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Search results

1000 results found for “visfatin”

Name

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  • View Data Sheet

    Name :

    Activin-A Human Active

    Description:

    Activin-A Human Recombinant, Active

    Inhba, Inhibin beta A, FSH releasing protein.

    Product # :

    CYT-145

    Price :

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    Description

    Active form Activin-A Human 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

    Human Activin-A was 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 cytotoxicity of MPC-11 cells and was found to be 8.95ng/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

      Human 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

      Title: Research on Activin A Human Recombinant: Molecular Characteristics, Signaling Pathways, Physiological Functions, and Therapeutic Potential

      Introduction:

      Activin A, a member of the transforming growth factor-beta (TGF-β) superfamily, is a multifunctional cytokine that plays a significant role in various biological processes in the human body. Its involvement in diverse physiological and pathological functions has garnered considerable attention in scientific research. This paper aims to provide an overview of Activin A, encompassing its molecular characteristics, signaling pathways, physiological functions, and therapeutic potential.

      Activin A is encoded by the INHBA gene and is produced as a precursor protein that undergoes post-translational modifications to generate the mature form. The mature Activin A protein consists of two β-subunits held together by disulfide bonds. These structural features contribute to its functional properties and interactions with specific receptors.

      Upon binding to its cell surface receptors, Activin A triggers intracellular signaling cascades, leading to various cellular responses. Canonical SMAD-dependent pathway as well as non-SMAD pathways, such as MAPK/ERK, PI3K/Akt, and JNK signaling, are activated by Activin A. The intricate network of signaling pathways enables Activin A to regulate diverse biological processes, including cell proliferation, differentiation, apoptosis, and tissue homeostasis.

      Activin A exerts its physiological functions in a tissue-specific manner. It plays a critical role in embryonic development, particularly in organogenesis and patterning. Additionally, Activin A is involved in reproductive biology, where it participates in folliculogenesis, spermatogenesis, and hormonal regulation. It also contributes to neural development, immune system modulation, and skeletal homeostasis.

      The multifunctional properties of Activin A have positioned it as a potential therapeutic target for various diseases. Its involvement in cancer, neurodegenerative disorders, fibrosis, and reproductive disorders has prompted extensive research to explore its therapeutic potential. Understanding the molecular mechanisms underlying Activin A's actions provides valuable insights for developing innovative therapeutic strategies.

      In conclusion, Activin A is a versatile cytokine with diverse roles in human biology. This research aims to deepen our understanding of its molecular characteristics, signaling pathways, physiological functions, and therapeutic potential. By elucidating the complexities of Activin A, we strive to pave the way for novel therapeutic interventions in various human diseases.

    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 Human
  • View Data Sheet

    Name :

    SCF Rat

    Description:

    Stem Cell Factor Rat Recombinant

    Kit ligand Precursor, C-kit ligand, SCF, Mast cell growth factor, MGF, SF, KL-1, Kitl, DKFZp686F2250, Hematopoietic growth factor KL.

    Product # :

    CYT-323

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    Description

    Stem cell factor Rat Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 164 amino acids (26-189) and having a molecular mass of 18.4 kDa.The Rat SCF is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Lyophilized from a concentrated (1mg/ml) solution in water containing 0.02% NaHCO3.

    Purity

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

    Biological Activity

    The ED50 is determined by the dose-dependant stimulation of the proliferation of human TF-1 cells which is < 10 ng/ml, corresponding to a specific activity of 100,000units/mg.

    Citations

    More Info

    • Introduction

      Stem cell factor / KIT ligand (SCF) is a cytokine which binds CD117 (c-Kit). SCF is also known as "steel factor" or "c-kit ligand". SCF exists in two forms, cell surface bound SCF and soluble (or free) SCF. Soluble SCF is produced by the cleavage of surface bound SCF by metalloproteases.
      SCF is a growth factor important for the survival, proliferation, and differentiation of hematopoietic stem cells and other hematopoietic progenitor cells. One of its roles is to change the BFU-E (burst-forming unit-erythroid) cells, which are the earliest erythrocyte precursors in the erythrocytic series, into the CFU-E (colony-forming unit-erythroid).

    • Synonyms

      Kit ligand Precursor, C-kit ligand, SCF, Mast cell growth factor, MGF, SF, KL-1, Kitl, DKFZp686F2250, Hematopoietic growth factor KL.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Amino Acid Sequence

      MQEICRNPVT DNVKDITKLV ANLPNDYMIT LNYVAGMDVL PSHCWLRDMV THLSVSLTTL LDKFSNISEG LSNYSIIDKL GKIVDDLVAC MEENAPKNVK ESLKKPETRN FTPEEFFSIF NRSIDAFKDF MVASDTSDCV LSSTLGPEKD SRVSVTKPFM LPPVA.

    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.

    Scf Rat
  • View Data Sheet

    Name :

    GFRA3 Human

    Description:

    GDNF Family Receptor Alpha 3 Human Recombinant

    GDNF Family Receptor Alpha3, GDNFR-alpha-3, GFR-alpha-3, GDNF Receptor Alpha-3, GDNFR3, GDNF Family Receptor Alpha-3, Glial Cell Line-Derived Neurotrophic Factor Receptor Alpha-3, GPI-Linked Receptor.

    Product # :

    CYT-399

    Price :

    Quantity :

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    Shipped with Ice Packs

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    • description
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    • More Info
    • sds-page
    • Citations

    Description

    GFRA3 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 366 amino acids (32-374a.a) and having a molecular mass of 40.7kDa.GFRA3 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    GFRA3 protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH 8.0) 0.4M urea and 10% glycerol.

    Purity

    Greater than 85% as determined by SDS-PAGE.

    sds-page

    GFRA3 Human - Product image 1

    Citations

    More Info

    • Introduction

      GDNF Family Receptor Alpha 3 (GFRA3) belongs to the GDNF receptor family. GFRA3 creates a signaling receptor complex with RET tyrosine kinase receptor and binds the ligand, artemin (ARTN).

    • Synonyms

      GDNF Family Receptor Alpha3, GDNFR-alpha-3, GFR-alpha-3, GDNF Receptor Alpha-3, GDNFR3, GDNF Family Receptor Alpha-3, Glial Cell Line-Derived Neurotrophic Factor Receptor Alpha-3, GPI-Linked Receptor.

    • 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).Please avoid freeze thaw cycles.

