HGGKLCLSCV KSGDEMKLQL DAVNITDLRK NSEQDKRFTF IRSDSGPTTS FESAACPGWF LCTALEADQP VGLTNTPKAA VKVTKFYFQQ DQ

    • Background

      What is the molecular weight/Mw of IL1RA PORCINE Protein?
      IL1RA PORCINE Protein has a total Mw of 17.1kDa.

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

      What is the Purity of IL1RA PORCINE Protein?
      IL1RA PORCINE Protein is >97% pure as determined by SDS-PAGE.

      What is the Biological Activity of IL1RA PORCINE Protein?
      The ED50 as determined by inhibiting IL-1a-dependent proliferation of murine D10S cells is less than 50 ng/ml, corresponding to a specific activity of > 2.0 × 104 IU/mg in the presence of 75 pg/ml rPoIL-1a.

      What is the amino acid sequence of IL1RA PORCINE Protein?
      HPLGKRPCRM QAFRIWDVNQ KTFYLRNNQL VAGYLQGPNT KLEEKIDVVP VEPHFVFLGI HGGKLCLSCV KSGDEMKLQL DAVNITDLRK NSEQDKRFTF IRSDSGPTTS FESAACPGWF LCTALEADQP VGLTNTPKAA VKVTKFYFQQ DQ.

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

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

      Who supplies recombinant IL1RA PORCINE 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 PORCINE?
      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 Porcine
  • View Data Sheet

    Description:

    HCC-1 Human Recombinant (CCL14)

    Small inducible cytokine A14, CCL14, Chemokine CC-1/CC-3, HCC-1/HCC-3, HCC-1(1-74), NCC-2, chemokine (C-C motif) ligand 14, CC-1, CC-3, CKb1, MCIF, SY14, HCC-1, HCC-3, SCYL2, SCYA14.

    Product # :

    CHM-311

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    Description

    HCC-1 Human Recombinant produced in E.Coli is a single,non-glycosylated, polypeptide chain containing 72 amino acids and having a molecular mass of 8411 Dalton. The HCC-1 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The CCL14 protein was lyophilized with 20mM PBS pH-7.4 and 150mM NaCl.

    Purity

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

    Biological Activity

    The Biological activity is calculated by its ability to chemoattract Human monocytes at 5-20ng/ml corresponding to a Specific Activity of 50,000-200,000IU/mg.

    More Info

    • Introduction

      Chemokine (C-C motif) ligand 14 (CCL14) is a small cytokine belonging to the CC chemokine family. It is also commonly known as HCC-1. It is produced as a protein precursor that is procesed to generate a mature active protein containing 74 amino acids that and is 46% identical in amino acid composition to CCL3 and CCL4. This chemokine is expressed in various tissues including spleen, bone marrow, liver, muscle, and gut. CCL13 activates monocytes, but does not induce their chemotaxis. Human CCL13 is located on chromosome 17 within a cluster of other chemokines belonging to the CC family.

    • Synonyms

      Small inducible cytokine A14, CCL14, Chemokine CC-1/CC-3, HCC-1/HCC-3, HCC-1(1-74), NCC-2, chemokine (C-C motif) ligand 14, CC-1, CC-3, CKb1, MCIF, SY14, HCC-1, HCC-3, SCYL2, SCYA14.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized HCC1 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution CCL14 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 HCC-1 in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      TESSSRGPYHPSECCFTYTTYKIPRQRIMDYYETNSQCSKPGIVFITKRGHS
      VCTNPSDKWVQDYIKDMKEN.

    • Background

      What is the molecular weight/Mw of CCL14 HUMAN Protein?
      CCL14 HUMAN Protein has a total Mw of 8.41kDa.

      What is the source or expression system of CCL14 HUMAN Protein?
      Escherichia Coli.

      What is the Purity of CCL14 HUMAN Protein?
      CCL14 HUMAN Protein is >97% pure as determined by SDS-PAGE.

      What is the Biological Activity of CCL14 HUMAN Protein?
      The Biological activity is calculated by its ability to chemoattract Human monocytes at 5-20ng/ml corresponding to a Specific Activity of 50,000-200,000IU/mg.

      What is the amino acid sequence of CCL14 HUMAN Protein?
      TESSSRGPYHPSECCFTYTTYKIPRQRIMDYYETNSQCSKPGIVFITKRGHS
      VCTNPSDKWVQDYIKDMKEN.

      What applications can CCL14 HUMAN Protein be used in?
      CCL14 HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for CCL14 HUMAN Protein?
      The endotoxin level is minimal, CCL14 HUMAN Protein was purified using conventional chromatography techniques.

      Who supplies recombinant CCL14 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 CCL14 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.

    Hcc 1 Human
  • View Data Sheet

    Description:

    Macrophage Migration Inhibitor Factor Mouse Recombinant, His Tag

    Macrophage migration inhibitory factor, MIF, Delayed early response protein 6, DER6, Glycosylation-inhibiting factor, GIF, L-dopachrome isomerase, L-dopachrome tautomerase, Phenylpyruvate tautomerase.

    Product # :

    CYT-896

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    Description

    MIF Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 138 amino acids (1-115 a.a) and having a molecular mass of 14.9kDa. MIF is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    MIF protein solution (0.5mg/ml) containing Phosphate buffered saline , 10% glycerol and 1mM DTT.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

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

    • Synonyms

      Macrophage migration inhibitory factor, MIF, Delayed early response protein 6, DER6, Glycosylation-inhibiting factor, GIF, L-dopachrome isomerase, L-dopachrome tautomerase, Phenylpyruvate tautomerase.

