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172 results found for “SDF (CXCL12)”

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  • View Data Sheet

    Description:

    Granulocyte-Colony Stimulating Factor Human Recombinant

    CSF-3, MGI-1G, GM-CSF beta, Pluripoietin, Lenograstim, G-CSF, MGC45931, GCSF.

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    CYT-220

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    Description

    Granulocyte Colony Stimulating Factor Human Recombinant produced in E.coli is a single, non-glycosylated, polypeptide chain containing 175 amino acids and having a molecular mass of 18.8 KD.GCSF is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    GCSF was lyophilized after extensive dialysis against 10mM sodium acetate buffer pH= 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 NFS-60 indicator cells (measured by 3H-thymidine uptake) is < 0.1 ng/ml, corresponding to a Specific Activity of 100,000,000 IU/mg.

    More Info

    • Introduction

      GCSF is a cytokine that controls the production, differentiation, and function of granulocytes. The active protein is found extracellularly. Three transcript variants encoding three different isoforms have been found for the GCSF gene. 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. This csf induces granulocytes.

    • Synonyms

      CSF-3, MGI-1G, GM-CSF beta, Pluripoietin, Lenograstim, G-CSF, MGC45931, GCSF.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized GCSF although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution GCSF 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 GCSF in sterile 20mM AcOH 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 GCSF was determined and was found to be Met-Thr-Pro-Leu-Gly.

    • Background

      What is the molecular weight/Mw of GDF15 HUMAN, HIS Protein?
      GDF15 HUMAN, HIS Protein has a total Mw of 18.8kDa.

      What is the source or expression system of GDF15 HUMAN, HIS Protein?
      Escherichia Coli.

      What is the Purity of GDF15 HUMAN, HIS Protein?
      GDF15 HUMAN, HIS Protein is >98% pure as determined by SDS-PAGE.

      What is the Biological Activity of GDF15 HUMAN, HIS Protein?
      The ED50, calculated by the dose-dependant proliferation of murine NFS-60 indicator cells (measured by 3H-thymidine uptake) is < 0.1 ng/ml, corresponding to a Specific Activity of 100,000,000 IU/mg.

      What is the amino acid sequence of GDF15 HUMAN, HIS Protein?
      GDF15 HUMAN, HIS Protein is composed from 175 amino acids.

      What applications can GDF15 HUMAN, HIS Protein be used in?
      GDF15 HUMAN, HIS Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for GDF15 HUMAN, HIS Protein?
      The endotoxin level is minimal, GDF15 HUMAN, HIS Protein was purified using conventional chromatography techniques.

    • Protein content

      GCSF quantitation was carried out by two independent methods:1. UV spectroscopy at 280 nm using the absorbency value of 0.815 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 calibrated solution of GCSF 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.

    G Csf Human
  • View Data Sheet

    Description:

    Sarcoglycan Delta Human Recombinant

    35DAG, CMD1L, DAGD, SG-delta, SGCDP, SGD, Delta-sarcoglycan, 35 kDa dystrophin-associated glycoprotein.

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    PRO-1373

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    Description

    SGCD Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 257 amino acids (57-289a.a) and having a molecular mass of 28kDa. SGCD is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    SGCD protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.4M Urea and 10% glycerol.

    Purity

    Greater than 85% as determined by SDS-PAGE.

    More Info

    • Introduction

      Sarcoglycan Delta (SGCD) is one of the four known components of the sarcoglycan complex, which is a subcomplex of the dystrophin-glycoprotein complex (DGC) and is expressed mainly in skeletal and cardiac muscle. DGC forms a link between the F-actin cytoskeleton and the extracellular matrix. SGCD protein’s mutations have been associated with autosomal recessive limb-girdle muscular dystrophy and dilated cardiomyopathy. SGCD gene expression is regulated by MITF In melanocytic cells.

    • Synonyms

      35DAG, CMD1L, DAGD, SG-delta, SGCDP, SGD, Delta-sarcoglycan, 35 kDa dystrophin-associated glycoprotein.

    • 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 RSHMKVMNFT IDGMGNLRIT EKGLKLEGDS EFLQPLYAKE IQSRPGNALY FKSARNVTVN ILNDQTKVLT QLITGPKAVE AYGKKFEVKT VSGKLLFSAD NNEVVVGAER LRVLGAEGTV FPKSIETPNV RADPFKELRL ESPTRSLVME APKGVEINAE AGNMEATCRT ELRLESKDGE IKLDAAKIRL PRLPHGSYTP TGTRQKVFEI CVCANGRLFL SQAGAGSTCQ INTSVCL.

    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.

    Sgcd Human
  • View Data Sheet

    Description:

    Soluble CD-40 Ligand/TRAP Human Recombinant

    CD40-L, Tumor necrosis factor ligand superfamily member 5, TNF-related activation protein, TRAP, T cell antigen Gp39, CD154 antigen, sCD40, IGM, IMD3, HIGM1, T-BAM, TNFSF5, hCD40L.

    Product # :

    CYT-245

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    Description

    sCD40L Human Recombinant produced in E.Coli is a non-glycosylated, Polypeptide chain containing 149 amino acids and having a molecular mass of 16308 Dalton. The sCD40L is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Lyophilized from a 0.2µm filtered concentrated (1mg/ml) solution in PBS, pH 7.0.

    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 the dose-dependant stimulation of IL-12 induction & IL-8 production by human PBMC was found to be 5-10 ng/ml.

    More Info

    • Introduction

      CD40L or CD154 is a membrane glycoprotein and differentiation antigen expressed on the surface of T-cells. The CD40 ligand stimulates B-cell proliferation and secretion of all immunoglobulin isotypes in the presence of cytokines . CD40 ligand has been shown to induce cytokine production and tumoricidal activity in peripheral blood monocytes. It also costimulates proliferation of activated T-cells and this is accompanied by the production of IFN-gamma , TNF-alpha , and IL2 .

    • Synonyms

      CD40-L, Tumor necrosis factor ligand superfamily member 5, TNF-related activation protein, TRAP, T cell antigen Gp39, CD154 antigen, sCD40, IGM, IMD3, HIGM1, T-BAM, TNFSF5, hCD40L.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized sCD40L although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution CD154 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 sCD40L in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Protein content

      Protein quantitation was carried out by two independent methods:1. UV spectroscopy at 280 nm using the absorbency value of 1.1 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 CD40 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.

    Cd40 Human
  • View Data Sheet

    Description:

    Macrophage Colony Stimulating Factor Human Recombinant, Baculovirus

    CSF-1, Lanimostim, MCSF, MGC31930, M-CSF, Macrophage colony-stimulating factor 1, CSF1.

    Product # :

    CYT-637

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    Description

    Macrophage Colony Stimulating Factor Human Recombinant produced in Baculovirus is a disulfide linked homodimer, glycosylated, polypeptide chain containing 2 x 149 amino acids and having a total molecular mass of 42 kDa.MCSF is purified by proprietary chromatographic techniques.

    Source

    Baculovirus infected Silkworm.

    Formulation

    The lyophilized protein (1mg/ml) was lyophilized with 20mM phosphate buffer, 1% HSA and 3% manntiol.