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MGSDPLPTES RLMNSCLQAR RKCQADPTCS AAYHHLDSCT SSISTPLPSE EPSVPADCLE AAQQLRNSSL IGCMCHRRMK NQVACLDIYW TVHRARSLGN YELDVSPYED TVTSKPWKMN LSKLNMLKPD SDLCLKFAML CTLNDKCDRL RKAYGEACSGPHCQRHVCLR QLLTFFEKAA EPHAQGLLLC PCAPNDRGCG ERRRNTIAPN CALPPVAPNC LELRRLCFSD PLCRSRLVDF QTHCHPMDIL GTCATEQSRC LRAYLGLIGT AMTPNFVSNV NTSVALSCTC RGSGNLQEEC EMLEGFFSHN PCLTEAIAAK MRFHSQLFSQ DWPHPTFAVMAHQNEN

    • Background

      What is the molecular weight/Mw of GFRA3 HUMAN Protein?
      GFRA3 HUMAN Protein has a total Mw of 40.7kDa.

      What is the source or expression system of GFRA3 HUMAN Protein?
      Escherichia Coli.

      What is the Purity of GFRA3 HUMAN Protein?
      GFRA3 HUMAN Protein is >85% pure as determined by SDS-PAGE.

      What is the Biological Activity of GFRA3 HUMAN Protein?
      The biological functionality of GFRA3 HUMAN Protein will be determined in the future.

      What is the amino acid sequence of GFRA3 HUMAN Protein?
      MGSSHHHHHH SSGLVPRGSH MGSDPLPTES RLMNSCLQAR RKCQADPTCS AAYHHLDSCT SSISTPLPSE EPSVPADCLE AAQQLRNSSL IGCMCHRRMK NQVACLDIYW TVHRARSLGN YELDVSPYED TVTSKPWKMN LSKLNMLKPD SDLCLKFAML CTLNDKCDRL RKAYGEACSGPHCQRHVCLR QLLTFFEKAA EPHAQGLLLC PCAPNDRGCG ERRRNTIAPN CALPPVAPNC LELRRLCFSD PLCRSRLVDF QTHCHPMDIL GTCATEQSRC LRAYLGLIGT AMTPNFVSNV NTSVALSCTC RGSGNLQEEC EMLEGFFSHN PCLTEAIAAK MRFHSQLFSQ DWPHPTFAVMAHQNEN

      What applications can GFRA3 HUMAN Protein be used in?
      GFRA3 HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for GFRA3 HUMAN Protein?
      The endotoxin level is minimal, GFRA3 HUMAN Protein was purified using conventional chromatography techniques.


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

    Gfra3 Human
  • View Data Sheet

    Name :

    Desmin Chicken

    Description:

    Desmin Chicken Gizzard

    Desmin, DES, CSM1, CSM2, CMD1I, FLJ12025, FLJ39719, FLJ41013, FLJ41793.

    Product # :

    PRO-2783

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    Description

    Desmin Chicken having a calculated molecular mass of 53 kDa, pI-5.4.

    Source

    Chicken gizzard.

    Formulation

    Desmin was lyophilized from a 1mg/ml solution containing 10 mM sodium phosphate buffer pH 7.5, 6M urea, 1mM EDTA, 2mM DTT and 10mM methylammonium chloride.

    Purity

    Greater than 98.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Synonyms

      Desmin, DES, CSM1, CSM2, CMD1I, FLJ12025, FLJ39719, FLJ41013, FLJ41793.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Store the lyophilized Desmin between 2-8°C, do not freeze. Upon reconstitution Desmin should be stored at -20°C. Please prevent freeze-thaw cycles.

    • Solubility

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

    • Background

      Desmin, an intermediate filament protein, plays a fundamental role in maintaining the structural integrity and function of muscle cells. While extensive research has been conducted on desmin in mammals, the study of desmin in chickens is an emerging area with considerable potential for advancing our understanding of muscle biology. Chickens are valuable model organisms for studying muscle development, growth, and regeneration due to their relatively simple muscular system and economic significance in poultry production. This research aims to provide a comprehensive exploration of desmin in chickens, shedding light on its functions and implications for muscle structure and function.

      The primary objective of this research is to elucidate the role of desmin in chicken muscle structure and development. In vitro and in vivo experiments, utilizing chicken cell cultures and embryonic models, will be conducted to investigate how desmin contributes to the organization of muscle fibers, sarcomere assembly, and myofibrillogenesis. Understanding these mechanisms is fundamental for deciphering the complexities of muscle development in chickens.

      The second objective is to assess the clinical and economic relevance of desmin in poultry production. Studies involving broiler chickens will be conducted to evaluate the impact of desmin mutations or variations on muscle growth, meat quality, and disease susceptibility. These investigations may provide valuable insights into potential strategies for enhancing poultry production efficiency and meat quality.

      The third objective is to explore the potential applications of desmin in biotechnology and tissue engineering. Research will investigate the use of desmin-expressing chicken cells as models for studying muscle-related diseases and for developing tissue engineering approaches for muscle repair and regeneration.

      By delving into the functions and roles of desmin in chickens, this research aims to expand our knowledge of muscle biology, its implications for poultry production, and its potential applications in biotechnology and regenerative medicine.

    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.

    Desmin Chicken
  • View Data Sheet

    Name :

    HTF Human

    Description:

    Holo Transferrin Human

    Serotransferrin, Transferrin, Siderophilin, Beta-1-metal-binding globulin, TF, PRO1557, PRO2086, DKFZp781D0156, Holo Transferrin, HTF.

    Product # :

    PRO-315

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    Description

    Human Holo Transferrin is a glycoprotein of approximately 77 kDa.

    Source

    Human serum.

    Formulation

    The protein (10mg/ml) was lyophilized from 20mM NH4HC03 solution.
    May contain traces of buffer salts.

    Purity

    Greater than 98.0% as determined by coomassie blue stained SDS-PAGE and Cellulose Acetate electrophoresis.

    Citations

    More Info

    • Introduction

      Transferrin is the iron-transport protein of vertebrate serum and donates iron to cells through interaction with a specific membrane receptor, CD71. Transferrin appears to be indispensable for most cells growing in tissue culture.
      It is referred to frequently as a growth factor because, in analogy to other growth factor-receptor interactions, proliferating cells express high numbers of transferrin receptors, and the binding of transferrin to their receptors is needed for cells to initiate and maintain their DNA synthesis. Apart from its role as an iron transport protein transferrin acts as a cytokine and has functions that may not be related to its iron-carrying capacity.
      Human Transferrin is a crucial component for the cultivation of mammalian cells in-vitro. Human Transferrin is Critical for long-term cells growth in-vitro. Human Transferrin is used as detoxificant in media by binding contaminating metal ions. Human Transferrin is often used as a nutrient in fermentation media for recombinant protein and biopharmaceutical production. Additional common uses of Human Transferrin areMolecular weight, Affinity purification of anti-human transferrin antibodies and also as receptor mediated transfection of molecules such as DNA, into cells.

    • Synonyms

      Serotransferrin, Transferrin, Siderophilin, Beta-1-metal-binding globulin, TF, PRO1557, PRO2086, DKFZp781D0156, Holo Transferrin, HTF.

