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Search results

1000 results found for “Follistatin”

Name

Description

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  • View Data Sheet

    Name :

    Activin-A Rat

    Description:

    Activin-A Rat Recombinant

    Inhba, Inhibin beta A, FSH releasing protein.

    Product # :

    CYT-147

    Price :

    Quantity :

    Shipping Method :

    Room Temp Icon

    Shipped at Room temp

    Add To Cart

    More Info

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

    Description

    Active form Activin-A Rat Recombinant produced in e.coli is a homodimeric, non-glycosylated, polypeptide chain containing 2 x 117 amino acids and having a molecular weight of 26.2kDa.The Active form Activin-A is purified by standard chromatographic techniques.

    Source

    E.Coli.

    Formulation

    Rat Activin-A was lyophilized from a concentrated 1mg/ml protein solution containing 0.02% TFA.

    Purity

    Greater than 95% as obsereved by SDS-PAGE.

    Biological Activity

    Biological activity is assessed by the ability to induce cytoxicity of MPC-11 cells and was found to be 8.8ng/ml

    Citations

    More Info

    • Introduction

      Activins are homodimers or heterodimers of the different β subunit isoforms, part of the TGFβ family. Mature Activin A has two 116 amino acids residues βA subunits (βA-βA). Activin displays an extensive variety of biological activities, including mesoderm induction, neural cell differentiation, bone remodelling, haematopoiesis, and reproductive physiology. Activins takes part in the production and regulation of hormones such as FSH, LH, GnRH and ACTH. Cells that are identified to express Activin A include fibroblasts, endothelial cells, hepatocytes, vascular smooth muscle cells, macrophages, keratinocytes, osteoclasts, bone marrow monocytes, prostatic epithelium, neurons, chondrocytes, osteoblasts, Leydig cells, Sertoli cells, and ovarian granulosa cells.

    • Synonyms

      Inhba, Inhibin beta A, FSH releasing protein.

    • Physical Appearance

      Lyophilized freeze dried powder.

    • Stability

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

    • Solubility

      Rat INHBA protein should be reconstituted in distilled pyrogen free water to a concentration of 100ug /ml which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      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 26.2 kDa.

      What is the source or expression system of Activin A Protein?
      Ecoli

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

      What is the Biological Activity of Activin A Protein?
      Biological activity is assessed by the ability to induce cytoxicity of MPC-11 cells and was found to be 8.8ng/ml corresponding to a specific activity of 110,000units/mg.

      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?
      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.

    Inhba Rat
  • View Data Sheet

    Name :

    Activin B Human

    Description:

    Activin-B Human Recombinant

    Inhibin beta B (activin AB beta polypeptide), Inhibin, beta-2, Activin beta-B chain, MGC157939.

    Product # :

    CYT-058

    Price :

    Quantity :

    Shipping Method :

    Room Temp Icon

    Shipped at Room temp

    Add To Cart

    More Info

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

    Description

    Activin B human Recombinant produced in Nicotiana benthamiana plant is a beta-B single chain (aa 293-406) containing 123 amino acids (molecular formula C615H910N178O177S12). Activin B is fused to a 10-His-tag at the N-terminal having the total molecular mass of 14kDa and purified by standard chromatographic techniques.

    Source

    Nicotiana benthamiana plant

    Formulation

    Lyophilized from 1mg/ml solution in 0.05M Tris-HCl buffer pH 7.4.

    Purity

    Greater than 97.0% as determined by Analysis by SDS-PAGE.

    Citations

    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

      Inhibin beta B (activin AB beta polypeptide), Inhibin, beta-2, Activin beta-B chain, MGC157939.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Amino Acid Sequence

      HHHHHHHHHH GLECDGRTNL CCRQQFFIDF RLIGWNDWII APTGYYGNYC EGSCPAYLAG VPGSASSFHT AVVNQYRMRG LNPGTVNSCC IPTKLSTMSM LYFDDEYNIV KRDVPNMIVE ECG

    • Background

      What is the molecular weight / Mw of Activin B Protein?
      Activin A Protein has a total Mw of 14 kDa.

      What is the source or expression system of Activin B Protein?
      Nicotinia

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

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

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

      What is the amino acid sequence of ACTIVIN B Protein?
      HHHHHHHHHH GLECDGRTNL CCRQQFFIDF RLIGWNDWII APTGYYGNYC EGSCPAYLAG VPGSASSFHT AVVNQYRMRG LNPGTVNSCC IPTKLSTMSM LYFDDEYNIV KRDVPNMIVE ECG

      What applications can ACTIVIN B 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 B Human Plant
  • 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 :

    Shipping Method :

    Ice Icon

    Shipped with Ice Packs

    Add To Cart

    More Info

    • description
    • source
    • formulation
    • purity
    • More Info
    • sds-page
    • Citations

    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

    Citations

    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 :

    Polcalcin Phl p 7

    Description:

    Pollen Allergen Phl p 7 Recombinant

    Polcalcin Phl p 7, Calcium-binding pollen allergen Phl p 7, P7, Phl p 7.

    Product # :

    ALR-015

    Price :

    Quantity :

    Shipping Method :

    Ice Icon

    Shipped with Ice Packs

    Add To Cart

    More Info

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

    Description

    Recombinant Polcalcin Phl p 7 produced in SF9 is a glycosylated, polypeptide chain having a calculated molecular mass of 9.0 kDa. Polcalcin Phl p 7 is purified by proprietary chromatographic techniques.