    Purity

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

    Biological Activity

    The ED50, calculated by the dose-dependant stimulation of the proliferation of murine M-NFS-60 indicator cells was found < 3ng/ml, corresponding to a specific activity of less than 333,333.33units/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, MGC31930, M-CSF, Macrophage colony-stimulating factor 1, CSF1.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized Macrophage Colony Stimulating Factor 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

      EEVSEYCSHM IGSGHLQSLQ RLIDSQMETS CQITFEFVDQ EQLKDPVCYL KKAFLLVQDI MEDTMRFRDN TPNAIAIVQL QELSLRLKSC FTKDYEEHDK ACVRTFYETP LQLLEKVKNV FNETKNLLDK DWNIFSKNCN NSFAECSSQ.

    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.

    Mcsf Human Baculovirus
  • View Data Sheet

    Description:

    Sterile Alpha Motif Domain Containing 13 Human Recombinant

    Sterile alpha motif domain-containing protein 13, SAM domain-containing protein 13, SAMD13, HSD-42, HSD42, RP11-376N17.1.

    Product # :

    PRO-355

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    Description

    SAMD13 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 125 amino acids (1-102 a.a) and having a molecular mass of 13.8kDa.SAMD13 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    SAMD13 protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.2M NaCl, 50% glycerol and 1mM DTT.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Sterile Alpha Motif Domain Containing 13 (SAMD13) is a putative protein interaction module which is present in various proteins involved in numerous biological processes. SAMD13 contains one SAM (sterile alpha motif) domain. The SAM domain, which spreads over around 70 residues, is found in various eukaryotic organisms. SAM domains are known to homo- and hetero-oligomerise, forming multiple self-association constructions and also binding to various non-SAM domain-containing proteins, however with a low affinity constant.

    • Synonyms

      Sterile alpha motif domain-containing protein 13, SAM domain-containing protein 13, SAMD13, HSD-42, HSD42, RP11-376N17.1.

    • 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 MGSMLSVDME NKENGSVGVK NSMENGRPPD PADWAVMDVV NYFRTVGFEE QASAFQEQEI DGKSLLLMTR NDVLTGLQLK LGPALKIYEY HVKPLQTKHL KNNSS.

    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.

    Samd13 Human
  • View Data Sheet

    Description:

    Sclerostin Domain Containing 1 Human Recombinant

    Sclerostin domain-containing protein 1, Ectodermal BMP inhibitor, Ectodin, Uterine sensitization-associated gene 1 protein, USAG-1, SOSTDC1, USAG1, CDA019.

    Product # :

    PRO-426

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    Description

    SOSTDC1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 206 amino acids (24-206 a.a) and having a molecular mass of 23kDa.SOSTDC1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    SOSTDC1 protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.4M UREA and 10% glycerol.

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Sclerostin Domain Containing 1 (SOSTDC1) belongs to the sclerostin family and an N-glycosylated, secreted protein with a C-terminal cystine knot-like domain. The SOSTDC1 protein acts as a bone morphogenetic protein (BMP) antagonist. Specifically, SOSTDC1 directly associates with BMPs, prohibiting them from binding their receptors, thus regulating BMP signaling throughout cellular proliferation, differentiation, and programmed cell death. SOSTDC1 may also be involved in the onset of endometrial receptivity for implantation/sensitization for the decidual cell reaction Enhances Wnt signaling and hinders TGF-beta signaling. In addition, SOSTDC1 directly antagonizes the activity of BMP2, BMP4, BMP6 and BMP7 in a dose-dependent manner.

    • Synonyms

      Sclerostin domain-containing protein 1, Ectodermal BMP inhibitor, Ectodin, Uterine sensitization-associated gene 1 protein, USAG-1, SOSTDC1, USAG1, CDA019.

    • 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 MGSFKNDATE ILYSHVVKPV PAHPSSNSTL NQARNGGRHF SNTGLDRNTR VQVGCRELRS TKYISDGQCT SISPLKELVC AGECLPLPVL PNWIGGGYGT KYWSRRSSQE WRCVNDKTRT QRIQLQCQDG STRTYKITVV TACKCKRYTR QHNESSHNFE SMSPAKPVQH HRERKRASKS SKHSMS.

    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.

    Sostdc1 Human
  • View Data Sheet

    Description:

    Macrophage-Derived Chemokine (CCL22) Rat Recombinant

    C-C motif chemokine 22, Small-inducible cytokine A22, Macrophage-derived chemokine, MDC(1-69), Stimulated T-cell chemotactic protein 1, CC chemokine STCP-1, CCL22, MDC, SCYA22, ABCD-1, DC/B-CK, MGC34554, A-152E5.1, CC chemokine ABCD-1, Activated B and dendritic cell-derived, DCBCK.

    Product # :

    CHM-279

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    Description

    CCL22 Rat Recombinant produced in E.Coli is a non-glycosylated, Polypeptide chain containing 68 amino acids and having a molecular mass of 7.9kDa. The Rat CCL22 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The protein was lyophilized from a 0.2µm filtered concentrated solution in 1×PBS, pH7.4.

    Purity

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

    Biological Activity

    Determined by its ability to chemoattract human activated lymphocytes using a concentration range of 10.0-100.0 ng/ml.

    More Info

    • Introduction

      MDC (CCL22) is a small cytokine that belongs to the CC chemokine family. CCL22 is one of several Cys-Cys (CC) cytokine genes clustered on the q arm of chromosome 16.
      MDC shows chemotactic activity for natural killer cells, chronically activated T lymphocytes, monocytes and dendritic cells. On the other hand, MDC shows a mild activity for primary activated T lymphocytes and has no chemoattractant activity for neutrophils, eosinophils and resting T lymphocytes. MDC may also have a role in the trafficking of activated T lymphocytes to inflammatory sites and other aspects of activated T lymphocyte physiology. MDC interacts with cell surface chemokine receptors CCR4.
      CCL22 is vastly expressed in macrophage and in monocyte-derived dendritic cells, and thymus. CCL22 is also found in the lymph node, appendix, activated monocytes, resting and activated macrophages. Lower expression of CCL22 can be seen in the lung and the spleen and very weak expression in the small intestine. In the lymph node CCL22 is expressed in a mature subset of Langerhans' cells (CD1a+ and CD83+).
      Furthermore, CCL22 is expressed in atopic dermatitis, allergic contact dermatitis skin, and psoriasis, in both the epidermis and dermis. In addition, MDC has a role in hindering progression of lung cancer. Moreover, significantly higher CCL22 expression is linked to gastric cancer.

    • Synonyms

      C-C motif chemokine 22, Small-inducible cytokine A22, Macrophage-derived chemokine, MDC(1-69), Stimulated T-cell chemotactic protein 1, CC chemokine STCP-1, CCL22, MDC, SCYA22, ABCD-1, DC/B-CK, MGC34554, A-152E5.1, CC chemokine ABCD-1, Activated B and dendritic cell-derived, DCBCK.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized MDC although stable at room temperature for 3 weeks, should be stored desiccated below -18C. Upon reconstitution MDC should be stored at 4C between 2-7 days and for future use below -18C.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 MDC in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      GPYGANVEDS ICCQDYIRHP LPPRFVKEFY WTSKSCRKPG VVLITIKNRD ICADPRMLWV KKILHKLA.