    • Physical Appearance

      Sterile Filtered Pink lyophilized (freeze-dried) powder.

    • Stability

      Store the lyophilized Holo Transferrin between 2-8°C, do not freeze. Upon reconstitution Apo Transferrin 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 Holo Transferrin in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Human Virus Test

      FDA approved Plasma from each donor has been tested and found negative for antibodies to HIV-1 & 2, HCV, HBsAG, HBc, HBV, HAV, HIV and Syphilis.

    • Iron Content

      The Iron content was estimated by ICP and was found to be 1232 ppm.

    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.

    Holo Transferrin Human
  • View Data Sheet

    Name :

    HTF Bovine

    Description:

    Holo Transferrin Bovine

    Serotransferrin, Transferrin, Siderophilin, Beta-1-metal-binding globulin, TF, PRO1557, PRO2086, DKFZp781D0156, Holo Transferrin, HTF.

    Product # :

    PRO-510

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    Description

    Bovine Holo Transferrin is a glycoprotein of approximately 80 kDa.

    Formulation

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

    Purity

    Greater than 97.0% as determined by Cellulose Acetate.

    Citations

    More Info

    • Introduction

      Transferrin is the iron-transport protein of vertebrate serum and donates iron to cells through interaction with a specific membrane receptor, CD71. Transferrin appears to be indispensable for most cells growing in tissue culture.
      It is referred to frequently as a growth factor because, in analogy to other growth factor-receptor interactions, proliferating cells express high numbers of transferrin receptors, and the binding of transferrin to their receptors is needed for cells to initiate and maintain their DNA synthesis. Apart from its role as an iron transport protein transferrin acts as a cytokine and has functions that may not be related to its iron-carrying capacity.

    • Synonyms

      Serotransferrin, Transferrin, Siderophilin, Beta-1-metal-binding globulin, TF, PRO1557, PRO2086, DKFZp781D0156, Holo Transferrin, HTF.

    • Physical Appearance

      Sterile Filtered Pink lyophilized (freeze-dried) powder.

    • Stability

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

    • Human Virus Test

      FDA approved Plasma from each donor has been tested and found negative for antibody to HIV-1, HIV-2, HCV, HBSAG, HBc, ALT and Syphilis.Viral inactivation by pasteurization (60°C for 10 hours) has been validated using three different test viruses, with removal of 8-14.5 logs of virus documented. The purification process has also been found to remove significant additional quantities of virus.

    • Applications

      Bovine Transferrin is a crucial component for the cultivation of mammalian cells in-vitro. Bovine Transferrin is Critical for long-term cells growth in-vitro. Bovine Transferrin is used as detoxificant in media by binding contaminating metal ions. Bovine Transferrin is often used as a nutrient in fermentation media for recombinant protein and biopharmaceutical production. Additional common uses of Bovine Transferrin areMolecular weight, Affinity purification of anti-human transferrin antibodies and also as receptor mediated transfection of molecules such as DNA, into cells.

    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.

    Holo Transferrin Bovine
  • View Data Sheet

    Name :

    FGF 1 Rat

    Description:

    Fibroblast Growth Factor-Acidic Rat Recombinant

    Fibroblast growth factor 1, FGF-1, Acidic fibroblast growth factor, aFGF, binding growth factor 1, HBGF-1, Fgf1, Fgfa, HBGF1.

    Product # :

    CYT-075

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    Description

    Fibroblast Growth Factor-acidic Rat Recombinant (FGF-1) produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 141 amino acids and having a molecular mass of 15.9 kDa.The FGF acidic is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Lyophilized at a concentration of 1 mg/ml in 5mM Na2PO4, pH-7.5 and 50mM NaCl.

    Purity

    Greater than 98.0% as determined by SDS-PAGE.

    Biological Activity

    The ED50 as determined by the dose-dependent proliferation of mouse BALB/c 3T3 cells, is less than 0.2ng/ml corresponding to a Specific Activity of 5x106IU/mg.

    Citations

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    • Introduction

      Acidic fibroblast growth factor is a member of the fibroblast growth factor (FGF) family. FGF family members possess broad mitogenic and cell survival activities, and are involved in a variety of biological processes, including embryonic development, cell growth, morphogenesis, tissue repair, tumor growth and invasion. This protein functions as a modifier of endothelial cell migration and proliferation, as well as an angiogenic factor. It acts as a mitogen for a variety of mesoderm- and neuroectoderm-derived cells in vitro, thus is thought to be involved in organogenesis. Three alternatively spliced variants encoding different isoforms have been described. The binding growth factors are angiogenic agents in vivo and are potent mitogens for a variety of cell types in vitro. There are differences in the tissue distribution and concentration of these 2 growth factors.

    • Synonyms

      Fibroblast growth factor 1, FGF-1, Acidic fibroblast growth factor, aFGF, binding growth factor 1, HBGF-1, Fgf1, Fgfa, HBGF1.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Amino Acid Sequence

      MFNLPLGNYK KPKLLYCSNG GHFLRILPDG TVDGTRDRSD QHIQLQLSAE SAGEVYIKGT ETGQYLAMDT EGLLYGSQTP NEECLFLERL EENHYNTYTS KKHAEKNWFV GLKKNGSCKR GPRTHYGQKA ILFLPLPVSS D.

    • Background

      What is the molecular weight/Mw of FGF 1 Protein?
      FGF 1 Protein has a total Mw of 15.9kDa.

      What is the source or expression system of FGF 1 Protein?
      Escherichia Coli.

      What is the Purity of FGF 1 Protein?
      FGF 1 Protein is >98% pure as determined by SDS-PAGE.

      What is the Biological Activity of FGF 1 Protein?
      The ED50 as determined by the dose-dependent proliferation of mouse BALB/c 3T3 cells, is less than 0.2ng/ml corresponding to a Specific Activity of 5x106IU/mg.

      What is the amino acid sequence of FGF 1 Protein?
      MFNLPLGNYK KPKLLYCSNG GHFLRILPDG TVDGTRDRSD QHIQLQLSAE SAGEVYIKGT ETGQYLAMDT EGLLYGSQTP NEECLFLERL EENHYNTYTS KKHAEKNWFV GLKKNGSCKR GPRTHYGQKA ILFLPLPVSS D.

      What applications can FGF 1 Protein be used in?
      FGF 1 Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for FGF 1 Protein?
      The endotoxin level is minimal, FGF 1 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.

    Fgf 1 Rat
  • View Data Sheet

    Name :

    OPG Human, His

    Description:

    Osteoprotegerin Human Recombinant, His Tag

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

    Product # :

    CYT-290

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    Description

    Recombinant Human OCIF produced in E.coli cells is a single, non-glycosylated, polypeptide chain containing amino acids 201-401 and having a molecular mass of 31 kDa which includes a 4 kDa His tag.The OPG is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The protein was lyophilized from a concentrated (1mg/ml) solution with 1X PBS, 0.1% SDS and 1mM DTT.

