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Search results

1000 results found for “Syndecan”

Name

Description

Product #

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  • View Data Sheet

    Name :

    CoV-2 S1, Sf9

    Description:

    Coronavirus 2019 Spike Glycoprotein-S1 Sf9, Recombinant

    Product # :

    SARS-019

    Price :

    Quantity :

    Shipping Method :

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    Shipped with Ice Packs

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    • More Info

    Description

    The Sf9 derived recombinant protein contains the Coronavirus 2019 CoV-2 Spike Glycoprotein S1, Wuhan-Hu-1 strain, amino acids 1-674 fused to His tag at C-terminal.

    Source

    Sf9, Baculovirus Cells.

    Formulation

    CoV-2 S1 protein solution is supplied in DPBS.

    Purity

    Protein is >85% pure as determined SDS-PAGE.

    More Info

    • Introduction

      A human infecting coronavirus (viral pneumonia) called 2019 novel coronavirus, 2019-nCoV was found in the fish market at the city of Wuhan, Hubei province of China on December 2019.

      The 2019-nCoV shares an 87% identity to the 2 bat-derived severe acute respiratory syndrome 2018 SARS-CoV-2 located in Zhoushan of eastern China. 2019-nCoV has an analogous receptor-BD-structure to that of 2018 SARS-CoV, even though there is a.a. diversity so thus the 2019-nCoV might bind to ACE2 receptor protein (angiotensin-converting enzyme 2) in humans.

      While bats are possibly the host of 2019-nCoV, researchers suspect that animal from the ocean sold at the seafood market was an intermediate host. RSCU analysis proposes that the 2019-nCoV is a recombinant within the viral spike glycoprotein between the bat coronavirus and an unknown coronavirus.

    • Physical Appearance

      Sterile Filtered clear solution.

    • Stability

      CoV-2 S1 Glycoprotein is shipped on ice packs. Upon arrival, Store at -20°C.

    • Purification Method

      Purified by Metal-Afinity chromatographic technique.

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

    product_image.jpg
  • View Data Sheet

    Name :

    TNF alpha human

    Description:

    Tumor Necrosis Factor-Alpha Human Recombinant

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

    Product # :

    CYT-223

    Price :

    Quantity :

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    Shipped at Room temp

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    Description

    Tumor Necrosis Factor-a Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 158 amino acids (157 a.a. of the mature human TNF-alpha and an N-terminal methionine) and having a molecular mass of 17.5kDa. The TNF-alpha is purified by standard chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    TNF-a Human was lyophilized from a concentrated 1mg/ml solution containing 20mM PB, pH-7.2, and 100mM NaCl.

    Purity

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

    Biological Activity

    The Specific Activity is >5.0×107 IU/mg as determined by the cytolysis of murine L929 cells in the presence of Actinomycin D.

    More Info

    • Introduction

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

    • Synonyms

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

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Solubility

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

    • Amino Acid Sequence

      MVRSSSRTPS DKPVAHVVAN PQAEGQLQWL NRRANALLAN GVELRDNQLV VPSEGLYLIY SQVLFKGQGC PSTHVLLTHT ISRIAVSYQT KVNLLSAIKS PCQRETPEGA E AKPWYEPIY LGGVFQLEKG DRLSAEINRP DYLDFAESGQ VYFGIIAL.

    • Background

      TNF Alpha Human: An Overview of Its Role and Importance in Immunology

      TNF alpha human, also known as Tumor Necrosis Factor-alpha, is a critical cytokine in the immune system. Macrophages mainly produce this protein, and it plays a key role in inflammation and the acute phase reaction.

      This protein is involved in various cellular functions, including cell death, differentiation, proliferation, and immune regulation.

      Production and Properties

      Tumor Necrosis Factor-alpha is produced recombinantly in E. coli and consists of a single, non-glycosylated polypeptide chain. It includes 157 amino acids of the mature human TNF-alpha and an N-terminal methionine, resulting in a molecular mass of approximately 17.5 kDa.

      Furthermore, the protein is purified through standard chromatographic techniques to ensure high purity and biological activity.

      Solubility and Usage

      The lyophilized form of TNF appears as a sterile, white powder. It is recommended to reconstitute this powder in sterile water to achieve a solution of no less than 100µg/ml.

      This solution can then be further diluted for various experimental applications. TNF alpha is used extensively in research, particularly for studying its effects on cell signaling and immune response.

      Storage and Stability

      For long-term storage, TNF should be kept desiccated below -18°C. Once reconstituted, it should be used within a week if stored at 4°C or kept below -18°C for future use. Avoiding freeze-thaw cycles is crucial to maintain the protein's functionality.

      Biological Role and Implications

      TNF alpha human is involved in the regulation of immune cells and is known for its role in inflammatory processes.

      Dysregulation of TNF alpha production is linked to various diseases, such as autoimmune disorders, insulin resistance, and cancer. It is also a target for therapeutic interventions, particularly in conditions like rheumatoid arthritis and inflammatory bowel disease.

      Mechanism of Action

      TNF alpha can induce fever, apoptotic cell death, and can inhibit tumorigenesis and viral replication. Moreover, it is a potent mediator of the acute phase reaction, which influences the activity of various cells involved in systemic inflammation.

      Research and Clinical Importance

      Scientific research on TNF has provided insights into its complex role in disease mechanisms. Its interaction with receptors such as TNFRSF1A underscores its multifaceted effects across different organ systems, from liver function to brain activity.

      Ongoing studies continue to explore its therapeutic potential, especially how it can be modulated to treat diseases without harmful side effects.

      In essence, TNF alpha human is a versatile and powerful component of the immune system, important for both health and disease. Understanding its pathways and functions helps scientists develop better treatments for various inflammatory and autoimmune 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.

    Tnf Alpha Human
  • View Data Sheet

    Name :

    FGF 2 Human (147 a.a.)

    Description:

    Fibroblast Growth Factor Basic 147 a.a. Human Recombinant

    Prostatropin, HBGH-2, HBGF-2, FGF-2, FGF-b.

    Product # :

    CYT-557

    Price :

    Quantity :

    Shipping Method :

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    Shipped at Room temp

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    • description
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    • More Info

    Description

    Fibroblast Growth Factor-2 Human Recombinant (FGF-2) produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 147 amino acids and having a molecular mass of 16.5kDa. The FGF2 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The bFGF was lyophilized from a sterile filtered solution containing 20mM Tris-HCl, pH 7.6 and 150mM NaCl.

    Purity

    Greater than 98.0% as determined by SDS-PAGE.

    Biological Activity

    The ED50, Calculated by the dose- dependent proliferation of mouse BALB/c 3T3 cells is < 0.05ng/ml corresponding to a specific activity of 2.0x107 units/mg.

    More Info

    • Introduction

      FGF-basic 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 heparin-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

      Prostatropin, HBGH-2, HBGF-2, FGF-2, FGF-b.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Amino Acid Sequence

      MPALPEDGGS GAFPPGHFKD PKRLYCKNGG FFLRIHPDGR VDGVREKSDP HIKLQLQAEE RGVVSIKGVC ANRYLAMKED GRLLASKCVT DECFFFERLE SNNYNTYRSR KYTSWYVALK RTGQYKLGSK TGPGQKAILF LPMSAKS.

