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Search results

1000 results found for “placental growth factor”

Name

Description

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  • View Data Sheet

    Name :

    Activin A Human

    Description:

    Activin A Human Recombinant

    Activin Beta-A chain, Erythroid differentiation protein, EDF, FRP, Activin-A, Inhibin-B, Inihibin-Beta A chain.

    Product # :

    CYT-569

    Price :

    Quantity :

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    • sds-page

    Description

    Activin-A Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 137 amino acids (311-426) and having a molecular mass of 15.2kDa.Activin-A is fused to a 21 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Activin-A protein solution (1mg/ml) contains 20mM Tris pH 8.0 and 10% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    sds-page

    Activin A Human sds-page - Product image 1

    More Info

    • Introduction

      Inhibins are dimeric peptide hormones produced by female ovarian granulose cells and male Sertoli cells as well as a variety of other tissues. Inhibins have two isoforms, A and B, with the same alpha subunit but different beta subunits. Inhibin A is a dimer of alpha and beta A subunits, inhibin B is a dimer of alpha and beta B subunits.
      Inhibins are thought to inhibit the production of follicle-stimulating hormone (FSH) by the pituitary gland. In addition, Inhibins are also thought to play a role in the control of gametogenesis, and embryonic and fetal development.

    • Synonyms

      Activin Beta-A chain, Erythroid differentiation protein, EDF, FRP, Activin-A, Inhibin-B, Inihibin-Beta A chain.

    • 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 MGLECDGKVN ICCKKQFFVS FKDIGWNDWI IAPSGYHANY CEGECPSHIA GTSGSSLSFH STVINHYRMR GHSPFANLKS CCVPTKLRPM SMLYYDDGQN IIKKDIQNMI VEECGCS.

    • Background

      What is the molecular weight / Mw of Activin A Protein?
      Activin A Protein has a total Mw of 15.2 kDa.

      What is the source or expression system of Activin A Protein?
      E.Coli

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

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

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

      What is the amino acid sequence of ACTIVIN A Protein?MGSSHHHHHH SSGLVPRGSH MGLECDGKVN ICCKKQFFVS FKDIGWNDWI IAPSGYHANY CEGECPSHIA GTSGSSLSFH STVINHYRMR GHSPFANLKS CCVPTKLRPM SMLYYDDGQN IIKKDIQNMI VEECGCS

      What applications can ACTIVIN-A Protein be used in?

      ACTIVIN A Protein can probably be used in western blot, ELISA and Lateral Flow.

    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.

    Activin A Human
  • View Data Sheet

    Name :

    PF4 Human, His

    Description:

    Platelet Factor-4 Human Recombinant (CXCL4), His Tag

    CXCL4, PF-4, PF4, Iroplact, Oncostatin-A, SCYB4, MGC138298.

    Product # :

    CHM-015

    Price :

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    Description

    PF4 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 91 amino acids (32-101 a.a) and having a molecular mass of 10kDa.PF4 is fused to a 21 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    PF4 protein solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.2M NaCl, 50% glycerol and 2mM DTT.

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Platelet factor-4 is a 70-amino acid protein that is released from the alpha-granules of activated platelets and binds with high affinity to heparin. Its major physiologic role appears to be neutralization of heparin-like molecules on the endothelial surface of blood vessels, thereby inhibiting local antithrombin III activity and promoting coagulation. As a strong chemoattractant for neutrophils and fibroblasts, PF4 probably has a role in inflammation and wound repair. Oncostatin-A is a member of the CXC chemokine family. Human PF4 is used for the proof of heparin-induced thrombocytopenia. Furthermore it is used as an inhibitor in the angiogenesis during tumor therapy.

    • Synonyms

      CXCL4, PF-4, PF4, Iroplact, Oncostatin-A, SCYB4, MGC138298.

    • Physical Appearance

      Sterile Filtered colorless clear solution.

    • Stability

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

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MEAEEDGDLQ CLCVKTTSQV RPRHITSLEV IKAGPHCPTA QLIATLKNGR KICLDLQAPL YKKIIKKLLE S.

    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.

    Pf4 Human His
  • View Data Sheet

    Name :

    GH Zebrafish

    Description:

    Growth Hormone Zebrafish Recombinant

    GH1, GH, GHN, GH-N, hGH-N, Pituitary growth hormone, Growth hormone 1, Somatotropin.

    Product # :

    CYT-710

    Price :

    Quantity :

    Shipping Method :

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    Shipped at Room temp

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    • description
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    • More Info

    Description

    Somatotropin Zebrafish Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 185 amino acids with an additional Ala at the N-terminus and having a molecular mass of 21.18 kDa. The Zebrafish Recombinant is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The protein was lyophilized from a concentrated (1mg/ml) solution with 0.05% NaHCO3 pH-8.

    Purity

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

    Biological Activity

    Zebrafish Growth-Hormone is biologically active in PDF-P1 3B9 cells stably transfected with rabbit GH receptors.

    More Info

    • Introduction

      GH is a member of the somatotropin/prolactin family of hormones which play an important role in growth control. The gene, along with four other related genes, is located at the growth hormone locus on chromosome 17 where they are interspersed in the same transcriptional orientation; an arrangement which is thought to have evolved by a series of gene duplications. The five genes share a remarkably high degree of sequence identity. Alternative splicing generates additional isoforms of each of the five growth hormones, leading to further diversity and potential for specialization. This particular family member is expressed in the pituitary but not in placental tissue as is the case for the other four genes in the growth hormone locus. Mutations in or deletions of the gene lead to growth hormone deficiency and short stature.

    • Synonyms

      GH1, GH, GHN, GH-N, hGH-N, Pituitary growth hormone, Growth hormone 1, Somatotropin.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized Zebrafish Growth-Hormone although stable at room temperature for at least two weeks, should be stored desiccated below -18°C. Upon reconstitution and filter sterilization GH can be stored at 4°C, pH 9 for up to 4 weeks. For long term storage and more diluted solutions 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 Zebrafish Growth-Hormone in 0.4% NaHCO3 or water adjusted to pH-9, not less than 100µg/ml, which can then be further diluted to other aqueous solutions, preferably in a presence of a carrier protein such as BSA or similar.

