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1000 results found for “melanoma inhibitory activity”

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  • View Data Sheet

    Description:

    Osteocrin Human Recombinant, HEK

    Osteocrin, Musclin, OSTN.

    Product # :

    PRO-2818

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    Description

    Osteocrin Human Recombinant is a single, glycosylated, polypeptide chain (28-133 a.a) containing a total of 112 amino acids and having a molecular mass of 12.5 kDa. Osteocrin is fused to a 6 a.a His-Tag at C-terminus and is purified by proprietary chromatographic techniques.

    Source

    HEK293 Cells.

    Formulation

    The Osteocrin solution (0.5mg/ml) contains 10% Glycerol and Phosphate-Buffered Saline (pH 7.4).

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Biological Activity

    The ED50 range ≤ 20 ng/ml measured by its binding ability in a functional ELISA with Human NPRC.

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    • Synonyms

      Osteocrin, Musclin, OSTN.

    • 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

      VDVTTTEAFD SGVIDVQSTP TVREEKSATD LTAKLLLLDE LVSLENDVIE TKKKRSFSGF GSPLDRLSAG SVDHKGKQRK VVDHPKRRFG IPMDRIGRNR LSNSRGHHHH HH.

    • Background

      Research has demonstrated that osteocrin influences bone formation by enhancing the anabolic effects of osteoblasts, the cells responsible for new bone formation. In addition to its skeletal roles, osteocrin has been shown to regulate cardiovascular functions by modulating blood pressure and cardiac hypertrophy. Furthermore, emerging evidence suggests that osteocrin may play a role in the central nervous system, impacting cognitive function and neuroprotection.

    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.

    Osteocrin Human
  • View Data Sheet

    Description:

    Flt3-Ligand Human Recombinant, HEK derived

    Fms-related tyrosine kinase 3 ligand, FLK2, STK1, CD135, Stem Cell Tyrosine Kinase 1, FLT3LG, Flt3.

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    CYT-706

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    Description

    Flt3-Ligand Human Recombinant produced in HEK cells is a glycosylated monomer, having a molecular weight range of 24-30kDa due to glycosylation. The Flt3-Ligand is purified by proprietary chromatographic techniques.

    Source

    HEK293 (Human Embryonic Kidney cell line).

    Formulation

    Flt3-Ligand was lyophilized from a 0.2µm filtered solution containing 1xPBS.

    Purity

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

    Biological Activity

    The activity was determined by the dose- dependent stimulation of the proliferation of the human acute myeloid leukemia cell line OCI-AML5. The ED50 is 0.56ng/ml.

    More Info

    • Introduction

      FLT3 ligand is a receptor for the fl cytokine has a tyrosine-protein kinase activity & a growth factor that regulates proliferation of early hematopoietic cells. Flt3-Ligand synergizes with other CSFs and interleukins to induce growth and differentiation.

    • Synonyms

      Fms-related tyrosine kinase 3 ligand, FLK2, STK1, CD135, Stem Cell Tyrosine Kinase 1, FLT3LG, Flt3.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized Flt3-Ligand although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Flt3-Ligand 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 Flt3-Ligand in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      TQDCSFQHSP ISSDFAVKIR ELSDYLLQDY PVTVASNLQD EELCGGLWRL VLAQRWMERL KTVAGSKMQG LLERVNTEIH FVTKCAFQPP PSCLRFVQTN ISRLLQETSE QLVALKPWIT RQNFSRCLEL QCQPDSSTLP PPWSPRPLEA TAPTAPQP.

    • Background

      What is the molecular weight/Mw of FLT3 LIGAND HUMAN, HEK Protein?
      FLT3 LIGAND HUMAN, HEK Protein has a total Mw of 27kDa.

      What is the source or expression system of FLT3 LIGAND HUMAN, HEK Protein?
      HEK293 (Human Embryonic Kidney cell line).

      What is the Purity of FLT3 LIGAND HUMAN, HEK Protein?
      FLT3 LIGAND HUMAN, HEK Protein is >95% pure as determined by SDS-PAGE.

      What is the Biological Activity of FLT3 LIGAND HUMAN, HEK Protein?
      The activity was determined by the dose- dependent stimulation of the proliferation of the human acute myeloid leukemia cell line OCI-AML5. The ED50 is 0.56ng/ml.

      What is the amino acid sequence of FLT3 LIGAND HUMAN, HEK Protein?
      TQDCSFQHSP ISSDFAVKIR ELSDYLLQDY PVTVASNLQD EELCGGLWRL VLAQRWMERL KTVAGSKMQG LLERVNTEIH FVTKCAFQPP PSCLRFVQTN ISRLLQETSE QLVALKPWIT RQNFSRCLEL QCQPDSSTLP PPWSPRPLEA TAPTAPQP.

      What applications can FLT3 LIGAND HUMAN, HEK Protein be used in?
      FLT3 LIGAND HUMAN, HEK Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for FLT3 LIGAND HUMAN, HEK Protein?
      The endotoxin level is minimal, FLT3 LIGAND HUMAN, HEK 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.

    Flt3 Ligand Human Hek
  • View Data Sheet

    Description:

    Beta-Secretase 2 Mouse Recombinant, HEK

    BAE2, CDA13, CEAP1, DRAP, ARP1, ASP1, ASP21, 1110059C24Rik, AEPLC, AI850424, ALP56, beta-site APPcleaving enzyme 2, beta-secretase 2, Aspartyl protease 1, Asp 1, Beta-site amyloid precursor protein cleaving enzyme 2, Memapsin-1, Membrane-associated aspartic protease 1, Theta-secretase.

    Product # :

    ENZ-1188

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    Description

    BACE2 Mouse Recombinant produced in HEK293 Cells is a single, glycosylated, polypeptide chain (20-462 a.a) containing a total of 449 amino acids, having a molecular mass of 48.6 kDa. BACE2 Mouse is fused to a 6 amino acid His-tag at C-terminus and is purified by proprietary chromatographic techniques.

    Source

    HEK293 Cells.

    Formulation

    BACE2 (0.25mg/ml) is filtered in 10% (w/v) glycerol and Phosphate-Buffered Saline pH 7.4.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Biological Activity

    Specific activity is > 20 pmol/min/ug in which one unit will convert 1.0pmole of Mca-SEVNLDAEFRK(Dnp)RR-NH2 to Mca- Pro-Leu-OH per minute at pH 3.5 at 25C.

    More Info

    • Synonyms

      BAE2, CDA13, CEAP1, DRAP, ARP1, ASP1, ASP21, 1110059C24Rik, AEPLC, AI850424, ALP56, beta-site APPcleaving enzyme 2, beta-secretase 2, Aspartyl protease 1, Asp 1, Beta-site amyloid precursor protein cleaving enzyme 2, Memapsin-1, Membrane-associated aspartic protease 1, Theta-secretase.

    • Physical Appearance

      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

      AVPALAPAPF TLPLQVARAT NHRASAVPGL GTPELPRADG LALALEPVRA TANFLAMVDN LQGDSGRGYY LEMLIGTPPQ KVQILVDTGS SNFAVAGAPH SYIDTYFDSE SSSTYHSKGF DVTVKYTQGS WTGFVGEDLV TIPKGFNSSF LVNIATIFES ENFFLPGIKW NGILGLAYAA LAKPSSSLET FFDSLVAQAK IPDIFSMQMC GAGLPVAGSG TNGGSLVLGG IEPSLYKGDI

      WYTPIKEEWY YQIEILKLEI GGQNLNLDCR EYNADKAIVD SGTTLLRLPQ KVFDAVVEAV ARTSLIPEFS DGFWTGAQLA CWTNSETPWA YFPKISIYLR DENASRSFRI TILPQLYIQP MMGAGFNYEC YRFGISSSTN ALVIGATVME GFYVVFDRAQ RRVGFAVSPC AEIEGTTVSE ISGPFSTEDI ASNCVPAQAL NEP HHHHHH.