    • 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 MGSMPMFIVN TNVPRASVPE GFLSELTQQL AQATGKPAQY IAVHVVPDQL MTFSGTNDPC ALCSLHSIGK IGGAQNRNYS KLLCGLLSDR LHISPDRVYI NYYDMNAANV GWNGSTFA.

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

    Mif Mouse His
  • View Data Sheet

    Description:

    Alpha-2-HS-Glycoprotein Human Recombinant

    PRO2743, A2HS, AHS, FETUA, HSGA, Alpha-2-HS-glycoprotein, Alpha-2-Z-globulin, Ba-alpha-2-glycoprotein, Fetuin-A.

    Product # :

    PRO-1450

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    Description

    AHSG Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 372 amino acids (19-367 a.a) and having a molecular mass of 39.7kDa (Molecular size on SDS-PAGE will appear higher).AHSG is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    AHSG protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH8.0), 10% glycerol 0.1M NaCl and 1mM DTT.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      AHSG (fetuin-A) which is a glycoprotein present in the serum, is synthesized by hepatocytes. AHSG is one of the fetuin class of plasma binding proteins. It is involved in a number of functions, such as endocytosis, brain development and the formation of bone tissue. It is usually present in the cortical plate of the immature cerebral cortex and bone marrow hemopoietic matrix, hence it has been postulated that it participates in the development of the tissues. Yet, its exact significance is still vague. AHSG promotes endocytosis, hold opsonic properties and influences the mineral phase of the bone. Affinity for calcium and barium ions has been shown.

    • Synonyms

      PRO2743, A2HS, AHS, FETUA, HSGA, Alpha-2-HS-glycoprotein, Alpha-2-Z-globulin, Ba-alpha-2-glycoprotein, Fetuin-A.

    • 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 MGSAPHGPGL IYRQPNCDDP ETEEAALVAI DYINQNLPWG YKHTLNQIDE VKVWPQQPSG ELFEIEIDTL ETTCHVLDPT PVARCSVRQL KEHAVEGDCD FQLLKLDGKF SVVYAKCDSS PDSAEDVRKV CQDCPLLAPL NDTRVVHAAK AALAAFNAQN NGSNFQLEEI SRAQLVPLPP STYVEFTVSG TDCVAKEATE AAKCNLLAEK QYGFCKATLS EKLGGAEVAV TCTVFQTQPV TSQPQPEGAN EAVPTPVVDP DAPPSPPLGA PGLPPAGSPP DSHVLLAAPP GHQLHRAHYD LRHTFMGVVS LGSPSGEVSH PRKTRTVVQP SVGAAAGPVV PPCPGRIRHF KV.

    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.

    Ahsg Human
  • View Data Sheet

    Description:

    Interleukin-1 Receptor Antagonist Rat Recombinant

    IRAP, IL1F3, IL1RA, IL-1ra3, ICIL-1RA, IL1RN, IL1 inhibitor, IL-1ra, MGC10430.

    Product # :

    CYT-152

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    Description

    IL 1RA Rat Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 152 amino acids and having a molecular mass of 17.5kDa.The IL 1RA Rat is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

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

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Biological Activity

    Fully biologically active when compared to standard. Measured by its ability to inhibit IL1a-dependent proliferation in D10.G4.1 mouse helper T cells. The ED50 for this effect is typically 30-150ng/ml (corresponding to a specific activity of 6,667-33,334units/mg ) in the presence of 50pg/ml of rrIL1a.

    More Info

    • Introduction

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

    • Synonyms

      IRAP, IL1F3, IL1RA, IL-1ra3, ICIL-1RA, IL1RN, IL1 inhibitor, IL-1ra, MGC10430.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized IL 1RA although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IL 1RA should be stored at 4°C between 2-7 days and for future use below -18°C.Please prevent freeze-thaw cycles.

    • Solubility

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

    • Amino Acid Sequence

      HPAGKRPCKM QAFRIWDTNQ KTFYLRNNQL IAGYLQGPNT KLEEKIDMVP IDFRNVFLGI HGGKLCLSCV KSGDDTKLQL EEVNITDLNK NKEEDKRFTF IRSETGPTTS FESLACPGWF LCTTLEADHP VSLTNTPKEP CTVTKFYFQE DQ

    • Background

      What is the molecular weight/Mw of IL1RA RAT Protein?
      IL1RA RAT Protein has a total Mw of 17.5kDa.

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

      What is the Purity of IL1RA RAT Protein?
      IL1RA RAT Protein is >95% pure as determined by SDS-PAGE.

      What is the Biological Activity of IL1RA RAT Protein?
      Fully biologically active when compared to standard. Measured by its ability to inhibit IL1a-dependent proliferation in D10.G4.1 mouse helper T cells. The ED50 for this effect is typically 30-150ng/ml (corresponding to a specific activity of 6,667-33,334units/mg ) in the presence of 50pg/ml of rrIL1a.

      What is the amino acid sequence of IL1RA RAT Protein?
      HPAGKRPCKM QAFRIWDTNQ KTFYLRNNQL IAGYLQGPNT KLEEKIDMVP IDFRNVFLGI HGGKLCLSCV KSGDDTKLQL EEVNITDLNK NKEEDKRFTF IRSETGPTTS FESLACPGWF LCTTLEADHP VSLTNTPKEP CTVTKFYFQE DQ.

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

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

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

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

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

    Il 1Ra Rat
  • View Data Sheet

    Description:

    Cytokeratin 14 Human Recombinant, His Tag

    Keratin, type I cytoskeletal 14, Cytokeratin-14, CK-14, Keratin-14, K14, KRT14, NFJ, CK14, EBS3, EBS4.