    • Background

      What is the molecular weight/Mw of CCL22 RAT Protein?
      CCL22 RAT Protein has a total Mw of 7.9kDa.

      What is the source or expression system of CCL22 RAT Protein?
      Escherichia Coli.

      What is the Purity of CCL22 RAT Protein?
      CCL22 RAT Protein is >97% pure as determined by SDS-PAGE.

      What is the Biological Activity of CCL22 RAT Protein?
      Determined by its ability to chemoattract human activated lymphocytes using a concentration range of 10.0-100.0 ng/ml.

      What is the amino acid sequence of CCL22 RAT Protein?
      GPYGANVEDS ICCQDYIRHP LPPRFVKEFY WTSKSCRKPG VVLITIKNRD ICADPRMLWV KKILHKLA

      What applications can CCL22 RAT Protein be used in?
      CCL22 RAT Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for CCL22 RAT Protein?
      The endotoxin level is minimal, CCL22 RAT Protein was purified using conventional chromatography techniques.

      Who supplies recombinant CCL22 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 CCL22 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.

    Mdc Rat
  • View Data Sheet

    Description:

    Interleukin-12 Human Recombinant

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

    Product # :

    CYT-101

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    Description

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

    Source

    HEK.

    Formulation

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

    Purity

    Greater than 95% as obsereved by SDS-PAGE.

    Biological Activity

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

    More Info

    • Introduction

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

    • Synonyms

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

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Solubility

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

    • Amino Acid Sequence

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

    • Background

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

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

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

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

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

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

      Who supplies recombinant IL12 HUMAN that is in stock and available to order?
      ProSpec has the protein in stock and available for immediate delivery.

      Where can I order bulk mg quantities of IL12 HUMAN?
      ProSpec supplies bulk mg quantities at affordable prices that meets research and academic budgets.

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

    Il 12 Human Hek
  • View Data Sheet

    Description:

    Ciliary-Neurotrophic Factor Human Recombinant

    HCNTF, CNTF, Ciliary Neurotrophic Factor.

    Product # :

    CYT-272

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    Description

    Ciliary Neurotrophic Factor Recombinant Human produced in E.Coli is a single, non-glycosylated polypeptide chain containing 199 amino acids and having a molecular mass of 22706 Dalton. The CNTF is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Lyophilized from a concentrated (1mg/ml) solution in water containing 5mM sodium Phosphate buffer pH=7.5 and 5mM sodium chloride.

    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 the dose-dependant stimulation of TF-1 cells is < 2 ng/ml, corresponding to a Specific Activity of 500,000IU/mg.

    More Info

    • Introduction

      CNTF is a polypeptide hormone whose actions appear to be restricted to the nervous system where it promotes neurotransmitter synthesis and neurite outgrowth in certain neuronal populations. The protein is a potent survival factor for neurons and oligodendrocytes and may be relevant in reducing tissue destruction during inflammatory attacks. A mutation in this gene, which results in aberrant splicing, leads to ciliary neurotrophic factor deficiency, but this phenotype is not causally related to neurologic disease. In addition to the predominant monocistronic transcript originating from this locus, the gene is also co-transcribed with the upstream ZFP91 gene. Co-transcription from the two loci results in a transcript that contains a complete coding region for the zinc finger protein but lacks a complete coding region for ciliary neurotrophic factor.
      CNTF is a survival factor for various neuronal cell types. Seems to prevent the degeneration of motor axons after axotomy.

    • Synonyms

      HCNTF, CNTF, Ciliary Neurotrophic Factor.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized Ciliary Neurotrophic Factor although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution CNTF 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 HCNTF 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-Ala-Phe-Thr-Glu.

    • Background

      Exploring the Potential of Human Recombinant Ciliary-Neurotrophic Factor: Implications and Applications

      Abstract:

      Ciliary-Neurotrophic Factor (CNTF) holds remarkable promise in neurobiology and therapeutic development due to its neuroprotective and regenerative properties. This paper delves into the significance of Human Recombinant CNTF, its production methodologies, and its potential applications in treating neurodegenerative disorders. The review sheds light on the therapeutic potential of CNTF and its role in advancing neuroregeneration research.

      Introduction:

      CNTF, a neurotrophic cytokine, is known for its pivotal role in neuronal survival and growth. The availability of Human Recombinant CNTF allows researchers to investigate its therapeutic potential and explore avenues for developing novel treatments for neurodegenerative diseases. CNTF's ability to support neuronal health and promote regeneration makes it a promising candidate for medical interventions.

      Mechanisms of Action:

      CNTF interacts with specific receptor complexes, activating various downstream signaling pathways, including Janus kinase (JAK) and Signal Transducer and Activator of Transcription (STAT) pathways. These pathways contribute to cell survival, differentiation, and axonal growth, forming the foundation for CNTF's neuroprotective effects.

      Production Methods:

      Human Recombinant CNTF is produced by introducing the CNTF gene into suitable expression systems, often employing bacterial or mammalian cells. Ensuring proper post-translational modifications is essential for maintaining the protein's biological activity and therapeutic potential.

      Therapeutic Applications:

      CNTF's neuroprotective and regenerative effects offer potential therapeutic applications in neurodegenerative disorders, such as amyotrophic lateral sclerosis (ALS), retinal degeneration, and Parkinson's disease. It holds promise for preserving and restoring neuronal function, thereby improving the quality of life for affected individuals.

      Challenges and Future Directions:

      While Human Recombinant CNTF shows great potential, challenges include precise dosing, delivery methods, and potential side effects. Further research is needed to optimize CNTF-based therapies and assess their long-term safety and efficacy in clinical settings.

      Conclusion:

      Human Recombinant Ciliary-Neurotrophic Factor emerges as a critical tool in advancing our understanding of neuroprotection and neuroregeneration. Its potential in treating neurodegenerative disorders highlights the ongoing quest for innovative therapeutic approaches that harness the body's inherent ability to heal and regenerate.

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

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

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

      What is the Biological Activity of CNTF Protein?
      The ED50 as determined by the dose-dependant stimulation of TF-1 cells is < 2 ng/ml, corresponding to a Specific Activity of 500,000IU/mg.

      What is the amino acid sequence of CNTF Protein?
      CNTF Protein is composed from 199 amino acids.

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

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

    • Protein content

      CNTF quantitation was carried out by two independent methods1. UV spectroscopy at 280 nm using the absorbency value of 1.28 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 CNTF Recombinant 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.

    Cntf Human
  • View Data Sheet

    Description:

    Starch Binding Domain 1 Human Recombinant

    Starch Binding Domain 1, Genethonin 1, GENEX3414, Starch-Binding Domain-Containing Protein 1.

    Product # :

    PRO-1545

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    Description

    STBD1 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 358 amino acids (24-358) and having a molecular mass of 39.1kDa.STBD1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The STBD1 solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 1mM DTT and 10% glycerol.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    More Info

    • Introduction

      STBD1 has one carbohydrate binding type-20 (CBM20) domain and has the ability to bind to carbohydrates. STBD1 is highly expressed in cardiac and skeletal muscles.