    Source

    Sf9 insect cells.

    Formulation

    Polcalcin Phl p 7 is supplied in 20mM HEPES buffer pH-8.0, 0.2M NaCl, 1mM CaCl2 and 20% Glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      Phl p 7.0101 is a secondary allergen of timothy grass pollen, which is non-glycosylated protein. Grass pollen-sensitized individuals show IgE antibodies in their blood system. Phl p 7.0101 is a calcium binding protein with similar sequence to pollen antigens that exist in different plants, hence, cross-reactions are possible.

    • Synonyms

      Polcalcin Phl p 7, Calcium-binding pollen allergen Phl p 7, P7, Phl p 7.

    • Physical Appearance

      Sterile Filtered clear solution.

    • Stability

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

    • Immunological Functions

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

    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.

    Polcalcin Phl P 7
  • View Data Sheet

    Name :

    Activin-A Mouse

    Description:

    Activin-A Mouse Recombinant

    Inhba, Inhibin beta A, FSH releasing protein.

    Product # :

    CYT-146

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    Description

    Active form Activin-A Murine Recombinant produced in e.coli is a homodimeric, non-glycosylated, polypeptide chain containing 2 x 117 amino acids and having a molecular weight of 26.2kDa.The Active form Activin-A is purified by standard chromatographic techniques.

    Source

    E.Coli.

    Formulation

    Mouse Activin-A lyophilized from a concentrated 1mg/ml protein solution containing 0.1% TFA.

    Purity

    Greater than 95% as obsereved by SDS-PAGE.

    Biological Activity

    Biological activity is assessed by the ability to induce cytoxicity of MPC-11 cells and was found to be 8.8ng/ml corresponding to a specific activity of 1.1 x 105 units/mg.

    Citations

    More Info

    • Introduction

      Activins are homodimers or heterodimers of the different β subunit isoforms, part of the TGFβ family. Mature Activin A has two 116 amino acids residues βA subunits (βA-βA). Activin displays an extensive variety of biological activities, including mesoderm induction, neural cell differentiation, bone remodelling, haematopoiesis, and reproductive physiology. Activins takes part in the production and regulation of hormones such as FSH, LH, GnRH and ACTH. Cells that are identified to express Activin A include fibroblasts, endothelial cells, hepatocytes, vascular smooth muscle cells, macrophages, keratinocytes, osteoclasts, bone marrow monocytes, prostatic epithelium, neurons, chondrocytes, osteoblasts, Leydig cells, Sertoli cells, and ovarian granulosa cells.

    • Synonyms

      Inhba, Inhibin beta A, FSH releasing protein.

    • Physical Appearance

      Lyophilized freeze dried powder.

    • Stability

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

    • Solubility

      Murine INHBA protein should be reconstituted in distilled pyrogen free water to a concentration of 100ug /ml which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      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 26.2 kDa.

      What is the source or expression system of Activin A Protein?
      Ecoli

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

      What is the Biological Activity of Activin A Protein?
      Biological activity is assessed by the ability to induce cytoxicity of MPC-11 cells and was found to be 8.8ng/ml corresponding to a specific activity of 110,000 units/mg.

      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?
      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.

    Inhba Mouse
  • View Data Sheet

    Name :

    Activin-A Human Plant-Active

    Description:

    Activin-A Human Recombinant, Plant-Active

    Inhba, Inhibin beta A, FSH releasing protein.

    Product # :

    CYT-414

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    Description

    Active form Activin-A Human Recombinant produced in Plant is a homodimeric, glycosylated, polypeptide chain containing 2 x 116 amino acids and having a molecular weight of 27.4kDa.The Active form Activin-A is fused to a 6-His tag at N-terminus and purified by standard chromatographic techniques.

    Source

    Nicotiana benthamiana.

    Formulation

    Active form Activin-A was lyophilized from a concentrated 1mg/ml protein solution containing 50mM Tris-HCl pH-7.4

    Purity

    Greater than 98% as obsereved by SDS-PAGE.

    Biological Activity

    The biological activity of INHBA is measured by its ability to inhibit mouse plasmacytoma cell line (MPC-11) cells proliferation ([3H]thymidine incorporation). ED50<5ng/ml.

    Citations

    More Info

    • Introduction

      Activins are homodimers or heterodimers of the different β subunit isoforms, part of the TGFβ family. Mature Activin A has two 116 amino acids residues βA subunits (βA-βA). Activin displays an extensive variety of biological activities, including mesoderm induction, neural cell differentiation, bone remodelling, haematopoiesis, and reproductive physiology. Activins takes part in the production and regulation of hormones such as FSH, LH, GnRH and ACTH. Cells that are identified to express Activin A include fibroblasts, endothelial cells, hepatocytes, vascular smooth muscle cells, macrophages, keratinocytes, osteoclasts, bone marrow monocytes, prostatic epithelium, neurons, chondrocytes, osteoblasts, Leydig cells, Sertoli cells, and ovarian granulosa cells.

    • Synonyms

      Inhba, Inhibin beta A, FSH releasing protein.

    • Physical Appearance

      Lyophilized freeze dried powder.

    • Stability

      For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA). Repeated freezing and thawing is not recommended.

    • Solubility

      INHBA protein should be reconstituted in distilled water to a concentration of 50 ug /ml. Due to the protein nature, dimmers and multimers may be observed.