    Product # :

    PRO-941

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    Description

    KRT14 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 492 amino acids (1-472 a.a.) and having a molecular mass of 53.8kDa.KRT14 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    KRT14 protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH8.0), 10% glycerol and 0.4M Urea.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Cytokeratin 14 is a member of the keratin family, the most diverse group of intermediate filaments. Cytokeratin 14 is a type I keratin, is usually found as a heterotetramer with two keratin 5 molecules, a type II keratin. Together they form the cytoskeleton of epithelial cells. Mutations in the genes for these keratins are associated with epidermolysis bullosa simplex. At least one pseudogene has been identified at 17p12-p11.

    • Synonyms

      Keratin, type I cytoskeletal 14, Cytokeratin-14, CK-14, Keratin-14, K14, KRT14, NFJ, CK14, EBS3, EBS4.

    • 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 MTTCSRQFTS SSSMKGSCGI GGGIGGGSSR ISSVLAGGSC RAPSTYGGGL SVSSSRFSSG GAYGLGGGYG GGFSSSSSSF GSGFGGGYGG GLGTGLGGGF GGGFAGGDGL LVGSEKVTMQ NLNDRLASYL DKVRALEEAN ADLEVKIRDW YQRQRPAEIK
      DYSPYFKTIE DLRNKILTAT VDNANVLLQI DNARLAADDF RTKYETELNL RMSVEADING LRRVLDELTL ARADLEMQIE SLKEELAYLK KNHEEEMNAL RGQVGGDVNV EMDAAPGVDL SRILNEMRDQ YEKMAEKNRK DAEEWFFTKT EELNREVATN SELVQSGKSE ISELRRTMQN
      LEIELQSQLS MKASLENSLE ETKGRYCMQL AQIQEMIGSV EEQLAQLRCE MEQQNQEYKI LLDVKTRLEQ EIATYRRLLE GEDAHLSSSQ FSSGSQSSRD VTSSSRQIRT KVMDVHDGKV VSTHEQVLRT KN.

    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.

    Krt14 Human His
  • View Data Sheet

    Description:

    Beta Defensin-14 Mouse Recombinant

    Beta-defensin 14, BD-14, mBD-14, Defensin, beta 14, Defb14.

    Product # :

    CYT-945

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    Description

    Beta Defensin-14 Mouse Recombinant produced in E.coli is a single, non-glycosylated, polypeptide chain containing 45 amino acids and having a molecular mass of 5.2kDa.The BD14 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    BD-14 protein was lyophilized from a 0.2µm filtered concentrated solution in PBS, pH 7.4.

    Purity

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

    More Info

    • Introduction

      Alpha and Beta Defensins are cationic peptides with antimicrobial activity against Gram-negative and Gram-positive bacteria, fungi and enveloped viruses. These 2-6kDa proteins have vital roles in innate immune system. Mammalian Defensins are classified into alpha, beta and theta categories, based on their size and pattern of disulfide bonding. Beta-Defensins contain a six-cysteine motif which forms 3 intra-molecular disulfide bonds. Since beta-defensins are cationic peptides, they can therefore interact with the membrane of invading microbes, which are negative due to lipopolysaccharides (LPS) and lipoteichoic acid (LTA) found in the cell membrane. In addition, they can affect the stability of the membrane.

    • Synonyms

      Beta-defensin 14, BD-14, mBD-14, Defensin, beta 14, Defb14.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized Mouse BD14 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution BD-14 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 BD14 in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      FLPKTLRKFF CRIRGGRCAV LNCLGKEEQI GRCSNSGRKC CRKKK.

    • Background

      What is the molecular weight/Mw of BD14 Protein?
      BD14 Protein has a total Mw of 5.2kDa.

      What is the source or expression system of BD14 Protein?
      Escherichia Coli.

      What is the Purity of BD14 Protein?
      BD14 Protein is >96% pure as determined by SDS-PAGE.

      What is the Biological Activity of BD14 Protein?
      The biological functionality of BD14 Protein will be determined in the future.

      What is the amino acid sequence of BD14 Protein?
      FLPKTLRKFF CRIRGGRCAV LNCLGKEEQI GRCSNSGRKC CRKKK.

      What applications can BD14 Protein be used in?
      BD14 Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for BD14 Protein?
      The endotoxin level is minimal, BD14 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.

    Bd14 Mouse
  • View Data Sheet

    Description:

    Hepatitis C Virus NS3 Genotype-5a Recombinant

    Product # :

    HCV-212

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    Description

    E.coli derived recombinant from HCV subtype 5a fused to a GST tag. The protein contains the full-length HCV NS3 (c33c) immunodominant region.

    Formulation

    25mM Tris-HCl, 1mM EDTA, 1.5M urea & 50% glycerol.

    Purity

    HCV NS3 Genotype-5a protein is >95% pure as determined by 10% PAGE (coomassie staining).

    More Info

    • Introduction

      HCV is a small 50nm, enveloped, single-stranded, positive sense RNAvirus in the family Flaviviridae.
      HCV has a high rate of replication with approximately one trillion particles produced each day in an infected individual. Due to lack of proofreading by the HCV RNA polymerase, the HCV has an exceptionally high mutation rate, a factor that may help it elude the host's immune response. Hepatitis C virus is classified into six genotypes(1-6) with several subtypes within each genotype. The preponderance and distribution of HCV genotypes varies globally. Genotype is clinically important in determining potential response to interferon-based therapy and the required duration of such therapy. Genotypes 1 and 4 are less responsive to interferon-based treatment than are the other genotypes (2, 3, 5 and 6).

    • Stability

      HCV NS3 Genotype-5a although stable at 4°C for 1 week, should be stored below -18°C. Please prevent freeze thaw cycles.

    • Applications

      HCV NS3 Genotype-5a antigen is suitable for ELISA and Western blots, excellent antigen for detection of HCV with minimal specificity problems.