    • Synonyms

      Starch Binding Domain 1, Genethonin 1, GENEX3414, Starch-Binding Domain-Containing Protein 1.

    • Physical Appearance

      Sterile Filtered clear solution.

    • Stability

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

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MGSRGGPGDT GKDGDAEQEK DAPLGGAAIP GGHQSGSSGL SPGPSGQELV TKPEHLQESN GHLISKTKDL GKLQAASWRL QNPSREVCDN SREHVPSGQF PDTEAPATSE TSNSRSYSEV SRNESLESPM GEWGFQKGQE ISAKAATCFA EKLPSSNLLK NRAKEEMSLS DLNSQDRVDH EEWEMVPRHS SWGDVGVGGS LKAPVLNLNQ GMDNGRSTLV EARGQQVHGK MERVAVMPAG SQQVSVRFQV HYVTSTDVQF IAVTGDHECL GRWNTYIPLH YNKDGFWSHS IFLPADTVVE WKFVLVENGG VTRWEECSNR FLETGHEDKV VHAWWGIH

    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.

    Stbd1 Human
  • View Data Sheet

    Description:

    Cerebral Neurotrophic Factor Human Recombinant

    Cerebral neurotrophic factor, arginine-rich, mutated in early stage tumors-like 1, Conserved neurotrophic factor, ARMET-like protein 1, ARMETL1.

    Product # :

    CYT-167

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    Description

    CDNF Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 161 amino acids and having a molecular mass of 18.5kDa.The CDNF is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    CDNF protein was lyophilized from a 0.2µm filtered concentrated solution in 1xPBS, pH 7.4.

    Purity

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

    Biological Activity

    The ED50 as determined by its ability to stimulate the proliferation of rat C6 cells is 15-25µg/ml, corresponding to a specific activity of 40-67units/mg.

    More Info

    • Introduction

      CDNF is a member of the ARMET family and acts as a trophic factor for neurons. CDNF inhibits the (6-OHDA)-induced degeneration of neurons. When CDNF controlled after 6-OHDA-lesioning, it reestablishes the function and inhibits the degeneration of neurons in substantia nigra. CDNF is universally expressed in neuronal and non-neuronal tissues. The highest levels in the brain are found in the optic nerve and corpus callosum.

    • Synonyms

      Cerebral neurotrophic factor, arginine-rich, mutated in early stage tumors-like 1, Conserved neurotrophic factor, ARMET-like protein 1, ARMETL1.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Amino Acid Sequence

      QEAGGRPGAD CEVCKEFLNR FYKSLIDRGV NFSLDTIEKE LISFCLDTKG KENRLCYYLG ATKDAATKIL SEVTRPMSVH MPAMKICEKL KKLDSQICEL KYEKTLDLAS VDLRKMRVAE LKQILHSWGE ECRACAEKTD YVNLIQELAP KYAATHPKTE L

    • Background

      Cerebral Neurotrophic Factor Human Recombinant: A Leap Forward in Neurobiology

      The field of neurobiology is replete with wonder, particularly due to the influential role of neurotrophic factors. These essential proteins, responsible for the survival and growth of neurons, have become a focal point in modern research. Among these, the Cerebral Neurotrophic Factor (CNF) stands out, offering novel insights and potential breakthroughs in our understanding of neurological health.

      Enter the world of bioengineering, a scientific arena where we have successfully replicated CNF, leading to the birth of Cerebral Neurotrophic Factor Human Recombinant (CNF-HR). This is a massive step towards conquering neurodegenerative disorders such as Alzheimer's and Parkinson's diseases, conditions that have perplexed scientists and clinicians for decades.

      The extraordinary capacity of CNF-HR lies in its dual functionality - it acts as a defender and a promoter. It defends neurons from harmful degenerative processes while promoting their growth and development. Picture a devoted gardener who tirelessly protects his garden from pests and nurtures the growth of each plant. In this context, the brain is the vibrant garden, and the neurons, the delicate plants we must care for.

      Although this scientific breakthrough sparks enthusiasm, it's crucial to remember the challenges that lie ahead. The path to determining the most effective method of delivering CNF-HR to the brain, identifying the optimal dosage, and monitoring potential side effects is a winding one. Nevertheless, with continuous research and relentless scientific curiosity, we are optimistic about overcoming these challenges.

      In conclusion, the development of CNF-HR is a significant milestone in the fascinating journey of neurobiology. Its potential to change the trajectory of treating neurodegenerative diseases and enhancing our understanding of neuronal function is tremendous. While the journey is strewn with complexities, the potential rewards we stand to reap promise a future where neurodegenerative diseases could be effectively managed or even cured.

      What is the molecular weight/Mw of CDNF Protein?
      CDNF Protein has a total Mw of 18.5kDa.

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

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

      What is the Biological Activity of CDNF Protein?
      The ED50 as determined by its ability to stimulate the proliferation of rat C6 cells is 15-25µg/ml, corresponding to a specific activity of 40-67units/mg.

      What is the amino acid sequence of CDNF Protein?
      QEAGGRPGAD CEVCKEFLNR FYKSLIDRGV NFSLDTIEKE LISFCLDTKG KENRLCYYLG ATKDAATKIL SEVTRPMSVH MPAMKICEKL KKLDSQICEL KYEKTLDLAS VDLRKMRVAE LKQILHSWGE ECRACAEKTD YVNLIQELAP KYAATHPKTE L

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

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

    Cdnf Human
  • View Data Sheet

    Description:

    CD72 Human Recombinant, Sf9

    CD72, CD72b, LYB2, B-cell differentiation antigen CD72, Lyb-2.

    Product # :

    PRO-2608

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    Description

    CD72 Human Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 485 amino acids (117-359a.a.) and having a molecular mass of 55.3kDa (Molecular size on SDS-PAGE will appear at approximately 50-70kDa).CD72 is expressed with a 242 amino acid hIgG-His tag at C-Terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    CD72 protein solution (0.5mg/ml) contains 50mM Tris-HCl buffer (pH6.8), 0.2M NaCl, 2mM DTT and 50% glycerol.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    More Info

    • Introduction

      CD72 antigen is a member of the type II integral membrane glycoproteins which includes other related cell surface moleculaes such as the asialoglycoprotein receptors, CD23 and the Kupffer cell recpeotr. The exposure of B cells to CD72 antibodies activates a variety of signalling pathways and can induce MHC class II expression and B cell proliferation. CD72 antigen is expressed on all cells of B cell lineage with the exception of plasma cells and weakly on human tissue macrophages.

    • Synonyms

      CD72, CD72b, LYB2, B-cell differentiation antigen CD72, Lyb-2.

    • 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

      ADPRYLQVSQ QLQQTNRVLE VTNSSLRQQL RLKITQLGQS AEDLQGSRRE LAQSQEALQV
      EQRAHQAAEG QLQACQADRQ KTKETLQSEE QQRRALEQKL SNMENRLKPF FTCGSADTCC
      PSGWIMHQKS CFYISLTSKN WQESQKQCET LSSKLATFSE IYPQSHSYYF LNSLLPNGGS
      GNSYWTGLSS NKDWKLTDDT QRTRTYAQSS KCNKVHKTWS WWTLESESCR SSLPYICEMT
      AFRFPDLEPK 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.