    • Background

      What is the molecular weight/Mw of FGF 2 Protein?
      FGF 2 Protein has a total Mw of 16.5kDa.

      What is the source or expression system of FGF 2 Protein?
      Escherichia Coli.

      What is the Purity of FGF 2 Protein?
      FGF 2 Protein is >98% pure as determined by SDS-PAGE.

      What is the Biological Activity of FGF 2 Protein?
      The ED50, Calculated by the dose- dependent proliferation of mouse BALB/c 3T3 cells is < 0.05ng/ml corresponding to a specific activity of 2.0x107 units/mg.

      What is the amino acid sequence of FGF 2 Protein?
      MPALPEDGGS GAFPPGHFKD PKRLYCKNGG FFLRIHPDGR VDGVREKSDP HIKLQLQAEE RGVVSIKGVC ANRYLAMKED GRLLASKCVT DECFFFERLE SNNYNTYRSR KYTSWYVALK RTGQYKLGSK TGPGQKAILF LPMSAKS.

      What applications can FGF 2 Protein be used in?
      FGF 2 Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for FGF 2 Protein?
      The endotoxin level is minimal, FGF 2 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 2 147 Aa Human
  • View Data Sheet

    Name :

    SAA Paired Antibody

    Description:

    Anti Human Serum Amyloid A (APO-SAA) Paired Antibody Mouse

    Product # :

    ANT-785

    Price :

    Quantity :

    Shipping Method :

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    • description
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    Description

    SAA Paired monoclonal antibodies are used to develop rapid test for serum amyloid A protein rapid test. Please note that when ordering for example: 100µg paired antibody, you receive 50µg from each antibody (100µg in total).

    Formulation

    *SAA conjugation antibody in PBS, NaCl and 0.095% NaN3.

    * SAA coating antibody in PBS, NaCl and 0.095% NaN3.

    Purity

    Greater than 95%.

    More Info

    • Physical Appearance

      2 vials of sterile Filtered clear colorless solution.

    • Stability

      For periods up to 1month SAA Paired Antibody should be stored at 4°C, for longer periods of time, store at -20°C. Prevent freeze thaw cycles.

    • Applications

      Lateral flow immunoassay.

    • Background

      Serum amyloid A protein which is encoded by the SAA gene in humans, is a member of the SAA family. SAA is expressed by the liver and secreted in plasma. Serum amyloid A is the main acute phase reactant and apolipoprotein of the HDL complex. Elevated serum SAA protein levels may be linked with lung cancer. The level of Apo-SAA in plasma increases within 24 hours of an inflammatory stimulus and under these conditions is the most abundant HDL Apolipoprotein.

    • Type

      Mouse antibody Monoclonal.

    • Purification Method

      Purified monoclonal IgG1 by protein A chromatography.

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

    Saa Antibody
  • View Data Sheet

    Name :

    G CSF Human, PEG

    Description:

    Granulocyte-Colony Stimulating Factor Pegylated Human Recombinant

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

    Product # :

    CYT-018

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    Description

    Granulocyte Colony Stimulating Factor Human Recombinant produced in E.coli is a single, non-glycosylated, polypeptide chain containing 175 amino acids and having a molecular mass of 18.8kDa. The Pegylated G-CSF is produced by attaching a 20kDa methoxypolyethylene glycol propionaldehyde (mPEG-ALD) to the N-terminal amino acid of G-CSF giving a total molecular mass of 38.8kDa. G-CSF is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    G-CSF is supplied in solution (0.69mg/ml) containing 10mM Acetate Buffer (pH 4.0), and 0.004% Polysorbate 80.

    Purity

    Greater than 95.0% as determined by SEC-HPLC.

    Biological Activity

    The ED50, calculated by the dose-dependent proliferation of murine NFS-60 indicator cells is less than 0.1 ng/ml, corresponding to a Specific Activity of 10,000,000IU/mg.

    More Info

    • Introduction

      GCSF is a cytokine that controls the production, differentiation, and function of granulocytes. The active protein is found extracellularly. Three transcript variants encoding three different isoforms have been found for this gene. Granulocyte/macrophage colony-stimulating factors are cytokines that act in hematopoiesis by controlling the production, differentiation, and function of 2 related white cell populations of the blood, the granulocytes and the monocytes-macrophages. This csf induces granulocytes.

    • Synonyms

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

    • Physical Appearance

      Colorless, clear and transparent solution.

    • Stability

      G-CSF PEG should be stored refrigerated at 2° to 8°C. Vials should be kept in theirpackaging to protect from light until the time of use. Shaking and freezing should be avoided.

    • Background

      What is the molecular weight/Mw of G CSF HUMAN, PEG Protein?
      G CSF HUMAN, PEG Protein has a total Mw of 18.8kDa.

      What is the source or expression system of G CSF HUMAN, PEG Protein?
      Escherichia Coli.

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

      What is the Biological Activity of G CSF HUMAN, PEG Protein?
      The ED50, calculated by the dose-dependent proliferation of murine NFS-60 indicator cells is less than 0.1 ng/ml, corresponding to a Specific Activity of 10,000,000IU/mg.

      What is the amino acid sequence of G CSF HUMAN, PEG Protein?
      G CSF HUMAN, PEG Protein is composed from 175 amino acids.

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

      What is the endotoxin level for G CSF HUMAN, PEG Protein?
      The endotoxin level is minimal, G CSF HUMAN, PEG 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.

    G Csf Human Pegylated
  • View Data Sheet

    Name :

    PON1 Human, HEK

    Description:

    Paraoxonase-1 Human Recombinant, HEK

    Serum paraoxonase/arylesterase 1, Serum aryldialkylphosphatase 1, Aromatic esterase 1, A-esterase 1 , Serum aryldialkylphosphatase 1, paraoxonase 1, K-45, ESA, PON, MVCD5

    Product # :

    ENZ-1154

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    Description

    PON1 Human Recombinant produced in HEK cells is a single, glycosylated, polypeptide chain (16-355 a.a) containing a total of 346 amino acids, having a molecular mass of 39.0kDa. PON1 is fused to a 6 amino acid His-tag at C-terminus,and is purified by proprietary chromatographic techniques.

    Source

    HEK293 Cells.

    Formulation

    The PON1 solution (0.25mg/ml) contains 20% Glycerol and Phosphate-Buffered Saline (pH 7.4).

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    Biological Activity

    Specific activity is > 2,500 pmol/min/ug. Defined by the amount of enzyme that  hydrolyzes 1pmole of pnitrophenyl acetate to p-nitrophenol per minute at pH 7.5 at 37˚C.

    More Info

    • Introduction

      Paraoxonase-1 or PON1 is part of the paraoxonase group of proteins. PON1 is an enzyme, responsible to the toxic metabolites of a different of organophosphorus insecticides hydrolyzation. Furthermore, PON1 is a dominant anti-atherosclerotic part of HDL. The enzyme needs PPAR-gamma for activation, leading to synthesis and release of paraoxonase 1 from the liver tissue, resulting in atherosclerosis reduction. PON1 has many qualities for atheroprotective through inflammatory lipid peroxides metabolism. This enzyme can hydrolyze a large number of substrates, for example cyclic carbonates, lactones, nerve gases etc.