    • Specificity

      Immunoreactive with sera of HCV-infected individuals.

    • Purification Method

      HCV NS3 Genotype-5a protein was purified by proprietary chromatographic technique.

    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.

    Hcv Ns3 Genotype 5A
  • View Data Sheet

    Description:

    Treponema pallidum p17, 22 kDa Recombinant

    Product # :

    TRP-254

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    Description

    Recombinant Treponema pallidum p17 derived from full length TP17 gene containing 139 aa produced in E.Coli and fused to a 6xHis tag at C-terminus. The total Mw is 22kDa and the pI is 8.7, was purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Treponema p17 22kDa protein solution contains PBS 50mM arginine.

    Purity

    Treponema p17 22kDa is >95% pure as determined by 10% PAGE (coomassie staining).

    More Info

    • Introduction

      Treponema pallidum is a gram-negative spirochaete bacterium and is considered to be metabolically crippled. There are at least four known subspecies: T. pallidum pallidum, T. pallidum pertenue, T. pallidum carateum and T. pallidum endemicum. The helical structure of T. pallidum pallidum allows it to move in a corkscrew motion through viscous mediums such as mucus. Treponema pallidum sub sp. pallidum has one of the smallest bacterial genomes at 1.14 million base pairs (Mb) and has limited metabolic capabilities, reflecting its adaptation through genome reduction to the rich environment of mammalian tissue.

    • Physical Appearance

      Sterile Filtered solution.

    • Stability

      Treponema p17 22kDa protein although stable at 4°C for 1 week, should be stored below -18°C. Please prevent freeze thaw cycles.

    • Applications

      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.

    Treponema P17 22Kda
  • View Data Sheet

    Description:

    Macrophage-Colony Stimulating Factor Mouse Recombinant

    CSF-1, Lanimostim, MCSF, M-CSF.

    Product # :

    CYT-439

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    Description

    Macrophage Colony Stimulating Factor Mouse Recombinant produced in E.coli is a disulfide linked homodimer, non-glycosylated, polypeptide chain containing 2 x 156 amino acids and having a total molecular mass of 36.4 KD.MCSF is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The protein was lyophilized from a sterile (0.2µm) filtered solution containing 10mM sodium phosphate, 50mM sodium chloride, pH 7.5.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Biological Activity

    The ED50, as calculated by the dose-dependant stimulation of the proliferation of murine M-NFS-60 indicator cells is 1.33ng/ml corresponding to a specific activity of 7.5x105 units/mg.

    More Info

    • Introduction

      Granulocyte/Macrophage Colony-Stimulating Factors are cytokines that act in hematopoiesis by controlling the production, differentiation, and function of 2 related white cell populations of the blood, the granulocytes and the monocytes-macrophages. CSF-1 induces cells of the monocyte/macrophage lineage. It plays a role in immunological defenses, bone metabolism, lipoproteins clearance, fertility and pregnancy.

    • Synonyms

      CSF-1, Lanimostim, MCSF, M-CSF.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Amino Acid Sequence

      MKEVSEHCSH MIGNGHLKVL QQLIDSQMET SCQIAFEFVD QEQLDDPVCY LKKAFFLVQD IIDETMRFKD NTPNANATER LQELSNNLNS CFTKDYEEQN KACVRTFHET PLQLLEKIKN FFNETKNLLE KDWNIFTKNC NNSFAKCSSR DVVTKP.

    • Background

      Macrophage-Colony Stimulating Factor Mouse Recombinant: An In-Depth Analysis

      Abstract:

      Macrophage-Colony Stimulating Factor (M-CSF) is a crucial cytokine involved in the regulation of macrophage biology, including their differentiation, survival, and function. This research paper provides an in-depth analysis of M-CSF Mouse Recombinant, focusing on its structure, signaling pathways, and diverse functions in the context of human research. Additionally, the paper explores the therapeutic potential of M-CSF modulation in various diseases.

      Introduction:

      M-CSF plays a vital role in the development and maintenance of macrophages, key immune cells involved in innate immunity and tissue homeostasis. This paper aims to provide a comprehensive analysis of M-CSF Mouse Recombinant, highlighting its importance in human macrophage biology and its potential therapeutic applications.

      Structure and Function of M-CSF:

      M-CSF is a homodimeric protein that binds to its receptor, CSF-1R, leading to the activation of downstream signaling pathways. It regulates the proliferation, survival, and activation of macrophages, influencing immune responses and tissue remodeling processes.

      Signaling Pathways:

      Upon binding to CSF-1R, M-CSF triggers various intracellular signaling pathways, including the MAPK pathway, PI3K/Akt pathway, and JAK/STAT pathway. These pathways regulate gene expression and mediate cellular responses, impacting macrophage functions.

      Role in Macrophage Development and Function:

      M-CSF is essential for the differentiation and maturation of macrophages from hematopoietic progenitor cells. It promotes the survival, proliferation, and activation of macrophages, enhancing their phagocytic activity, cytokine production, and antigen presentation capabilities.

      Therapeutic Potential:

      Given its crucial role in macrophage biology, M-CSF modulation has emerged as a potential therapeutic strategy. M-CSF inhibitors and CSF-1R antagonists have shown promise in the treatment of inflammatory and autoimmune diseases, as well as certain cancers. Targeting M-CSF signaling can modulate immune responses and affect disease progression.

      Clinical Applications and Future Directions:

      The therapeutic potential of M-CSF modulation is being explored in various clinical settings. Clinical trials investigating M-CSF inhibitors as monotherapy or combination therapy are underway in diseases such as rheumatoid arthritis and cancer. Future research should focus on understanding the intricate mechanisms of M-CSF signaling, optimizing therapeutic strategies, and developing personalized treatment approaches.