    • Amino Acid Sequence

      AQRLFNNAVIRVQHLHQLAAKMINDFEEGLMPEERRQLSKIFPL

      SFCNSDSIETPTGKDETQKSSMLKLLRISFRLIESWEFPSQTLSS

      TISNSLTIGNPNLITEKLVDLKMGISVLIKGCLDGQPNMDDNDSL

      PLPFEDFYLTVGETSLRESFRLLACFKKDMHKVETYLRVANCRRSLDSNCTL

    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.

    Growth Hormone Zebrafish
  • View Data Sheet

    Name :

    SDF 1b Mouse

    Description:

    Stromal Cell Derived Factor-1 Beta Mouse Recombinant (CXCL12)

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

    Product # :

    CHM-326

    Price :

    Quantity :

    Shipping Method :

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    Shipped at Room temp

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    • More Info

    Description

    Stromal Cell-Derived Factor-1 beta Mouse Recombinant produced in E.Coli is a non-glycosylated, Polypeptide chain containing 72 amino acids and having a molecular mass of 8513 Dalton. The SDF-1b is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The CXCL12 protein was lyophilized from a concentrated (1mg/ml) sterile solution containing no additives.

    Purity

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

    Biological Activity

    The specific activity as determined by its ability to chemoattract human monocytes at 50-100ng/ml corresponding to a Specific Activity of 10,000-20,000IU/mg.

    More Info

    • Introduction

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

    • Synonyms

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

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized SDF-1b although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution CXCL12 should be stored at 4°C between 2-7 days and for future use below -18°C.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.

    • Solubility

      It is recommended to reconstitute the lyophilized Stromal Cell-Derived Factor-1b 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 Lys-Pro-Val-Ser-Leu.

    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.

    Sdf 1 B Mouse
  • View Data Sheet

    Name :

    hCG Protein

    Description:

    Chorionic Gonadotropin Human

    Chorionic gonadotropin, hCG, CG.

    Product # :

    HOR-250

    Price :

    Quantity :

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    • description
    • source
    • formulation
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    • More Info
    • Activity Assay

    Description

    Human Chorionic Gonadotropin is produced from a sterile preparation of placental glucoprotein urine of pregnant women having a total molecular mass of 36,700 Dalton. The hCG consists of 237 amino acids, a chain-92 amino acids and b chain-145 amino acids. The hCG is purified by proprietary chromatographic techniques.

    Source

    Urine of pregnant women.

    Formulation

    The hCG was lyophilized with no additives.

    Biological Activity

    The activity was found to be 5212IU/mg.

    Activity Assay

    hcg activity assay - Product image 1
    hcg bioactivity assay - Product image 2

    More Info

    • Introduction

      Human chorionic gonadotropin (hCG) is a peptide hormone produced in pregnancy, that is made by the embryosoon after conception and later by the syncytiotrophoblast(part of the placenta). Its role is to prevent the disintegration of the corpus luteumof the ovaryand thereby maintain progesterone production that is critical for a pregnancy in humans. hCG may have additional functions, for instance it is thought that it affects the immune tolerance of the pregnancy. Early pregnancy testing generally is based on the detection or measurement of hCG.

    • Synonyms

      Chorionic gonadotropin, hCG, CG.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Solubility

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

    • Contaminants

      Free of: HbsAg and antibodies to HIV and HCV.

    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.

    Hcg Human
  • View Data Sheet

    Name :

    GHBP Rabbit

    Description:

    Growth Hormone Binding Protein Rabbit Recombinant

    GHR, GHBP, GH receptor, Somatotropin receptor.

    Product # :

    CYT-593

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    Description

    Growth Hormone Binding Protein Rabbit Extracellular Domain Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 249 amino acids and having a molecular mass of 28 kDa. GHBP Rabbit is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The Growth Hormone Binding Protein Rabbit was lyophilized from a concentrated (1mg/ml) solution with 0.0045mM NaHCO3.

    Purity

    Greater than 98.0% as determined bySDS-PAGE.

    Biological Activity

    Evidenced by its ability of forming 2:1 complex with non-primate Growth Hormones.

    More Info

    • Introduction

      GHBP is a transmembrane receptor for growth hormone. Binding of growth hormone to the receptor leads to receptor dimerization and the activation of an intra- and intercellular signal transduction pathway leading to growth. A common alternate allele of this gene, called GHRd3, lacks exon three and has been well-characterized. Mutations in this gene have been associated with Laron syndrome, also known as the growth hormone insensitivity syndrome (GHIS), a disorder characterized by short stature. Other splice variants, including one encoding a soluble form of the protein (GHRtr), have been observed but have not been thoroughly characterized.

    • Synonyms

      GHR, GHBP, GH receptor, Somatotropin receptor.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized Growth Hormone Binding Protein Rabbit although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution GHBP Rabbit 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 GHBP Rabbit in sterile 0.4% NaHCO3 pH 10, not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      AFSGSEATPATLGRASESVQRVHPGLGTNSSGKPKFTKCRSPELETFSCHWTDGVHHGLK
      SPGSVQLFYIRRNTQEWTQEWKECPDYVSAGENSCYFNSSYTSIWIPYCIKLTNNGGMVD
      QKCFSVEEIVQPDPPIGLNWTLLNVSLTGIHADIQVRWEPPPNADVQKGWIVLEYELQYK
      EVNETQWKMMDPVLSTSVPVYSLRLDKEYEVRVRSRQRSSEKYGEFSEVLYVTLPQMSPFTCEEDFRFP.

    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.

    Gh Receptor Rabbit
  • View Data Sheet

    Name :

    CNTFR Rat

    Description:

    Ciliary Neurotrophic Factor Receptor Rat Recombinant

    Ciliary neurotrophic factor receptor subunit alpha, CNTF receptor subunit alpha, CNTFR-alpha.