    Purity

    Greater than 80.0% as determined by(a) Analysis by RP-HPLC.
    (b) Analysis by SDS-PAGE.

    Citations

    More Info

    • Introduction

      Osteoprotegerin, which is a member of the tumor necrosis factor receptor superfamily and is involved in the regulation of bone metabolism. OPGand its ligand (OPGL) are cytokines regulating osteoclasto-genesis. OPGL binds to receptors on the surface of preosteoclasts and stimulates their differentiation into active osteoclasts. This leads to osteoresorption. OPG inhibits this osteoclasto-genesis (OPG is secreted by osteoblasts, and binds to OPGL, thus inhibiting maturation of osteoclasts and osteoresorption). The degree and activity of osteoresorption depend mainly on the balance between OPG and its ligand (OPGL); factors increasing OPGL expression mostly reduce OPG expression and vice versa.

    • Synonyms

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

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Applications

      1. Positive control for Western blot.
      2. Antibody production.
      3. Protein assay.

    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 His
  • View Data Sheet

    Name :

    TIGIT Human

    Description:

    T-Cell Immunoreceptor With Ig And ITIM Domains Human Recombinant

    VSIG9, VSTM3, WUCAM, V-set and immunoglobulin domain-containing protein 9, V-set and transmembrane domain-containing protein 3.

    Product # :

    PRO-2498

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    Description

    TIGIT produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 359 amino acids (22-141a.a.) and having a molecular mass of 40.0kDa. (Molecular size on SDS-PAGE will appear at approximately 40-57kDa).TIGIT is expressed with a 239 amino acid hlgG-His tag at C-Terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    TIGIT protein solution (0.5mg/ml) contains phosphate buffered saline (pH7.4) and 10% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      T cell immunoreceptor with Ig and ITIM domains or TIGIT, is an immune receptor located on part of T cells and Natural Killer Cells(NK). TIGIT is also known as Vstm3 and WUCAM. The receptor can bind with high affinity to dendritic cells(DCs), CD155(PVR) on macrophages, etc., and it can bind with lower affinity to CD112(PVRL2). TIGIT can inhibit the cytotoxicity of Natural Killer Cells through its ITIM domain via antibodies against the interaction with PVR and the activity is directed. It has been show on research that TIGIT-Fc fusion molecule can have interaction with PVR on dendritic cells and elevate its IL-10 secretion level or lower the secretion on IL-12 under the stimulation of LPS, moreover, it can inhibit the activation of T cell in vivo.

    • Synonyms

      VSIG9, VSTM3, WUCAM, V-set and immunoglobulin domain-containing protein 9, V-set and transmembrane domain-containing protein 3.

    • 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

      MMTGTIETTG NISAEKGGSI ILQCHLSSTT AQVTQVNWEQ QDQLLAICNA DLGWHISPSF KDRVAPGPGL GLTLQSLTVN DTGEYFCIYH TYPDGTYTGR IFLEVLESSV AEHGARFQIP LEPKSCDKTH TCPPCPAPEL LGGPSVFLFP PKPKDTLMIS RTPEVTCVVV DVSHEDPEVK FNWYVDGVEV HNAKTKPREE QYNSTYRVVS VLTVLHQDWL NGKEYKCKVS NKALPAPIEK TISKAKGQPR EPQVYTLPPS RDELTKNQVS LTCLVKGFYP SDIAVEWESN GQPENNYKTT PPVLDSDGSF FLYSKLTVDK SRWQQGNVFS CSVMHEALHN HYTQKSLSLS PGKHHHHHH.

    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.

    Tigit Human
  • View Data Sheet

    Name :

    CHGA Human, His

    Description:

    Chromogranin-A Human Recombinant, His Tag

    CGA, CHGA, Vasostatin-2, Pituitary secretory protein I, SP-I.

    Product # :

    PRO-699

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    Description

    Recombinant Human CHGA produced in E.Coli is a single, non-glycosylated polypeptide chain containing 460 amino acids (19-457 a.a) and having a molecular mass of 51.2kDa (Molecular weight on SDS-PAGE will appear higher). Chromgranin-A is fused to 21 amino acid His Tag at N-terminus and purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The CHGA protein (0.5mg/ml) contains 20mM Tris-HCl buffer pH-7.5, 2mM EDTA, 0.1mM PMSF and 10% glycerol.

    Purity

    Greater than 80.0% as determined by Analysis by SDS-PAGE.

    Citations

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    • Introduction

      Chromgranin-A is part of the neuroendocrine secretory protein family. CHGA is located in secretory vesicles of neurons and endocrine cells. Chromgranin-A is a precursor to three biologically active peptides; vasostatin, pancreastatin, and parastatin. These peptides act as autocrine or paracrine negative modulators of the neuroendocrine system. Other peptides, including chromostatin, beta-granin, WE-14 and GE-25, are also derived from the full-length protein. Chromgranin-A has numerous biological activities on some tissues and organs and exerts a large spectrum of homeostatic actions, including antifungal and antimicrobial effect, modulation of cell adhesion, and inhibition of parathyroid hormone secretion.

    • Synonyms

      CGA, CHGA, Vasostatin-2, Pituitary secretory protein I, SP-I.

    • 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 MLPVNSPMNK GDTEVMKCIV EVISDTLSKP SPMPVSQECF ETLRGDERIL SILRHQNLLK ELQDLALQGA KERAHQQKKH SGFEDELSEV LENQSSQAEL KEAVEEPSSK DVMEKREDSK EAEKSGEATD GARPQALPEP MQESKAEGNN QAPGEEEEEE EEATNTHPPA SLPSQKYPGP QAEGDSEGLS QGLVDREKGL SAEPGWQAKR EEEEEEEEEA EAGEEAVPEE EGPTVVLNPH PSLGYKEIRK GESRSEALAV DGAGKPGAEE AQDPEGKGEQ EHSQQKEEEE EMAVVPQGLF RGGKSGELEQ EEERLSKEWE DSKRWSKMDQ LAKELTAEKR LEGQEEEEDN RDSSMKLSFR ARAYGFRGPG PQLRRGWRPS SREDSLEAGL PLQVRGYPEE KKEEEGSANR RPEDQELESL SAIEAELEKV AHQLQALRRG.

    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.

    Chromogranin A Human His
  • View Data Sheet

    Name :

    WIBG Human

    Description:

    within BCGN Homolog Human Recombinant

    PYM, Partner of Y14 and mago, MGC13064, WIBG, BCGN Homolog, Protein wibg homolog.