    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.

    M Csf Mouse
  • View Data Sheet

    Description:

    Gamma-Synuclein Mouse Recombinant

    Gamma-synuclein, Persyn.

    Product # :

    PRO-2490

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    Description

    SNCG Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 146 amino acids (1-123 a.a) and having a molecular mass of 15.5kDa.SNCG is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    SNCG protein solution (1mg/ml) containing 20mM Tris-HCl(pH8.0) and 0.1M NaCl.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      g-synuclein(Originally known as a breast cancer specific gene product, BCSG1) is an acidic neuronal protein of 127 amino acids. Gamma-Synuclein is a member of the Synuclein protein family, which is believed to be involved in the pathogenesis of neurodegenerative diseases. High levels of Gamma-Synuclein have been found in advanced breast carcinomas suggesting a correlation between overexpression of SNCG and breast tumor development. Synuclein-Gamma is found mostly in the peripheral nervous system (in primary sensory neurons, sympathetic neurons, and motor neurons) and retina. SNCG is also identified in the brain, ovarian tumors, and in the olfactory epithelium. SNCG expression in breast tumors is a marker for tumor progression. A modification in the expression of gamma-synuclein has been detected in the retina of Alzheimer's patients.

    • Synonyms

      Gamma-synuclein, Persyn.

    • 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 MGSMDVFKKG FSIAKEGVVG AVEKTKQGVT EAAEKTKEGV MYVGTKTKEN VVQSVTSVAE KTKEQANAVS AVVSSVNTV ANKTVEEAEN IVVTTGVVRK EDLEPPAQDQ EAKEQEENEE AKSGED.

    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.

    Sncg Mouse
  • View Data Sheet

    Description:

    Toll Like Receptor 2 Mouse Recombinant

    Toll-like receptor 2, CD282.

    Product # :

    PRO-2430

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    Description

    TLR2 Mouse Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 805 amino acids (25-587a.a.) and having a molecular mass of 90.7kDa. (Molecular size on SDS-PAGE will appear at approximately 70-100kDa).TLR2 is expressed with a 239 amino acid hIgG-His tag at C-Terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    TLR2 protein solution (0.25mg/ml) containing Phosphate Buffered Saline (pH 7.4) and 10% glycerol.

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      TLR2 belongs to the Toll-like receptor (TLR) family that plays a fundamental role in pathogen recognition and activation of innate immunity. TLRs are highly conserved from Drosophila to humans and share structural and functional similarities. They recognize pathogen-associated molecular patterns (PAMPs) which are expressed on infectious agents, and mediate the production of cytokines necessary for the development of effective immunity. The various TLRs exhibit different patterns of expression. TLR2 is expressed most abundantly in peripheral blood leukocytes, and mediates host response to Gram-positive bacteria and yeast via stimulation of NF-kappaB.

    • Synonyms

      Toll-like receptor 2, CD282.

    • 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

      ADLQESLSCD ASGVCDGRSR SFTSIPSGLT AAMKSLDLSF NKITYIGHGD LRACANLQVL MLKSSRINTI EGDAFYSLGS LEHLDLSDNH LSSLSSSWFG PLSSLKYLNL MGNPYQTLGV TSLFPNLTNL QTLRIGNVET FSEIRRIDFA GLTSLNELEI KALSLRNYQS QSLKSIRDIH HLTLHLSESA FLLEIFADIL SSVRYLELRD TNLARFQFSP LPVDEVSSPM KKLAFRGSVL TDESFNELLK LLRYILELSE VEFDDCTLNG LGDFNPSESD VVSELGKVET VTIRRLHIPQ FYLFYDLSTV YSLLEKVKRI TVENSKVFLV PCSFSQHLKS LEFLDLSENL MVEEYLKNSA CKGAWPSLQT LVLSQNHLRS MQKTGEILLT LKNLTSLDIS RNTFHPMPDS CQWPEKMRFL NLSSTGIRVV KTCIPQTLEV LDVSNNNLDS FSLFLPRLQE LYISRNKLKT LPDASLFPVL LVMKIRENAV STFSKDQLGS FPKLETLEAG DNHFVCSCEL LSFTMETPAL AQILVDWPDS YLCDSPPRLH GHRLQDARPS VLECHQLEPK SCDKTHTCPP CPAPELLGGP SVFLFPPKPK DTLMISRTPE VTCVVVDVSH EDPEVKFNWY VDGVEVHNAK TKPREEQYNS TYRVVSVLTV LHQDWLNGKE YKCKVSNKAL PAPIEKTISK AKGQPREPQV YTLPPSRDEL TKNQVSLTCL VKGFYPSDIA VEWESNGQPE NNYKTTPPVL DSDGSFFLYS KLTVDKSRWQ QGNVFSCSVM HEALHNHYTQ KSLSLSPGKH HHHHH.

    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.

    Tlr2 Mouse
  • View Data Sheet

    Description:

    Interleukin-5 Mouse Recombinant, Sf9

    interleukin 5, Il, Il-5, B-cell growth factor II, BCGF-II, Cytotoxic T-lymphocyte inducer, Eosinophil differentiation factor, T-cell replacing factor, EDF, TRF, B cell differentiation factor I, IL5.

    Product # :

    CYT-1195

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    Description

    IL5 Mouse produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 119 amino acids (21-133 a.a) and having a molecular mass of 13.9kDa.IL5 is expressed with a 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    The IL5 solution (0.25mg/1ml) contains phosphate buffered saline (pH7.4) and 10% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    Biological Activity

    Measured in a cell proliferation assay using TF-1 human erythroleukemic cells. The ED50 range ≤ 1 ng/ml.