    • Background

      BACE2 protein, a member of the beta-secretase family, has gained attention as a key player in the pathogenesis of neurological disorders, particularly Alzheimer's disease. This research aims to explore the function and potential therapeutic implications of BACE2 protein in neurodegenerative conditions. Understanding the role of BACE2 protein can provide valuable insights into its significance as a therapeutic target for the development of novel treatment strategies.

      Function of BACE2 Protein:

      BACE2 is a transmembrane aspartic protease predominantly expressed in the central nervous system. It exhibits distinct cleavage activity on various protein substrates, including neuregulins, APP-like proteins, and TGF-β. Unlike its close homolog BACE1, BACE2 has been proposed to have non-amyloidogenic processing capabilities and has shown potential neuroprotective effects.

      Implications of BACE2 Protein in Alzheimer's Disease:

      Alzheimer's disease is characterized by the accumulation of amyloid-beta (Aβ) peptides in the brain, which are generated through the sequential cleavage of amyloid precursor protein (APP). BACE1 is primarily responsible for the cleavage of APP, leading to the production of toxic Aβ peptides. In contrast, BACE2 has been suggested to compete with BACE1, thereby reducing the levels of Aβ generation. This has led to speculation about the neuroprotective role of BACE2 and its potential as a therapeutic target for Alzheimer's disease.

      BACE2 Protein and Neuronal Survival:

      Emerging evidence suggests that BACE2 may play a role in promoting neuronal survival and function. Studies have shown that BACE2 deficiency leads to impaired synaptic plasticity, reduced dendritic branching, and altered neurotransmitter release. BACE2 has also been implicated in the regulation of axonal growth and guidance during development. These findings highlight the potential importance of BACE2 in maintaining neuronal integrity.

      Association of BACE2 Protein with Other Neurological Disorders:

      Apart from Alzheimer's disease, BACE2 has been implicated in other neurological conditions as well. Genetic studies have identified BACE2 gene variants associated with an increased risk of Parkinson's disease, suggesting its involvement in the pathogenesis of this disorder. Furthermore, BACE2 has been linked to the regulation of insulin signaling and glucose homeostasis, making it a potential target for diabetes-associated cognitive decline.

      Therapeutic Implications of BACE2 Protein:

      Given its potential neuroprotective effects and modulatory role in amyloid processing, BACE2 protein has emerged as a promising therapeutic target for neurodegenerative disorders. Strategies aimed at enhancing BACE2 activity or selectively activating BACE2-mediated non-amyloidogenic processing pathways hold promise for reducing amyloid pathology and preserving neuronal function. However, further research is needed to better understand the complex mechanisms underlying BACE2 function and to develop safe and effective therapeutic interventions.

      Conclusion:

      The investigation of BACE2 protein has provided valuable insights into its role in neurodegenerative diseases, particularly Alzheimer's disease. The potential neuroprotective effects and modulation of amyloid processing pathways by BACE2 make it an intriguing therapeutic target. Future studies should focus on unraveling the precise mechanisms by which BACE2 influences disease pathogenesis and developing strategies to harness its therapeutic potential. The exploration of BACE2 protein opens new avenues for the development of innovative treatment approaches for neurodegenerative disorders.

    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.

    Bace2 Mouse Hek
  • View Data Sheet

    Description:

    Interleukin-12 Human Recombinant

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

    Product # :

    CYT-101

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    Description

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

    Source

    HEK.

    Formulation

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

    Purity

    Greater than 95% as obsereved by SDS-PAGE.

    Biological Activity

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

    More Info

    • Introduction

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

    • Synonyms

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

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Solubility

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

    • Amino Acid Sequence

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

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

    Il 12 Human Hek
  • View Data Sheet

    Description:

    Interleukin-1 Alpha Rhesus Macaque Recombinant

    Hematopoietin-1, Lymphocyte-activating factor (LAF), Endogenous Pyrogen (EP), Leukocyte Endogenous Mediator (LEM), Mononuclear Cell Factor (MCF), IL-1 alpha,IL1, IL-1A, IL1F1.

    Product # :

    CYT-790

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    Description

    Recombinant IL 1 alpha Rhesus Macaque produced in E.coli cells is a non-glycosylated, homodimeric protein containing 159 amino acid chain and having a molecular mass of 18.1kDa. The IL 1 alpha is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The IL 1 alpha was lyophilized from a 0.2µm filtered concentrated solution in PBS, pH 7.4.

    Purity

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

    Biological Activity

    The ED50 as determined by a cell proliferation assay using murine D10S cells is less than 10 pg/ml, corresponding to a specific activity of > 1.0×108IU/mg.

    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

      Hematopoietin-1, Lymphocyte-activating factor (LAF), Endogenous Pyrogen (EP), Leukocyte Endogenous Mediator (LEM), Mononuclear Cell Factor (MCF), IL-1 alpha,IL1, IL-1A, IL1F1.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Solubility

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

    • Amino Acid Sequence

      SAPFSFLSNM TYHFIRIIKH EFILNDTLNQ TIIRANDQHL TAAAIHNLDE AVKFDMGAYT SSKDDTKVPV ILRISKTQLY VSAQDEDQPV LLKEMPEINK TITGSETNFL FFWETHGTKN YFISVAHPNL FIATKHDNWV CLAKGLPSIT DFQILENQA

    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 Rhesus Macaque
  • View Data Sheet

    Description:

    Interferon Alpha 2a Human Recombinant, Tobacco

    Leukocyte interferon, B cell interferon, Type I interferon, IFNA2, IFN-a 2a.

    Product # :

    CYT-543

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    Description

    Interferon Alpha Human 2a Recombinant produced in Plant is a single, glycosylated, polypeptide chain containing 165 amino acids and having a molecular mass of 19 kDa.The Interferon-a 2a contains affinity 6xHis tag on C-terminus.The IFN-A 2a is purified by proprietary chromatographic techniques.

    Source

    Nicotiana Sp.Plant.

    Formulation

    Lyophilized, containing 50% SDS.

    Purity

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

    Biological Activity

    The specific activity was determined by a quantitative gene report bioassay using human Type I interferon-sensitive cells. Compared with bacterial derived recombinant IFN-a 2a, assayed in the same conditions, plant derived IFN-alpha 2a showed 6.1 × 108 Units/mg in reference to a viral resistance assay using bovine kidney MDBK cells.

    More Info

    • Introduction

      IFN-alpha is produced by macrophages and has antiviral activities. Interferon stimulates the production of two enzymes: protein kinase and an oligoadenylate synthetase.

    • Synonyms

      Leukocyte interferon, B cell interferon, Type I interferon, IFNA2, IFN-a 2a.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized Interferon alpha 2a although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IFN-alpha 2a 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 Interferon-alpha 2a 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 twelve N-terminal amino acids was determined and was found to be Cys-Asp-Leu-Pro-Gln-Thr-His-Ser-Leu-Gly-Ser-Arg.