    Product # :

    PRO-864

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    Description

    WIBG Recombinant Human produced in E.Coli is a single, non-glycosylated polypeptide chain containing 212 amino acids (1-204 a.a.) and having a molecular mass of 23.7 kDa. The WIBG is fused to 8 amino acid His-Tag at C-terminus and purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    WIBG Human solution containing 20mM Tris pH-8, 0.1M NaCl & 10% glycerol.

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      WIBG is a cooperateing partner of Mago-Y14. The Mago-Y14 heterodimer is a key protein of the EJC(exon junction complex) that is deposited on mRNAs as a consequence of splicing and influences postsplicing mRNA metabolism. WIBG is a cytoplasmic RNA-binding protein that is excluded from the nucleus by Crm1. WIBG relates directly with Mago-Y14 by means of its N-terminal domain.

    • Synonyms

      PYM, Partner of Y14 and mago, MGC13064, WIBG, BCGN Homolog, Protein wibg homolog.

    • 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

      MEAAGSPAAT ETGKYIASTQ RPDGTWRKQR RVKEGYVPQE EVPVYENKYV KFFKSKPELP PGLSPEATAP VTPSRPEGGE PGLSKTAKRN LKRKEKRRQQ QEKGEAEALS RTLDKVSLEE TAQLPSAPQG SRAAPTAASD QPDSAATTEK AKKIKNLKKK LRQVEELQQR IQAGEVSQPS KEQLEKLARR RALEEELEDL ELGLLEHHHH HH.

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

    Wibg Human
  • View Data Sheet

    Name :

    TGFB2 Human, HEK

    Description:

    Transforming Growth Factor-Beta 2 Human Recombinant, HEK

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

    Product # :

    CYT-112

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    Description

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

    Source

    HEK.

    Formulation

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

    Purity

    Greater than 95% as obsereved by SDS-PAGE.

    Biological Activity

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

    Citations

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    • Introduction

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

    • Synonyms

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

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Solubility

      It is recommended to reconstitute the lyophilized TGF-b 2 in sterile solution containing 20% ethanol, 50mM sodium acetate and 75mM acetic acid.

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

    Tgf B 2 Human Hek
  • View Data Sheet

    Name :

    MCSFR Human

    Description:

    Colony Stimulating Factor 1 Receptor Human Recombinant

    Macrophage colony-stimulating factor 1 receptor, CSF-1 receptor (EC:2.7.10.1), CSF-1-R, CSF-1R, M-CSF-R, Proto-oncogene c-Fms, CD115, CSF1R, FMS. 

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    CYT-1068

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    Description

    MCSFR produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 737 amino acids (20-517a.a.) and having a molecular mass of 82.1kDa. (Molecular size on SDS-PAGE will appear at approximately 70-100kDa).MCSFR is expressed with a 239 amino acid hIgG-His tag at C-Terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    MCSFR 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.

    Biological Activity

    Measured by its ability to inhibit M-CSF dependent proliferation of M-NFS-60 mouse myelogenous leukemia lymphoblast cells. The ED50 for this effect is less or equal to 100ng/ml in the presence of 10 ng/ml M-CSF.

    Citations

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    • Introduction

      MCSFR which is also familiar as CSF1R, is part of the type3 subfamily of receptor tyrosine kinases. MCSFR is expressed mainly on cells of the monocyte and macrophage lineage, stem cells, and in the growing placenta. Most of the biological effects of this cytokine are mediated by MCSFR. MCSFR contains an extracellular ligand-binding domain, a single membrane-spanning segment, and an intracellular tyrosine kinase domain. Originally CSF1 and this receptor were implicated as vital for normal trophoblastic implantation as well as monocyte development. The role of CSF1/CSF1R in normal mammary gland development is actually very interesting since this connection has also been discovered in the biology of breast cancer with the results of abnormal expression of CSF1 and its receptor. Likewise, in Alzheimer's disease and after brain injuries an increased level of CSF1R was found in the microglia, which causes the microglia to become more active.

    • Synonyms

      Macrophage colony-stimulating factor 1 receptor, CSF-1 receptor (EC:2.7.10.1), CSF-1-R, CSF-1R, M-CSF-R, Proto-oncogene c-Fms, CD115, CSF1R, FMS.

    • 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

      IPVIEPSVPE LVVKPGATVT LRCVGNGSVE WDGPPSPHWT LYSDGSSSIL STNNATFQNT GTYRCTEPGD PLGGSAAIHL YVKDPARPWN VLAQEVVVFE DQDALLPCLL TDPVLEAGVS LVRVRGRPLM RHTNYSFSPW HGFTIHRAKF IQSQDYQCSA LMGGRKVMSI SIRLKVQKVI PGPPALTLVP AELVRIRGEA AQIVCSASSV DVNFDVFLQH NNTKLAIPQQ SDFHNNRYQK VLTLNLDQVD FQHAGNYSCV ASNVQGKHST SMFFRVVESA YLNLSSEQNL IQEVTVGEGL NLKVMVEAYP GLQGFNWTYL GPFSDHQPEP KLANATTKDT YRHTFTLSLP RLKPSEAGRY SFLARNPGGW RALTFELTLR YPPEVSVIWT FINGSGTLLC AASGYPQPNV TWLQCSGHTD RCDEAQVLQV WDDPYPEVLS QEPFHKVTVQ SLLTVETLEH NQTYECRAHN SVGSGSWAFI PISAGAHTHP PDEFLFTPLE PKSCDKTHTC PPCPAPELLG GPSVFLFPPK PKDTLMISRT PEVTCVVVDV SHEDPEVKFN WYVDGVEVHN AKTKPREEQY NSTYRVVSVL TVLHQDWLNG KEYKCKVSNK ALPAPIEKTI SKAKGQPREP QVYTLPPSRD ELTKNQVSLT CLVKGFYPSD IAVEWESNGQ PENNYKTTPP VLDSDGSFFL YSKLTVDKSR WQQGNVFSCS VMHEALHNHY TQKSLSLSPG KHHHHHH.

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

    Csf1R Human
  • View Data Sheet

    Name :

    SNF8 Human

    Description:

    SNF8, ESCRT-II Complex Subunit Human Recombinant

    SNF8 ESCRT-II complex subunit homolog (S. cerevisiae), ESCRT-II complex subunit VPS22, ELL-associated protein of 30 kDa, EAP30 subunit of ELL complex, vacuolar-sorting protein SNF8, EAP30, VPS22, Dot3.

    Product # :

    PRO-1135

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    Description

    SNF8 Human Recombinant produced in E. coli is a single polypeptide chain containing 282 amino acids (1-258) and having a molecular mass of 31.4 kDa.SNF8 is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    The SNF8 solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.2M NaCl, 2mM DTT and 50% glycerol.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      SNF8 belongs to the SNF8 family of vacuolar sorting proteins and is restricts to both the nucleus and the cytoplasm. SNF8 is a subunit of the endosomal sorting complex essential for transport II (ESCRT-II), which is necessary for multivesicular body (MVB) formation and sorting of endosomal cargo proteins into MVBs. The MVB pathway facilitates transfer of transmembrane proteins into the lumen of the lysosome for degradation. Additionally, the ESCRT-II complex takes part in transcription regulation by contributing to derepression of transcription by RNA polymerase II, probably by its interface with ELL.