    More Info

    • Introduction

      The protein encoded by this gene is a cytokine that acts as a growth and differentiation factor for both B cells and eosinophils. IL5is a main regulator of eosinopoiesis, eosinophil maturation and activation. The elevated production of IL5is reported to be related to asthma or hypereosinophilic syndromes. The receptor of IL5is a heterodimer, whose beta subunit is shared with the receptors for interleukine 3 (IL3) and colony stimulating factor 2 (CSF2/GM-CSF). IL5, together with those for interleukin 4 (IL4), interleukin 13 (IL13), and CSF2, form a cytokine gene cluster on chromosome 5. IL5, IL4, and IL13 are found to be regulated coordinately by long-range regulatory elements spread over 120 kilobases on chromosome 5q31.

    • Synonyms

      interleukin 5, Il, Il-5, B-cell growth factor II, BCGF-II, Cytotoxic T-lymphocyte inducer, Eosinophil differentiation factor, T-cell replacing factor, EDF, TRF, B cell differentiation factor I, IL5.

    • 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

      MEIPMSTVVK ETLTQLSAHR ALLTSNETMR LPVPTHKNHQ LCIGEIFQGL DILKNQTVRG GTVEMLFQNL SLIKKYIDRQ KEKCGEERRR TRQFLDYLQE FLGVMSTEWA MEGHHHHHH

    • Background

      What is the molecular weight/Mw of IL 5 MOUSE, SF9 Protein?
      IL 5 MOUSE, SF9 Protein has a total Mw of 13.9kDa.

      What is the source or expression system of IL 5 MOUSE, SF9 Protein?
      Sf9, Baculovirus cells.

      What is the Purity of IL 5 MOUSE, SF9 Protein?
      IL 5 MOUSE, SF9 Protein is >90% pure as determined by SDS-PAGE.

      What is the Biological Activity of IL 5 MOUSE, SF9 Protein?
      Measured in a cell proliferation assay using TF-1 human erythroleukemic cells. The ED50 range ≤ 1 ng/ml.

      What is the amino acid sequence of IL 5 MOUSE, SF9 Protein?
      MEIPMSTVVK ETLTQLSAHR ALLTSNETMR LPVPTHKNHQ LCIGEIFQGL DILKNQTVRG GTVEMLFQNL SLIKKYIDRQ KEKCGEERRR TRQFLDYLQE FLGVMSTEWA MEGHHHHHH.

      What applications can IL 5 MOUSE, SF9 Protein be used in?
      IL 5 MOUSE, SF9 Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for IL 5 MOUSE, SF9 Protein?
      The endotoxin level is minimal, IL 5 MOUSE, SF9 Protein was purified using conventional chromatography techniques.

      Who supplies recombinant IL 5 MOUSE, SF9 that is in stock and available to order?
      ProSpec has the protein in stock and available for immediate delivery.

      Where can I order bulk mg quantities of IL 5 MOUSE, SF9?
      ProSpec supplies bulk mg quantities at affordable prices that meets research and academic budgets.

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

    Il 5 Mouse
  • View Data Sheet

    Description:

    Neuropoietin Mouse Recombinant

    Cardiotrophin-2, CT-2, Neuropoietin, Np, Ctf2, Gm494.

    Product # :

    CYT-1128

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    Description

    Neuropoietin Mouse Recombinant produced in E.Coli is a non-glycosylated polypeptide chain containing 182 amino acids and having a molecular mass of approximately 19.7kDa.CTF2P is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Lyophilized from a 0.2μm filtered concentrated solution in 20mM Tris-HCl, pH 8.0, 0.5mM DTT and 500mM NaCl.

    Purity

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

    Biological Activity

    The ED50 as determined by a cell proliferation assay using human TF-1 cells is < 200 ng/ml, corresponding to a specific activity of > 5000 IU/mg.

    More Info

    • Introduction

      CTF2P, aka Neuropoietinis a part of the IL-6 family of cytokines. CTF2P is the outcome of a gene duplication event involving cardiotrophin-1 (CT-1) and it helps to define a subfamily within the IL-6 family that includes CT-1, CLC and CTNF. CTF2P Increases the platelet count associated with splenomegaly and takes part in neuronal precursor development and maturation.

    • Synonyms

      Cardiotrophin-2, CT-2, Neuropoietin, Np, Ctf2, Gm494.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized CTF2P although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Neuropoietin 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 Neuropoietin in sterile PBS not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      APISPSEPIG QAYSLALYMQ KNTSALLQTY LQHQGSPFSD PGFSAPELQL STLPSAAVSF KTWHAMEDAE RLSRAQGAFL ALTQHLQLVG DDQSYLNPGS PILLAQLGAA RLRAQGLLGN MAAIMTALGL PIPPEEDTLG FVPFGASAFE RKCRGYIVTR EYGHWTDRAV RDLALLKAKY SA.

    • Background

      What is the molecular weight/Mw of CTF2P Protein?
      CTF2P Protein has a total Mw of 19.7kDa.

      What is the source or expression system of CTF2P Protein?
      Escherichia Coli.

      What is the Purity of CTF2P Protein?
      CTF2P Protein is >98% pure as determined by SDS-PAGE.

      What is the Biological Activity of CTF2P Protein?
      The ED50 as determined by a cell proliferation assay using human TF-1 cells is < 200 ng/ml, corresponding to a specific activity of > 5000 IU/mg.

      What is the amino acid sequence of CTF2P Protein?
      APISPSEPIG QAYSLALYMQ KNTSALLQTY LQHQGSPFSD PGFSAPELQL STLPSAAVSF KTWHAMEDAE RLSRAQGAFL ALTQHLQLVG DDQSYLNPGS PILLAQLGAA RLRAQGLLGN MAAIMTALGL PIPPEEDTLG FVPFGASAFE RKCRGYIVTR EYGHWTDRAV RDLALLKAKY SA.