    • Amino Acid Sequence

      HHHHHHGLECDGKVNICCKKQFFVSFKDIGWNDWIIAPSG
      YHANYCEGECPSHIAGTSGSSLSFHSTVINHYRMRGHSPFA
      NLKSCCVPTKLRPMSMLYYDDGQNIIKKDIQNMIVEECGCS.

    • Background

      What is the molecular weight / Mw of Activin A Protein?
      Activin A Protein has a total Mw of 27.4 kDa.

      What is the source or expression system of Activin A Protein?
      Nicotiana benthamiana.

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

      What is the Biological Activity of Activin A Protein?
      The biological activity of INHBA is measured by its ability to inhibit mouse plasmacytoma cell line (MPC-11) cells proliferation ([3H]thymidine incorporation). ED50<5ng/ml.

      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?HHHHHHGLECDGKVNICCKKQFFVSFKDIGWNDWIIAPSGYHANYCEGECPSHIAGTSGSSLSFHSTVINHYRMRGHSPFANLKSCCVPTKLRPMSMLYYDDGQNIIKKDIQNMIVEECGCS

      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 Active
  • View Data Sheet

    Name :

    Resistin Human (64-110)

    Description:

    Resistin (64-110) Human Recombinant

    Cysteine-rich secreted protein FIZZ3, Adipose tissue-specific secretory factor, ADSF.

    Product # :

    CYT-1232

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    Description

    The Resistin Human is created as a recombinant protein with a 4kda N-terminal fusion of His Tag. The Resistin His-Tagged Fusion Protein, produced in E. coli, is a 12kDa protein containing 47 amino acid residues of the Resistin Human, 64-110 amino acids.

    Source

    Escherichia Coli.

    Formulation

    Each mg was lyophilized with 1xPBS, 0.4% SDS and 4mM DTT.

    Purity

    Greater than 80% as determined by SDS-PAGE.

    Citations

    More Info

    • Synonyms

      Cysteine-rich secreted protein FIZZ3, Adipose tissue-specific secretory factor, ADSF.

    • Physical Appearance

      Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Store lyophilized Resistin at -20°C. Aliquot the product after reconstitution to avoid repeated freezing/thawing cycles. Reconstituted protein can be stored at 4°C for a limited period of time; it does not show any change after two weeks at 4°C.

    • Solubility

      It is recommended to add deionized water to prepare a working stock solution of approximately 0.5mg/ml and let the lyophilized pellet dissolve completely. Product is not sterile! Please filter the product by an appropriate sterile filter before using it on cell culture.

    • Background

      Human resistin is an adipokine primarily secreted by adipose tissue, mainly in response to obesity and inflammatory conditions.

      Resistin Function

      Resistin takes part in insulin resistance, which can be the cause of the development of type 2 diabetes. Resistin can also affect glucose metabolism and insulin signalling.

      Regulation

      Levels of resistin are influenced by factors such as inflammation, obesity and certain hormones. It tends to increase in conditions associated with obesity and metabolic syndrome.

      Clinical Relevance

      Elevated levels of resistin have been associated with obesity-related conditions, cardiovascular diseases, and metabolic disorders. Resisting is considered as a potential biomarker for these conditions.

      Resistin Mechanism

      Resistin promotes insulin resistance through different pathways such as the modulation of inflammatory processes and the inhibition of insulin signaling in target tissues like liver and muscle.

      Research

      Ongoing studies are exploring resistin’s role in metabolic regulation, the exact mechanisms of action of resistin and its potential as a therapeutic target for treating metabolic diseases.

      Overall, resistin is a critical factor in metabolic health, mainly in the context of diabetes and obesity.

    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.

    Resistin Human Protein
  • View Data Sheet

    Name :

    Myostatin Human

    Description:

    Myostatin Human Recombinant

    GDF-8, MSTN, Growth Differentiation Factor 8, MSTN Muscle Hypertrophy.

    Product # :

    CYT-418

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    Description

    Myostatin Human Recombinant produced in E.Coli is a homodimer, non-glycosylated polypeptide chain containing 2 x 109 amino acids and having a total molecular mass of 24814 Dalton. The GDF-8 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

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

    Purity

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

    Biological Activity

    The ED50 as determined by the inhibition of the proliferation of MPC-11 cells is < 20ng/ml, corresponding to a Specific Activity of 50,000units/mg.

    Citations

    More Info

    • Introduction

      GDF8 is a member of the bone morphogenetic protein (BMP) family and the TGF-beta superfamily. This group of proteins is characterized by a polybasic proteolytic processing site which is cleaved to produce a mature protein containing seven conserved cysteine residues. The members of this family are regulators of cell growth and differentiation in both embryonic and adult tissues. This gene is thought to encode a secreted protein which negatively regulates skeletal muscle growth.

    • Synonyms

      GDF-8, MSTN, Growth Differentiation Factor 8, MSTN Muscle Hypertrophy.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized Myostatin although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Myostatin 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 Myostatin in sterile 20mM HCl at 0.1 mg/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 Asp-Phe-Gly-Leu-Asp.

    • Protein content

      Protein quantitation was carried out by two independent methods:1. UV spectroscopy at 280 nm using the absorbency value of 1.55 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 Myostatin 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.

    Myostatin Human
  • View Data Sheet

    Name :

    SOSTDC1 Human

    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.

    Citations

    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

    Name :

    Leptin-A Tilapia

    Description:

    Leptin-A Tilapia Recombinant

    Product # :

    CYT-1109

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    Description

    Leptin-A Tilapia Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 161 amino acids and having a molecular mass of 16,491 Dalton. The Leptin-A Tilapia is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Lyophilized from a concentrated (1mg/ml) solution containing NaHCO3 at 1:2 salt: protein ratio.