    • Synonyms

      Serum paraoxonase/arylesterase 1, Serum aryldialkylphosphatase 1, Aromatic esterase 1, A-esterase 1 , Serum aryldialkylphosphatase 1, paraoxonase 1, K-45, ESA, PON, MVCD5

    • 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

      LFRNHQSSYQ TRLNALREVQ PVELPNCNLV KGIETGSEDL EILPNGLAFI SSGLKYPGIK SFNPNSPGKI LLMDLNEEDP TVLELGITGS KFDVSSFNPH GISTFTDEDN AMYLLVVNHP DAKSTVELFK FQEEEKSLLH LKTIRHKLLP NLNDIVAVGP EHFYGTNDHY FLDPYLQSWE MYLGLAWSYV VYYSPSEVRV VAEGFDFANG INISPDGKYV YIAELLAHKI HVYEKHANWT LTPLKSLDFN TLVDNISVDP ETGDLWVGCH PNGMKIFFYD SENPPASEVL RIQNILTEEP KVTQVYAENG TVLQGSTVAS VYKGKLLIGT VFHKALYCEL HHHHHH

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    Pon1 Enzyme
  • View Data Sheet

    Name :

    HCV NS3 His

    Description:

    Hepatitis C Virus NS3 Recombinant, His Tag

    Product # :

    HCV-267

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    Description

    The E.coli derived recombinant protein contains a total of 268 amino acids having a Mw of 27.9 kDa. The protein contains the HCV NS3 immunodominant regions, amino acids 1225-1456. The HCV NS3 protein is fused to a 36 His Tag at N-terminus and purified by standard chromatography techniques.

    Formulation

    HCV NS3 in 20mM Tris-HCl pH-8, 1mM DTT & 10% Glycerol.

    Purity

    Protein is >95% pure as determined by SDS-PAGE.

    More Info

    • Introduction

      HCV is a small 50nm, enveloped, single-stranded, positive sense RNA virus in the family Flaviviridae. HCV has a high rate of replication with approximately one trillion particles produced each day in an infected individual. Due to lack of proofreading by the HCV RNA polymerase, the HCV has an exceptionally high mutation rate, a factor that may help it elude the host''s immune response. Hepatitis C virus is classified into six genotypes (1-6) with several subtypes within each genotype. The preponderance and distribution of HCV genotypes varies globally. Genotype is clinically important in determining potential response to interferon-based therapy and the required duration of such therapy. Genotypes 1 and 4 are less responsive to interferon-based treatment than are the other genotypes (2, 3, 5 and 6).

    • Stability

      HCV-NS3 His although stable at 4°C for 1 week, should be stored below -18°C. Please prevent freeze thaw cycles.

    • Amino Acid Sequence

      MRGSHHHHHH GMASMTGGQQ MGRDLYDDDD KDRWGSVAHL HAPTGSGKST KVPAAYAAQG YKVLVLNPSV AATLGFGAYM SKAHGVDPNI RTGVRTITTG SPITYSTYGK FLADGGCSGG AYDIIICDEC HSTDATSILG IGTVLDQAET AGARLVVLAT ATPPGSVTVS HPNIEEVALS TTGEIPFYGK AIPLEVIKGG RHLIFCHSKK KCDELAAKLV ALGINAVAYY RGLDVSVIPT SGDVVVVSTD ALMTGFTGDF DSVIDCNT.

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    Hcv Ns3 His
  • View Data Sheet

    Name :

    C8 Human

    Description:

    Complement C8 Human

    Product # :

    PRO-2695

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    Description

    Human Complement C8 produced in Human plasma is glycosylated polypeptide chain conteining 3 chains and having a total molecular mass of 151kDa.

    Source

    Human Plasma.

    Formulation

    C8 protein solution contains PBS pH 7.2.

    Purity

    Greater than 95% as determined by SDS-PAGE.

    More Info

    • Introduction

      Native human C8 is a glycosylated protein consist of 3 polypeptide chains: The alpha chain and the gamma chain are disulfide linkedwhereas, The beta chain is non-covalently bound to the a-g complex. C8 is necessary for formation of the membrane attack complex and is activated by binding on the cell membrane newly-formed C5b,C6,C7 complexes. Each pathway of complement activation generates proteolytic enzyme complexes which bind the target surface. These enzymes cleave a peptide bond in the larger alpha chain of C5 releasing C5a and activating C5b. Although C5b is unstable it remains bound to the activating complex for a few minutes during which it binds a single C6 from the surrounding fluid or it decays and is no longer capable of forming MAC.The C5b,6 complex may also remain connected to the C3/C5 convertase where the binding of a single C7 exposes a membrane-binding region and C5b,6,7 can enter into the bilipid layer of the target cell. Each C5b-7 complex can bind 1 molecule of C8 causing the complex to enter more firmly into the membrane.

    • Physical Appearance

      Sterile filtered solution.

    • Stability

      C8 Human is stable at 4°C if entire vial will be used within 2-4 weeks.Store, frozen below -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.

    • Human Virus Test

      Plasma from each donor has been tested and found negative for antibody to HIV-1, HIV-2, HCV and HBSAG.

    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.

    C8 Human
  • View Data Sheet

    Name :

    MMP 7 Human

    Description:

    Matrix Metalloproteinase-7 Human Recombinant

    Matrilysin, EC 3.4.24.23, Pump-1 protease, Uterine metalloproteinase, Matrix metalloproteinase-7, MMP-7, Matrin, MPSL1, PUMP-1, MMP7.

    Product # :

    ENZ-867

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    Description

    MMP-7 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 174 amino acids (95-267 a.a) and having a molecular mass of 19.2kDa.MMP7 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    MMP7 protein solution (1mg/ml) containing 20mM Tris 8.0 and 10% glycerol.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    More Info

    • Introduction

      Matrix metalloproteinase-7 (MMP-7) also known as matrilysin and PUMP (EC 3.4.24.23) cleaves a number of substrates including collagen types IV and X, elastin, fibronectin, gelatin, laminin and proteoglycans. MMP-7 is closely related to the stromelysin family members but is encoded by a different gene. MMP-7 is the smallest of all the MMPs consisting of a pro-peptide domain and a catalytic domain. It lacks the hemopexin-like domain common to other members of the MMPs. MMP-7 is secreted as a 28 kDa proenzyme and can be activated in vitro by organomercurials and trypsin and in vivo by MMP-3 to a 18 kDa active MMP-7 enzyme. Once activated, MMP-7 can activate pro-MMP-1 and pro-MMP-9 but not pro-MMP-2. MMP-7 is widely expressed having been reported in elevated levels in cycling endometrium as well as in colorectal cancers and adenomas, hepatocellular carcinomas, rectal carcinomas, and approximately 50% of gliomas.

    • Synonyms

      Matrilysin, EC 3.4.24.23, Pump-1 protease, Uterine metalloproteinase, Matrix metalloproteinase-7, MMP-7, Matrin, MPSL1, PUMP-1, MMP7.