    Product # :

    CYT-959

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    Description

    CNTFR Rat Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 328 amino acids (23-342a.a) and having a molecular mass of 36.9kDa (Molecular size on SDS-PAGE will appear at approximately 40-57kDa). CNTFR is fused to an 8 amino acid His-tag at C-terminus & purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

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

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Ciliary Neurotrophic Factor Receptor, also known as CNTFR is a member of the type I cytokine receptor family. CNTFR binds to CNTF.The alpha subunit provides the receptor specificity.Sole nucleotide polymorphisms in CNTFR has been associated with variations in muscle strength, in addition to early onset of eating disorders.

    • Synonyms

      Ciliary neurotrophic factor receptor subunit alpha, CNTF receptor subunit alpha, CNTFR-alpha.

    • Physical Appearance

      Sterile Filtered colorless clear solution.

    • Stability

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

      QKHSPQEAPH VQYERLGTDV TLPCGTASWD AAVTWRVNGT DLAPDLLNGS QLILRSLELG HSGLYACFHR DSWHLRHQVL LHVGLPPREP VLSCRSNTYP KGFYCSWHLS APTYIPNTFN VTVLHGSKMM VCEKDPALKN RCHIRYMHLF STIKYKVSIS VSNALGHNTT AITFDEFTIV KPDPPENVVA RPVPSNPRRL EVTWQTPSTW PDPESFPLKF FLRYRPLILD QWQHVELSNG TAHTITDAYA GKEYIIQVAA KDNEIGTWSD WSVAAHATPW TEEPRHLTTE AQAPETTTST TSSLAPPPTT KICDPGELSS LEHHHHHH.

    • Background

      What is the molecular weight/Mw of CNTFR Protein?
      CNTFR Protein has a total Mw of 36.9kDa.

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

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

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

      What is the amino acid sequence of CNTFR Protein?
      QKHSPQEAPH VQYERLGTDV TLPCGTASWD AAVTWRVNGT DLAPDLLNGS QLILRSLELG HSGLYACFHR DSWHLRHQVL LHVGLPPREP VLSCRSNTYP KGFYCSWHLS APTYIPNTFN VTVLHGSKMM VCEKDPALKN RCHIRYMHLF STIKYKVSIS VSNALGHNTT AITFDEFTIV KPDPPENVVA RPVPSNPRRL EVTWQTPSTW PDPESFPLKF FLRYRPLILD QWQHVELSNG TAHTITDAYA GKEYIIQVAA KDNEIGTWSD WSVAAHATPW TEEPRHLTTE AQAPETTTST TSSLAPPPTT KICDPGELSS LEHHHHHH.

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

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

    Cntfr Rat
  • View Data Sheet

    Name :

    G CSF Antibody, Biotin

    Description:

    Granulocyte Colony Stimulating Factor, Mouse Anti-Human, Biotin

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

    Product # :

    ANT-240

    Price :

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    • More Info

    Formulation

    1 mg/ml in PBS (after reconstitution).

    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 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 Biotin
  • View Data Sheet

    Name :

    PEDF PAT13D9AT Antibody

    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

    Price :

    Quantity :

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    • More Info

    Formulation

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

    More Info

    • 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

    Name :

    BMP4 Human, Active

    Description:

    Bone Morphogenetic protein-4 Active Active, Human Recombinant

    BMP4, ZYME, BMP2B, BMP2B1.

    Product # :

    CYT-1293

    Price :

    Quantity :

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    Description

    Bone Morphogenetic protein-4 Active Human Recombinant produced in E.coli is a homodimer , non-glycosylated, polypeptide chain containing 2x116 amino acids (ser293-arg408) and having a total molecular mass of 26.2kDa. BMP4 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The protein was lyophilized from a sterile (0.2µm) filtered solution containing 4mM HCL.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Biological Activity

    The ED50, as calculated by Alkaline phosphatase activity induced in ATDC-5 cells is 157.2ng/ml corresponding to a specific activity which is 6361 units/mg.

    More Info

    • Synonyms

      BMP4, ZYME, BMP2B, BMP2B1.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized BMP4 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution BMP4 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 BMP4 in sterile 4mM HCl at a concentration of 0.1 mg/ml, which can then be further diluted to other aqueous solutions

    • Amino Acid Sequence

      SPKHHSQRAR KKNKNCRRHS LYVDFSDVGW NDWIVAPPGY QAFYCHGDCP FPLADHLNST NHAI VQT LVN SVNSSIPKAC CVPTELSAIS MLYLDEYDKV VLKNYQEMVV EGCGCR.

    • Background

      The protein encoded by this gene is a member of the bone morphogenetic protein family which is part of the transforming growth factor-beta superfamily.

      The superfamily includes large families of growth and differentiation factors.

      Bone morphogenetic proteins were originally identified by an ability of demineralized bone extract to induce endochondral osteogenesis in vivo in an extraskeletal site.

      This particular family member plays an important role in the onset of endochondral bone formation in humans, and a reduction in expression has been associated with a variety of bone diseases, including the heritable disorder Fibrodysplasia Ossificans Progressiva.

      What is the molecular weight/Mw of BMP4 Protein?
      BMP4 Protein has a total Mw of 26.2kDa.

      What is the source or expression system of BMP4 Protein?
      Escherichia Coli.

      What is the Purity of BMP4 Protein?
      BMP4 Protein is >95% pure as determined by SDS-PAGE.

      What is the Biological Activity of BMP4 Protein?

      The ED50, as calculated by Alkaline phosphatase activity induced in ATDC-5 cells is 157.2ng/ml corresponding to a specific activity which is 6361 units/mg.

      What is the amino acid sequence of BMP4 Protein?
      SPKHHSQRAR KKNKNCRRHS LYVDFSDVGW NDWIVAPPGY QAFYCHGDCP FPLADHLNST NHAI VQT LVN SVNSSIPKAC CVPTELSAIS MLYLDEYDKV VLKNYQEMVV EGCGCR.