    Purity

    Greater than 95.0% as determined by:
    (a) Gel filtration analysis.
    (b) Analysis by SDS-PAGE.

    Biological Activity

    Tilapia leptins were found to be biologically active in promoting proliferation of BAF/3 cells stably transfected with the long form of human leptin receptor, but their activity was lower than that of mammalian leptin. Furthermore, the Tilapia leptins were biologically active in promoting STAT‐LUC activation in COS7 cells transfected with Tilapia leptin receptor but not in cells transfected with human leptin receptor. Tilapia Leptin A was more active than Tilapia Leptin B.

    Citations

    More Info

    • Introduction

      Leptin is a protein hormone. It is mainly produced in adipose cells that regulate energy homeostasis by restraining hunger. Leptin ties to nuclear receptors in the hypothalamus (arcuate nucleus). Similar to insulin resistance in type II diabetes, in obesity there is a decrease in the sensitivity towards leptin, ending in a failure to identify satiety, even in high levels of energy stores or leptin itself. Full-length cDNA encoding 2 leptin sequences (tLepA and tLepB) and 1 leptin receptor sequence (tLepR) exists in tilapia (Oreochromis niloticus). The full-length cDNA of tLepR is 3423 bp, encoding a protein of 1140 amino acid which contained all functionally important domains conserved among vertebrate leptin receptors. The cDNAs of tLepA and tLepB are 486 bp and 459 bp in length, encoding proteins of 161 aa and 152 aa, respectively. The three-dimensional structures of tLepA and tLepB demonstrates strong conservation of tertiary structure with that of human leptin comprised of 4 helixes.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized Leptin-A Tilapia although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Leptin-A Tilapia 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-A Tilapia in sterile water or 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 first six N-terminal amino acids of recombinant Tilapia leptin A are Ala-Pro-Leu-Pro-Val-Glu.

    • Protein content

      Protein quantitation was carried out by UV spectroscopy at 280 nm using the absorbency value of 1.33 for 1 mg/ml Leptin-A Tilapia as the extinction coefficient for a 0.1% (1mg/ml) solution at pH 8.0. This value is calculated by the DNAman computer analysis program of protein sequences.

    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 A
  • View Data Sheet

    Name :

    Myostatin Human, HEK

    Description:

    Myostatin Human Recombinant, HEK

    GDF-8, MSTN, Growth Differentiation Factor 8, MSTN Muscle Hypertrophy.

    Product # :

    CYT-833

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    Description

    Myostatin Human Recombinant produced in HEK cells is a single, glycosylated, polypeptide chain (Asn24-Ser375) containing a total of 360 amino acids, having a calculated molecular mass of 41.1kDa. Myostatin is fused to a 2 aa N-terminal linker and a 6 aa His tag at N-Terminus.

    Source

    HEK 293.

    Formulation

    Myostatin solution at a concentration of 0.25mg/ml in phosphate buffered saline (PBS) pH 8.0 and 20% (w/v) glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      GDF8 is a member of the bone morphogenetic protein (BMP) family and the TGF-beta superfamily. This group of proteins is characterized by a polybasic proteolytic processing site which is cleaved to produce a mature protein containing seven conserved cysteine residues. The members of this family are regulators of cell growth and differentiation in both embryonic and adult tissues. This gene is thought to encode a secreted protein which negatively regulates skeletal muscle growth.

    • Synonyms

      GDF-8, MSTN, Growth Differentiation Factor 8, MSTN Muscle Hypertrophy.

    • Physical Appearance

      Filtered colorless solution.

    • Stability

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

    • Amino Acid Sequence

      HHHHHHASNE NSEQKENVEK EGLCNACTWR QNTKSSRIEA IKIQILSKLR LETAPNISKD VIRQLLPKAP PLRELIDQYD VQRDDSSDGS LEDDDYHATT ETIITMPTES DFLMQVDGKP KCCFFKFSSK IQYNKVVKAQ LWIYLRPVET PTTVFVQILR LIKPMKDGTR YTGIRSLKLD MNPGTGIWQS IDVKTVLQNW LKQPESNLGI EIKALDENGH DLAVTFPGPG EDGLNPFLEV KVTDTPKRSR RDFGLDCDEH STESRCCRYP LTVDFEAFGW DWIIAPKRYK ANYCSGECEF VFLQKYPHTH LVHQANPRGS AGPCCTPTKM SPINMLYFNG KEQIIYGKIP AMVVDRCGCS.

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    Myostatin Human Hek
  • View Data Sheet

    Name :

    Secretin Human

    Description:

    Secretin Human

    Product # :

    HOR-273

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    Description

    Secretin has a molecular formula of C130H220N44O41, a.a. sequence of H-His-Ser-Asp-Gly-Thr-Phe-Thr-Ser-Glu-Leu-Ser-Arg-Leu-Arg- Asp-Ser-Ala-Arg-Leu-Gln-Arg-Leu-Leu-Gln-Gly-Leu-Val-NH2 and having an Mw of 3055.4 Dalton.

    Formulation

    The protein (1mg/ml) was lyophilized with no additives.

    Purity

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

    Citations

    More Info

    • Introduction

      Human Secretin stimulates the secretion of bicarbonate by the pancreas and inhibits the production of gastrin and acid production in the stomach. It also potentiates the release of digestive enzymes from the pancreas triggered by cholecystokinin.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    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.

