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Search results

1000 results found for “HDGF”

Name

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  • View Data Sheet

    Name :

    HSV-1 gD (84-175)

    Description:

    Herpes Simplex Virus-1 gD (84-175 a.a.) Recombinant

    Product # :

    HSV-231

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    Description

    The E.Coli derived recombinant protein contains the HSV-1 gD (84-175) immunodominant region.

    Source

    Escherichia Coli.

    Formulation

    0.1 % SDS, 50% glycerol and 100 mM NaCl.

    Purity

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

    More Info

    • Introduction

      Receptors across the cell membrane interact with some viral glycoproteins therefor enabling HSV to enter the host cell. The HSV enter through pores created by the binding of particular receptors across the cell membrane with the virus's coating envelope, following by a fusion of the HSV and the host cell. HSV enters the host cell through the same mechanism and stages as other viruses do. Initially, matching receptors across the virus's envelope and host cell's membrane interacts and bring the two together. During the transitional stage, begins fusion between the host cell and virus (hemifusion state). The closing stage happens when a steady pore was made; through these pores the virus's particles enter the cell.

    • Physical Appearance

      Sterile Filtered clear solution.

    • Stability

      HSV-1 gD although stable at 4°C for 1 week, should be stored below -18°C. Please prevent 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.

    Hsv1 Gd
  • View Data Sheet

    Name :

    BMP3 Human

    Description:

    Bone Morphogenetic protein-3 Human Recombinant

    Bone Morphogenetic Protein 3, Osteogenin, Bone Morphogenetic Protein 3 (Osteogenic), Bone Morphogenetic Protein 3A, BMP-3A, BMP-3, Bone Morphogenetic Protein-3, BMP3A, BMP3.

    Product # :

    CYT-937

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    Shipped at Room temp

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    • biological activity
    • More Info

    Description

    BMP3 Human Recombinant produced in E.coli is a non-glycosylated disulfide linked homodimer containing 2 chains of 110 amino acids and having a molecular mass of 24.8kDa.The BMP-3 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    BMP-3 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 HPLC. (b) Analysis by SDS-PAGE.

    Biological Activity

    The ED50 as determined by its ability to inhibit BMP-2-induced activity in murine MC3T3- E1 cells.

    More Info

    • Introduction

      Bone Morphogenetic Protein 3 (BMP3) is one of the BMPs, some of which are members of the TGF-beta superfamily (BMP2-7). There are more than 13 BMPs, which are involved in inducing cartilage and bone formation, embryogenesis and morphogenesis of various tissues and organs. In addition, BMPs regulate the growth, differentiation, chemotaxis, and apoptosis of various cell types. Akin to most other TGF-beta family proteins, BMPs are extremely conserved across animal species. At the amino acid sequence level, mature human and rat BMP3 are 98% identical.

    • Synonyms

      Bone Morphogenetic Protein 3, Osteogenin, Bone Morphogenetic Protein 3 (Osteogenic), Bone Morphogenetic Protein 3A, BMP-3A, BMP-3, Bone Morphogenetic Protein-3, BMP3A, BMP3.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized BMP3 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution BMP-3 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 BMP3 in sterile 4mM HCl not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      QWIEPRNCAR RYLKVDFADI GWSEWIISPK SFDAYYCSGA CQFPMPKSLK PSNHATIQSI VRAVGVVPGI PEPCCVPEKM SSLSILFFDE NKNVVLKVYP NMTVESCACR.

    • Background

      Bone Morphogenetic Protein-3 Human Recombinant: Unveiling the Potential of a Key Regulator in Tissue Regeneration

      Abstract:

      Bone Morphogenetic Protein-3 (BMP-3) human recombinant is a critical member of the bone morphogenetic protein family, known for its role in tissue development, repair, and regeneration. This research paper provides a comprehensive analysis of BMP-3, including its characteristics, signaling pathways, and potential therapeutic applications. Additionally, innovative methodologies for the production and optimization of BMP-3 human recombinant are proposed, shedding light on its future implications in the field of regenerative medicine.

      Introduction:

      Tissue regeneration is a complex biological process requiring precise molecular cues. BMP-3, a crucial member of the BMP family, plays a significant role in tissue development and regeneration. This paper explores the unique features of BMP-3 and presents novel approaches for its production and optimization, aiming to unlock its therapeutic potential in various regenerative contexts.