    Cd72 Protein
  • View Data Sheet

    Description:

    CD30 Ligand Human Recombinant, Sf9

    Tumor Necrosis Factor Superfamily Member 8, Tumor Necrosis Factor (Ligand) Superfamily, Member 8, CD153 Antigen, CD30 Ligand, CD30LG, CD30-L, CD30L, Tumor Necrosis Factor (Ligand) Superfamily Member 8, Tumor Necrosis Factor Ligand 3A, CD30 Antigen Ligand, TNLG3A, CD153, Tumor necrosis factor ligand superfamily member 8, TNFSF8, CD30 ligand.

    Product # :

    CYT-954

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    Description

    TNFSF8 produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 181 amino acids (63-234a.a.) and having a molecular mass of 20.7kDa (Molecular size on SDS-PAGE will appear at approximately 18-40kDa). TNFSF8 is expressed with a 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    TNFSF8 protein solution (0.5mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 10% glycerol.

    Purity

    Greater than 85% as determined by SDS-PAGE.

    More Info

    • Introduction

      CD30 Ligand (TNFSF8) is a cytokine which is a member of the tumor necrosis factor (TNF) ligand family. The TNFSF8 cytokine is a ligand for TNFRSF8/CD30, which is a cell surface antigen and a marker for Hodgkin lymphoma and related hematologic malignancies. The employment of the TNFSF8 cytokine expressed on B cell surface has an inhibitory role in modulating Ig class switch. TNFSF8 enhances cell proliferation of some lymphoma cell lines, while inducing cell death and reducing cell proliferation of other lymphoma cell lines. The pleiotropic biological activities of the TNFSF8 cytokine on different CD30+ lymphoma cell lines has a pathophysiologic role in Hodgkin's and some non-Hodgkin's lymphomas.

    • Synonyms

      Tumor Necrosis Factor Superfamily Member 8, Tumor Necrosis Factor (Ligand) Superfamily, Member 8, CD153 Antigen, CD30 Ligand, CD30LG, CD30-L, CD30L, Tumor Necrosis Factor (Ligand) Superfamily Member 8, Tumor Necrosis Factor Ligand 3A, CD30 Antigen Ligand, TNLG3A, CD153, Tumor necrosis factor ligand superfamily member 8, TNFSF8, CD30 ligand.

    • 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

      ADPQRTDSIP NSPDNVPLKG GNCSEDLLCI LKRAPFKKSW AYLQVAKHLN KTKLSWNKDG ILHGVRYQDG NLVIQFPGLY FIICQLQFLV QCPNNSVDLK LELLINKHIK KQALVTVCES GMQTKHVYQN LSQFLLDYLQ VNTTISVNVD TFQYIDTSTF PLENVLSIFL YSNSDHHHHH H.

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    Tnfsf8 Human Sf9
  • View Data Sheet

    Description:

    Macrophage Colony Stimulating Factor Human Recombinant, His Tag

    CSF-1, Lanimostim, MCSF, MGC31930, M-CSF.

    Product # :

    CYT-695

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    Description

    Macrophage Colony Stimulating Factor Human Recombinant produced in E.coli is a single, non-glycosylated, polypeptide chain containing 179 amino acids (33-190 a.a.) and having a total molecular mass of 20.7 kDa.MCSF is fused to a 20 amino acid His Tag at N-terminus and purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The MCSF protein solution contains 20mM Tris-HCl, pH-8, 2mM DTT & 10% Glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    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, MGC31930, M-CSF.

    • 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 MEEVSEYCSH MIGSGHLQSL QRLIDSQMET SCQITFEFVD QEQLKDPVCY LKKAFLLVQD IMEDTMRFRD NTPNAIAIVQ LQELSLRLKS CFTKDYEEHD KACVRTFYET PLQLLEKVKN VFNETKNLLD KDWNIFSKNC NNSFAECSSQ DVVTKPDCN.

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    M Csf Human His
  • View Data Sheet

    Description:

    Soluble CD23 Human Recombinant

    Low affinity immunoglobulin epsilon Fc receptor, Lymphocyte IgE receptor, Fc-epsilon-RII, BLAST-2, Immunoglobulin E-binding factor, CD23 antigen, FCER2, CD23, FCE2, CD23A, IGEBF, CLEC4J.

    Product # :

    PRO-1789

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    Description

    sCD23 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 172 amino acids and having a molecular mass of 19.2kDa.The sCD23 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 97.0% as determined by:
    (a) Analysis by RP-HPLC.
    (b) Analysis by SDS-PAGE.

    Biological Activity

    The ED50 is determined by its ability to induce TNF-alpha production by human PBMCs. 

    More Info

    • Introduction

      CD23 is a 45kDa glycoprotein, which is present on a subpopulation of freshly isolated peripheral blood and tonsil B cells and strongly expressed on EBV-transformed B lymphoblasts. The CD23 molecule is identical to the low affinity IgE receptor found on B cells. Expression of CD23 has been detected in neoplastic cells from cases of B cell chronic lymphocyctic leukaemia and some cases of centroblastic/centrocytic lymphoma.

    • Synonyms

      Low affinity immunoglobulin epsilon Fc receptor, Lymphocyte IgE receptor, Fc-epsilon-RII, BLAST-2, Immunoglobulin E-binding factor, CD23 antigen, FCER2, CD23, FCE2, CD23A, IGEBF, CLEC4J.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized sCD23 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution sCD23 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 sCD23 in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      MELQVSSGFV CNTCPEKWIN FQRKCYYFGK GTKQWVHARY ACDDMEGQLV SIHSPEEQDF LTKHASHTGS WIGLRNLDLK GEFIWVDGSH VDYSNWAPGE PTSRSQGEDC VMMRGSGRWN DAFCDRKLGA WVCDRLATCT PPASEGSAES MGPDSRPDPD GRLPTPSAPL HS

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    Scd23 Human
  • View Data Sheet

    Description:

    Interleukin 12 Receptor Beta 1 Human Recombinant, Sf9

    Interleukin 12 Receptor, Beta 1, IL-12 Receptor Beta Component, IL-12 Receptor Subunit Beta-1, IL-12R Subunit Beta-1, IL12RB, Interleukin-12 Receptor Subunit Beta-1, Interleukin-12 Receptor Beta-1 Chain, Cluster Of Differentiation 212, CD212 Antigen, IL-12R-Beta-1, IL-12R-BETA1, IL-12RB1, CD212, IMD30, IL12R, IL12RB1.

    Product # :

    CYT-894

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    • SDS-PAGE

    Description

    IL12RB1 produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain (24-545 a.a.) and fused to a 6 aa His Tag at C-terminus containing a total of 528 amino acids and having a molecular mass of 58.4kDa.IL12RB1 shows multiple bands between 50-70kDa on SDS-PAGE, reducing conditions and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    IL12RB1 protein solution (0.25mg/ml) contains Phosphate buffered saline (pH7.4), 30% glycerol, 1mM EDTA and 0.1mM PMSF.