    • 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

      MYSLFPNSPK WTSKVVTYRI VSYTRDLPHI TVDRLVSKAL NMWGKEIPLH FRKVVWGTAD IMIGFARGAH GDSYPFDGPG NTLAHAFAPG TGLGGDAHFD EDERWTDGSS LGINFLYAAT HELGHSLGMG HSSDPNAVMY PTYGNGDPQN FKLSQDDIKG IQKLYGKRSN SRKK.

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    Mmp 7 Human
  • View Data Sheet

    Name :

    Placental Lactogen Bovine

    Description:

    Placental Lactogen Bovine Recombinant

    Chorionic Somatomammotropin Hormone 1, CSH1, CSB, CS-1, hCS-B, BPL, BPLP-I.

    Product # :

    CYT-511

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    Description

    Placental Lactogen Bovine Recombinant, is a single polypeptide chain containing 199 amino acids and an additional Ala at the N-terminus having a molecular mass of 23 kDa. Placental Lactogen Recombinant is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The protein was lyophilized from a concentrated (1mg/ml) solution with 0.02-0.03% NaHCO3.

    Purity

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

    Biological Activity

    Placental Lactogen Bovine is biologically active as evidenced by inducing proliferation of Nb2 cells.

    More Info

    • Introduction

      Placental Lactogen is a polypeptide hormone that is produced by the Syncytiotrophoblasts of the Placenta, also known as chorionic somatomammotropin. It has both Growth Hormone and Prolactin activities on growth, lactation, and luteal steroid production. In women, placental lactogen secretion begins soon after implantation and increases to 1 g or more a day in late pregnancy. Placental lactogen is also an insulin antagonist.
      Placental Lactogen Bovine is also capable of activating human and other heterologous GH receptors but not ruminat GH receptors.

    • Synonyms

      Chorionic Somatomammotropin Hormone 1, CSH1, CSB, CS-1, hCS-B, BPL, BPLP-I.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized Placental Lactogen Bovine Recombinant although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Placental Lactogen 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 Placental Lactogen 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 six N-terminal amino acids was determined and was found to be Ala-Glu-Asp-Tyr-Ala-Pro.

    • Protein content

      UV spectroscopy at 280 nm using the absorbency value of 0.86 as the extinction coefficient for a 0.1% (1mg/ml) solution at pH 8. 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.

    Placental Lactogen Bovine
  • View Data Sheet

    Name :

    MIF Human His C

    Description:

    Macrophage Migration Inhibitory Factor Human Recombinant, His Tag C-Terminus

    Phenylpyruvate tautomerase, Glycosylation-inhibiting factor, GIF, MMIF, MIF.

    Product # :

    CYT-521

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    Description

    MIF human Recombinant, fused to His-tag at C-terminus, was cloned into an E. coli expression vector and was purified to apparent homogeneity by using conventional column chromatography techniques.Macrophage Inducing Factor Human Recombinant is a single, non-glycosylated, polypeptide chaincontaining 123 amino acidsand having a molecular mass of 13.5 kDa.

    Source

    Escherichia Coli.

    Formulation

    Human MIF was lyophilized from a 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

    Measured by its ability to bind rhCD74 in a functional ELISA.

    More Info

    • Introduction

      The cytokine Macrophage migration inhibitory factor (MIF) has been identified to be secreted by the pituitary gland and the monocyte/macrophage and to play an important role in endotoxic shock. MIF has the unique property of being released from macrophages and T cells in response to physiological concentrations of glucocorticoids. The secretion of MIF is tightly regulated and decreases at high, anti-inflammatory steroid concentration.

    • Synonyms

      Phenylpyruvate tautomerase, Glycosylation-inhibiting factor, GIF, MMIF, MIF.

    • Physical Appearance

      Sterile Filtered lyophilized powder.

    • Stability

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

    • Amino Acid Sequence

      MPMFIVNTNVPRASVPDGFLSELTQQLAQATGKPPQYIAVHVVPDQLMAFGGSSEPC
      ALCSLHSIGKIGGAQNRSYSKLLCGLLAERLRISPDRVYINYYDMNAANVGWNNSTF
      ALEHHHHHH.

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    Mif Human His C
  • View Data Sheet

    Name :

    S.Typhi OMP

    Description:

    Salmonella Typhi Outer Membrane Protein Recombinant

    Product # :

    STY-002

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    Description

    Recombinant Salmonella Typhi Outer Membrane Protein produced in E.coli contains 315 amino acids, and fused to a 6 His Tag at C-terminus, migrating as a 33kDa band on SDS-PAGE.S. typhi outer membrane protein is a central pathogen in S. typhi infection, and is directly exposed to the outside to interact with the human immune system.

    Source

    Escherichia Coli.

    Formulation

    Sterile Filtered solution containing 10mM Tris-HCl, 1mM EDTA and 50mM arginine.

    Purity

    Protein is >95% pure as determined by 12% PAGE (coomassie staining).

    More Info

    • Introduction

      Salmonella Typhi is a pathogen causing typhoid fever, affecting over 17 million people with approximately 600,000 deaths annually worldwide. If untreated, typhoid fever cases result in mortality rates ranging from 12-30%.

    • Physical Appearance

      Sterile Filtered solution.

    • Stability

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

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    Styphi Omp
  • View Data Sheet

    Name :

    TNF a Mouse

    Description:

    Tumor Necrosis Factor-Alpha Mouse Recombinant

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

    Product # :

    CYT-252

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    Description

    Tumor Necrosis Factor-a Mouse Recombinant produced in E. coli is a single, non glycosylated, polypeptide chain containing 157 amino acids and having a molecular mass of 17301.32 Dalton. The TNF-alpha is purified by standard chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Lyophilized from a 0.2µm filtered concentrated solution in PBS, pH 7.2.

    Purity

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

    Biological Activity

    The ED50 as determined by the cytolysis of murine L929 cells in the presence of Actinomycin D is < 0.1ng/ml, corresponding to a Specific Activity of 10,000,000 Units/mg.

    More Info

    • Introduction

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

    • Synonyms

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

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Solubility

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

    • Amino Acid Sequence

      MLRSSSQNSS DKPVAHVVAN HQVEEQLEWL SQRANALLAN GMDLKDNQLV VPADGLYLVY SQVLFKGQGC PDYVLLTHTV SRFAISYQEK VNLLSAVKSP CPKDTPEGAE LKPWYEPIYL GGVFQLEKGD QLSAEVNLPK YLDFAESGQV YFGVIAL

    • Background

      Tumor Necrosis Factor-alpha (TNF-α) is a pro-inflammatory cytokine that plays a critical role in the regulation of immune responses, inflammation, and cell survival. It is primarily produced by activated macrophages, but can also be secreted by other immune cells, such as T cells, natural killer cells, and mast cells. TNF-α is involved in a wide range of physiological and pathological processes, including the defense against infections, the development of autoimmune diseases, and the progression of cancer.