      What applications can BMP4 Protein be used in?
      BMP4 Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for BMP4 Protein?
      The endotoxin level is minimal, BMP4 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.

    Bmp4 Human Active
  • View Data Sheet

    Name :

    PRL R Rabbit

    Description:

    Prolactin Rabbit Soluble Receptor Recombinant

    PRL-R.

    Product # :

    CYT-268

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    Description

    Prolactin Receptor Rabbit Extra Celleular Domain Recombinant ?produced in E.Coli is a non-glycosylated, Polypeptide chain containing 207 amino acids and having a molecular mass of 23972 Dalton. The Prolactin Receptor is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The protein was lyophilized from a concentrated (1mg/ml) solution with 0.0045mM NaHCO3.

    Purity

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

    Biological Activity

    Activity is determined by the dose-dependant inhibition of Prolactin-stimuled proliferation of Nb2 cells and by high affinity binding of oPLR and other lactogenic hormones. Refs:
    1) Bignon et al. (1994) JBC 269; 3318-24
    2) Gertler et al. (1996) JBC 271; 24482-91.

    More Info

    • Introduction

      Prolactin is a pituitary hormone involved in the stimulation of milk production, salt and water regulation, growth, development and reproduction. The initial step in its action is the binding to a specific membrane receptor (prolactin receptor) which belongs to the superfamily of class 1 cytokine receptors. The function of the prolactin receptor is mediated, at least in part, by two families of signaling molecules: Janus kinases and signal transducers and activators of transcription. Prolactin (PRL) is a hormone involved in a variety of important functions including ion transport and osmoregulation, stimulation of milk, protein synthesis as well as the regulation of numerous reproductive functions. PRL exerts its influence on different cell types through a signal transduction pathway which begins with the binding of the hormone to a transmembrane PRL receptor. Immunoreactive PRL receptor, a member of the cytokine receptor family, varies in size (short and long forms) with tissue source and species, from ~40 kDa to 100 kDa. The PRL receptor consists of at least three separate domains: an extracellular region with 5 cysteines which contains the prolactin binding site, a single transmembrane domain and a cytoplasmic region, the length of which appears to influence ligand binding and regulate cellular function.

    • Synonyms

      PRL-R.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized PRL-R although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Prolactin Receptor 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 PRL-R 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-Lys-Pro-Phe-Ile.

    • Protein content

      UV spectroscopy at 280 nm using the absorbency value of 2.63 as the extinction coefficient for a 0.1% (1mg/ml) solution. This value is calculated by the PC GENEcomputer analysis program of protein sequences (IntelliGenetics).

    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.

    Prlr Rabbit
  • View Data Sheet

    Name :

    KIT Human

    Description:

    KIT Proto-Oncogene Receptor Tyrosine Human Recombinant

    Mast/stem cell growth factor receptor Kit, SCFR, Piebald trait protein, PBT, Proto-oncogene c-Kit, Tyrosine-protein kinase Kit, p145 c-kit, v-kit Hardy-Zuckerman 4 feline sarcoma viral oncogene homolog, CD117.

    Product # :

    PKA-102

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    • More Info

    Description

    KIT produced in Sf9 Insect cells is a single, glycosylated polypeptide chain containing 507 amino acids (26-524 a.a.) and having a molecular mass of 57.1kDa (Molecular size on SDS-PAGE will appear at approximately 50-70kDa).KIT is expressed with an 8 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus.

    Formulation

    KIT 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

      KIT, also known as KIT Proto-Oncogene Receptor Tyrosine, is a cytokine receptor which is expressed not only in hematopoietic stem cells but likewise in other cell types. KIT binds to receptor tyrosine kinase type III, which is a stem cell factor, also named a "rigid factor" or "c-kit ligand". Once this receptor binds to stem cell factor (SCF), it forms a dimer which activates intrinsic tyrosine kinase activity, which sequentially phosphorylates & activates signaling molecules which breed signals in cells. This receptor protects vascular smooth muscle cells from apoptosis in addition to restoring cardiac function after myocardial infarction.

    • Synonyms

      Mast/stem cell growth factor receptor Kit, SCFR, Piebald trait protein, PBT, Proto-oncogene c-Kit, Tyrosine-protein kinase Kit, p145 c-kit, v-kit Hardy-Zuckerman 4 feline sarcoma viral oncogene homolog, CD117.

    • 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

      QPSVSPGEPS PPSIHPGKSD LIVRVGDEIR LLCTDPGFVK WTFEILDETN ENKQNEWITE KAEATNTGKY TCTNKHGLSN SIYVFVRDPA KLFLVDRSLY GKEDNDTLVR CPLTDPEVTN YSLKGCQGKP LPKDLRFIPD PKAGIMIKSV KRAYHRLCLH CSVDQEGKSV LSEKFILKVR PAFKAVPVVS VSKASYLLRE GEEFTVTCTI KDVSSSVYST WKRENSQTKL QEKYNSWHHG DFNYERQATL TISSARVNDS GVFMCYANNT FGSANVTTTL EVVDKGFINI FPMINTTVFV NDGENVDLIV EYEAFPKPEH QQWIYMNRTF TDKWEDYPKS ENESNIRYVS ELHLTRLKGT
      EGGTYTFLVS NSDVNAAIAF NVYVNTKPEI LTYDRLVNGM LQCVAAGFPE PTIDWYFCPG TEQRCSASVL PVDVQTLNSS GPPFGKLVVQ SSIDSSAFKH NGTVECKAYN DVGKTSAYFN FAFKGNNKEQ IHPHTLFTPL EHHHHHH.

    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.

    Kit Human
  • View Data Sheet

    Name :

    EEF1G Human

    Description:

    Eukaryotic Translation Elongation Factor 1 Gamma Human Recombinant

    EF1G, GIG35, Elongation factor 1-gamma, Eukaryotic Translation Elongation Factor 1 Gamma, EEF1G, EF-1-gamma, eEF-1B gamma, PRO1608.