    • Background

      What is the molecular weight/Mw of IFN A 2A HUMAN, PLANT Protein?
      IFN A 2A HUMAN, PLANT Protein has a total Mw of 19kDa.

      What is the source or expression system of IFN A 2A HUMAN, PLANT Protein?
      Nicotiana Sp.Plant.
      What is the Purity of IFN A 2A HUMAN, PLANT Protein?
      IFN A 2A HUMAN, PLANT Protein is >99% pure as determined by SDS-PAGE.

      What is the Biological Activity of IFN A 2A HUMAN, PLANT Protein?
      The specific activity was determined by a quantitative gene report bioassay using human Type I interferon-sensitive cells. Compared with bacterial derived recombinant IFN-a 2a, assayed in the same conditions, plant derived IFN-alpha 2a showed 6.1 × 108 Units/mg in reference to a viral resistance assay using bovine kidney MDBK cells.

      What is the amino acid sequence of IFN A 2A HUMAN, PLANT Protein?
      The sequence of the first twelve N-terminal amino acids was determined and was found to be Cys-Asp-Leu-Pro-Gln-Thr-His-Ser-Leu-Gly-Ser-Arg.

      What applications can IFN A 2A HUMAN, PLANT Protein be used in?
      IFN A 2A HUMAN, PLANT Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for IFN A 2A HUMAN, PLANT Protein?
      The endotoxin level is minimal, IFN A 2A HUMAN, PLANT Protein was purified using conventional chromatography techniques.

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

    Interferon Alpha 2A Plant
  • View Data Sheet

    Description:

    Treponema pallidum p47 (Partial) Recombinant

    Product # :

    TRP-249

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    Description

    The E.Coli derived recombinant protein is fused at the C- terminus with a 6xHis Tag and contains the T.Pallidum p47 immunodominant regions.

    Source

    Escherichia Coli.

    Formulation

    70mM Tris-HCl pH8.0, 50mM NaCl, 50% Glycerol and 1.5M urea.

    Purity

    Treponema Pallidum protein 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 subsp. 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.

    • Stability

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

    • Applications

      Treponema Pallidum protein is suitable for ELISA and Western blots, excellent antigen for detection of T.Pallidum with minimal specificity problems.

    • Specificity

      Immunoreactive with sera of T.Pallidum infected individuals.

    • Purification Method

      Treponema Pallidum 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.

    Tpallidum P47 Partial
  • View Data Sheet

    Description:

    BCA-1/BLC Mouse Recombinant (CXCL13)

    C-X-C motif chemokine 13, B lymphocyte chemoattractant, CXC chemokine BLC, Small-inducible cytokine B13, Cxcl13, Blc, Scyb13.

    Product # :

    CHM-030

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    Description

    CXCL13 Mouse Recombinant (22-109) produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 88 amino acids and having a molecular mass of 10kDa.The BCA-1 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The BCA1 protein was lyophilized from a 0.2µm filtered solution in Acetonitrile and TFA.

    Purity

    Greater than 97.0% as determined by SDS-PAGE.

    Biological Activity

    The ED50, as measured by its ability to chemoattract human CXCR5-transfected mouse BaF3 cells, is less than 2µg/ml.

    More Info

    • Introduction

      BCA-1 is a CXC chemokine that is highly expressed in thesecondary lymphoid organs, such as follicles of the spleen, lymph nodes, and Peyer's patches. CXCL13 promotes the migration of B lymphocytes (compared to T cells and macrophages), by stimulating calcium influx into, and chemotaxis of, cells expressing Burkitt's lymphoma receptor 1 (BLR1). BCA1 therefore function in the homing of B lymphocytes to follicles. Human BCA-1 shares a 64% amino acid sequence similarity with the mouse protein and 23 - 34% amino acid sequence identity with other known CXC chemokines. Recombinant or chemically synthesized BCA1 is a potent chemoattractant for B lymphocytes but not T lymphocytes, monocytes or neutrophils. BLR1, a G protein-coupled receptor originally isolated from Burkitt’s lymphoma cells, has now been shown to be the specific receptor for BCA1. Among cells of the hematopoietic lineages, the expression of BLR-1, now designated CXCR-5, is restricted to B lymphocytes and a subpopulation of T helper memory cells.

    • Synonyms

      C-X-C motif chemokine 13, B lymphocyte chemoattractant, CXC chemokine BLC, Small-inducible cytokine B13, Cxcl13, Blc, Scyb13.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized BCA1 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution BCA1 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 CXCL13 in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      ILEAHYTNLK CRCSGVISTV VGLNIIDRIQ VTPPGNGCPK TEVVIWTKMK KVICVNPRAK WLQRLLRHVQ SKSLSSTPQA PVSKRRAA.

    • Background

      What is the molecular weight/Mw of CXCL13 MOUSE Protein?
      CXCL13 MOUSE Protein has a total Mw of 10kDa.

      What is the source or expression system of CXCL13 MOUSE Protein?
      Escherichia Coli.

      What is the Purity of CXCL13 MOUSE Protein?
      CXCL13 MOUSE Protein is >97% pure as determined by SDS-PAGE.

      What is the Biological Activity of CXCL13 MOUSE Protein?
      The ED50, as measured by its ability to chemoattract human CXCR5-transfected mouse BaF3 cells, is less than 2µg/ml.

      What is the amino acid sequence of CXCL13 MOUSE Protein?
      ILEAHYTNLK CRCSGVISTV VGLNIIDRIQ VTPPGNGCPK TEVVIWTKMK KVICVNPRAK WLQRLLRHVQ SKSLSSTPQA PVSKRRAA.

      What applications can CXCL13 MOUSE Protein be used in?
      CXCL13 MOUSE Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for CXCL13 MOUSE Protein?
      The endotoxin level is minimal, CXCL13 MOUSE Protein was purified using conventional chromatography techniques.


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

    Bca 1 Mouse
  • View Data Sheet

    Description:

    Betacellulin Human Recombinant

    Product # :

    CYT-330

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    Description

    Betacellulin Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 80 amino acids and having a molecular mass of 9 kDa. Betacellulin Human Recombinant is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The Betacellulin Human Recombinant was lyophilized from a 0.2µm filtered concentrated solution in PBS, pH 7.4.

    Purity

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

    Biological Activity

    The ED50, calculated by the dose-dependant proliferation of murine BALB\C 3T3 cells (measured by 3H-thymidine uptake) is < 0.05 ng/ml. corresponding to a Specific Activity of >20,000,000IU/mg.

    More Info

    • Introduction

      Btc is a potent mitogen for retinal pigment epithelial cells and vascular smooth muscle cells. The effects of betacellulin are probably mediated by the egf receptor and other related receptors.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Solubility

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

    • Amino Acid Sequence

      DGNSTRSPET NGLLCGDPEE NCAATTTQSK RKGHFSRCPK QYKHYCIKGR CRFVVAEQTP SCVCDEGYIG ARCERVDLFY

    • Background

      Betacellulin Human Recombinant: Illuminating Pathways in Regenerative Medicine

      Introduction

      In the ever-evolving landscape of regenerative medicine, a promising new chapter unfolds with the arrival of Betacellulin Human Recombinant (BTC). This growth factor holds tremendous potential, offering a glimpse into the future of transformative therapeutic interventions.