      TNF-α exerts its effects by binding to two distinct cell surface receptors, TNF receptor 1 (TNFR1) and TNF receptor 2 (TNFR2). Upon binding to its receptors, TNF-α activates multiple signaling pathways, including the nuclear factor-kappa B (NF-κB) pathway, the mitogen-activated protein kinase (MAPK) pathway, and the apoptotic pathway. These signaling pathways regulate various cellular processes, such as inflammation, cell proliferation, differentiation, and apoptosis.

      In the context of infections, TNF-α plays a crucial role in the body's defense against pathogens. It promotes the recruitment and activation of immune cells, enhances the production of other pro-inflammatory cytokines, and stimulates the expression of adhesion molecules on endothelial cells, facilitating the migration of immune cells to the site of infection. TNF-α also helps to induce fever, which is an important component of the body's immune response to infections.

      However, excessive or prolonged production of TNF-α can contribute to the development of chronic inflammatory diseases, such as rheumatoid arthritis, inflammatory bowel disease, and psoriasis. In these conditions, elevated levels of TNF-α promote the infiltration of immune cells into the affected tissues, leading to tissue damage and the perpetuation of inflammation. The central role of TNF-α in the pathogenesis of these diseases has led to the development of anti-TNF-α therapies, which have revolutionized the treatment of chronic inflammatory diseases. These therapies include monoclonal antibodies, such as infliximab and adalimumab, and soluble TNF receptor fusion proteins, such as etanercept. Anti-TNF-α therapies have been shown to be effective in reducing inflammation, improving symptoms, and slowing disease progression in patients with chronic inflammatory diseases.

      In the context of cancer, TNF-α has complex and context-dependent effects on tumor development and progression. On one hand, TNF-α can promote anti-tumor immunity by activating immune cells and stimulating the production of other pro-inflammatory cytokines. On the other hand, chronic inflammation driven by TNF-α can promote tumor growth, angiogenesis, and metastasis. Therefore, the role of TNF-α in cancer is still an area of active research, and the development of TNF-α-targeted therapies for cancer remains a challenge.

      In conclusion, TNF-α is a pro-inflammatory cytokine that plays a critical role in the regulation of immune responses, inflammation, and cell survival. Its involvement in various physiological and pathological processes has made it an important target for the development of therapies for chronic inflammatory diseases and cancer. Anti-TNF-α therapies have revolutionized the treatment of chronic inflammatory diseases, but the complex role of TNF-α in cancer remains an area of ongoing research. Understanding the precise mechanisms by which TNF-α contributes to disease pathogenesis will be crucial for the development of more effective and targeted therapies.

    • Protein content

      Protein quantitation was carried out by two independent methods1. UV spectroscopy at 280 nm using the absorbency value of 1.24 as the extinction coefficient for a 0.1% (1mg/ml) solution. This value is calculated by the PC GENE computer analysis program of protein sequences (IntelliGenetics). 2. Analysis by RP-HPLC, using a calibrated solution of TNF-a as a Reference Standard.

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    Tnf Alpha Mouse
  • View Data Sheet

    Name :

    Rantes Rhesus Macaque

    Description:

    Rantes Rhesus Macaque Recombinant (CCL5)

    C-C motif chemokine 5, Small-inducible cytokine A5, T-cell-specific protein RANTES, CCL5.

    Product # :

    CHM-033

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    Description

    Rantes Rhesus Macaque Recombinant produced in E.coli is a single, non-glycosylated, polypeptide chain containing 68 amino acids and having a molecular mass of 7.8kDa.The CCL5 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Rantes protein was lyophilized from a 0.2µm filtered concentrated solution in 20mM PB pH 6.0 and 500mM NaCl.

    Purity

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

    Biological Activity

    The biological activity determined by a chemotaxis bioassay using human peripheral blood monocytes is in a concentration range of 1.0-10 ng/ml.

    More Info

    • Introduction

      Regulated upon Activation, Normal T-cell Expressed, and Secreted or RANTES is an 8 kDa protein classified as a chemotactic cytokine or chemokine. It has recently been renamed CCL5. RANTES is chemotactic for T cells, eosinophils and basophils and plays an active role in recruiting leukocytes into inflammatory sites. With the help of particular cytokines (i.e. IL-2 and IFN-?) that are released by T cells, RANTES also induces the proliferation and activation of certain natural killer (NK) cells to form CHAK (CC-Chemokine-activated killer) cells. It is also a HIV-suppressive factor released from CD8+ T cells. This chemokine has been localized to chromosome 17 in humans.

    • Synonyms

      C-C motif chemokine 5, Small-inducible cytokine A5, T-cell-specific protein RANTES, CCL5.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized Rantes although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution CCL5 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 Rantes in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      SPHASDTTPC CFAYIARPLP RAHIKEYFYT SGKCSNPAVV FVTRKNRQVC ANPEKKWVRE YINSLEMS.

    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.

    Rantes Rhesus Macaque
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    Name :

    BD 1 Mouse

    Description:

    BD 1 Mouse

    Beta-defensin 1, BD-1, Defensin beta 1, hBD-1, HBD1, HBP1, DEFB1, HBD-1, HBP-1, DEFB101, DEFB-1, MGC51822.

    Product # :

    CYT-044

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    Description

    BD 1 Mouse Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 37 amino acids and having a molecular mass of 4.1 KDa.The BD 1 Mouse is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Lyophilized from a 0.2µm filtered concentrated solution in PBS, pH7.4.

    Purity

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

    Biological Activity

    Measured by its ability to chemoattract CD34+ dendritic cells using a concentration range of 0.1-1.0 ug/ml, corresponding to a specific activity of 1,000-10,000units/mg.

    More Info

    • Introduction

      The Defensin family are highly similar in their protein sequence and are microbicidal & cytotoxic peptides made by neutrophils. Beta Defensin-1 is an antimicrobial peptide having the resistance of epithelial surfaces to microbial colonization. Beta Defensin-1 has close proximity to Defensin Alpha-1 and has been implicated in the pathogenesis of cystic fibrosis.
      Skin of patients having atopic dermatitis patients and mycosis fungoides (non-lesional and lesional) show lower human Beta Defensin-1 mRNA expression and higher human Beta Defensin-2 and human Beta Defensin-3 mRNA expression.
      Beta Defensin is highly expressed by epithelial cells.
      Beta-defensin 1 may play a role in the pathogenesis of severe sepsis.

    • Synonyms

      Beta-defensin 1, BD-1, Defensin beta 1, hBD-1, HBD1, HBP1, DEFB1, HBD-1, HBP-1, DEFB101, DEFB-1, MGC51822.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Amino Acid Sequence

      DQYKCLQHGG FCLRSSCPSN TKLQGTCKPD KPNCCKS.

    • Background

      What is the molecular weight/Mw of BD1 Protein?
      BD1 Protein has a total Mw of 4.1kDa.

      What is the source or expression system of BD1 Protein?
      Escherichia Coli.

      What is the Purity of BD1 Protein?
      BD1 Protein is >97% pure as determined by SDS-PAGE.

      What is the Biological Activity of BD1 Protein?
      Measured by its ability to chemoattract CD34+ dendritic cells using a concentration range of 0.1-1.0 ug/ml, corresponding to a specific activity of 1,000-10,000units/mg.

      What is the amino acid sequence of BD1 Protein?
      DQYKCLQHGG FCLRSSCPSN TKLQGTCKPD KPNCCKS.