    Product # :

    PRO-2048

    Price :

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    • description
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    • More Info

    Description

    EEF1G Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 460 amino acids (1-437) and having a molecular mass of 52.5 kDa.EEF1G is fused to a 23 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    The EEF1G solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 10% glycerol and 1mM DTT.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    More Info

    • Introduction

      Eukaryotic Translation Elongation Factor 1 Gamma (EEF1G) takes part in anchoring the complex to additional cellular components. EEF1G is a multi-protein complex which is in charge of the delivery of aminoacyl-tRNAs to the ribosome. Over expression of EEF1G is linked with pancreatic cancer, due to the role of EEF1G protein in the oncogenic transformation process.

    • Synonyms

      EF1G, GIG35, Elongation factor 1-gamma, Eukaryotic Translation Elongation Factor 1 Gamma, EEF1G, EF-1-gamma, eEF-1B gamma, PRO1608.

    • 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 MGSMAAGTLY TYPENWRAFK ALIAAQYSGA QVRVLSAPPH FHFGQTNRTP EFLRKFPAGK VPAFEGDDGF CVFESNAIAY YVSNEELRGS TPEAAAQVVQ WVSFADSDIV PPASTWVFPT LGIMHHNKQA TENAKEEVRR ILGLLDAYLK TRTFLVGERV TLADITVVCT LLWLYKQVLE PSFRQAFPNT NRWFLTCINQ PQFRAVLGEV KLCEKMAQFD AKKFAETQPK KDTPRKEKGS REEKQKPQAE RKEEKKAAAP APEEEMDECE QALAAEPKAK DPFAHLPKST FVLDEFKRKY SNEDTLSVAL PYFWEHFDKD GWSLWYSEYR FPEELTQTFM SCNLITGMFQ RLDKLRKNAF ASVILFGTNN SSSISGVWVF RGQELAFPLS PDWQVDYESY TWRKLDPGSE ETQTLVREYF SWEGAFQHVG KAFNQGKIFK.

    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.

    Eef1G Human
  • View Data Sheet

    Name :

    LIF Human

    Description:

    Leukemia Inhibitory Factor Human Recombinant

    CDF, HILDA, D-FACTOR, Differentiation- stimulating factor, Melanoma-derived LPL inhibitor, MLPLI, Emfilermin, Leukemia inhibitory factor, LIF, DIA.

    Product # :

    CYT-644

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    Description

    Leukemia Inhibitory Factor (LIF) Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 180 amino acids and having a molecular mass of 19.7kDa. The Leukemia Inhibitory Factor (LIF) is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Leukemia Inhibitory Factor (LIF) was lyophilized from a concentrated (1mg/ml) sterile solution containing 1xPBS 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 was determined by the M1 cell differentiation assay is < 0.01 ng/ml, corresponding to a specific activity of 100,000,000IU/mg.

    More Info

    • Introduction

      Leukemia Inhibitory Factor also called LIF is a lymphoid factor that promotes long-term maintenance of embryonic stem cells by suppressing spontaneous differentiation. Leukemia Inhibitory Factor has several functions such as cholinergic neuron differentiation, control of stem cell pluripotency, bone & fat metabolism, mitogenesis of factor dependent cell lines & promotion of megakaryocyte production in vivo. Human and mouse LIF exhibit a 78% identity in its amino acid sequence.

    • Synonyms

      CDF, HILDA, D-FACTOR, Differentiation- stimulating factor, Melanoma-derived LPL inhibitor, MLPLI, Emfilermin, Leukemia inhibitory factor, LIF, DIA.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Amino Acid Sequence

      SPLPITPVNA TCAIRHPCHN NLMNQIRSQL AQLNGSANAL FILYYTAQGE PFPNNLDKLC GPNVTDFPPF HANGTEKAKL VELYRIVVYL GTSLGNITRD QKILNPSALS LHSKLNATAD ILRGLLSNVL CRLCSKYHVG HVDVTYGPDT SGKDVFQKKK LGCQLLGKYK QIIAVLAQAF.

    • Background

      Leukemia Inhibitory Factor (LIF) Background

      Leukemia Inhibitory Factor (LIF) is a cytokine within the interleukin-6 family. It is influential in the hypothalamus and involved in energy balance.

      LIF stimulates ACTH secretion and affects the stress and immune response in the body. Administration of LIF has been shown to correct low plasma ACTH and repair hypothalamic-pituitary-adrenal (HPA) axis responses.

      Function and Applications of LIF

      LIF prevents the proliferation of myeloid leukemia cells by inducing their terminal differentiation. Beyond cancer, LIF influences bone metabolism, embryogenesis, and inflammation.

      Moreover, it supports the self-renewal of stem cells in culture by activating Stat3, thus preventing spontaneous differentiation, and is studied for potential benefits in fertility treatments.

      Structure and Interactions

      LIF's structure consists of a four alpha-helix bundle similar to other hematopoietic cytokines. It interacts with components such as the ciliary neurotrophic factor (CNTF) through multimeric receptors, influencing both cytokine's effects on cells. This interaction is crucial for forming high-affinity binding sites that mediate their biological activities.

    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.

    Lif Human
  • View Data Sheet

    Name :

    CPSF4 Human

    Description:

    Cleavage And Polyadenylation Specific Factor 4 Human Recombinant

    CPSF30, NAR, NEB1, Neb-1, CPSF 30 kDa subunit, NS1 effector domain-binding protein 1.

    Product # :

    PRO-1406

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    Description

    CPSF4 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 267 amino acids (1-244 a.a.) and having a molecular mass of 29.9kDa.CPSF4 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    CPSF4 protein solution (1mg/ml) contains 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

      Cleavage And Polyadenylation Specific Factor 4 (CPSF4) is a member of the CPSF4/YTH1 family. CPSF4 complex plays a vital role in pre-mRNA 3'-end formation, distinguishing the AAUAAA signal sequence and interacting with poly(A) polymerase and further factors to bring about cleavage and poly(A) additive. CPSF4 binds RNA polymers with a preference for poly(U).