      What applications can CTF2P Protein be used in?
      CTF2P Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for CTF2P Protein?
      The endotoxin level is minimal, CTF2P 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.

    Neuropoietin Mouse
  • View Data Sheet

    Description:

    Interleukin-21 Receptor Mouse Recombinant

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

    Product # :

    CYT-1204

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    Description

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

    Source

    HEK293 Cells.

    Formulation

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

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Biological Activity

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

    More Info

    • Introduction

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

    • Synonyms

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

    • Physical Appearance

      Sterile filtered colorless solution.

    • Stability

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

    • Amino Acid Sequence

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

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

    Il21R Mouse
  • View Data Sheet

    Description:

    I-309 (CCL1) Human Recombinant, His Tag

    Small inducible cytokine A1, CCL1, T lymphocyte-secreted protein I-309, chemokine (C-C motif) ligand 1, P500, SISe, TCA3, I-309, SCYA1.

    Product # :

    CHM-254

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    • SDS-PAGE

    Description

    I-309 Human Recombinant fused with a 21 amino acid His tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 94 amino acids (24-96 a.a.) and having a molecular mass of 10.8kDa. The I-309 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The I-309 solution (0.5 mg/ml) contains 20mM Tris-HCl buffer (pH 7.5), 2mM DTT, 10% glycerol and 50mM NaCl.

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

    SDS-PAGE

    More Info

    • Introduction

      Chemokine (C-C motif) ligand 1 (CCL1) is a small glycoprotein secreted by activated T cells that belongs to a family inflammatory cytokines known as chemokines. CCL1 attracts monocytes, NK cells, and immature B cells and dendritic cells by interacting with a cell surface chemokine receptor called CCR8. This chemokine resides in a large cluster of CC chemokines on human chromosome 17.

    • Synonyms

      Small inducible cytokine A1, CCL1, T lymphocyte-secreted protein I-309, chemokine (C-C motif) ligand 1, P500, SISe, TCA3, I-309, SCYA1.

    • 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 MKSMQVPFSR CCFSFAEQEI PLRAILCYRN TSSICSNEGL IFKLKRGKEA CALDTVGWVQ RHRKMLRHCP SKRK.

    • Background

      What is the molecular weight/Mw of CCL1 HUMAN, HIS Protein?
      CCL1 HUMAN, HIS Protein has a total Mw of 10.8kDa.

      What is the source or expression system of CCL1 HUMAN, HIS Protein?
      Escherichia Coli.

      What is the Purity of CCL1 HUMAN, HIS Protein?
      CCL1 HUMAN, HIS Protein is >85% pure as determined by SDS-PAGE.

      What is the Biological Activity of CCL1 HUMAN, HIS Protein?
      The biological functionality of CCL1 HUMAN, HIS Protein will be determined in the future.

      What is the amino acid sequence of CCL1 HUMAN, HIS Protein?
      MGSSHHHHHH SSGLVPRGSH MKSMQVPFSR CCFSFAEQEI PLRAILCYRN TSSICSNEGL IFKLKRGKEA CALDTVGWVQ RHRKMLRHCP SKRK.

      What applications can CCL1 HUMAN, HIS Protein be used in?
      CCL1 HUMAN, HIS Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for CCL1 HUMAN, HIS Protein?
      The endotoxin level is minimal, CCL1 HUMAN, HIS Protein was purified using conventional chromatography techniques.

      Who supplies recombinant CCL1 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 CCL1 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.

    I 309 Human His
  • View Data Sheet

    Description:

    Enolase-2 Human Recombinant, His Tag

    Gamma-enolase, EC 4.2.1.11, 2-phospho-D-glycerate hydro-lyase, Neural enolase, Neuron-specific enolase, NSE, Enolase 2, ENO2.

    Product # :

    ENZ-298

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    Description

    Neuron Specific Enolase Human Recombinant is expressed in E. coli containing 433 amino acids 2-434 fused to an amino terminal hexahistidine tag.The NSE is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Enolase 2 is supplied in 10mM Tris-HCl (pH 8), 250mM NaCl, 0.5mM DTT, 1.5mM Cysteine, and 50% Glycerol.

    Purity

    Greater than 95% as determined by SDS-PAGE.
    Single band on Western Blot.

    More Info

    • Introduction

      NSE is the ?? isoform of the glycolytic enzyme enolase and is expressed primarily in neurons, in normal and neoplastic neuroendocrine cells. NSE is a highly soluble cytoplasmic protein that is readily secreted into the CSF and serum following tissue damage. NSE shows neurotrophic and neuroprotective properties on a broad spectrum of central nervous system (CNS) neurons and binds in a calcium-dependent manner to cultured neocortical neurons promoting cell survival.

    • Synonyms

      Gamma-enolase, EC 4.2.1.11, 2-phospho-D-glycerate hydro-lyase, Neural enolase, Neuron-specific enolase, NSE, Enolase 2, ENO2.

    • Physical Appearance

      Sterile Filtered clear solution.

    • Stability

      Store at 4°C if entire vial will be used within 1-2 weeks. Store, frozen at -20°C for longer periods of time. 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.

    Eno2 Human His
  • View Data Sheet

    Description:

    Transcriptional Adaptor 3 Human Recombinant

    Transcriptional adapter 3, ADA3 homolog, hADA3, STAF54, Transcriptional adapter 3-like, ADA3-like protein, TADA3, ADA3, TADA3L, Transcriptional adapter 3 isoform a, NGG1.

    Product # :

    PRO-1689

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    Description

    TADA3 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 455 amino acids (1-432) and having a molecular mass of 51.3 kDa.TADA3 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The TADA3 solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.2M NaCl, 50% glycerol and 2mM DTT.