      BTC: The Architect of Cellular Revitalization

      BTC, a member of the EGF family, has long been recognized for its pivotal role in cellular proliferation and differentiation. The emergence of BTC in its recombinant form has sparked excitement, igniting new possibilities for regenerative medicine.

      Crafting the Alchemist: Pioneering Methodologies

      Through the adept utilization of biotechnological techniques, we successfully synthesized BTC human recombinant. Our meticulous in vitro investigations delved into BTC's capacity to orchestrate intricate cellular processes, paving the way for therapeutic advancements.

      Unveiling the Biological Tapestry

      Buoyed by encouraging in vitro findings, we embarked on in vivo studies utilizing animal models. This natural setting allowed us to witness BTC human recombinant's impact within a living organism, unraveling the intricate nuances of its regenerative potential.

      A Flourish of Results

      The journey from laboratory to living system yielded promising results. BTC human recombinant showcased a significant influence on cellular proliferation and differentiation, underscoring its role as a key player in tissue regeneration and regenerative therapies.

      Charting a Transformative Future

      As the story of BTC human recombinant unfolds, it beckons further exploration through extensive human-centric clinical trials. These trials will serve as a compass, guiding us towards harnessing the full therapeutic potential of BTC, ushering in a new era of healing and regeneration.

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

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

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

      What is the Biological Activity of BTC Protein?
      The ED50, calculated by the dose-dependant proliferation of murine BALB\C 3T3 cells (measured by 3H-thymidine uptake) is < 0.05 ng/ml. corresponding to a Specific Activity of >20,000,000IU/mg.

      What is the amino acid sequence of BTC Protein?
      DGNSTRSPET NGLLCGDPEE NCAATTTQSK RKGHFSRCPK QYKHYCIKGR CRFVVAEQTP SCVCDEGYIG ARCERVDLFY

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

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

    Betacellulin Human
  • View Data Sheet

    Description:

    Tumor Necrosis Factor-Alpha Rhesus Macaque Recombinant

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

    Product # :

    CYT-737

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    Description

    TNF-a Rhesus Macaque Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 157 amino acids and having a molecular mass of 17.3kDa.The TNFA Rhesus Macaque is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

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

    Purity

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

    Biological Activity

    The ED50 as determined by a cytotoxicity assay using murine L929 cells is less than 0.05 ng/ml, corresponding to a specific activity of > 2.0 × 107 IU/mg in the presence of actinomycin D.

    More Info

    • Introduction

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

    • Synonyms

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

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Solubility

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

    • Amino Acid Sequence

      VRSSSRTPSD KPVAHVVANP QAEGQLQWLN RRANALLANG VELTDNQLVV PSEGLYLIYS QVLFKGQGCP SNHVLLTHTI SRIAVSYQTK VNLLSAIKSP CQRETPEGAE AKPWYEPIYL GGVFQLEKGD RLSAEINLPD YLDFAESGQV YFGIIAL.

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    Tnf A Rhesus Macaque
  • View Data Sheet

    Description:

    Transforming Growth Factor-Beta 2 Human Recombinant, HEK

    Transforming growth factor, beta 2, cetermin, Glioblastoma-derived T-cell suppressor factor, polyergin, G-TSF, TGF-beta2, TGF-beta-2, transforming growth factor beta-2, BSC-1 cell growth inhibitor, TGFB-2.

    Product # :

    CYT-112

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    Description

    TGF-b 2 Human Recombinant produced in HEK cells is a non-glycosylated homodimer, having a total molecular weight of 25kDa.The TGF-b 2 is purified by proprietary chromatographic techniques.

    Source

    HEK.

    Formulation

    TGF-b 2 was lyophilized from a 0.2µm filtered solution containing 50mM sodium acetate pH 4.5.

    Purity

    Greater than 95% as obsereved by SDS-PAGE.

    Biological Activity

    The specific activity was determined by the dose-dependent inhibition of IL-4 induced proliferation of mouse HT-2 cells (BALB/c spleen activated by sheep erythrocytes in the presence of IL-2), the ED50 is 0.16ng/ml.

    More Info

    • Introduction

      TGFB2 is a 27.08 kDa protein having two identical 118 amino acid peptide chains linked by a single disulfide bond. TGFB2 is part of a family of five related cytokines that have an extensive variation of normal and neoplastic cells, indicating the importance of these homo-dimmer proteins as multi-functional regulators of cellular activity. The three mammalian isoforms of TGF-beta (TGFb1, TGFb2 and TGFb3) signal through the same receptor and stimulate similar biological responses. They are involved in physiological processes as embryogenesis, tissue remodelling and wound healing.

    • Synonyms

      Transforming growth factor, beta 2, cetermin, Glioblastoma-derived T-cell suppressor factor, polyergin, G-TSF, TGF-beta2, TGF-beta-2, transforming growth factor beta-2, BSC-1 cell growth inhibitor, TGFB-2.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized TGF-b 2 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution TGF-b 2 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 TGF-b 2 in sterile solution containing 20% ethanol, 50mM sodium acetate and 75mM acetic acid.

    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.

    Tgf B 2 Human Hek
  • View Data Sheet

    Description:

    Interleukin-17E Human Recombinant

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

    Product # :

    CYT-583

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    Description

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

    Source

    Escherichia Coli.

    Formulation

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

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Biological Activity

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

    More Info

    • Introduction

      IL-25 also called IL-17E cytokine has a sequence similarity with IL17. IL-17E indluces NF-kappaB activation, and stimulates the production of IL-8. IL17E and IL17B are ligands for the cytokine receptor IL17BR. IL-25 is a proinflammatory cytokine favoring Th2-type immune response. The upregulation of costimulation-induced IL-17E receptors and release of cytokines and chemokines from IL-17E treated costimulated Th cells are differentially regulated by intracellular JNK, p38 MAPK and NF-kappaB activity. Blocking Iinterleukin-25 prevents airway hyperresponsiveness, a critical feature of clinical asthma. IL25 produced by innate effector eosinophils and basophils increase the allergic inflammation by enhancing the maintenance and functions of TSLP-DC activated adaptive Th2 memory cells. Over expression of IL-25 up-regulates gene expression of Th2 cytokines and induces growth retardation, jaundice, and multiorgan inflammation in a transgenic mouse model. IL-25 contributes to the induction and maintenance of eosinophilic inflammation by acting on lung fibroblasts which supports the fact that IL-17E is an important factor in asthma pathophysiology. IL-17E operates by amplifying TH2 cell-mediated allergic airway inflammation but doesn’t induce allergic inflammation in vivo.

    • Synonyms

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

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized Interleukin Human IL17E although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Human IL-25 should be stored at 4°C between 2-7 days and for future use below -18°C.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.

    • Solubility

      It is recommended to reconstitute the lyophilized Interleukin Human IL25 in sterile 10mM HCl not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

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

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

    Il 17E Human
  • View Data Sheet

    Description:

    Mitogen-Activated Protein Kinase Kinase 6 Human Recombinant, sf9

    Angiopoietin-1 receptor, Endothelial tyrosine kinase, HYK, STK1, Tunica interna endothelial cell kinase, Tyrosine kinase with Ig and EGF homology domains-2, Tyrosine-protein kinase receptor TEK, Tyrosine-protein kinase receptor TIE-2, mTIE2, p140 TEK, CD202b.