    • Synonyms

      SNF8 ESCRT-II complex subunit homolog (S. cerevisiae), ESCRT-II complex subunit VPS22, ELL-associated protein of 30 kDa, EAP30 subunit of ELL complex, vacuolar-sorting protein SNF8, EAP30, VPS22, Dot3.

    • 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 MGSHMHRRGV GAGAIAKKKL AEAKYKERGT VLAEDQLAQM SKQLDMFKTN LEEFASKHKQ EIRKNPEFRV QFQDMCATIG VDPLASGKGF WSEMLGVGDF YYELGVQIIE VCLALKHRNG GLITLEELHQ QVLKGRGKFA QDVSQDDLIR AIKKLKALGT GFGIIPVGGT YLIQSVPAEL NMDHTVVLQL AEKNGYVTVS EIKASLKWET ERARQVLEHL LKEGLAWLDL QAPGEAHYWL PALFTDLYSQ EITAEEAREA LP

    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.

    Snf8 Human
  • View Data Sheet

    Name :

    PF 4 Protein

    Description:

    Platelet Factor-4 Human (CXCL4)

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

    Product # :

    CHM-234

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    Description

    Human PF-4 a 7.8 kDa protein consisting of 70 amino acid residues.

    Source

    Human Platelets.

    Formulation

    The CXCL4 protein was lyophilized in PBS buffer pH-7.4.

    Purity

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

    Citations

    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 white lyophilized powder.

    • Stability

      Human CXCL4 although stable at 25°C 1 week, should be stored desiccated below -18°C. Please prevent freeze-thaw cycles.

    • Solubility

      It is recommended to reconstitute the lyophilized CXCL4 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 four N-terminal amino acids was determined and was found to be Glu-Ala-Glu-Glu.

    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.

    Pf 4 Human
  • View Data Sheet

    Name :

    FIS1 Human

    Description:

    Fission-1 Human Recombinant

    TTC11, Tetratricopeptide repeat domain 11, Fission 1 (mitochondrial outer membrane) homolog (S. cerevisiae).

    Product # :

    PRO-829

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    Description

    FIS1 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 142 amino acids (1-122 a.a.) and having a molecular mass of 16.3 kDa. FIS1 protein is fused to a 20 amino acid His tag at N-terminus and is purified by standard chromatography.

    Source

    Escherichia Coli.

    Formulation

    FIS1 protein solution (1mg/ml) containing 20mM Tris-HCl pH-8 and 10% glycerol.

    Purity

    Greater than 95% as determined by SDS-PAGE.

    Citations

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    • Introduction

      FIS1 is part of the mitochondrial complex that promotes mitochondrial fission. FIS1 induces cytochrome C discharge from the mitochondrion to the cytosol, eventually leading to apoptosis. FIS1 participates in peroxisomal growth and division. The C terminus is required for mitochondrial localisation, while the N teminus is necessary for mitochondrial fission.

    • Synonyms

      TTC11, Tetratricopeptide repeat domain 11, Fission 1 (mitochondrial outer membrane) homolog (S. cerevisiae).

    • 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 MEAVLNELVS VEDLLKFEKK FQSEKAAGSV SKSTQFEYAW CLVRSKYNDD IRKGIVLLEE LLPKGSKEEQ RDYVFYLAVG NYRLKEYEKA LKYVRGLLQT EPQNNQAKEL ERLIDKAMKK DG.

    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.

    Fis1 Human
  • View Data Sheet

    Name :

    LCN1 Human

    Description:

    Lipocalin-1 Human Recombinant

    Lipocalin-1, PMFA, TLC, TP, VEGP, Tear lipocalin, Tear prealbumin, Von Ebner gland protein, VEG protein.

    Product # :

    ENZ-825

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    Description

    LCN1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 183 amino acids (19-176 a.a) and having a molecular mass of 20.1kDa. LCN1 is fused to a 25 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    LCN1 protein solution (1mg/ml) containing Phosphate buffered saline (pH7.4), 10% glycerol and 1mM DTT.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      Lipocalin-1 (LCN1) belongs to the lipocalin family of small secretory proteins. Lipocalins are extracellular transport proteins, which bind to various hydrophobic ligands. LCN1 protein is the principal lipid binding protein in tears and is overproduced in response to numerous stimuli including infection and stress. LCN1 is a marker for chromosome aneuploidy as well as an autoantigen in Sjogren's syndrome.

    • Synonyms

      Lipocalin-1, PMFA, TLC, TP, VEGP, Tear lipocalin, Tear prealbumin, Von Ebner gland protein, VEG protein.

    • 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 MGSHMHHLLA SDEEIQDVSG TWYLKAMTVD REFPEMNLES VTPMTLTTLE GGNLEAKVTM LISGRCQEVK AVLEKTDEPG KYTADGGKHV AYIIRSHVKD HYIFYCEGEL HGKPVRGVKL VGRDPKNNLE ALEDFEKAAG ARGLSTESIL IPRQSETCSP GSD.

    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.

    Lcn1 Human
  • View Data Sheet

    Name :

    S100A9 Human

    Description:

    S100 Calcium Binding Protein A9 Human Recombinant

    Calgranulin B, 60B8AG, CAGB, CFAG, CGLB, L1AG, LIAG, MAC387, MIF, MRP14, NIF, P14, Protein S100-A9, S100 calcium-binding protein A9.

    Product # :

    PRO-814

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    Description

    S100A9 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 122 amino acids (1-114 a.a.) and having a molecular mass of 14.3kDa. S100A9 protein is fused to an 8 amino acid His-Tag at C-terminus and purified by standard chromatography.

    Source

    Escherichia Coli.

    Formulation

    S100A9 Human solution containing 20mM Tris HCl pH-8, 0.1M NaCl and 10% glycerol.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      S100A9 is part of the S100 family of proteins containing 2 EF-hand calcium-binding motifs. S100A9 protein is localized in the cytoplasm and/or nucleus of a wide range of cells, and participates in the regulation of several cellular processes such as cell cycle progression and differentiation. S100 genes include no less than 13 proteins which are localized as a cluster on chromosome 1q21. S100A9 is involved in the inhibition of casein kinase and altered expression of this protein is associated with the disease cystic fibrosis.

    • Synonyms

      Calgranulin B, 60B8AG, CAGB, CFAG, CGLB, L1AG, LIAG, MAC387, MIF, MRP14, NIF, P14, Protein S100-A9, S100 calcium-binding protein A9.