    Secretin Human
  • View Data Sheet

    Name :

    PMSG

    Description:

    Pregnant Mare Serum Gonadotropin

    Product # :

    HOR-272

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    Description

    PMSG is a complex glycoprotein obtained from the serum of pregnant mares. This 43-63 kda protein is capable of supplementing and being substituted for the follicle stimulating and interstitial cell-stimulating hormone of the anterior pituitary gland in both the male and female. Thus PMSG-Intervet stimulates development of the ovarian follicle in the female.

    Source

    Serum of pregnant mares.

    Formulation

    The PMSG was lyophilized with no additives.

    Citations

    More Info

    • Introduction

      PMSG Hormone is a well know used hormone together with progestogen to increase ovulation just before to artificial insemination. PMSG hormone is a placental glycoprotein produced from the serum of pregnant mares. PMSG comprises of an alfa subunit and a beta subunit. PMSG hormone is secreted from endometrial cups within the pregnant mare uterus aging from 40 to 130 days into their maturation, and once extracted, it can been used to promote artificially estrus in female animals. These assemblies produce PMSG hormone to induce mare's ovarian and repsouctive structures. PMSG can induce the growth of follicles by ovaries and results in ovulatation. PMSG hormone has an about a 4 day half-life of bioactivity in species other than horses. The extended biological activity can cause ovarian stimulation and ovulation. However, PMSG use alone often causes cystic ovarian disease because of the unrestrained ovarian stimulation and due to the sugar molecules which decrease clearance of the hormone. PMSG is more likely to be used than other pituitary hormones due to the extended circulatory half-life. PMSG solely exhibits luteinizing hormone like activity, however in other animal classes it has FSH & LH like activity.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized PMSG although stable at room temperature for 3 weeks, should be stored between 2-8°C.

    • Solubility

      It is recommended to reconstitute the lyophilized PMSG in sterile 18M-cm H2O at a concentration of 1000 IU/ml, which can then be further diluted to other aqueous solutions.

    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.

    Pmsg
  • View Data Sheet

    Name :

    Elcatonin

    Description:

    Elcatonin

    Product # :

    HOR-302

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    • biological activity
    • More Info
    • Citations

    Description

    Elcatonin Synthetic is a single, non-glycosylated polypeptide chain containing 31 amino acids, having a molecular mass of 3363.2 Dalton and a Molecular formula of C148H244N42O47.

    Formulation

    The protein was lyophilized with no additives.

    Purity

    Greater than 93.3% as determined by:
    (a) Analysis by RP-HPLC.
    (b) Analysis by SDS-PAGE.

    Biological Activity

    Biological Activity (based on net peptide) was found to be 6695.2 IU/mg.

    Citations

    More Info

    • Introduction

      Elcatonin is a Calcitonin derivative which is transformed from eel´s calcitonin by changing the S-S bond into the stable C-N bond. It inhibits the absorption and autolysis of bones, thus leads to blood calcium descending. In addition, it inhibits the bone salts dissolving and transferring and promotes the excretion of calcium and phosphorus in urine. Meanwhile, it inhibits renal tubules reabsorbing calcium, phosphorus and sodium and keeps blood calcium at normal level. It is mainly used for remitting or eliminating the pain caused by Osteoporosis.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Amino Acid Sequence

      Ser-Asn-Leu-Ser-Thr-Asu-Val-Leu-Gly-Lys-Leu-Ser-Gln-Glu-Leu-His-Lys-Leu-Gln-Thr-Tyr-Pro-Arg-Thr-Asn-Val-Gly-Ala-Gly-Thr-Pro-NH2.

    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.

    Elcatonin
  • View Data Sheet

    Name :

    Inhibin a Human

    Description:

    Inhibin Alpha Human Recombinant

    Product # :

    HOR-303

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    Description

    Inhibin-Alpha Human Recombinant produced in E.Coli is a non-glycosylated, polypeptide chain containing 264 amino acids comprising of both A and B chains, having a molecular mass of 33.5 kDa.The Inhibin-Alpha is fused with an amino-terminal hexahistidine tag. The Inhibin-Alpha is purified by standard chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Inhibin-A alpha chain is supplied in 20mM Tris and 50% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE analysis.

    Citations

    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.

    • 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.Please avoid freeze thaw cycles.

    • Amino Acid Sequence

      Alpha chain:
      STPLMSWPWSPSALRLLQRPPEEPAAHANCHRVALNISFQELGWERWIVYPPSFIFHYCHGGCGLHIP PNLSLPVPGAPPTPAQPYSLLPGAQPCCAALPGTMRPLHVRTTSDGGYSFKYETVPNLLTQHCACI.

      Beta Chain:
      GLECDGKVNICCKKQFFVSFKDIGWNDWIIAPSGYHANYCEGECPSHIAGTSGSSLSFHSTVINHYRMR
      GHSPFANLKSCCVPTKLRPMSMLYYDDGQNIIKKDIQNMIVEECGCS.

    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.

    Inhibin A Human
  • View Data Sheet

    Name :

    Cystatin-C Protein

    Description:

    Cystatin-C Human Recombinant

    Cystatin-C, Cystatin-3, Neuroendocrine basic polypeptide, Gamma-trace, Post-gamma-globulin, CST3, MGC117328.