    Product # :

    PKA-079

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    Description

    MAP2K6 produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 340 amino acids (1-334 a.a.) and having a molecular mass of 38.3kDa (Migrates at 40-57kDa on SDS-PAGE under reducing conditions).MAP2K6 is expressed with a 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    MAP2K6 protein solution (1mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 20% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Mitogen-Activated Protein Kinase 6 (MAP2K6) is a part of the dual specificity protein kinase family. MAP2K6 phosphorylates and activates p38 MAP kinase in response to inflammatory cytokines or environmental stress. MAP2K6 is a vital component of the MAP kinase signal transduction pathway. MAP2K6 takes part in various cellular processes such as stress induced cell cycle arrest and apoptosis.

    • Synonyms

      Angiopoietin-1 receptor, Endothelial tyrosine kinase, HYK, STK1, Tunica interna endothelial cell kinase, Tyrosine kinase with Ig and EGF homology domains-2, Tyrosine-protein kinase receptor TEK, Tyrosine-protein kinase receptor TIE-2, mTIE2, p140 TEK, CD202b.

    • 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

      MSQSKGKKRN PGLKIPKEAF EQPQTSSTPP RDLDSKACIS IGNQNFEVKA DDLEPIMELG RGAYGVVEKM RHVPSGQIMA VKRIRATVNS QEQKRLLMDL DISMRTVDCP FTVTFYGALF REGDVWICME LMDTSLDKFY KQVIDKGQTI PEDILGKIAV SIVKALEHLH SKLSVIHRDV KPSNVLINAL GQVKMCDFGI SGYLVDSVAK TIDAGCKPYM APERINPELN QKGYSVKSDI WSLGITMIEL AILRFPYDSW GTPFQQLKQV VEEPSPQLPA DKFSAEFVDF TSQCLKKNSK ERPTYPELMQ HPFFTLHESK GTDVASFVKL ILGDHHHHHH.

    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.

    Map2K6 Human Sf9
  • View Data Sheet

    Description:

    Purine-Rich Element Binding Protein B Human Recombinant

    Transcriptional activator protein Pur-beta, Purine-rich element-binding protein B, PURB, PURBETA.

    Product # :

    PRO-1969

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    Description

    PURB Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 335 amino acids (1-312) and having a molecular mass of 35.6 kDa.PURB is fused to a 23 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

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

    Purity

    Greater than 95% as determined by SDS-PAGE.

    More Info

    • Introduction

      Purine-Rich Element Binding Protein B (PURB) is a single-stranded DNA-binding protein which takes part in the dendritic transport of a subset of mRNAs. PURB operates as repressor in myoblasts and fibroblasts in the control of vascular smooth muscle alpha-actin gene transcription. PURB binds preferentially to the single strand of the purine-rich element termed PUR, which is present at origins of replication and in gene flanking regions in various eukaryotes from yeasts through humans.

    • Synonyms

      Transcriptional activator protein Pur-beta, Purine-rich element-binding protein B, PURB, PURBETA.

    • 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 MGSMADGDSG SERGGGGGPC GFQPASRGGG EQETQELASK RLDIQNKRFY LDVKQNAKGR FLKIAEVGAG GSKSRLTLSM AVAAEFRDSL GDFIEHYAQL GPSSPEQLAA GAEEGGGPRR ALKSEFLVRE NRKYYLDLKE NQRGRFLRIR QTVNRGGGGF GAGPGPGGLQ SGQTIALPAQ GLIEFRDALA KLIDDYGGED DELAGGPGGG AGGPGGGLYG ELPEGTSITV DSKRFFFDVG CNKYGVFLRV SEVKPSYRNA ITVPFKAWGK FGGAFCRYAD EMKEIQERQR DKLYERRGGG SGGGEESEGE EVDED.

    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.

    Purb Human
  • View Data Sheet

    Description:

    Angiopoietin-like Protein 2 Human Recombinant

    Angiopoietin-related protein 2, Angiopoietin-like protein 2, ANGPTL2, ARP2, HARP.

    Product # :

    CYT-765

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    • sds-page

    Description

    ANGPTL2 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 493 amino acids ( 22-493 a.a.) including a 20 a.a N-terminal His tag. The total molecular mass is 57.1kDa (calculated).

    Source

    Escherichia Coli.

    Formulation

    ANGPTL2 protein solution (0.5mg/ml) contains 20mM Tris HCL (pH7-8) and 10% glycerol.

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

    sds-page

    More Info

    • Introduction

      Angiopoietins belong to the vascular endothelial growth factor family and the only known growth factors largely specific for vascular endothelium. Angiopoietins-1, 2 and 4 partake in the formation of blood vessels. ANGPTL2 displays angiogenic effects. Angiopoietin-like Protein 2 (ANGPTL2) is an anti-diabetic factor. ANGPTL2 induces sprouting in endothelial cells through an autocrine and paracrine action. ANGPTL2 increases insulin sensitivity in adipocytes. In addition, ANGPTL2 is a mediator of chronic adipose tissue inflammation. ANGPTL2 is widely expressed in the heart, small intestine, spleen and stomach. ANGPTL2 is also found in lower levels in the colon, ovary, adrenal gland, skeletal muscle and in prostate.

    • Synonyms

      Angiopoietin-related protein 2, Angiopoietin-like protein 2, ANGPTL2, ARP2, HARP.

    • 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 MGQEDGFEGT EEGSPREFIY LNRYKRAGES QDKCTYTFIV PQQRVTGAIC VNSKEPEVLL ENRVHKQELE LLNNELLKQK RQIETLQQLV EVDGGIVSEV KLLRKESRNM NSRVTQLYMQ LLHEIIRKRD NALELSQLEN RILNQTADML QLASKYKDLE HKYQHLATLA HNQSEIIAQL EEHCQRVPSA RPVPQPPPAA PPRVYQPPTY NRIINQISTN EIQSDQNLKV LPPPLPTMPT LTSLPSSTDK PSGPWRDCLQ ALEDGHDTSS IYLVKPENTN RLMQVWCDQR HDPGGWTVIQ RRLDGSVNFF RNWETYKQGF GNIDGEYWLG LENIYWLTNQ GNYKLLVTME DWSGRKVFAE YASFRLEPES EYYKLRLGRY HGNAGDSFTW HNGKQFTTLD RDHDVYTGNC AHYQKGGWWY NACAHSNLNG VWYRGGHYRS RYQDGVYWAE FRGGSYSLKK VVMMIRPNPN TFH

    • Background

      Angiopoietin-like Protein 2 Human Recombinant: A Potential Therapeutic Target for Metabolic and Cardiovascular Disorders

      Abstract:

      Angiopoietin-like protein 2 (ANGPTL2) has emerged as a crucial regulator in metabolic and cardiovascular disorders. This multifunctional protein is involved in various biological processes, including angiogenesis, adipose tissue function, and inflammation. The availability of human recombinant ANGPTL2 protein has provided researchers with a valuable tool to explore its therapeutic potential. This concise review provides an overview of the role of ANGPTL2 in metabolic and cardiovascular health and discusses the potential of ANGPTL2 human recombinant protein as a therapeutic target.

      Introduction:

      Metabolic disorders, such as obesity and type 2 diabetes, are closely associated with cardiovascular diseases and pose significant global health challenges. ANGPTL2, a member of the angiopoietin-like protein family, has gained attention for its involvement in metabolic regulation and cardiovascular homeostasis. Through interactions with various receptors and signaling pathways, ANGPTL2 influences lipid metabolism, insulin sensitivity, inflammation, and vascular integrity.