    • 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

      MTCKMSQLER NIETIINTFH QYSVKLGHPD TLNQGEFKEL VRKDLQNFLK KENKNEKVIE HIMEDLDTNA DKQLSFEEFI MLMARLTWAS HEKMHEGDEG PGHHHKPGLG EGTPLEHHHH HH.

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

    S100A9 Human
  • View Data Sheet

    Name :

    Leptin Mouse

    Description:

    Leptin Mouse Recombinant

    OB Protein, Obesity Protein, OBS, Obesity factor.

    Product # :

    CYT-351

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    Description

    Leptin Mouse Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 147 amino acids and having a molecular mass of 16 kDa. The Leptin is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The mouse Leptin was lyophilized from a concentrated (1mg/ml) solution containing 0.0045mM NaHCO3.

    Purity

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

    Biological Activity

    Biological activity of Mouse Leptin is performed by including proliferation of BAF/3 cells stably transfected with the long form of human leptin receptor.

    Citations

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    • 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 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      AVPIQKVQDD TKTLIKTIVT RINDISHTQS VSAKQRVTGL DFIPGLHPIL SLSKMDQTLA VYQQVLTSLP SQNVLQIAND LENLRDLLHL LAFSKSCSLP QTSGLQKPES LDGVLEASLY STEVVALSRL QGSLQDILQQ LDVSPEC.

    • 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 Mouse
  • View Data Sheet

    Name :

    VEGF E (Orf Virus)

    Description:

    Vascular Endothelial Growth Factor-E Recombinant (Orf Virus)

    Product # :

    CYT-263

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    Description

    A DNA sequence encoding the mature variant of ovVEGF-E isolate D1701 (Dehio et al., 1999; GenBank accession No. AF106020) was expressed in E. coli as a 132 amino acid residue fusion protein with an N-terminal His-tag sequence and a thrombin cleavage site. Recombinant VEGF-E homodimer was dimerized in vitro and has a predicted mass of approximately 35 kDa.

    Source

    Escherichia Coli.

    Formulation

    The protein was lyophilized from a concentrated (1mg/ml) solution containing PBS.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    Biological Activity

    The biological activity was determined (1) by the ability to induce VEGFR-2/KDR receptor phosphorylation in PAE/KDR cells and (2) in a cell proliferation assay using primary HUVECs. The ED50 for this effect is typically 1-5ng/ml.

    Citations

    More Info

    • Introduction

      Based on sequence similarity to VEGF-A, a gene encoding a VEGF homologue has recently been discovered in the genome of Orf virus (OV) (Lyttle et al., 1994). Different isolates of Orf virus show significant amino acid sequence similarity to VEGF-A and described as a viral virulence factor that appears to be derived from captured host genes. All eight cysteine residues of the central cysteine knot motif characteristic of members of the VEGF family are conserved among other residues in the VEGF-E proteins (Dehio et al., 1999; Wise et al., 1999). Alignment of all mammalian VEGF sequences indicated that VEGF-E is distinct from the previously described VEGFs but most closely related to VEGF-A. Like VEGF-A, VEGF-E was found to bind with high affinity to VEGF receptor-2 (KDR) resulting in receptor autophosphorylation, whilst in contrast to VEGF-A, VEGF-E can not bind to VEGF receptor-1 (Flt-1). Furthermore VEGF-E can also not bind to VEGF receptor-3 (FLT-4). Therefore VEGF-E is a potent angiog

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized Vascular Endothelial Growth Factor-E Orf Virus although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution VEGF E -OV should be stored at 4°C between 2-7 days and for future use below -18°C.Please prevent freeze-thaw cycles.

    • Solubility

      The lyophilized oVEGF-E Orf Virus should be reconstituted in water or medium to a concentration not lower than 50µg/ml. For long term storage we would recommend to add at least 0.1% human or bovine serum albumin.

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH DSTKTWSEVF ENSGCKPRPM VFRVHDEHPE LTSQRFNPPC VTLMRCGGCC NDESLECVPT EEANVTMQLM GASVSGGNGM QHLSFVEHKK CDCKPPLTTT PPTTTRPPRR RR

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    Vegf E Orf Virus
  • View Data Sheet

    Name :

    Adipsin Human, Sf9

    Description:

    Complement Factor D Human Recombinant, Sf9

    Complement Factor D (Adipsin), Properdin Factor D, D Component Of Complement (Adipsin), C3 Convertase Activator, EC 3.4.21.46, ADIPSIN, PFD, AND, DF, Complement Factor D Preproprotein, Complement Factor D, EC 3.4.21, Complement factor D.

    Product # :

    PRO-2213

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    Description

    Adipsin produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 241 amino acids (21-253a.a.) and having a molecular mass of 26.01kDa. (Molecular size on SDS-PAGE will appear at approximately 28-40kDa). Adipsin is expressed with an 8 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    Adipsin protein solution (1mg/ml) contains phosphate buffered saline (pH7.4).

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      Complement Factor D (Adipsin), which belongs to the trypsin family of peptidases, is involved in the alternative complement pathway of the complement system where it cleaves factor B. In the alternative complement pathway, Adipsin is best known for its role in humoral suppression of infectious agents. In addition, Adipsin is a serine protease which is secreted by adipocytes into the bloodstream. Ultimately, Adipsin has a high level of expression in fat, proposing a role for adipose tissue in immune system biology.

    • Synonyms

      Complement Factor D (Adipsin), Properdin Factor D, D Component Of Complement (Adipsin), C3 Convertase Activator, EC 3.4.21.46, ADIPSIN, PFD, AND, DF, Complement Factor D Preproprotein, Complement Factor D, EC 3.4.21, Complement factor D.

    • 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

      PPRGRILGGR EAEAHARPYM ASVQLNGAHL CGGVLVAEQW VLSAAHCLED AADGKVQVLL GAHSLSQPEP SKRLYDVLRA VPHPDSQPDT IDHDLLLLQL SEKATLGPAV RPLPWQRVDR DVAPGTLCDV AGWGIVNHAG RRPDSLQHVL LPVLDRATCN RRTHHDGAIT ERLMCAESNR RDSCKGDSGG PLVCGGVLEG VVTSGSRVCG NRKKPGIYTR VASYAAWIDS VLAVEHHHHH H.

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

    Adipsin Human Sf9
  • View Data Sheet

    Name :

    NENF Human

    Description:

    Neudesin Neurotrophic Factor Human Recombinant

    Neudesin, Cell immortalization-related protein 2, Neuron-derived neurotrophic factor, Secreted protein of unknown function, SPUF protein, NENF, CIR2, SPUF, SCIRP10.

    Product # :

    CYT-778

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    Description

    NENF Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain (aa 32-172) containing 151 amino acids including a 10 a.a N-terminal His tag and having a molecular mass of 16.9kDa.