    • Synonyms

      CPSF30, NAR, NEB1, Neb-1, CPSF 30 kDa subunit, NS1 effector domain-binding 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 MGSMQEIIAS VDHIKFDLEI AVEQQLGAQP LPFPGMDKSG AAVCEFFLKA ACGKGGMCPF RHISGEKTVV CKHWLRGLCK KGDQCEFLHE YDMTKMPECY FYSKFGECSN KECPFLHIDP ESKIKDCPWY DRGFCKHGPL CRHRHTRRVI CVNYLVGFCP EGPSCKFMHP RFELPMGTTE QPPLPQQTQP PAKQRTPQVI GVMQSQNSSA GNRGPRPLEQ VTCYKCGEKG HYANRCTKGH LAFLSGQ.

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    Cpsf4 Human
  • View Data Sheet

    Name :

    ING1 Human

    Description:

    Inhibitor of Growth Family, Member 1 Human Recombinant

    Inhibitor Of Growth Family, Member 1, Growth Inhibitory Protein ING1, Tumor Suppressor ING1, Growth Inhibitor ING1, Inhibitor Of Growth Protein 1, Inhibitor Of Growth 1, P24ING1c,P33ING1b, P47ING1a, P33ING1, P33, P47, ING1 .

    Product # :

    PRO-2130

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    Description

    ING1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 302 amino acids (1-279 a.a) and having a molecular mass of 34.3kDa.ING1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    ING1 protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH 8.0) and 10% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Inhibitor of Growth Family Member 1, also known as ING1 is a tumor suppressor protein which is able to induce cell growth arrest and apoptosis. ING1 is a nuclear protein which physically act together with the tumor suppressor protein TP53 and is a component of the p53 signaling pathway. In addition, Reduced expression and rearrangement of ING1 have been identified in various cancers. Multiple alternatively spliced transcript variants encoding distinct isoforms have been described for ING1.

    • Synonyms

      Inhibitor Of Growth Family, Member 1, Growth Inhibitory Protein ING1, Tumor Suppressor ING1, Growth Inhibitor ING1, Inhibitor Of Growth Protein 1, Inhibitor Of Growth 1, P24ING1c,P33ING1b, P47ING1a, P33ING1, P33, P47, ING1 .

    • 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 MGSMLSPANG EQLHLVNYVE DYLDSIESLP FDLQRNVSLM REIDAKYQEI LKELDECYER FSRETDGAQK RRMLHCVQRA LIRSQELGDE KIQIVSQMVE LVENRTRQVD SHVELFEAQQ ELGDTAGNSG KAGADRPKGE AAAQADKPNS KRSRRQRNNE NRENASSNHD HDDGASGTPK EKKAKTSKKK KRSKAKAERE ASPADLPIDP NEPTYCLCNQ VSYGEMIGCD NDECPIEWFH FSCVGLNHKP KGKWYCPKCR GENEKTMDKA LEKSKKERAY NR.

    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.

    Ing1 Human
  • View Data Sheet

    Name :

    OPG Human, Hi-5

    Description:

    Osteoprotegerin Human Recombinant, Hi-5

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

    Product # :

    CYT-633

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    Description

    Recombinant Osteoprotegerin produced in baculovirus is a signle, glycosylated polypeptide chain containing 389 amino acid residues (22-401 a.a.), having a calculated molecular mass of 44.7 kDa. The Osteoprotegerin is fused to a 6 amino acid His tag at C-terminus and purified by proprietary chromatographic techniques.

    Source

    Hi-5.

    Formulation

    Osteoprotegerin protein contains PBS pH-7.4 and 10% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    Biological Activity

    The ED50 range ≤ 8 ng/ml and is measured by its ability to inhibit cytotoxicity using Jurkat human acute T cell leukemia cells in the presence of 2ng/ml of human TRAIL (CAT# cyt-1014).

    More Info

    • Introduction

      Osteoprotegerin acts as decoy receptor for rankl and thereby neutralizes its function in osteoclastogenesis. OPG inhibits the activation of osteoclasts and promotes osteoclast apoptosis in vitro. Bone homeostasis seems to depend on the local rankl/opg ratio. Osteoprotegerin may also play a role in preventing arterial calcification. May act as decoy receptor for trail and protect against apoptosis. Trail binding blocks the inhibition of osteoclastogenesis.

    • Synonyms

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

    • Physical Appearance

      Sterile Filtered colorless clear solution.

    • Stability

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

    • Amino Acid Sequence

      ADPETFPPKY LHYDEETSHQ LLCDKCPPGT YLKQHCTAKW KTVCAPCPDH YYTDSWHTSD ECLYCSPVCK ELQYVKQECN RTHNRVCECK EGRYLEIEFC LKHRSCPPGF GVVQAGTPER NTVCKRCPDG FFSNETSSKA PCRKHTNCSV FGLLLTQKGN ATHDNICSGN SESTQKCGID VTLCEEAFFR FAVPTKFTPN WLSVLVDNLP GTKVNAESVE RIKRQHSSQE QTFQLLKLWK HQNKDQDIVK KIIQDIDLCE NSVQRHIGHA NLTFEQLRSL MESLPGKKVG AEDIEKTIKA CKPSDQILKL LSLWRIKNGD QDTLKGLMHA LKHSKTYHFP KTVTQSLKKT IRFLHSFTMY KLYQKLFLEM IGNQVQSVKI SCLSHHHHHH.

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

    Osteoprotegerin Human Hi 5
  • View Data Sheet

    Name :

    CDNF Human

    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

    Name :

    GroES Human

    Description:

    GroES (HSP10) Human Recombinant

    CPN10, GROES, HSP10, HSPE1, Chaperonin-10, 10 kDa heat shock protein mitochondrial, 10 kDa chaperonin, Early-pregnancy factor, EPF.

    Product # :

    HSP-015

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    Description

    Recombinant GroES produced in E.Coli is a single, non-glycosylated polypeptide chain containing 102 amino acids and having a molecular mass of 10 kDa.

    Source

    Escherichia Coli.