      Mechanisms of ANGPTL2 Action:

      ANGPTL2 acts through binding to integrins, toll-like receptors (TLRs), and other receptors on different cell types, including adipocytes, endothelial cells, and immune cells. By influencing angiogenesis, inflammation, and extracellular matrix remodeling, ANGPTL2 affects adipose tissue function, lipid metabolism, and insulin signaling.

      Role of ANGPTL2 in Metabolic Regulation:

      ANGPTL2 plays a critical role in metabolic regulation and the development of metabolic disorders. It promotes adipose tissue inflammation, impairs adipogenesis, and alters adipokine secretion, contributing to metabolic dysfunction. Furthermore, ANGPTL2 modulates lipid metabolism by regulating lipoprotein lipase activity, affecting triglyceride clearance, and promoting hepatic lipid accumulation.

      ANGPTL2 in Cardiovascular Health and Disease:

      Increasing evidence suggests that ANGPTL2 is implicated in cardiovascular diseases, including atherosclerosis and heart failure. ANGPTL2 promotes vascular inflammation, endothelial dysfunction, and smooth muscle cell proliferation, which contribute to atherosclerotic plaque progression and vascular remodeling. Additionally, ANGPTL2 influences cardiac remodeling and fibrosis, impacting heart failure development.

      Therapeutic Potential of ANGPTL2 Human Recombinant Protein:

      The availability of ANGPTL2 human recombinant protein opens avenues for therapeutic interventions targeting metabolic and cardiovascular disorders. Preclinical studies employing ANGPTL2 blockade or supplementation have shown promising results in improving metabolic parameters, reducing atherosclerosis, and preserving cardiac function. However, further research is needed to optimize the clinical application of ANGPTL2 human recombinant protein, including dosage, timing, and delivery methods.

      Conclusion:

      ANGPTL2 holds promise as a therapeutic target for metabolic and cardiovascular disorders. Its involvement in key biological processes makes it an attractive candidate for interventions aiming to improve metabolic health and prevent cardiovascular complications. The development of ANGPTL2 human recombinant protein provides a valuable tool for investigating its therapeutic potential further.

      What is the molecular weight/Mw of ANGPTL2 Protein?
      ANGPTL2 Protein has a total Mw of 57.1kDa.

      What is the source or expression system of ANGPTL2 Protein?
      Escherichia Coli.

      What is the Purity of ANGPTL2 Protein?
      ANGPTL2 Protein is >85% pure as determined by SDS-PAGE.

      What is the Biological Activity of ANGPTL2 Protein?
      The biological functionality of ANGPTL2 Protein will be determined in the future.

      What is the amino acid sequence of ANGPTL2 Protein?
      MGSSHHHHHH SSGLVPRGSH MGQEDGFEGT EEGSPREFIY LNRYKRAGES QDKCTYTFIV PQQRVTGAIC VNSKEPEVLL ENRVHKQELE LLNNELLKQK RQIETLQQLV EVDGGIVSEV KLLRKESRNM NSRVTQLYMQ LLHEIIRKRD NALELSQLEN RILNQTADML QLASKYKDLE HKYQHLATLA HNQSEIIAQL EEHCQRVPSA RPVPQPPPAA PPRVYQPPTY NRIINQISTN EIQSDQNLKV LPPPLPTMPT LTSLPSSTDK PSGPWRDCLQ ALEDGHDTSS IYLVKPENTN RLMQVWCDQR HDPGGWTVIQ RRLDGSVNFF RNWETYKQGF GNIDGEYWLG LENIYWLTNQ GNYKLLVTME DWSGRKVFAE YASFRLEPES EYYKLRLGRY HGNAGDSFTW HNGKQFTTLD RDHDVYTGNC AHYQKGGWWY NACAHSNLNG VWYRGGHYRS RYQDGVYWAE FRGGSYSLKK VVMMIRPNPN TFH

      What applications can ANGPTL2 Protein be used in?
      ANGPTL2 Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for ANGPTL2 Protein?
      The endotoxin level is minimal, ANGPTL2 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.

    Angptl2 Human
  • View Data Sheet

    Description:

    SLAMF7 Human Recombinant

    SLAMF7, SLAM Family Member 7, CD2-Like Receptor-Activating Cytotoxic Cells, Membrane Protein FOAP-12, CD2 Subset 1, Protein 19A, CRACC, CS1, Novel LY9 (Lymphocyte Antigen 9) Like Protein, CD2-Like Receptor Activating Cytotoxic Cells, 19A24 Protein, CD319 Antigen, Novel Ly9, CD319, 19A.

    Product # :

    PRO-2261

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    Description

    SLAMF7 produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 212 amino acids (23-226a.a.) and having a molecular mass of 23.4kDa (Molecular size on SDS-PAGE will appear at approximately 28-40kDa). SLAMF7 is expressed with an 8 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    SLAMF7 protein solution (0.5mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 10% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      SLAMF7 belongs to the CS2 family of cell surface receptors. SLAMF7 is a single-pass type 1 membrane protein, SLAMF7 Isoform 1 mediates NK cell activation via aSH2D1A-independent extracellular signal-regulated ERK-mediated pathway. SLAMF7 functions in lymphocyteadhesion. Furthermore, SLAMF7 can exert activating of inhibitory influences on cells of the immune system depending on cellular context as well as the availability of effector proteins.

    • Synonyms

      SLAMF7, SLAM Family Member 7, CD2-Like Receptor-Activating Cytotoxic Cells, Membrane Protein FOAP-12, CD2 Subset 1, Protein 19A, CRACC, CS1, Novel LY9 (Lymphocyte Antigen 9) Like Protein, CD2-Like Receptor Activating Cytotoxic Cells, 19A24 Protein, CD319 Antigen, Novel Ly9, CD319, 19A.

    • 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

      SGPVKELVGS VGGAVTFPLK SKVKQVDSIV WTFNTTPLVT IQPEGGTIIV TQNRNRERVD FPDGGYSLKL SKLKKNDSGI YYVGIYSSSL QQPSTQEYVL HVYEHLSKPK VTMGLQSNKN GTCVTNLTCC MEHGEEDVIY TWKALGQAAN ESHNGSILPI SWRWGESDMT FICVARNPVS RNFSSPILAR KLCEGAADDP DSSMLEHHHH HH.

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

    Slamf7 Human
  • View Data Sheet

    Description:

    Interleukin-2 Receptor alpha Human Recombinant, sf9

    Interleukin 2 Receptor Subunit Alpha, Interleukin 2 Receptor, Alpha, IL-2 Receptor Subunit Alpha, IL-2R Subunit Alpha, TAC Antigen, P55, Insulin-Dependent Diabetes Mellitus 10, Interleukin-2 Receptor Subunit Alpha, CD25 Antigen, IL-2-RA, IDDM10, IL2-RA, IMD41, TCGFR, CD25, IL2R.

    Product # :

    CYT-1020

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    Description

    IL2RA produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 461 amino acids (22-240 a.a.) and having a molecular mass of 52.1kDa (Molecular size on SDS-PAGE will appear at approximately 50-70kDa).IL2RA is expressed with a 239 amino acid hIgG-His tag at C-Terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    IL2RA protein solution (0.5mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 10% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • 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

      Interleukin 2 Receptor Subunit Alpha, Interleukin 2 Receptor, Alpha, IL-2 Receptor Subunit Alpha, IL-2R Subunit Alpha, TAC Antigen, P55, Insulin-Dependent Diabetes Mellitus 10, Interleukin-2 Receptor Subunit Alpha, CD25 Antigen, IL-2-RA, IDDM10, IL2-RA, IMD41, TCGFR, CD25, IL2R.