    Source

    Escherichia Coli.

    Formulation

    NENF was filtered (0.4µm) and lyophilized from 0.5mg/ml in 0.05M phosphate buffer and 0.075M NaCl, pH 7.4.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      Neudesin Neurotrophic Factor (NENF) is a member of the cytochrome b5 family, MAPR subfamily. NENF contains 1 cytochrome b5 heme-binding domain. NENF exhibits neurotrophic activity and activates phosphorylation of MAPK1/ERK2, MAPK3/ERK1 and AKT1/AKT in primary cultured neurons. NENF doesn’t have mitogenic activity in primary cultured astrocytes. NENF may play a part in neuronal differentiation and may have a transient influence on neural cell proliferation in neural precursor cells. NENF neurotrophic activity is increased by binding to heme. NENF is up-regulated in immortal cells and induced in estrogen receptor positive breast cancer expressing progesterone receptor.

    • Synonyms

      Neudesin, Cell immortalization-related protein 2, Neuron-derived neurotrophic factor, Secreted protein of unknown function, SPUF protein, NENF, CIR2, SPUF, SCIRP10.

    • Physical Appearance

      Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Store lyophilized protein 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 0.5 mg/ml and let the lyophilized pellet dissolve completely. NENF is not sterile! Please filter the product by an appropriate sterile filter before using it in the cell culture.

    • Amino Acid Sequence

      MKHHHHHHASGQTPRPAERG PPVRLFTEEE LARYGGEEED QPIYLAVKGV VFDVTSGKEF YGRGAPYNAL TGKDSTRGVA KMSLDPADLT HDTTGLTAKE LEALDEVFTK VYKAKYPIVG YTARRILNED GSPNLDFKPE DQPHFDIKDE F.

    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.

    Nenf Human
  • View Data Sheet

    Name :

    EFNA1 Human, Sf9

    Description:

    Ephrin A1 Human Recombinant, Sf9

    Ephrin A1, Immediate Early Response Protein B61, TNF Alpha-Induced Protein 4, Ephrin-A1, TNFAIP4, LERK-1, EPLG1, LERK1, Tumor Necrosis Factor, Alpha-Induced Protein 4, Eph-Related Receptor Tyrosine Kinase Ligand 1, EPH-Related Receptor Tyrosine Kinase Ligand 1, Tumor Necrosis Factor Alpha-Induced Protein 4, Ligand Of Eph-Related Kinase 1, ECKLG, EFL1, B61, EPH-related receptor tyrosine kinase ligand 1, LERK-1.

    Product # :

    PRO-2538

    Price :

    Quantity :

    Shipping Method :

    Ice Icon

    Shipped with Ice Packs

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    More Info

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

    Description

    EFNA1 produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 406 amino acids (19-182a.a.) and having a molecular mass of 46.6kDa. (Molecular size on SDS-PAGE will appear at approximately 40-57kDa).EFNA1 is expressed with a 242 amino acid hIgG-His-tag at C-Terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    EFNA1 protein solution (0.5mg/ml) contains 10% glycerol & Phosphate Buffered Saline (pH 7.4).

    Purity

    Greater than 90% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      EFNA1 belongs to the ephrin (EPH) family. The EPH subfamily is the biggest group of receptor protein kinases and they take part in vital nervous system function and development.

    • Synonyms

      Ephrin A1, Immediate Early Response Protein B61, TNF Alpha-Induced Protein 4, Ephrin-A1, TNFAIP4, LERK-1, EPLG1, LERK1, Tumor Necrosis Factor, Alpha-Induced Protein 4, Eph-Related Receptor Tyrosine Kinase Ligand 1, EPH-Related Receptor Tyrosine Kinase Ligand 1, Tumor Necrosis Factor Alpha-Induced Protein 4, Ligand Of Eph-Related Kinase 1, ECKLG, EFL1, B61, EPH-related receptor tyrosine kinase ligand 1, LERK-1.

    • Physical Appearance

      Sterile Filtered colorless solution.

    • Stability

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

    • Amino Acid Sequence

      ADPDRHTVFW NSSNPKFRNE DYTIHVQLND YVDIICPHYE DHSVADAAME QYILYLVEHE EYQLCQPQSK DQVRWQCNRP SAKHGPEKLS EKFQRFTPFT LGKEFKEGHS YYYISKPIHQ HEDRCLRLKV TVSGKITHSP QAHVNPQEKR LAADDPEVRV LHSIGHSLEP KSCDKTHTCP PCPAPELLGG PSVFLFPPKP KDTLMISRTP EVTCVVVDVS HEDPEVKFNW YVDGVEVHNA KTKPREEQYN STYRVVSVLT VLHQDWLNGK EYKCKVSNKA LPAPIEKTIS KAKGQPREPQ VYTLPPSRDE LTKNQVSLTC LVKGFYPSDI AVEWESNGQP ENNYKTTPPV LDSDGSFFLY SKLTVDKSRW QQGNVFSCSV MHEALHNHYT QKSLSLSPGK HHHHHH

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

    Ephrin A1
  • View Data Sheet

    Name :

    OSM Human

    Description:

    Oncostatin-M Human Recombinant

    OSM, MGC20461.

    Product # :

    CYT-231

    Price :

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    Shipped at Room temp

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

    Description

    Oncostatin-M Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 227 amino acids and having a molecular mass of 26kDa. The OSM is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Lyophilized from a concentrated (1mg/ml) solution containing PBS pH-7.4.

    Purity

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

    Biological Activity

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

    Citations

    More Info

    • Introduction

      Oncostatin M is a member of a cytokine family that includes leukemia-inhibitory factor, granulocyte colony-stimulating factor, and interleukin 6. This gene encodes a growth regulator which inhibits the proliferation of a number of tumor cell lines. It regulates cytokine production, including IL-6, G-CSF and GM-CSF from endothelial cells.

    • Synonyms

      OSM, MGC20461.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Amino Acid Sequence

      AAIGSCSKEY RVLLGQLQKQ TDLMQDTSRL LDPYIRIQGL DVPKLREHCR
      ERPGAFPSEE TLRGLGRRGF LQTLNATLGC VLHRLADLEQ RLPKAQDLER
      SGLNIEDLEK LQMARPNILG LRNNIYCMAQ LLDNSDTAEP TKAGRGASQP
      PTPTPASDAF QRKLEGCRFL HGYHRFMHSV GRVFSKWGES PNRSRRHSPH
      QALRKGVRRT RPSRKGKRLM TRGQLPR.

    • Protein content

      Protein quantitation was carried out by two independent methods1. UV spectroscopy at 280 nm using the absorbency value of 0.45 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 standard solution of Oncostatin as Reference.

    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.

    Oncostatin M Human
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