    Formulation

    The GroES protein contains 20mM Tris buffer pH-8 & 50mM NaCl.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      HSP10 is part of the molecular chaperons, that are crucial for thir efficient folding of proteins in normal as well as stress conditions. GroES function is to bind to HSP60 in the presence of ATP, thus causing a change in the HSP60 conformation & enclosing the protein substrate within the complex. ATP hydrolysis by chaperonin-60 which destabilizes the HSP10-HSP60 complex, thereby allowing it to dissociate and secrete the substrate protein.
      GroES having the NCBI accession number of NP_002148 was purified by using conventional chromatography techniques.

    • Synonyms

      CPN10, GROES, HSP10, HSPE1, Chaperonin-10, 10 kDa heat shock protein mitochondrial, 10 kDa chaperonin, Early-pregnancy factor, EPF.

    • 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

      MAGQAFRKFL PLFDRVLVER SAAETVTKGG IMLPEKSQGK VLQATVVAVG SGSKGKGGEI QPVSVKVGDK VLLPEYGGTK VVLDDKDYFL FRDGDILGKY VD.

    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.

    Groes Human
  • View Data Sheet

    Name :

    CNTF Human, His

    Description:

    Ciliary Neurotrophic Factor Human Recombinant, His Tag

    HCNTF, CNTF, Ciliary Neurotrophic Factor.

    Product # :

    CYT-573

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    Description

    Ciliary Neurotrophic Factor Recombinant Human produced in E.Coli is a single, non-glycosylated polypeptide chain (aa 1-200) containing a total of 220 amino acids and having a molecular mass of 25kDa. The CNTF protein is fused to a 20 aa His Tag at N-terminus and purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    CNTF protein solution (1mg/ml) contains 20mM Tris-HCl buffer pH-8 and 1mM DTT.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    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 colorless clear solution.

    • Stability

      Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. 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 MAFTEHSPLT PHRRDLCSRS IWLARKIRSDLTALTESYVK HQGLNKNINL DSADGMPVAS TDQWSELTEA ERLQENLQAY RTFHVLLARL LEDQQVHFTP TEGDFHQAIH TLLLQVAAFA YQIEELMILL EYKIPRNEAD GMPINVGDGG LFEKKLWGLK VLQELSQWTV RSIHDLRFIS SHQTGIPARG SHYIANNKKM.

    • Background

      What is the molecular weight/Mw of CNTF Protein?
      CNTF Protein has a total Mw of 25kDa.

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

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

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

      What is the amino acid sequence of CNTF Protein?
      MGSSHHHHHH SSGLVPRGSH MAFTEHSPLT PHRRDLCSRS IWLARKIRSDLTALTESYVK HQGLNKNINL DSADGMPVAS TDQWSELTEA ERLQENLQAY RTFHVLLARL LEDQQVHFTP TEGDFHQAIH TLLLQVAAFA YQIEELMILL EYKIPRNEAD GMPINVGDGG LFEKKLWGLK VLQELSQWTV RSIHDLRFIS SHQTGIPARG SHYIANNKKM.

      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.

    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 His
  • View Data Sheet

    Name :

    Leptin Dog

    Description:

    Leptin Dog Recombinant

    OB Protein, Obesity Protein, OBS, Obesity factor.

    Product # :

    CYT-506

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    Description

    Leptin Dog Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 146 amino acids and having a molecular mass of 16 kDa.The Leptin is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The protein was lyophilized from a concentrated (1mg/ml) solution with 0.02% NaHCO3.

    Purity

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

    Biological Activity

    Biological active as evidenced by inducing proliferation of BAF/3 cells stably transfected with the long form of human leptin receptor.

    More Info

    • Introduction

      A 16-kDa peptide hormone secreted from white adipocytes and implicated in the regulation of food intake and energy balance. Leptin provides the key afferent signal from fat cells in the feedback system that controls body fat stores.

    • Synonyms

      OB Protein, Obesity Protein, OBS, Obesity factor.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized Leptin although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Leptin 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 Leptin in sterile 0.4% NaHCO3 adjusted to pH 8-9, not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      The sequence of the first five N-terminal amino acids was determined and was found to be Ala-Val-Pro-Ile-Arg.

    • Protein content

      Protein quantitation was carried out by UV spectroscopy at 280 nm using the absorbency value of 0.20 as the extinction coefficient for a 0.1% (1mg/ml) solution at pH 8.0. This value is calculated by the PC GENE computer analysis program of protein sequences (IntelliGenetics).

    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.

    Leptin Dog
  • View Data Sheet

    Name :

    LGALS7 Human, His

    Description:

    Galectin-7 Human Recombinant, His Tag

    Galectin-7, Gal-7, HKL-14, PI7, p53-induced gene 1 protein, LGALS7, PIG1, LGALS7B, GAL7, LGALS7A.

    Product # :

    CYT-617

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    • description
    • source
    • formulation
    • purity
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    • SDS-PAGE

    Description

    Galectin-7 Human Recombinant fused with a 20 amino acid His tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 156 amino acids (1-136 a.a.) and having a molecular mass of 17.2kDa. The Galectin-7 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The Galectin-7 solution (1 mg/ml) 20mM Tris-HCl buffer (pH 8.0), 10% glycerol and 1mM DTT.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    SDS-PAGE

    LGALS7 Human, His-SDS-PAGE - Product image 1

    More Info

    • Introduction

      Galectins are a family of animal lectins with an affinity for beta-galactosides. This family has at least 14 identified members. Galectins share similarities in the CRD (the carbohydrate recognition domain). Galectins are synthesized as cytosolic proteins. Though localized principally in the cytoplasm and lacking a classical signal peptide, galectins can also be stimulated to secretion by non-classical pathways or alternatively targeted to the nucleus. Galectins are involved in modulating cell-cell and cell-matrix interactions. Human Galectin-7 belongs to the prototypical Galectins containing a single CRD, which is initially identified in human epidermis as a monomer. The Galectin-7 expression is induced by tumor suppressor protein p53 and associated with apoptosis. Galectin-7 is a pro-apoptotic protein which functions intracellularlly upstream of JNK activation and mitochondrial cytochrome c release. The correlation of Galectin-7 with the UV-induced apoptosis of keratinocytes presents a critical mechanism in the maintenance of epidermal homeostasis. Human Galectin-7 is localized in both nucleus and cytoplasm.