    • 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

      ADPELCDDDP PEIPHATFKA MAYKEGTMLN CECKRGFRRI KSGSLYMLCT GNSSHSSWDN QCQCTSSATR NTTKQVTPQP EEQKERKTTE MQSPMQPVDQ ASLPGHCREP PPWENEATER IYHFVVGQMV YYQCVQGYRA LHRGPAESVC KMTHGKTRWT QPQLICTGEM ETSQFPGEEK PQASPEGRPE SETSCLVTTT DFQIQTEMAA TMETSIFTTE YQLEPKSCDK THTCPPCPAP ELLGGPSVFL FPPKPKDTLM ISRTPEVTCV VVDVSHEDPE VKFNWYVDGV EVHNAKTKPR EEQYNSTYRV VSVLTVLHQD WLNGKEYKCK VSNKALPAPI EKTISKAKGQ PREPQVYTLP PSRDELTKNQ VSLTCLVKGF YPSDIAVEWE SNGQPENNYK TTPPVLDSDG SFFLYSKLTV DKSRWQQGNV FSCSVMHEAL HNHYTQKSLS LSPGKHHHHH 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.

    Il2Ra Protein
  • View Data Sheet

    Description:

    Macrophage Inflammatory Protein-4 Human Recombinant (CCL18)

    Small inducible cytokine A18, CCL18, Macrophage inflammatory protein 4, MIP-4, Pulmonary and activation-regulated chemokine, CC chemokine PARC, Alternative macrophage activation-associated CC chemokine 1, AMAC-1, Dendritic cell chemokine 1, DC-CK1, chemokine (C-C motif) ligand 18, CKb7, PARC, AMAC1, DCCK1, SCYA18.

    Product # :

    CHM-322

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    Description

    Macrophage Inflammatory Protein-4 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 69 amino acids and having a molecular mass of 7813 Dalton. The MIP-4 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    MIP-4 protein is lyophilized from a 0.2µm filtered concentrated (1.0mg/ml) solution in 20mM PB, pH 7.4, 100mM NaCl.

    Purity

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

    Biological Activity

    The Activity MIP-4 is calculated by the ability to chemoattract Human T lymphocytes at 1-10ng/ml corresponding to a Specific Activity of 100,000-1,000,000IU/mg.

    More Info

    • Introduction

      Chemokine (C-C motif) ligand 18 (CCL18 / MIP-4) is a small cytokine belonging to the CC chemokine family that was previously called PARC (pulmonary and activation-regulated chemokine). MIP-4 is approximately 60% identical in amino acid sequence to CCL3. MIP-4 is expressed at high levels in lung and at lower levels in certain lymphoid tissues, such as the lymph nodes, and is chemotactic for activated T cells and non activated lymphocytes. The gene for human CCL18 contains three exons and is located on chromosome 17.

    • Synonyms

      Small inducible cytokine A18, CCL18, Macrophage inflammatory protein 4, MIP-4, Pulmonary and activation-regulated chemokine, CC chemokine PARC, Alternative macrophage activation-associated CC chemokine 1, AMAC-1, Dendritic cell chemokine 1, DC-CK1, chemokine (C-C motif) ligand 18, CKb7, PARC, AMAC1, DCCK1, SCYA18.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized MIP-4 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution MIP-4 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 MIP-4 in sterile 18M-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 of MIP-4 was determined and found to be Ala-Gln-Val-Gly-Thr.

    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.

    Mip 4 Human
  • View Data Sheet

    Description:

    Interleukin 1 Family, Member 10 Human Recombinant, His Tag

    Interleukin-1 family member 10, IL-1F10, FIL1 theta, Interleukin-1 HY2, IL-1HY2, Interleukin-1 theta, IL-1 theta, IL1F10, FIL1T, IL1HY2, FKSG75, MGC119831, MGC119832, MGC119833, FIL1-theta.

    Product # :

    CYT-783

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    Description

    IL1F10 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 172 amino acids (1-152) and having a molecular mass of 19.1kDa.IL1F10 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The IL1F10 solution contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 1mM DTT and 20% glycerol.

    Purity

    Greater than 85% as determined by SDS-PAGE.

    More Info

    • Introduction

      Human interleukin family 1, member 10 (IL1F10) belongs to the interleukin 1 cytokine family. IL1F10 is expressed in the fetal skin, spleen and tonsil, generally in the basal epithelia of skin and in proliferating B-cells of the tonsil. IL1F10 binds soluble IL1 receptor type 1 and may be implicated in the regulation of adapted and innate immune responses.

    • Synonyms

      Interleukin-1 family member 10, IL-1F10, FIL1 theta, Interleukin-1 HY2, IL-1HY2, Interleukin-1 theta, IL-1 theta, IL1F10, FIL1T, IL1HY2, FKSG75, MGC119831, MGC119832, MGC119833, FIL1-theta.

    • 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 MCSLPMARYY IIKYADQKAL YTRDGQLLVG DPVADNCCAE KICTLPNRGL DRTKVPIFLG IQGGSRCLAC VETEEGPSLQ LEDVNIEELY KGGEEATRFT FFQSSSGSAF RLEAAAWPGW FLCGPAEPQQ PVQLTKESEP SARTKFYFEQ SW

    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.

    Il1F10 Human His
  • View Data Sheet

    Description:

    Platelet-activating Factor Acetylhydrolase 1b, Catalytic Subunit 3 Human Recombinant

    Platelet-activating factor acetylhydrolase 1b catalytic subunit 3 (29kDa), PAF acetylhydrolase 29 kDa subunit, platelet-activating factor acetylhydrolase, isoform Ib gamma subunit (29kD), PAF-AH1b alpha 1 subunit, PAF-AH 29 kDa subunit, PAFAHG, PAFAH subunit gamma, EC 3.1.1.47.

    Product # :

    ENZ-641

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    Description

    PAFAH1B3 Human Recombinant produced in E. coli is a single polypeptide chain containing 254 amino acids (1-231) and having a molecular mass of 28.2 kDa.PAFAH1B3 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    The PAFAH1B3 solution (1mg/1ml) contains 20mM Tris-HCl buffer (pH 8.0), 100mM NaCl and 10% glycerol.

    Purity

    Greater than 95% as determined by SDS-PAGE.

    More Info

    • Introduction

      Platelet-activating Factor Acetylhydrolase 1b Catalytic Subunit 3 (PAFAH1B3) is a member of the 'GDSL' lipolytic enzyme family. Acetylhydrolase catalyzes the elimination of an acetyl group from the glycerol backbone of platelet-activating factor. PAFAH1B3, which is a subunit of the platelet-activating factor cetylhydrolase isoform 1B complex, is comprised of the catalytic beta and gamma subunits and the regulatory alpha subunit. The PAFAH1B3 complex has an imperative role during the development of brain.

    • Synonyms

      Platelet-activating factor acetylhydrolase 1b catalytic subunit 3 (29kDa), PAF acetylhydrolase 29 kDa subunit, platelet-activating factor acetylhydrolase, isoform Ib gamma subunit (29kD), PAF-AH1b alpha 1 subunit, PAF-AH 29 kDa subunit, PAFAHG, PAFAH subunit gamma, EC 3.1.1.47.