    Product # :

    PRO-2601

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    Description

    Cystatin-C Human Recombinant produced in E.Coli is a single, non- glycosylated polypeptide chain containing 120 amino acids and having a molecular mass of 13.3kDa. Cystatin-C is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Cystatin-C is supplied as a 0.2 μm filtered solution containing 20mM Tris-HCl, 50 % glycerol, pH 8.0 and 300mM NaCl.

    Purity

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

    Citations

    More Info

    • Introduction

      Cystatins are a superfamily of cysteine proteinase inhibitors found in both plants and animals. They comprise a group of proteinase inhibitors, widely distributed in tissues and body fluids, and form tight complexes with cysteine proteases such as cathepsin B, H, L and S. Cystatin C, a secreted molecule of this family, is of interest from biochemical, medicine and evolutionary points of view. Cystatin C is increased in patients with malignant diseases, and is related to the insufficiency of renal function and appears to be a better marker than creatinine. On the other hand, low levels of cystatin C involve cause the breakdown of the elastic laminae and subsequently, the atherosclerosis and abdominal aortic aneurysm.

    • Synonyms

      Cystatin-C, Cystatin-3, Neuroendocrine basic polypeptide, Gamma-trace, Post-gamma-globulin, CST3, MGC117328.

    • 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

      SSPGKPPRLV GGPMDASVEE EGVRRALDFA VGEYNKASND MYHSRALQVV RARKQIVAGV NYFLDVELGR TTCTKTQPNL DNCPFHDQPH LKRKAFCSFQ IYAVPWQGTM TLSKSTCQDA.

    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.

    Cystatin C
  • View Data Sheet

    Name :

    Omentin Human

    Description:

    Omentin Human Recombinant

    Intelectin-1, HL1, LFR, HL-1, INTL, ITLN, hIntL.

    Product # :

    CYT-301

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    Description

    Omentin Human Recombinant is produced in E.Coli by recombinant DNA technology is a single, polypeptide chain containing 313 amino acids and having a molecular mass of 35 kDa. Intelectin is purified by proprietary chromatographic techniques.

    Source

    E.Coli.

    Formulation

    Each mg of lyophilized powder contains 10mM NaP, pH-7.5 and 5:1 mannitol to protein.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      Omentin is a recently recognized gene highly localized to the mental tissue (visceral adipose tissue). Omentin is present in the stromal vascular cells in the adipose tissue rather than in the adipocytes. Omentin is predominantly expressed in the visceral adipose tissue than the subcutaneous tissue, with the omentin mRNA being 150 times higher in the visceral adipose tissue. Omentin has also been detected in human blood using western blot analysis, and seems to increase INSstimulated glucose uptake in 3T3-L1 adipocytes in mice. Omentin seems to increase Akt phosphorylation irrespective of INS presence. Its role in glucose metabolism and obesity remains to be described; an INS-sensitizing action is possible.Differences in Omentin expression has been noted in adipose tissue from normals and patients with inflammatory bowel disease although its significance is unknown.

    • Synonyms

      Intelectin-1, HL1, LFR, HL-1, INTL, ITLN, hIntL.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Amino Acid Sequence

      MNQLSFLLFL IATTRGWSTD EANTYFKEWTCSSSPSLPRS CKEIKDECPS AFDGLYFLRT ENGVIYQTFC DMTSGGGGWT LVASVHENDM RGKCTVGDRW SSQQGSKADY PEGDGNWANY NTFGSAEAAT SDDYKNPGYY DIQAKDLGIW HVPNKSPMQH WRNSSLLRYR TDTGFLQTLG HNLFGIYQKY PVKYGEGKCW TDNGPVIPVV YDFGDAQKTA SYYSPYGQRE FNNERAANAL CAGMRVTGCN TEHHCIGGGG YFPEASPQQC GDFSGFDWSG YGTHVGYSSS REITEAAVLLFYR.

    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.

    Omentin Human
  • View Data Sheet

    Name :

    Resistin Rat

    Description:

    Resistin Rat Recombinant

    Cysteine-rich secreted protein FIZZ3, Adipose tissue-specific secretory factor, ADSF, C/EBP-epsilon-regulated myeloid-specific secreted cysteine-rich protein, Cysteine-rich secreted protein A12-alpha-like 2, RSTN, XCP1, RETN1, MGC126603, MGC126609.

    Product # :

    CYT-1129

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    Description

    Resistin Rat Recombinant produced in E.Coli is disulfide-linked homodimer consisting of 2x95 amino acid polypeptide chains and having a molecular mass of approximately 20.2kDa.Resistin is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Lyophilized from a 0.2μm filtered concentrated solution in PBS, pH7.4 and 0.02 % Tween-20.

    Purity

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

    Citations

    More Info

    • Introduction

      Resistin, a product of the RSTN gene, is a peptide hormone belongs to the class of cysteine-rich secreted proteins (monomeric peptide contains 11 cysteine residues) referred to as the RELM family, and is also described as ADSF (Adipose Tissue-Specific Secretory Factor) or FIZZ3 (Found in Inflammatory Zone 3). Resistin may be an important link between obesity. Mouse resistin, specifically produced and secreted by adipocyte, acts on skeletal muscle myocytes, hepatocytes and adipocytes themselves so that it reduces their sensitivity. Steppan et al. have suggested that resistin suppressed the ability to stimulate glucose uptake. They have also suggested that resistin was present at elevated levels in blood of obese mice, and was down regulated by fasting and by antidiabetic drugs. Way et al., on the other hand, have found that resistin expression is severely suppressed in obesity.
      Other studies have shown that mouse resistin increases during the differentiation of adipocytes, but it also seems to inhibit adipogenesis. In contrast, the human adipogenic differentiation is likely to be associated with a down regulation of resistin gene expression.