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

    SDS-PAGE

    More Info

    • Introduction

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

    • Synonyms

      Interleukin 12 Receptor, Beta 1, IL-12 Receptor Beta Component, IL-12 Receptor Subunit Beta-1, IL-12R Subunit Beta-1, IL12RB, Interleukin-12 Receptor Subunit Beta-1, Interleukin-12 Receptor Beta-1 Chain, Cluster Of Differentiation 212, CD212 Antigen, IL-12R-Beta-1, IL-12R-BETA1, IL-12RB1, CD212, IMD30, IL12R, IL12RB1.

    • 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

      CRTSECCFQD PPYPDADSGS ASGPRDLRCY RISSDRYECS WQYEGPTAGV SHFLRCCLSS GRCCYFAAGS ATRLQFSDQA GVSVLYTVTL WVESWARNQT EKSPEVTLQL YNSVKYEPPL GDIKVSKLAG QLRMEWETPD NQVGAEVQFR HRTPSSPWKL GDCGPQDDDT ESCLCPLEMN VAQEFQLRRR QLGSQGSSWS KWSSPVCVPP ENPPQPQVRF SVEQLGQDGR RRLTLKEQPT QLELPEGCQG LAPGTEVTYR LQLHMLSCPC KAKATRTLHL GKMPYLSGAA YNVAVISSNQ FGPGLNQTWH IPADTHTEPV ALNISVGTNG TTMYWPARAQ SMTYCIEWQP VGQDGGLATC SLTAPQDPDP AGMATYSWSR ESGAMGQEKC YYITIFASAH PEKLTLWSTV LSTYHFGGNA SAAGTPHHVS VKNHSLDSVS VDWAPSLLST CPGVLKEYVV RCRDEDSKQV SEHPVQPTET QVTLSGLRAG VAYTVQVRAD TAWLRGVWSQ PQRFSIEVQV SDHHHHHH

    • Background

      What is the molecular weight/Mw of IL12RB1 HUMAN, SF9 Protein?
      IL12RB1 HUMAN, SF9 Protein has a total Mw of 58.4kDa.

      What is the source or expression system of IL12RB1 HUMAN, SF9 Protein?
      Sf9, Baculovirus cells.

      What is the Purity of IL12RB1 HUMAN, SF9 Protein?
      IL12RB1 HUMAN, SF9 Protein is >85% pure as determined by SDS-PAGE.

      What is the Biological Activity of IL12RB1 HUMAN, SF9 Protein?
      The biological functionality of IL12RB1 HUMAN, SF9 Protein will be determined in the future.

      What is the amino acid sequence of IL12RB1 HUMAN, SF9 Protein?
      CRTSECCFQD PPYPDADSGS ASGPRDLRCY RISSDRYECS WQYEGPTAGV SHFLRCCLSS GRCCYFAAGS ATRLQFSDQA GVSVLYTVTL WVESWARNQT EKSPEVTLQL YNSVKYEPPL GDIKVSKLAG QLRMEWETPD NQVGAEVQFR HRTPSSPWKL GDCGPQDDDT ESCLCPLEMN VAQEFQLRRR QLGSQGSSWS KWSSPVCVPP ENPPQPQVRF SVEQLGQDGR RRLTLKEQPT QLELPEGCQG LAPGTEVTYR LQLHMLSCPC KAKATRTLHL GKMPYLSGAA YNVAVISSNQ FGPGLNQTWH IPADTHTEPV ALNISVGTNG TTMYWPARAQ SMTYCIEWQP VGQDGGLATC SLTAPQDPDP AGMATYSWSR ESGAMGQEKC YYITIFASAH PEKLTLWSTV LSTYHFGGNA SAAGTPHHVS VKNHSLDSVS VDWAPSLLST CPGVLKEYVV RCRDEDSKQV SEHPVQPTET QVTLSGLRAG VAYTVQVRAD TAWLRGVWSQ PQRFSIEVQV SDHHHHHH
      What applications can IL12RB1 HUMAN, SF9 Protein be used in?
      IL12RB1 HUMAN, SF9 Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for IL12RB1 HUMAN, SF9 Protein?
      The endotoxin level is minimal, IL12RB1 HUMAN, SF9 Protein was purified using conventional chromatography techniques.

      Who supplies recombinant IL12RB1 HUMAN, SF9 that is in stock and available to order?
      ProSpec has the protein in stock and available for immediate delivery.

      Where can I order bulk mg quantities of IL12RB1 HUMAN, SF9?
      ProSpec supplies bulk mg quantities at affordable prices that meets research and academic budgets.

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

    Il12Rb1 Human Sf9
  • View Data Sheet

    Description:

    Retinol Dehydrogenase 12 Human Recombinant

    Retinol dehydrogenase 12 (all-trans/9-cis/11-cis), LCA3, LCA13, SDR7C2, All-trans and 9-cis retinol dehydrogenase, short chain dehydrogenase/reductase family 7C, member 2, FLJ30273, EC 1.1.1.100.

    Product # :

    ENZ-233

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    Description

    RDH12 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 303 amino acids (39-316) and having a molecular mass of 33.5kDa.RDH12 is fused to a 25 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    The RDH12 solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 200mM NaCl, 2mM DTT and 40% glycerol.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    More Info

    • Introduction

      RDH12 is a member of the short-chain Dehydrogenases / Reductases (SDR) family. RDH12 is found generally in brain, stomach, eye, skeletal muscle and kidney. RDH12 is a NADPH-dependent retinal reductase whose main activity is toward 9-cis and all-trans-retinol. In addition, RDH12 takes part in the metabolism of short-chain aldehydes but does not display steroid dehydrogenase activity.

    • Synonyms

      Retinol dehydrogenase 12 (all-trans/9-cis/11-cis), LCA3, LCA13, SDR7C2, All-trans and 9-cis retinol dehydrogenase, short chain dehydrogenase/reductase family 7C, member 2, FLJ30273, EC 1.1.1.100.

    • 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 MGSHMGKVVV ITGANTGIGK ETARELASRG ARVYIACRDV LKGESAASEI RVDTKNSQVL VRKLDLSDTK SIRAFAEGFL AEEKQLHILI NNAGVMMCPY SKTADGFETH LGVNHLGHFL LTYLLLERLK VSAPARVVNV SSVAHHIGKI PFHDLQSEKR YSRGFAYCHS KLANVLFTRE LAKRLQGTGV TTYAVHPGVV RSELVRHSSL LCLLWRLFSP FVKTAREGAQ TSLHCALAEG LEPLSGKYFS DCKRTWVSPR ARNNKTAERL WNVSCELLGI RWE

    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.

    Rdh12 Human
  • View Data Sheet

    Description:

    Granulocyte Macrophage-Colony Stimulating Factor Porcine Recombinant, His Tag

    CSF-2, MGI-1GM, GM-CSF, Pluripoietin-alpha, Molgramostin, Sargramostim

    Product # :

    CYT-1160

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    Description

    GMCSF Poricne Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 148 amino acids (18-144a.a.) and having a molecular mass of 16.6kDa.GMCSF is fused to a 21 amino acid His tag at N-Terminus and purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    GMCSF protein solution (0.5mg/ml) containing Phosphate-Buffered Saline (pH7.4).