    • Synonyms

      Galectin-7, Gal-7, HKL-14, PI7, p53-induced gene 1 protein, LGALS7, PIG1, LGALS7B, GAL7, LGALS7A.

    • 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 MSNVPHKSSL PEGIRPGTVL RIRGLVPPNA SRFHVNLLCG EEQGSDAALH FNPRLDTSEV VFNSKEQGSW GREERGPGVP FQRGQPFEVL IIASDDGFKA VVGDAQYHHF RHRLPLARVR LVEVGGDVQL DSVRIF.

    • Background

      What is the molecular weight/Mw of LGALS7 HUMAN, HIS Protein?
      LGALS7 HUMAN, HIS Protein has a total Mw of 17.2kDa.

      What is the source or expression system of LGALS7 HUMAN, HIS Protein?
      Escherichia Coli.

      What is the Purity of LGALS7 HUMAN, HIS Protein?
      LGALS7 HUMAN, HIS Protein is >95% pure as determined by SDS-PAGE.

      What is the Biological Activity of LGALS7 HUMAN, HIS Protein?
      The biological functionality of LGALS7 HUMAN, HIS Protein will be determined in the future.

      What is the amino acid sequence of LGALS7 HUMAN, HIS Protein?
      MGSSHHHHHH SSGLVPRGSH MSNVPHKSSL PEGIRPGTVL RIRGLVPPNA SRFHVNLLCG EEQGSDAALH FNPRLDTSEV VFNSKEQGSW GREERGPGVP FQRGQPFEVL IIASDDGFKA VVGDAQYHHF RHRLPLARVR LVEVGGDVQL DSVRIF.
      What applications can LGALS7 HUMAN, HIS Protein be used in?
      LGALS7 HUMAN, HIS Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for LGALS7 HUMAN, HIS Protein?
      The endotoxin level is minimal, LGALS7 HUMAN, 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.

    Lgals7 Human His
  • View Data Sheet

    Name :

    Leptin Bovine

    Description:

    Leptin Bovine Recombinant

    OB Protein, Obesity Protein, OBS, Obesity factor.

    Product # :

    CYT-502

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    Shipped at Room temp

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    • description
    • source
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    • biological activity
    • More Info

    Description

    Leptin Bovine Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 146 amino acids and having a molecular mass of 16 kDa.The Leptin is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The protein was lyophilized from a concentrated (1mg/ml) solution with 0.02% NaHCO3.

    Purity

    Greater than 98.0% as determined by:
    (a) Gel filtration analysis.
    (b) Analysis by SDS-PAGE.

    Biological Activity

    Biological active as evidenced by inducing proliferation of BAF/3 cells stably transfected with the long form of human leptin receptor.

    More Info

    • Introduction

      A 16-kDa peptide hormone secreted from white adipocytes and implicated in the regulation of food intake and energy balance. Leptin provides the key afferent signal from fat cells in the feedback system that controls body fat stores.

    • Synonyms

      OB Protein, Obesity Protein, OBS, Obesity factor.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized Leptin although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Leptin 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 Leptin in sterile 0.4% NaHCO3 not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      The sequence of the first five N-terminal amino acids was determined and was found to be Ala-Val-Pro-Ile-Arg.

    • Protein content

      Protein quantitation was carried out by UV spectroscopy at 280 nm using the absorbency value of 0.2 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).

    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.

    Leptin Bovine
  • View Data Sheet

    Name :

    Midkine Human

    Description:

    Midkine Human Recombinant

    NEGF-2, Neurite Growth-Promoting Factor 2, MK, Neurite outgrowth-promoting protein, Midgestation and kidney protein, Amphiregulin-associated protein, ARAP, Neurite outgrowth-promoting factor 2, FLJ27379, Midkine, MK1, NEGF2.

    Product # :

    CYT-192

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    • description
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    • More Info

    Description

    Midkine Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 123 amino acids and having a molecular mass of 13.4kDa. The Midkine is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

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

    Purity

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

    Biological Activity

    Determined by its ability to chemoattract human neutrophils using a concentration range of 0.1-10 ng/ml corresponding to a specific activity of 100,000-10,000,000IU/mg.

    More Info

    • Introduction

      Midkine (MK) is the product of a retinoic acid responsive gene. It contains 121 amino acid residues including 10 conserved cysteine residues, all of which appear to be disulphide linked.
      Midkine is expressed during embryogenesis, showing an expression pattern that suggests functions in neurogenesis, cell migration, secondary organogenetic induction, and mesoderm-epithelial interaction.
      The widespread downregulation of MK in the adult human is reverted in a number of cancers, in which polypeptides are able to act as both transforming growth factors and promoters of angiogenesis.
      Midkine (MK), induces chemotaxis of human neutrophils and was found to trigger mobilization of intracellular calcium of these cells.
      Midkine induces histamine release from rat peritoneal mast cells with a rapid response in a dose dependent manner.
      Midkine is also a potent stimulator of collagen and glycosaminoglycan synthesis.

    • Synonyms

      NEGF-2, Neurite Growth-Promoting Factor 2, MK, Neurite outgrowth-promoting protein, Midgestation and kidney protein, Amphiregulin-associated protein, ARAP, Neurite outgrowth-promoting factor 2, FLJ27379, Midkine, MK1, NEGF2.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Amino Acid Sequence

      VAKKKDKVKK GGPGSECAEW AWGPCTPSSK DCGVGFREGT CGAQTQRIRC RVPCNWKKEF GADCKYKFEN WGACDGGTGT KVRQGTLKKA RYNAQCQETI RVTKPCTPKT KAKAKAKKGK GKD.

    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.

    Midkine Human
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