    • Synonyms

      Cysteine-rich secreted protein FIZZ3, Adipose tissue-specific secretory factor, ADSF, C/EBP-epsilon-regulated myeloid-specific secreted cysteine-rich protein, Cysteine-rich secreted protein A12-alpha-like 2, RSTN, XCP1, RETN1, MGC126603, MGC126609.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Amino Acid Sequence

      MPSMSLCPMD EAISKKINQD FSSLLPAAMK NTVLHCWSVS SRGRLASCPE GTTVTSCSCG SGCGSWDVRE DTMCHCQCGS IDWTAARCCT LRVGS.

    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.

    Rat Resistin Protein
  • View Data Sheet

    Name :

    Myostatin Propeptide Human, HEK

    Description:

    Myostatin Propeptide Human Recombinant, HEK

    GDF-8, MSTN, Growth Differentiation Factor 8, MSTN Muscle Hypertrophy.

    Product # :

    CYT-936

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    Description

    Myostatin Propetide Human Recombinant produced in HEK cells is a single, glycosylated, polypeptide chain (Asn24-Arg266) containing a total of 253 amino acids, having a calculated molecular mass of 29.1kDa. Myostatin Propetide is fused to a 10 aa C-terminal His tag.

    Source

    HEK 293.

    Formulation

    Myostatin Propetide solution at a concentration of 0.25mg/ml in phosphate buffered saline (PBS) pH 8.0 and 20% (w/v) glycerol.

    Purity

    Greater than 80.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      GDF8 is a member of the bone morphogenetic protein (BMP) family and the TGF-beta superfamily. This group of proteins is characterized by a polybasic proteolytic processing site which is cleaved to produce a mature protein containing seven conserved cysteine residues. The members of this family are regulators of cell growth and differentiation in both embryonic and adult tissues. This gene is thought to encode a secreted protein which negatively regulates skeletal muscle growth.

    • Synonyms

      GDF-8, MSTN, Growth Differentiation Factor 8, MSTN Muscle Hypertrophy.

    • Physical Appearance

      Filtered colorless solution.

    • Stability

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

    • Amino Acid Sequence

      NENSEQKENV EKEGLCNACT WRQNTKSSRI EAIKIQILSK LRLETAPNIS KDVIRQLLPK APPLRELIDQ YDVQRDDSSD GSLEDDDYHA TTETIITMPT ESDFLMQVDG KPKCCFFKFS SKIQYNKVVK AQLWIYLRPV ETPTTVFVQI LRLIKPMKDG TRYTGIRSLK LDMNPGTGIW QSIDVKTVLQ NWLKQPESNL GIEIKALDEN GHDLAVTFPG PGEDGLNPFL EVKVTDTPKR SRR HHHHHHH HHH.

    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.

    Myostatin Propeptide Human Hek
  • View Data Sheet

    Name :

    SOST Mouse

    Description:

    Sclerostin Mouse Recombinant

    SOST, Sclerostin, 5430411E23Rik.

    Product # :

    PRO-2670

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    Description

    SOST Mouse Recombinant produced in HEK293 cells is a single, glycosylated polypeptide chain (24-211 a.a) containing 194 amino acids and having a molecular mass of 21.9 kDa.SOST is fused to a 6 amino acid His-tag at C-terminus & purified by proprietary chromatographic techniques.

    Source

    HEK293 cells.

    Formulation

    SOST protein (0.25mg/ml) contains 10% glycerol and Phosphate-Buffered Saline (pH 7.4).

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      Sclerostin (SOST) is a secreted glycoprotein with a C-terminal cysteine knot-like (CTCK) domain and sequence similarity to the DAN (differential screening-selected gene aberrative in neuroblastoma) family of bone morphogenetic protein antagonists. Sclerostin functions as a negative regulator of bone growth, by inhibiting bone formation. SOST is expressed mainly in the bone, cartilage, kidney, liver, bone marrow and primary osteoblasts differentiated for 21 days. SOST gene defects cause sclerosteosis and bone dysplasia.

    • Synonyms

      SOST, Sclerostin, 5430411E23Rik.

    • 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

      QGWQAFRNDA TEVIPGLGEY PEPPPENNQT MNRAENGGRP PHHPYDAKDV SEYSCRELHY TRFLTDGPCR SAKPVTELVC SGQCGPARLL PNAIGRVKWW RPNGPDFRCI PDRYRAQRVQ LLCPGGAAPR SRKVRLVASC KCKRLTRFHN QSELKDFGPE TARPQKGRKP RPGARGAKAN QAELENAYHH HHHH

    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.

    Sclerostin Mouse
  • View Data Sheet

    Name :

    Leptin tA Ovine

    Description:

    Leptin Antagonist Triple Mutant Ovine Recombinant

    Product # :

    CYT-356

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    Description

    Leptin Antagonist Triple Mutant Ovine Recombinant is a single non-glycosilated polypeptide chain containing 146 amino and additional Ala at N-terminus acids and having a molecular mass of ~ 16 kDa, Leptin was mutated, resulting in L39A/D40A/F41A mutant. Leptin Antagonist Triple Mutant Ovine Recombinant was purified by proprietary chromatographic techniques.