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Biological Activity

    The ED50 range is ≤ 40 ng/ml, and is measured in a cell proliferation assay using TF-1 human erythroleukemic cells.

    More Info

    • Introduction

      The hematopoietic growth factor GM-CSF or granulocyte macrophage colony-stimulating factor, stimulates the development of neutrophils & macrophages, enhance proliferation and development of early erythroid megakaryocytic & eosinophilic progenitor cells. GM-CSF is secreted from the fibroblasts, monocytes, T-lymphocytes & endothelial cells. This protein blocks the migration of neutrophils & induces the biological activity of mature end-cells.

    • Synonyms

      CSF-2, MGI-1GM, GM-CSF, Pluripoietin-alpha, Molgramostin, Sargramostim

    • 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 MAPTRPPSPV TRPWQHVDAI KEALSLLNNS NDTAAVMNET VDVVCEMFDP QEPTCVQTRL NLYKQGLRGS LTRLKSPLTL LAKHYEQHCP LTEETSCETQ SITFKSFKDS LNKFLFTIPF DCWGPVKK

    • Background

      What is the molecular weight/Mw of GM-CSF PORCINE, HIS Protein?
      GM-CSF PORCINE, HIS Protein has a total Mw of 16.6kDa.

      What is the source or expression system of GM-CSF PORCINE, HIS Protein?
      Escherichia Coli.

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

      What is the Biological Activity of GM-CSF PORCINE, HIS Protein?
      The ED50 range is ≤ 40 ng/ml, and is measured in a cell proliferation assay using TF-1 human erythroleukemic cells.

      What is the amino acid sequence of GM-CSF PORCINE, HIS Protein?
      MGSSHHHHHH SSGLVPRGSH MAPTRPPSPV TRPWQHVDAI KEALSLLNNS NDTAAVMNET VDVVCEMFDP QEPTCVQTRL NLYKQGLRGS LTRLKSPLTL LAKHYEQHCP LTEETSCETQ SITFKSFKDS LNKFLFTIPF DCWGPVKK

      What applications can GM-CSF PORCINE, HIS Protein be used in?
      GM-CSF PORCINE, HIS Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for GM-CSF PORCINE, HIS Protein?
      The endotoxin level is minimal, GM-CSF PORCINE, HIS Protein was purified using conventional chromatography techniques.


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

    Porcine Gm Csf
  • View Data Sheet

    Description:

    Granulocyte Colony Stimulating Factor, Mouse Anti-Human, FITC

    CSF-3, MGI-1G, GM-CSF beta, Pluripoietin, Filgrastim, Lenograstim, G-CSF, MGC45931, GCSF.

    Product # :

    ANT-241

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    Formulation

    1 mg/ml in PBS (after reconstitution).

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    • Introduction

      GCSF is a cytokine that controls the production, differentiation, and function of granulocytes. The active protein is found extracellularly. Three transcript variants encoding three different isoforms have been found for this gene.
      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. This csf induces granulocytes.

    • Synonyms

      CSF-3, MGI-1G, GM-CSF beta, Pluripoietin, Filgrastim, Lenograstim, G-CSF, MGC45931, GCSF.

    • Solubility

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

    • Immunogen

      r.Human G-CSF.

    • Ig Subclass

      Mouse IgG.

    • Clone

      NYRhGCSF.

    • Applications

      Direct ELISA, Western Blot, Intra-cellular staining.

    • Titer

      For intra-cellular staining use 10µl per 1,000,000 cells.

    • Shipping Conditions

      Antibody is shipped lyophilized at ambient temperature.

    • Type

      Mouse Anti Human Monoclonal.

    • Storage Procedures

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

    • Purification Method

      Protein A.

    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.

    G Csf Antibody Fitc
  • 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:

    Mouse Anti Human Pigment Epithelium-Derived Factor Clone PAT13D9AT

    Pigment epithelium-derived factor,PEDF, Serpin-F1, SerpinF1, EPC-1, EPC1, PIG35.

    Product # :

    ANT-714

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    Formulation

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

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    • Introduction

      PEDF is a noninhibitory serpin with neurotrophic, anti-angiogenic, and anti-tumorigenic properties. PEDF is a 50,000 dalton glycoprotein created and secreted in many tissues all the way through the body. A key component of the anti-angiogenic action of PEDF is the induction of apoptosis in proliferating endothelial cells. Additionally, PEDF is capable to inhibit the activity of angiogenic factors such as VEGF and FGF-2. The neuro-protective effects of PEDF are achieved through suppression of neuronal apoptosis induced by peroxide, glutamate, or other neurotoxins. The recognition of a lipase-linked cell membrane receptor for PEDF (PEDF-R) that binds to PEDF with high affinity should facilitate further elucidation of the underlying mechanisms of this pluripotent serpin. To date, PEDF-R is the only signaling receptor known to be used by a serpin family member. The unique range of PEDF activities associate it as a potential therapeutic agent for the treatment of vasculature related neurodegenerative diseases such as age-related macular degeneration (AMD) and proliferative diabetic retinopathy (PDR). PEDF in addition has the potential to be functional in the treatment of various angiogenesis-related diseases including a number of cancers.

    • Synonyms

      Pigment epithelium-derived factor,PEDF, Serpin-F1, SerpinF1, EPC-1, EPC1, PIG35.

    • Physical Appearance

      Sterile filtered colorless solution.

    • Immunogen

      Anti-human PEDF mAb, is derived from hybridization of mouse F0 myeloma cells with spleen cells from BALB/c mice immunized with a recombinant human PEDF protein 20-418 amino acids purified from E. coli.

    • Ig Subclass

      Mouse IgG1 heavy chain and κ light chain.

    • Clone

      PAT13D9AT.

    • Applications

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

    • Type

      Mouse Anti Human Monoclonal.

    • Storage Procedures

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

    • Purification Method

      PEDF antibody was purified by protein-A affinity chromatography.

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

    Pedf Pat13D9At Antibody
  • View Data Sheet

    Description:

    Cathepsin D, Mouse Anti Human

    Cathepsin D, EC 3.4.23.5, CTSD, CPSD, CLN10, MGC2311.

    Product # :

    ANT-324

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    Formulation

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

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    • Introduction

      Cathepsin D is synthesized as a 54kDa precursor, which is proteolytically processed to an intermediate 48kDa single chain, which matures into more stable 34kDa and 14kDa two chain form. It is an estrogen-regulated lysosomal protease that has been suggested to facilitate cancer cell migration and invasion by digesting the basement membrane, extracellular matrix, and xonnective tissue. Because of its mitogenic and proteolytic activities, it has been implicated as a prognostic marker in many tumor types. Cathepsin D is expressed in epithelial cells as well as in macrophages.

    • Synonyms

      Cathepsin D, EC 3.4.23.5, CTSD, CPSD, CLN10, MGC2311.

    • Physical Appearance

      Sterile Filtered colorless solution.