      Characteristics and Signaling Pathways:

      BMP-3 is a secreted protein that binds to cell surface receptors, initiating intracellular signaling cascades. It influences cell differentiation, proliferation, and extracellular matrix synthesis through both Smad-dependent and Smad-independent signaling pathways. BMP-3 signaling regulates critical processes involved in tissue regeneration, including chondrogenesis and osteogenesis.

      Production of BMP-3 Human Recombinant:

      Efficient production methodologies are essential for harnessing the therapeutic potential of BMP-3 human recombinant. Recombinant protein expression systems, such as Escherichia coli or mammalian cells, have been utilized to produce functional BMP-3. Optimization strategies, including codon optimization, signal peptide engineering, and protein folding optimization, have been employed to enhance the yield and activity of BMP-3 recombinant protein.

      Potential Therapeutic Applications:

      BMP-3 human recombinant holds significant promise in the field of regenerative medicine. It plays a crucial role in bone and cartilage regeneration, making it a potential candidate for the treatment of skeletal disorders and tissue injuries. Additionally, BMP-3 signaling influences tissue remodeling and wound healing, suggesting its broader therapeutic applications in other regenerative processes.

      Conclusion:

      BMP-3 human recombinant represents a key regulator in tissue regeneration, with immense potential in regenerative medicine. Optimizing production methodologies and further unraveling its signaling mechanisms will enhance its therapeutic applications. With its implications in bone and cartilage regeneration and its role in tissue remodeling, BMP-3 human recombinant emerges as a promising tool for promoting tissue repair and regeneration.

      What is the molecular weight/Mw of BMP3 Protein?
      BMP3 Protein has a total Mw of 24.8kDa.

      What is the source or expression system of BMP3 Protein?
      Escherichia Coli.

      What is the Purity of BMP3 Protein?
      BMP3 Protein is >95% pure as determined by SDS-PAGE.

      What is the Biological Activity of BMP3 Protein?
      The ED50 as determined by its ability to inhibit BMP-2-induced activity in murine MC3T3- E1 cells.

      What is the amino acid sequence of BMP3 Protein?
      QWIEPRNCAR RYLKVDFADI GWSEWIISPK SFDAYYCSGA CQFPMPKSLK PSNHATIQSI VRAVGVVPGI PEPCCVPEKM SSLSILFFDE NKNVVLKVYP NMTVESCACR.

      What applications can BMP3 Protein be used in?
      BMP3 Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for BMP3 Protein?
      The endotoxin level is minimal, BMP3 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.

    Bmp3 Human
  • View Data Sheet

    Name :

    GFRA1 Rat

    Description:

    GDNF Family Receptor Alpha 1 Rat Recombinant

    GDNF family receptor alpha-1, GDNF receptor alpha-1, GDNFR-alpha-1, GFR-alpha-1, RET ligand 1, TGF-beta-related neurotrophic factor receptor 1, Gfra1, Gdnfra, Retl1, Trnr1.

    Product # :

    CYT-1012

    Price :

    Quantity :

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    Description

    GFRA1 Rat Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 645 amino acids (25-430a.a.) and having a molecular mass of 72.3kDa (Molecular size on SDS-PAGE will appear at approximately 70-100kDa). GFRA1 is expressed with a 239 amino acid hIgG-His tag at C-Terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    GFRA1 protein solution (0.25mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 10% glycerol.

    Purity

    Greater than 85% as determined by SDS-PAGE.

    More Info

    • Introduction

      GDNF family receptor alpha-1 (GFRA1) belongs to the GDNF receptor family. GFRA1 is a glycosyl-phosphatidylinositol(GPI)-linked cell surface receptor for both Glial cell line-derived growth factor (GDNF), neurturin (NTN), and mediates activation of the RET tyrosine kinase receptor. The GFRA1 protein is a potent survival factor for central and peripheral neurons, and is vital for the development of kidneys and the enteric nervous system.

    • Synonyms

      GDNF family receptor alpha-1, GDNF receptor alpha-1, GDNFR-alpha-1, GFR-alpha-1, RET ligand 1, TGF-beta-related neurotrophic factor receptor 1, Gfra1, Gdnfra, Retl1, Trnr1.