      What applications can BD1 Protein be used in?
      BD1 Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for BD1 Protein?
      The endotoxin level is minimal, BD1 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.

    Bd 1 Mouse
  • View Data Sheet

    Name :

    Bartonella 17kDa

    Description:

    Bartonella Henselae 17kDa Recombinant

    Product # :

    PRO-2568

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    Description

    Recombinant Bartonella Henselae 17kDa produced in E.Coli is a single, non-glycosylated polypeptide chain having a molecular mass of 18kDa. Bartonella 17kDa is expressed with a -10x His tag at N-terminus and purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Bartonella 17kDa is supplied at a 20mM HEPES buffer pH-8.0 and 6M Urea.

    Purity

    Greater than 95% as determined by SDS-PAGE.

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    • Introduction

      Numerous forms of Bartonellosis are caused by Bartonella henselae as well as Cat Scratch Disease & Bacillary Angiomatosis. It has been found that up to 95% of patients with Cat Scratch Disease show antibodies against Bartonella henselae antigens.

      P17 is the 1st antigen which was discovered to be strongly reactive with sera from Cat Scratch Disease patients. Bartonella henselae participates in host recognition by the type IV secretion system as a homolog of the virB5 family.

      Highly immunoreactive proteins which are produced by the Bartonella henselae are the most important antigens used for the diagnosis of Cat Scratch Disease.

    • Physical Appearance

      Sterile Filtered 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.

    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.

    Bartonella Henselae 17Kda
  • View Data Sheet

    Name :

    CTF1 Human

    Description:

    Cardiotrophin-1 Human Recombinant

    CTF1, CT1, CT-1, Cardiophin 1, Cardiotrophin-1.

    Product # :

    CYT-944

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    Description

    Cardiotrophin-1 Human Recombinant produced in E.coli is a single, non-glycosylated, polypeptide chain containing 201 amino acids and having a molecular mass of 21.2kDa.The CTF1 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    CTF-1 protein was lyophilized from a 0.2µm filtered concentrated solution in 30% Acetonitrile and 0.1% TFA.

    Purity

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

    Biological Activity

    The ED50 as determined by a cell proliferation assay using human TF-1 cells is less than 1.0 ng/ml, corresponding to a specific activity of > 1.0×106 IU/mg.

    More Info

    • Introduction

      Cardiotrophin 1 (CT-1) is a 201 amino acid member of the interleukin-6 superfamily. It was identified by its ability to induce hypertrophic response in cardiac myocytes. CT-1 mRNA levels were found both in cardiac myocytes and in cardiac nonmyocytes. CT 1 was also detected in abundance in normal adult human lung and was expressed in both fetal and adult airway smooth muscle cells. CT 1 activates gp130 dependent signaling and stimulates the Janus kinase/signal transducers and activators of transcription (JAK/STAT) pathway to transduce hypertrophic and cytoprotective signals in cardiac myocytes.
      CT 1 has also a neurotrophic function. CTF1 deficiency causes increased motoneuron cell death in spinal cord and brainstem nuclei of mice during a period between embryonic day 14 and the first postnatal week. Moreover, CT-1 is a hepatocyte survival factor that efficiently reduces hepatocellular damage in animal models of acute liver injury. Cardiotrophin 1 expression is augmented after hypoxic stimulation and it can protect cardiac cells when added either prior to simulated ischaemia or at the time of reoxygenation following simulated ischaemia. Cardiotrophin 1 can induce expression of the protective heat shock proteins (hsps) in cardiac cells.
      Cardiotrophin-1 increased ventricular expression of ANP, brain natriuretic peptide (BNP) and angiotensinogen mRNA.
      Cardiophin 1 levels were significantly elevated in patients with heart failure, patients with dilatative cardiomyopathy, moderate/severe mitral regurgitation, stable and unstable angina and after acute myocardial infarction.

    • Synonyms

      CTF1, CT1, CT-1, Cardiophin 1, Cardiotrophin-1.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized CTF1 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution CTF-1 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 CTF1 in sterile 4mM HCl not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      MSRREGSLED PQTDSSVSLL PHLEAKIRQT HSLAHLLTKY AEQLLQEYVQ LQGDPFGLPS FSPPRLPVAG LSAPAPSHAG LPVHERLRLD AAALAALPPL LDAVCRRQAE LNPRAPRLLR RLEDAARQAR ALGAAVEALL AALGAANRGP RAEPPAATAS AASATGVFPA KVLGLRVCGL YREWLSRTEG DLGQLLPGGS A.

    • Background

      Title: Cardiotrophin-1 Human Recombinant: A Potential Therapeutic Target for Cardiovascular Diseases

      Abstract:


      Cardiotrophin-1 (CT-1) is a cytokine that plays a crucial role in cardiac development and homeostasis. This research paper provides a comprehensive analysis of human recombinant CT-1, focusing on its production, characterization, and potential therapeutic implications in cardiovascular diseases. The paper discusses the significance of CT-1 in cardiac cell survival, hypertrophy, and regeneration. Furthermore, it elucidates the ongoing research and clinical trials exploring the therapeutic potential of recombinant CT-1 in cardiovascular disorders. The information presented in this paper aims to enhance the understanding of human recombinant CT-1 and its utility as a research tool and a potential therapeutic agent for cardiovascular diseases.

      Introduction:


      Cardiotrophin-1 (CT-1) is a member of the interleukin-6 cytokine family, primarily produced by cardiac cells. It exerts its effects by binding to the CT-1 receptor complex, leading to the activation of various signaling pathways. Human recombinant CT-1, produced through genetic engineering techniques, provides researchers with a valuable tool to explore its biological functions and therapeutic potential.

      Production and Characterization:


      Recombinant CT-1 is typically produced using expression systems such as mammalian cells or bacteria. The protein is then purified and characterized to ensure its structural integrity and functional activity. Quality control measures are implemented to confirm the specificity and bioactivity of the recombinant CT-1.

      Role in Cardiovascular Physiology:


      CT-1 plays a critical role in cardiac cell survival, hypertrophy, and regeneration. It promotes cardiomyocyte growth and survival, contributing to the adaptation of the heart to stress and injury. CT-1 also exhibits angiogenic properties, stimulating the formation of new blood vessels in the heart. These functions make recombinant CT-1 an important tool for studying cardiac physiology and exploring potential therapeutic interventions.

      Therapeutic Implications:


      The dysregulation of CT-1 signaling has been implicated in various cardiovascular diseases, including heart failure, myocardial infarction, and cardiac hypertrophy. Recombinant CT-1 holds promise as a potential therapeutic agent for these conditions. Clinical trials are underway to evaluate the safety and efficacy of CT-1-based therapies, including recombinant CT-1 administration and gene therapy approaches.

      Conclusion:


      Human recombinant CT-1 is a valuable research tool and a potential therapeutic target for cardiovascular diseases. Its production, characterization, and applications in cardiac cell signaling contribute to our understanding of cardiovascular physiology and the development of novel treatments. Continued research and clinical trials exploring the therapeutic potential of recombinant CT-1 hold promise for improving outcomes in patients with cardiovascular disorders.