    • Immunogen

      Anti-human CTSD mAb is derived from hybridization of mouse SP2/O myeloma cells with spleen cells from BALB/c mice immunized with recombinant human CTSD amino acids 21-412 purified from E. coli.

    • Ig Subclass

      Mouse IgG2b heavy chain and κ light chain.

    • Clone

      P4G2AT.

    • Applications

      CTSD antibody has been tested by ELISA and Western blot analysis to assure specificity and reactivity. Since application varies, however, each investigation should be titrated by the reagent to obtain optimal results. Recommended dilution range for Western blot analysis is 1:500 ~ 2,000. Recommended starting dilution is 1:1,000.

    • Type

      Mouse Anti Human Monoclonal.

    • Storage Procedures

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

    • Purification Method

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

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

    Ctsd Antibody
  • View Data Sheet

    Description:

    Granulocyte Macrophage-Colony Stimulating Factor Canine Recombinant

    CSF-2, MGI-1GM, GM-CSF, Pluripoietin-alpha, MGC131935, MGC138897.

    Product # :

    CYT-724

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    Description

    GMCSF k9 Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 128 amino acids and having a molecular mass of 14.2 kDa. GM-CSF is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    GMCSF was lyophilized after extensive dialysis against 1xPBS pH 7.4.

    Purity

    Greater than 96.0% as determined by
    1. Analysis by RP-HPLC.
    2. Analysis by SDS-PAGE.

    Biological Activity

    The ED50 as calculated by the dose-dependent stimulation of the proliferation of human TF1 erythroleukemic cells is typically 1-4 ng/ml.

    More Info

    • Introduction

      GMCSF is a cytokine that controls the production, differentiation, and function of granulocytes and macrophages. The active form of the protein is found extracellularly as a homodimer. This gene has been localized to a cluster of related genes at chromosome region 5q31, which is known to be associated with interstitial deletions in the 5q- syndrome and acute myelogenous leukemia. Other genes in the cluster include those encoding interleukins 4, 5, and 13.
      GM-CSF stimulates the growth and differentiation of hematopoietic precursor cells from various lineages, including granulocytes, macrophages, eosinophils and erythrocytes.

    • Synonyms

      CSF-2, MGI-1GM, GM-CSF, Pluripoietin-alpha, MGC131935, MGC138897.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Amino Acid Sequence

      APTRSPTLVT RPSQHVDAIQ EALSLLNNSN DVTAVMNKAV KVVSEVFDPE
      GPTCLETRLQ LYKEGLQGSL TSLKNPLTMM ANHYKQHCPP TPESPCATQN
      INFKSFKENL KDFLFNIPFD CWKPVKK.

    • Background

      What is the molecular weight/Mw of GM-CSF K9 Protein?
      GM-CSF K9 Protein has a total Mw of 14.2kDa.

      What is the source or expression system of GM-CSF K9 Protein?
      Escherichia Coli.

      What is the Purity of GM-CSF K9 Protein?
      GM-CSF K9 Protein is >96% pure as determined by SDS-PAGE.

      What is the Biological Activity of GM-CSF K9 Protein?
      The ED50 as calculated by the dose-dependent stimulation of the proliferation of human TF1 erythroleukemic cells is typically 1-4 ng/ml.

      What is the amino acid sequence of GM-CSF K9 Protein?
      APTRSPTLVT RPSQHVDAIQ EALSLLNNSN DVTAVMNKAV KVVSEVFDPE
      GPTCLETRLQ LYKEGLQGSL TSLKNPLTMM ANHYKQHCPP TPESPCATQN
      INFKSFKENL KDFLFNIPFD CWKPVKK.

      What applications can GM-CSF K9 Protein be used in?
      GM-CSF K9 Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for GM-CSF K9 Protein?
      The endotoxin level is minimal, GM-CSF K9 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.

    Gmcsf Canine
  • View Data Sheet

    Description:

    TRAIL Receptor-1 Human Recombinant Fc

    Tumor Necrosis Factor Receptor Superfamily Member 10a, TRAILR1, APO2, DR4, TNF-Related Apoptosis-Inducing Ligand Receptor 1, Death Receptor 4, TRAIL Receptor 1, TRAIL-R1, Tumor Necrosis Factor Receptor Superfamily Member 10a Variant 2, Tumor Necrosis Factor Receptor Superfamily Member 10A, Cytotoxic TRAIL Receptor, CD261 Antigen, TRAILR-1, CD261, TNFRSF10A.

    Product # :

    CYT-877

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    Description

    TRAIL R1 Fc Human Recombinant (24-240) produced in E.Coli is a non-glycosylated, disulfide-linked homodimer containing two polypeptide chains of 217 amino acids each and having a molecular mass of 41kDa [including tag] each chain. TRAILR1 is fused to a 236 amino acid Fc tag at C-terminal and purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Lyophilized from a 0.2µm filtered solution in PBS.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Biological Activity

    The ED50, as measured by its ability to inhibit Trail-mediated cytotoxicity in mouse L-929 cells, is less than 1.25ng/ml.

    More Info

    • Introduction

      Human TNFRSF10A is a type 1 transmembrane protein in the TNF R superfamily. TNFRSF10A is not expressed in rodents. The trimeric ligand Trail binds TNFRSF10A and induces apoptosis, and recombinant, soluble forms of the receptor inhibit Trail-induced apoptosis. TNFRSF10A is expressed generally in damaged, infected, and malignant cells. TNFRSF10A functions in immune surveillance, inducing apoptosis in cancer cells but not normal cells.

    • Synonyms

      Tumor Necrosis Factor Receptor Superfamily Member 10a, TRAILR1, APO2, DR4, TNF-Related Apoptosis-Inducing Ligand Receptor 1, Death Receptor 4, TRAIL Receptor 1, TRAIL-R1, Tumor Necrosis Factor Receptor Superfamily Member 10a Variant 2, Tumor Necrosis Factor Receptor Superfamily Member 10A, Cytotoxic TRAIL Receptor, CD261 Antigen, TRAILR-1, CD261, TNFRSF10A.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized TNFRSF10A although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution TRAIL-R1 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 TNFRSF10A in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      ASGTEAAAAT PSKVWGSSAG RIEPRGGGRG ALPTSMGQHG PSARARAGRA PGPRPAREAS PRLRVHKTFK FVVVGVLLQV VPSSAATIKL HDQSIGTQQW EHSPLGELCP PGSHRSERPG ACNRCTEGVG YTNASNNLFA CLPCTACKSD EEERSPCTTT RNTACQCKPG TFRNDNSAEM CRKCSTGCPR GMVKVKDCTP WSDIECVHKE SGNGHNIEGR MDPKSCDKTH TCPPCPAPEL LGGPSVFLFP PKPKDTLMIS RTPEVTCVVV DVSHEDPEVK FNWYVDGVEV HNAKTKPREE QYNSTYRVVS VLTVLHQDWL NGKEYKCKVS NKALPAPIEK TISKAKGQPR EPQVYTLPPS RDELTKNQVS LTCLVKGFYP SDIAVEWESN GQPENNYKTT PPVLDSDGSF FLYSKLTVDK SRWQQGNVFS CSVMHEALHN HYTQKSLSLS PGK.

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    Tnfrsf10A Human Fc