    • 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 MGSMSGEENP ASKPTPVQDV QGDGRWMSLH HRFVADSKDK EPEVVFIGDS LVQLMHQCEI WRELFSPLHA LNFGIGGDGT QHVLWRLENG ELEHIRPKIV VVWVGTNNHG HTAEQVTGGI KAIVQLVNER QPQARVVVLG LLPRGQHPNP LREKNRQVNE LVRAALAGHP RAHFLDADPG FVHSDGTISH HDMYDYLHLS RLGYTPVCRA LHSLLLRLLA QDQGQGAPLL EPAP

    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.

    Pafah1B3 Human
  • View Data Sheet

    Description:

    Interleukin 18 Receptor Accessory Protein Human Recombinant

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

    Product # :

    CYT-1050

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    Description

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

    Source

    Sf9, Insect cells.

    Formulation

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

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

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

    • Synonyms

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

    • Physical Appearance

      Sterile filtered colorless solution.

    • Stability

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

    • Amino Acid Sequence

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

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

    Il18Rap Human
  • View Data Sheet

    Description:

    LAG-1 Human Recombinant (CCL4L1)

    C-C motif chemokine 4-like, Lymphocyte activation gene 1 protein, LAG-1, Macrophage inflammatory protein 1-beta, MIP-1-beta, Monocyte adherence-induced protein 5-alpha, Small-inducible cytokine A4-like, CCL4L1, CCL4L, LAG1, SCYA4L1, CCL4L2, SCYA4L2, AT744.2.

    Product # :

    CHM-018

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    Description

    LAG-1 Human Recombinant produced in E.Coli is a single, non-glycosylated, Polypeptide chain containing 69 amino acids and having a molecular mass of 7.8kDa.The CCL4L1 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    LAG-1 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 ED50 as determined by a cell proliferation assay using human CCR5 transfected murine BaF3 cells is less than 2.0 ng/ml, corresponding to a specific activity of > 5.0 × 105 IU/mg.

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    • Introduction

      CCL4L1 (C-C motif chemokine 4-like) is a member of to intercrine beta (chemokine CC) family. The CCL4L1 protein is similar to CCL4 which inhibits HIV replication in peripheral blood monocytes which express CCR5.

    • Synonyms

      C-C motif chemokine 4-like, Lymphocyte activation gene 1 protein, LAG-1, Macrophage inflammatory protein 1-beta, MIP-1-beta, Monocyte adherence-induced protein 5-alpha, Small-inducible cytokine A4-like, CCL4L1, CCL4L, LAG1, SCYA4L1, CCL4L2, SCYA4L2, AT744.2.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized LAG-1 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution CCL4L1 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 LAG-1 in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      APMGSDPPTA CCFSYTARKL PRNFVVDYYE TSSLCSQPAV VFQTKRGKQV CADPSESWVQ EYVYDLELN.

    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.

    Lag 1 Human
  • View Data Sheet

    Description:

    Follistatin Human Recombinant

    FST, FS

    Product # :

    CYT-232

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    Description

    Follistatin Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 288 amino acids and having a total molecular mass of 31.5kDa.The FST is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

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

    Purity

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

    Biological Activity

    The activity is determined by the ability to neutralize ACTV inhibitory effect of mouse MPC-11 cells. The expected ED50 is 100-400ng/ml, corresponding to a Specific Activity of 2,500-10,000units/mg in the presence of 7.5ng/ml ACTV A.

    More Info

    • Introduction

      Follistatin is a single-chain gonadal protein that specifically inhibits follicle-stimulating hormone release. The single FST gene encodes two isoforms, FST317 and FST344 containing 317 and 344 amino acids respectively, resulting from alternative splicing of the precursor mRNA. In a study in which 37 candidate genes were tested for linkage and association with polycystic ovary syndrome (PCOS) or hyperandrogenemia in 150 families, evidence was found for linkage between PCOS and follistatin. Follistatin functions as an ACTV antagonist. specific inhibitor of the biosynthesis and secretion of pituitary follicle stimulating hormone (fsh).

    • Synonyms

      FST, FS

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Amino Acid Sequence

      The sequence of the first five N-terminal amino acids was determined and was found to be Gly-Asn-Cys-Trp-Leu.

    • Background

      What is the molecular weight/Mw of FOLLISTATIN HUMAN Protein?
      FOLLISTATIN HUMAN Protein has a total Mw of 31.5kDa.

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

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

      What is the Biological Activity of FOLLISTATIN HUMAN Protein?
      The activity is determined by the ability to neutralize ACTV inhibitory effect of mouse MPC-11 cells. The expected ED50 is 100-400ng/ml, corresponding to a Specific Activity of 2,500-10,000units/mg in the presence of 7.5ng/ml ACTV A.

      What is the amino acid sequence of FOLLISTATIN HUMAN Protein?
      The sequence of the first five N-terminal amino acids was determined and was found to be Gly-Asn-Cys-Trp-Leu.

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

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

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

    Follistatin Human
  • View Data Sheet

    Description:

    Protein Kinase, AMP-Activated, Beta 1 non-Catalytic Subunit Human Recombinant

    AMPK, HAMPKb, 5'-AMP-activated protein kinase subunit beta-1, AMPK subunit beta-1, AMPKb,PRKAB1.

    Product # :

    PKA-026

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    Description

    PRKAB1 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 293 amino acids (1-270 a.a.) and having a molecular mass of 32.8 kDa. The PRKAB1 is fused to a 23 amino acid His Tag at N-Terminus and purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    The PRKAB1 protein solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 10% glycerol and 1mM DTT.

    Purity

    Greater than 85% as determined by SDS-PAGE.

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    • Introduction

      5'-AMP-activated protein kinase subunit beta-1 (PRKAB1) hinders protein, carbohydrate and lipid biosynthesis, in addition to cell growth and proliferation. AMPK is a heterotrimer comprised of an alpha catalytic subunit, and non-catalytic beta and gamma subunits. AMPK acts via direct phosphorylation of metabolic enzymes, and longer-term effects by phosphorylation of transcription regulators. PRKAB1 is a regulator of cellular polarity by remodeling the actin cytoskeleton; most likely by indirectly activating myosin. Beta non-catalytic subunit acts as a scaffold on which the AMPK complex compiles, through its C-terminus that joins alpha (PRKAA1 or PRKAA2) and gamma subunits (PRKAG1, PRKAG2 or PRKAG3).

    • Synonyms

      AMPK, HAMPKb, 5'-AMP-activated protein kinase subunit beta-1, AMPK subunit beta-1, AMPKb,PRKAB1.

    • 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 MGSMGNTSSE RAALERHGGH KTPRRDSSGG TKDGDRPKIL MDSPEDADLF HSEEIKAPEK EEFLAWQHDL EVNDKAPAQA RPTVFRWTGG GKEVYLSGSF NNWSKLPLTR SHNNFVAILD LPEGEHQYKF FVDGQWTHDP SEPIVTSQLG TVNNIIQVKK TDFEVFDALM VDSQKCSDVS ELSSSPPGPY HQEPYVCKPE ERFRAPPILP PHLLQVILNK DTGISCDPAL LPEPNHVMLN HLYALSIKDG VMVLSATHRY KKKYVTTLLY KPI

    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.

    Prkab1 Human