      What is the molecular weight/Mw of CTF1 Protein?
      CTF1 Protein has a total Mw of 21.2kDa.

      What is the source or expression system of CTF1 Protein?
      Escherichia Coli.

      What is the Purity of CTF1 Protein?
      CTF1 Protein is >95% pure as determined by SDS-PAGE.

      What is the Biological Activity of CTF1 Protein?
      The ED50 as determined by a cell proliferation assay using human TF-1 cells is less than 1.0 ng/ml, corresponding to a specific activity of > 1.0×106 IU/mg.

      What is the amino acid sequence of CTF1 Protein?
      MSRREGSLED PQTDSSVSLL PHLEAKIRQT HSLAHLLTKY AEQLLQEYVQ LQGDPFGLPS FSPPRLPVAG LSAPAPSHAG LPVHERLRLD AAALAALPPL LDAVCRRQAE LNPRAPRLLR RLEDAARQAR ALGAAVEALL AALGAANRGP RAEPPAATAS AASATGVFPA KVLGLRVCGL YREWLSRTEG DLGQLLPGGS A.

      What applications can CTF1 Protein be used in?
      CTF1 Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for CTF1 Protein?
      The endotoxin level is minimal, CTF1 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.

    Ctf1 Human
  • View Data Sheet

    Name :

    CSNK2A1 Human, His

    Description:

    Casein Kinase 2 alpha 1 Human Recombinant, His

    Casein kinase II subunit alpha, EC 2.7.11.1, CK II, CK2A1, CKII alpha, CSNK2A1, PKCK2, CSK21.

    Product # :

    PKA-225

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    Description

    CK2A Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain encoding the sequence of 411 amino acids and having a molecular mass of 47.3 kDa.Casein Kinase 2 alpha subunit is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    CSNK2A1 is supplied in 20mM Tris pH-8.0 , 500mM NaCl, 1mM DTT and 50% glycerol.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    More Info

    • Introduction

      The Casein kinase 2 (EC2.7.11.1) is a serine/threonine-selective protein kinasethat is a tetramer of two alpha subunits and two beta subunits. The alpha subunits have the catalytic kinase domain. Casein kinase 2 has been implicated in cell cyclecontrol, DNA repair, regulation of the circadian rhythmand other cellular processes.
      Casein kinase 2 activity has been reported to be activated following Wnt signaling pathwayactivation. A Pertussis toxin-sensitive G proteinand Disheveled appear to be an intermediary between Wnt-mediated activation of the Frizzled receptor and activation of casein kinase 2.
      Mice that lack casein kinase 2 alpha prime have a defect in the morphology of developing sperm.

    • Synonyms

      Casein kinase II subunit alpha, EC 2.7.11.1, CK II, CK2A1, CKII alpha, CSNK2A1, PKCK2, CSK21.

    • 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.

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MSGPVPSRAR VYTDVNTHRP REYWDYESHV VEWGNQDDYQLVRKLGRGKY SEVFEAINIT NNEKVVVKIL KPVKKKKIKR EIKILENLRG GPNIITLADI VKDPVSRTPA LVFEHVNNTD FKQLYQTLTD YDIRFYMYEI LKALDYCHSM GIMHRDVKPH NVMIDHEHRK LRLIDWGLAE FYHPGQEYNV RVASRYFKGP ELLVDYQMYD YSLDMWSLGC MLASMIFRKE PFFHGHDNYD QLVRIAKVLG TEDLYDYIDK YNIELDPRFN DILGRHSRKRWERFVHSENQ HLVSPEALDF LDKLLRYDHQ SRLTAREAME HPYFYTVVKD QARMGSSSMP GGSTPVSSAN MMSGISSVPT PSPLGPLAGS PVIAAANPLG MPVPAAAGAQ Q.

    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.

    Csnk2A1 Human His
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    Name :

    MYL5 (1-173 a.a.) Human

    Description:

    Myosin Light Chain 5 (1-173 a.a.) Human Recombinant

    Myosin light chain 5, Myosin regulatory light chain 5, Superfast myosin regulatory light chain 2, MYLC2, MyLC-2, MYL5.

    Product # :

    PRO-943

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    Description

    MYL5 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 197 amino acids (1-173 a.a.) and having a molecular mass of 22.1kDa.MYL5 is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    MYL5 protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH8.0), 20% glycerol, 0.1M NaCl,1mM DTT and 0.1mM PMSF.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

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    • Introduction

      Myosin regulatory light chain 5 (MYL5) is a hexameric ATPase cellular motor protein. Myosin is comprised of 2 heavy chains, 2 nonphosphorylatable alkali light chains, and 2 phosphorylatable regulatory light chains. MYL5 is a regulatory light chain and is expressed in the fetal muscle and in the adult retina, cerebellum, and basal ganglia. The reconstitution of myosin with MYL5 or alkali light chain increases filament velocity to intermediate rates, and the re-addition of both classes of light chains fully reinstates the original sliding pace.

    • Synonyms

      Myosin light chain 5, Myosin regulatory light chain 5, Superfast myosin regulatory light chain 2, MYLC2, MyLC-2, MYL5.

    • 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 MGSHMASRKT KKKEGGALRA QRASSNVFSN FEQTQIQEFK EAFTLMDQNR DGFIDKEDLK DTYASLGKTN VKDDELDAML KEASGPINFT MFLNLFGEKL SGTDAEETIL NAFKMLDPDG KGKINKEYIK RLLMSQADKM TAEEVDQMFQ FASIDVAGNL
      DYKALSYVIT HGEEKEE.

    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.

    Myl5 1 173 Aa Human
  • View Data Sheet

    Name :

    ARMC10 Human

    Description:

    Armadillo Repeat Containing 10 Human Recombinant

    Armadillo repeat-containing protein 10, Splicing variant involved in hepatocarcinogenesis protein, ARMC10, SVH.

    Product # :

    PRO-1453

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    Description

    ARMC10 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 304 amino acids (28-308 a.a) and having a molecular mass of 33.6 kDa.ARMC10 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    ARMC10 protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 10% glycerol and 1mM DTT.

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      AMRC10 is a protein which contains an armadillo repeat and transmembrane domain. Upregulation of the AMRC10 gene has a role in hepatocellular carcinoma. AMRC10 decreases the transcriptional activity of the tumor suppressor protein p53 through direct interaction with the DNA-binding domain of p53, moreover it might play a role in cell growth and survival.

    • Synonyms

      Armadillo repeat-containing protein 10, Splicing variant involved in hepatocarcinogenesis protein, ARMC10, SVH.

    • 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 MGSTRGRRRG DRELGIRSSK SAEDLTDGSY DDVLNAEQLQ KLLYLLESTE DPVIIERALI TLGNNAAFSV NQAIIRELGG IPIVANKINH SNQSIKEKAL NALNNLSVNV ENQIKIKIYI SQVCEDVFSG PLNSAVQLAG LTLLTNMTVT NDHQHMLHSY ITDLFQVLLT GNGNTKVQVL KLLLNLSENP AMTEGLLRAQ VDSSFLSLYD SHVAKEILLR VLTLFQNIKN CLKIEGHLAV QPTFTEGSLF FLLHGEECAQ KIRALVDHHD AEVKEKVVTI IPKI.