    • 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

      DRLDCVKASD QCLKEQSCST KYRTLRQCVA GKETNFSLTS GLEAKDECRS AMEALKQKSL YNCRCKRGMK KEKNCLRIYW SMYQSLQGND LLEDSPYEPV NSRLSDIFRA VPFISDVFQQ VEHISKGNNC LDAAKACNLD DTCKKYRSAY ITPCTTSMSN EVCNRRKCHK ALRQFFDKVP AKHSYGMLFC SCRDIACTER RRQTIVPVCS YEERERPNCL SLQDSCKTNY ICRSRLADFF TNCQPESRSV SNCLKENYAD CLLAYSGLIG TVMTPNYVDS SSLSVAPWCD CSNSGNDLED CLKFLNFFKD NTCLKNAIQA FGNGSDVTMW QPAPPVQTTT ATTTTAFRVK NKPLGPAGSE NEIPTHVLPP CANLQAQKLK SNVSGSTHLC LSDSDFGKDG LAGASSLEPK SCDKTHTCPP CPAPELLGGP SVFLFPPKPK DTLMISRTPE VTCVVVDVSH EDPEVKFNWY VDGVEVHNAK TKPREEQYNS TYRVVSVLTV LHQDWLNGKE YKCKVSNKAL PAPIEKTISK AKGQPREPQV YTLPPSRDEL TKNQVSLTCL VKGFYPSDIA VEWESNGQPE NNYKTTPPVL DSDGSFFLYS KLTVDKSRWQ QGNVFSCSVM HEALHNHYTQ KSLSLSPGKH HHHHH.

    • Background

      What is the molecular weight/Mw of GFRA1 RAT Protein?
      GFRA1 RAT Protein has a total Mw of 72.3kDa.

      What is the source or expression system of GFRA1 RAT Protein?
      Sf9, Baculovirus cells.

      What is the Purity of GFRA1 RAT Protein?
      GFRA1 RAT Protein is >85% pure as determined by SDS-PAGE.

      What is the Biological Activity of GFRA1 RAT Protein?
      The biological functionality of GFRA1 RAT Protein will be determined in the future.

      What is the amino acid sequence of GFRA1 RAT Protein?
      DRLDCVKASD QCLKEQSCST KYRTLRQCVA GKETNFSLTS GLEAKDECRS AMEALKQKSL YNCRCKRGMK KEKNCLRIYW SMYQSLQGND LLEDSPYEPV NSRLSDIFRA VPFISDVFQQ VEHISKGNNC LDAAKACNLD DTCKKYRSAY ITPCTTSMSN EVCNRRKCHK ALRQFFDKVP AKHSYGMLFC SCRDIACTER RRQTIVPVCS YEERERPNCL SLQDSCKTNY ICRSRLADFF TNCQPESRSV SNCLKENYAD CLLAYSGLIG TVMTPNYVDS SSLSVAPWCD CSNSGNDLED CLKFLNFFKD NTCLKNAIQA FGNGSDVTMW QPAPPVQTTT ATTTTAFRVK NKPLGPAGSE NEIPTHVLPP CANLQAQKLK SNVSGSTHLC LSDSDFGKDG LAGASSLEPK SCDKTHTCPP CPAPELLGGP SVFLFPPKPK DTLMISRTPE VTCVVVDVSH EDPEVKFNWY VDGVEVHNAK TKPREEQYNS TYRVVSVLTV LHQDWLNGKE YKCKVSNKAL PAPIEKTISK AKGQPREPQV YTLPPSRDEL TKNQVSLTCL VKGFYPSDIA VEWESNGQPE NNYKTTPPVL DSDGSFFLYS KLTVDKSRWQ QGNVFSCSVM HEALHNHYTQ KSLSLSPGKH HHHHH.

      What applications can GFRA1 RAT Protein be used in?
      GFRA1 RAT Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for GFRA1 RAT Protein?
      The endotoxin level is minimal, GFRA1 RAT 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.

    Gfra1 Rat
  • View Data Sheet

    Name :

    HCV NS4, HRP

    Description:

    Hepatitis C Virus NS4 Horseradish Peroxidase Recombinant

    Product # :

    HCV-220

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    Description

    The E.coli derived recombinant Horseradish Peroxidase Labeled protein contains the HCV NS4 immunodominant regions.

    Source

    Escherichia Coli.

    Formulation

    25mM Tris-HCl pH 8, 1mM EDTA, 1.5M urea & 50%glycerol.

    Purity

    HCV NS4 Protein is >95% pure as determined by 10% PAGE (coomassie staining).

    More Info

    • Introduction

      HCV is a small 50nm, enveloped, single-stranded, positive sense RNAvirus 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 NS4 a+b HRP although stable at 4°C for 1 week, should be stored below -18°C. Please prevent freeze thaw cycles.

    • Applications

      HCV NS4 Antigen is suitable for ELISA and Western blots, excellent antigen for detection of HCV with minimal specificity problems.

    • Specificity

      Immunoreactive with sera of HCV-infected individuals.

    • Purification Method

      HCV NS4 protein was purified by proprietary 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.