    Source

    Escherichia coli.

    Formulation

    The protein was lyophilized from a concentrated (0.65mg/ml) solution with 0.003mM NaHCO3.

    Purity

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

    Biological Activity

    ProSpec’s Leptin-Antagonist Triple Mutant Ovine Recombinant is capable of inhibiting leptin-induced proliferation of BAF/3 cells stably transfected with the long form of mouse leptin receptor. It also inhibits various leptin effects in several in vitro bioassays.

    Citations

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    • Physical Appearance

      White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized Leptin Antagonist Triple Mutant Ovine Recombinant although stable at room temperature for several weeks, should be stored desiccated below -18°C. Upon reconstitution at > 0.1 Lep-tA mutant mg/ml and up to 2 mM and filter sterilization Leptin mutant can be stored at 4°C or even room temperature for several weeks making it suitable for long term infusion studies using osmotic pumps. At lower concentration addition of a carrier protein (0.1% HSA or BSA) is suggested. Please prevent freeze-thaw cycles.

    • Solubility

      It is recommended to reconstitute the lyophilized Leptin-Antagonist Triple Mutant Ovine Recombinant in sterile water or sterile 0.4% NaHCO3 adjusted to pH 8, 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 0.21 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 Ta Ovine
  • View Data Sheet

    Name :

    a-Actinin

    Description:

    Actinin Alpha

    Alpha-actinin-1, Alpha-actinin cytoskeletal isoform, Non-muscle alpha-actinin-1, F-actin cross-linking protein, ACTN1.

    Product # :

    PRO-518

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    Description

    Ultra pure Alpha Actinin having a Molecular mass of 95,000 Dalton.

    Source

    Chicken Gizzard.

    Formulation

    The protein was lyophilized from a 1mg/ml solution containing 10mM Tris acetate buffer pH 7.6, 0.1mM EDTA, 2mM DTT, and 20mM NaCl.

    Purity

    Greater than 95.0% as determined by analysis by SDS-PAGE.

    Citations

    More Info

    • Introduction

      ACTN1 encodes a nonmuscle, cytoskeletal, alpha actinin isoform and maps to the same site as the structurally similar erythroid beta spectrin gene. Alpha actinins belong to the spectrin gene superfamily which represents a diverse group of cytoskeletal proteins, including the alpha and beta spectrins and dystrophins. Alpha actinin is an actin-binding protein with multiple roles in different cell types. In nonmuscle cells, the cytoskeletal isoform is found along microfilament bundles and adherens-type junctions, where it is involved in binding actin to the membrane. In contrast, skeletal, cardiac, and smooth muscle isoforms are localized to the Z-disc and analogous dense bodies, where they help anchor the myofibrillar actin filaments.

    • Synonyms

      Alpha-actinin-1, Alpha-actinin cytoskeletal isoform, Non-muscle alpha-actinin-1, F-actin cross-linking protein, ACTN1.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Applications

      Protein standard in 1D and 2D SDS gelelectrophoresis
      Immunoassays
      Immunization.

    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.

    Alpha Actinin
  • View Data Sheet

    Name :

    PFDN2 Human

    Description:

    Prefoldin Subunit 2 Human Recombinant

    Prefoldin subunit 2, PFDN2, PFD2.

    Product # :

    PRO-001

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    Description

    PFDN2 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 174 amino acids (1-154 a.a.) and having a molecular mass of 18.8kDa. The PFDN2 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The PFDN2 solution (0.5 mg/ml) contains 20mM Tris-HCl buffer (pH8.0), 10% glycerol, 1mM DTT and 50mM NaCl.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      Prefoldin subunit 2 (PFDN2) belongs to the prefoldin beta subunit family. The PFDN2 protein is one of 6 subunits of prefoldin, which is a molecular chaperone complex that binds and stabilizes newly synthesized polypeptides, thus allowing them to fold correctly. PFDN2 binds specifically to cytosolic chaperonin (c-CPN) and transfers target proteins to it. PFDN2 also binds to a nascent polypeptide chain and promotes folding in an setting in which there are many competing pathways for nonnative proteins.

    • Synonyms

      Prefoldin subunit 2, PFDN2, PFD2.

    • 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 MAENSGRAGK SSGSGAGKGA VSAEQVIAGF NRLRQEQRGL ASKAAELEME LNEHSLVIDT LKEVDETRKC YRMVGGVLVE RTVKEVLPAL ENNKEQIQKI IETLTQQLQA KGKELNEFRE KHNIRLMGED EKPAAKENSE GAGAKASSAG VLVS.

    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.

    Pfdn2 Human
  • View Data Sheet

    Name :

    Inhibin alpha A Chain Human

    Description:

    Inhibin-Alpha A Chain Human Recombinant

    Inhibin-Alpha, A-Inhibin Subunit, Inhibin Alpha Chain, INHA.

    Product # :

    HOR-293

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    Description

    Inhibin-Alpha A chain Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 134 amino acids fragment (233-366) and having an amino-terminal hexahistidine tag, having a total molecular weight of 19.2 kDa. The Inhibin-Alpha A chain is purified by standard chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Inhibin-A alpha chain is supplied in 20mM Tris HCl (pH-8), 5mM EDTA and 50% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Citations

    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

      Inhibin-Alpha, A-Inhibin Subunit, Inhibin Alpha Chain, INHA.

    • 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. Please avoid freeze thaw cycles.

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

    Inhibin A Alpha Chain Human
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