    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.

    Armc10 Human
  • View Data Sheet

    Name :

    ASS1 Human

    Description:

    Argininosuccinate Synthase 1 Human Recombinant

    ASS, CTLN1, EC 6.3.4.5, ASS1, Argininosuccinate Synthase 1.

    Product # :

    ENZ-548

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    Description

    ASS1 Recombinant Human produced in E.Coli is a single, non-glycosylated polypeptide chain containing 432 amino acids (1-412 a.a.) and having a molecular mass of 48.6 kDa. The ASS1 is fused to a 20 amino acids His-Tag at N-terminus and purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    ASS1 Human 0.5mg/ml solution containing 20mM Tris-HCl pH-8, 0.1M NaCl, 1mM DTT & 20% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      ASS1 is involved in the urea cycle, which is a sequence of chemical reactions that is localized in liver cells. The urea cycle processes excess nitrogen that is generated as the body uses proteins. The surplus nitrogen is used to create a molecule called urea, which is excreted from the body in urine.

    • Synonyms

      ASS, CTLN1, EC 6.3.4.5, ASS1, Argininosuccinate Synthase 1.

    • Physical Appearance

      Sterile filtered colorless solution.

    • Stability

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

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MSSKGSVVLA YSGGLDTSCI LVWLKEQGYD VIAYLANIGQ KEDFEEARKK ALKLGAKKVF IEDVSREFVE EFIWPAIQSS ALYEDRYLLG TSLARPCIAR KQVEIAQREG AKYVSHGATG KGNDQVRFEL SCYSLAPQIK VIAPWRMPEF YNRFKGRNDL MEYAKQHGIP IPVTPKNPWS MDENLMHISY EAGILENPKN QAPPGLYTKT QDPAKAPNTP DILEIEFKKG VPVKVTNVKD GTTHQTSLEL FMYLNEVAGK HGVGRIDIVE NRFIGMKSRG IYETPAGTIL YHAHLDIEAF TMDREVRKIK QGLGLKFAEL VYTGFWHSPE CEFVRHCIAK SQERVEGKVQ VSVLKGQVYI LGRESPLSLY NEELVSMNVQ GDYEPTDATG FININSLRLK EYHRLQSKVT AK.

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    Ass1 Human
  • 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.

    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 :

    CD99 Human

    Description:

    CD99 Human Recombinant

    CD99 antigen, T-cell surface glycoprotein E2, E2 antigen, Protein MIC2, 12E7, CD99, MIC2, MIC2X, MIC2Y.

    Product # :

    PRO-2444

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    • description
    • source
    • formulation
    • purity
    • More Info

    Description

    CD99 Human Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 342 amino acids (23-122a.a.) and having a molecular mass of 37.3kDa (Molecular size on SDS-PAGE will appear at approximately 40-57kDa).CD99 is expressed with a 239 amino acids hIgG-His tag at C-Terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    CD99 protein solution (1mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 10% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      CD99, or MIC2 gene product, or E2 antigen is expressed on the cell membrane of some lymphocytes, cortical thymocytes, and granulosa cells of the ovary. The antigen is also expressed by most pancreatic islet cells, Sertoli cells of the testis, and some endothelial cells. Mature granulocytes express very little or no CD99. MIC2 is strongly expressed on Ewing’s sarcoma cells and primitive peripheral neuroectodermal tumors.

    • Synonyms

      CD99 antigen, T-cell surface glycoprotein E2, E2 antigen, Protein MIC2, 12E7, CD99, MIC2, MIC2X, MIC2Y.

    • 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

      ADPDGGFDLS DALPDNENKK PTAIPKKPSA GDDFDLGDAV VDGENDDPRP PNPPKPMPNP NPNHPSSSGS FSDADLADGV SGGEGKGGSD GGGSHRKEGE EADLEPKSCD KTHTCPPCPA PELLGGPSVF LFPPKPKDTL MISRTPEVTC VVVDVSHEDP EVKFNWYVDG VEVHNAKTKP REEQYNSTYR VVSVLTVLHQ DWLNGKEYKC KVSNKALPAP IEKTISKAKG QPREPQVYTL PPSRDELTKN QVSLTCLVKG FYPSDIAVEW ESNGQPENNY KTTPPVLDSD GSFFLYSKLT VDKSRWQQGN VFSCSVMHEA LHNHYTQKSL SLSPGKHHHH 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.

    Cd99 Protein
  • View Data Sheet

    Name :

    CDH11 Human

    Description:

    Cadherin 11 Human Recombinant

    CAD11, CDHOB, OB, OSF-4, Cadherin 11, Osteoblast cadherin, OB-cadherin.

    Product # :

    PRO-1368

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    Description

    CDH11 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 601 amino acids (54-617 a.a) and having a molecular mass of 66.2kDa. CDH11 is fused to a 37 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    CDH11 protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH8.0), 10% glycerol and 0.1M NaCl.

    Purity

    Greater than 85% as determined by SDS-PAGE.

    More Info

    • Introduction

      Cadherin 11 (CDH11) belongs to the cadherin superfamily (integral membrane proteins) which mediate calcium-dependent cell-cell adhesion. CDH11 is defined based on lacking a HAV cell adhesion recognition sequence specific to type I cadherins. CDH11 protein’s expression in osteoblastic cell lines, and its upregulation during differentiation, suggests a specific function in bone development and maintenance. CDH11 contributes to the sorting of heterogeneous cell types.

    • Synonyms

      CAD11, CDHOB, OB, OSF-4, Cadherin 11, Osteoblast cadherin, OB-cadherin.

    • 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

      MRGSHHHHHH GMASMTGGQQ MGRDLYDDDD KDRWGSMGWV WNQFFVIEEY TGPDPVLVGR LHSDIDSGDG NIKYILSGEG AGTIFVIDDK SGNIHATKTL DREERAQYTL MAQAVDRDTN RPLEPPSEFI VKVQDINDNP PEFLHETYHA NVPERSNVGT SVIQVTASDA DDPTYGNSAK LVYSILEGQP YFSVEAQTGI IRTALPNMDR EAKEEYHVVI QAKDMGGHMG GLSGTTKVMI TLTDVNDNPP KFPQSVYQMS VSEAAVPGEE VGRVKAKDPD IGENGLVTYN IVDGDGMESF EITTDYETQE GVIKLKKPVD FETKRAYSLK VEAANVHIDP KFISNGPFKD TVTVKIAVED ADEPPMFLAP SYIHEVQENA AAGTVVGRVH AKDPDAANSP IRYSIDRHTD LDRFFTINPE DGFIKTTKPL DREETAWLNI TVFAAEIHNR HQEAKVPVAI RVLDVNDNAP KFAAPYEGFI CESDQTKPLS NQPIVTISAD DKDDTANGPR FIFSLPPEII HNPNFTVRDN RDNTAGVYAR RGGFSRQKQD LYLLPIVISD GGIPPMSSTN TLTIKVCGCD VNGALLSCNA EAYILNAGLS T.

    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.

    Cdh11 Human
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