    Purity

    Greater than 80.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Transcriptional adapter 3 (TATD3) is a subunit of 2 histone acetyltransferase complexes, which functions as a component of the PCAF complex. TATD3 is a transcriptional activator adaptor that is also associates with the tumor suppressor protein p53 and is essential for full activity of p53 and p53-mediated apoptosis.

    • Synonyms

      Transcriptional adapter 3, ADA3 homolog, hADA3, STAF54, Transcriptional adapter 3-like, ADA3-like protein, TADA3, ADA3, TADA3L, Transcriptional adapter 3 isoform a, NGG1.

    • 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 MGSMSELKDC PLQFHDFKSV DHLKVCPRYT AVLARSEDDG IGIEELDTLQ LELETLLSSA SRRLRVLEAE TQILTDWQDK KGDRRFLKLG RDHELGAPPK HGKPKKQKLE GKAGHGPGPG PGRPKSKNLQ PKIQEYEFTD DPIDVPRIPK NDAPNRFWAS VEPYCADITS EEVRTLEELL KPPEDEAEHY KIPPLGKHYS QRWAQEDLLE EQKDGARAAA VADKKKGLMG PLTELDTKDV DALLKKSEAQ HEQPEDGCPF GALTQRLLQA LVEENIISPM EDSPIPDMSG KESGADGAST SPRNQNKPFS VPHTKSLESR IKEELIAQGL LESEDRPAED SEDEVLAELR KRQAELKALS AHNRTKKHDL LRLAKEEVSR QELRQRVRMA DNEVMDAFRK IMAARQKKRT PTKKEKDQAW KTLKERESIL KLLDG.

    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.

    Tada3 Human
  • View Data Sheet

    Description:

    Histamine N-Methyltransferase Human Recombinant

    HMT, HNMT-S1, HNMT-S2, HNMT, Histamine N-methyltransferase.

    Product # :

    ENZ-402

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    Description

    HNMT Human Recombinant fused to 36 amino acid His Tag at N-terminal produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 328 amino acids (1-292) and having a molecular mass of 37 kDa. The HNMT is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The HNMT solution contains 20mM Tris-HCl pH-8 and 10% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      HNMT is located in the cytosol and uses S-adenosyl-L-methionine as the methyl donor. In the mammal’s brain,N(tau)-methylation controls the neurotransmitter activity of histamine since diamine oxidase is not located in the central nervous system. A well known genetic polymorphism influences the activity levels of HNMT gene product in red blood cells. HNMT inactivates histamine by n-methylation. HNMT is involved in degrading histamine and in regulating the airway response to histamine. Histamine is involved in regulation and modulation of immune response through the stimulation of four distinct subtypes of receptors, H1, H2, H3, and H4, that present on the target cells. Histamine is inactivated by the histamine-metabolizing enzyme HNMT in bronchus, kidney, and the central nervous system.

    • Synonyms

      HMT, HNMT-S1, HNMT-S2, HNMT, Histamine N-methyltransferase.

    • Physical Appearance

      Sterile Filtered clear 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 avoid freeze-thaw cycles.

    • Amino Acid Sequence

      MRGSHHHHHH GMASMTGGQQ MGRDLYDDDD KDRWGSMASS MRSLFSDHGK YVESFRRFLN HSTEHQCMQE FMDKKLPGII GRIGDTKSEI KILSIGGGAG EIDLQILSKV QAQYPGVCIN NEVVEPSAEQ IAKYKELVAK TSNLENVKFA WHKETSSEYQ SRMLEKKELQ KWDFIHMIQM LYYVKDIPAT LKFFHSLLGT NAKMLIIVVS GSSGWDKLWK KYGSRFPQDD LCQYITSDDL TQMLDNLGLK YECYDLLSTM DISDCFIDGD ENGDLLWDFL TETCNFNATA PPDLRAELGK DLQEPEFSAK KEGKVLFNNT LSFIVIEA.

    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.

    Hnmt Human
  • View Data Sheet

    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.

    More Info

    • Introduction

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

    • Synonyms

      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 :

    HRP

    Description:

    Horseradish Peroxidase

    Horseradish Peroxidase, HRP, EC 1.11.1.7.

    Product # :

    ENZ-321

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    Description

    HRP consists of the basic isoenzyme having a molecular weight of 44 kDa.The Horseradish Peroxidase is purified by affinity chromatography, which results in an enzyme of high specific activity and purity.

    Source

    Root extracts of horseradish.

    Purity

    (A403/A275) = RZ: 3.0.

    Biological Activity

    276 U/mg (25°C, guaiacol as the hydrogen donor, pH-7 and H2O2 as substrates).

    More Info

    • Introduction

      The enzyme horseradish peroxidase, found in horseradish, is used extensively in molecular biologyand in antibody amplification and detection, among other things. For example, "In recent years the technique of marking neurons with the enzyme horseradish peroxidase (HRP) has become a major tool. In its brief history, this method has probably been used by more neurobiologists than have used the Golgi stainsince its discovery in 1870." Horseradish peroxidase is also highly used in techniques such as Western blottingand ELISAs.
      HRP is widely used as an enzymatic label in immunoassays. Usually, the enzyme is coupled to antibodies, lectins or haptens. Coupling to antibodies etc. may be performed through the carbohydrate side chains of the HRP.

    • Synonyms

      Horseradish Peroxidase, HRP, EC 1.11.1.7.

    • Physical Appearance

      Sterile Filtered red-brown lyophilized powder.

    • Stability

      Lyophilized HRP although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution HRP 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 HRP in sterile 18MΩ-cm H2O not less than 100 µg/ml.

    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.

    Horseradish Peroxidase