    Hcv Ns4 Hrp
  • View Data Sheet

    Name :

    Tissue Factor Human

    Description:

    Coagulation Factor III Human Recombinant

    Tissue factor, Coagulation factor III, Thromboplastin, CD142, TF, F3, TFA.

    Product # :

    PRO-312

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    • sds-page

    Description

    Tissue factor Human Recombinant produced in E.Coli is single, a non-glycosylated, Polypeptide chain containing 219 amino acids of the extracellular domain (33-251) having a molecular mass of 29.39 kDa and fused with a 4.5kDa amino-terminal hexahistidine tag. The Tissue factor is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Tissue factor protein is supplied in 20mM Tris-HCl pH8.0, 1mM EDTA and 50% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    sds-page

    tissue factor human sds-page - Product image 1

    More Info

    • Introduction

      Tissue factor is well-known as the main cellular initiator of blood coagulation. The Tissue factor gene encodes coagulation factor III which is a cell surface glycoprotein that enables cells to initiate the blood coagulation cascades, and functions as the high-affinity receptor for the coagulation factor VII. Following vessel injury, the Tissue Factor and Factor VIIa complex activates the coagulation protease cascade, which leads to fibrin deposition and activation of platelets. The ensuing complex presents a catalytic event, which is responsible for initiation of the coagulation protease cascades by specific limited proteolysis. Therefore, Tissue factor has a role in normal hemostasis by initiating the cell-surface assembly and propagation of the coagulation protease cascade. Tissue Factor can also be stimulated by the inflammatory mediators interleukin 1 and TNF, as well as by endotoxin, to appear on monocytes and vascular endothelial cells as a component of cellular immune response.
      Tissue factor is the only one in the coagulation pathway for which a congenital deficiency has not been described. Certain levels of Tissue Factor are essential for the maintained viability and growth of endothelium and Tissue Factor-expressing tumor cells. Additionally, abnormal Tissue Factor expression inside the vasculature initiates life threatening thrombosis in various diseases, for example sepsis, atherosclerosis, and cancer. Alternative spliced Tissue Factor expression advances tumor growth, and is linked to increased tumor cell proliferation and angiogenesis in pancreatic cancer.

    • Synonyms

      Tissue factor, Coagulation factor III, Thromboplastin, CD142, TF, F3, TFA.

    • Physical Appearance

      Sterile Filtered clear solution.

    • Stability

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

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

    Tissue Factor Human
  • 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.

    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 Mouse
  • View Data Sheet

    Name :

    GH Rainbow Trout

    Description:

    Growth Hormone Rainbow Trout (Oncorhynchus mykiss) Recombinant

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

    Product # :

    CYT-1010

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    Description

    Somatotropin Rainbow Trout (Oncorhynchus mykiss) Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 188 amino acids with an additional Ala at the N-terminus and having a molecular mass of 21, 535 Dalton. The Rainbow Trout (Oncorhynchus mykiss) Growth-Hormone Recombinant is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The protein was lyophilized from a concentrated (1mg/ml) solution with 0.5% NaHCO3. Adjusted to pH-8.

    Purity

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

    Biological Activity

    Somatotropin Rainbow Trout (Oncorhynchus mykiss) Recombinant is biologically active in PDF-P1 3B9 cells stable transfected with rabbit GH receptors, though its activity is about 10 fold lower than that of human GH.

    More Info

    • Introduction

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

    • Synonyms

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

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized Growth-Hormone Rainbow Trout (Oncorhynchus mykiss) although stable at room temperature for at least two weeks, should be stored desiccated below -18°C. Upon reconstitution and filter sterilization GH can be stored at 4°C, pH 9 for up to 4 weeks. For long term storage and more diluted solutions it is recommended to add a carrier protein (0.1% HSA or BSA). Please prevent freeze-thaw cycles.

    • Solubility

      It is recommended to reconstitute the lyophilized Growth-Hormone Rainbow Trout (Oncorhynchus mykiss) in 0.4% NaHCO3 or water adjusted to pH 8-9, not less than 100µg/ml and not more than 3mg/ml, which can then be further diluted to other aqueous solutions, preferably in a presence of a carrier protein such as BSA or similar.

    • Amino Acid Sequence

      AIENQRLFNIAVSRVQHLHLLAQKMFNDFDGTLLPDERRQLNKIFLLDFCNSDSIVSPVD
      KHETQKSSVLKLLHISFRLIESWEYPSQTLIISNSLMVRNANQISEKLSDLKVGINLLIT
      GSQDGVLSLDDNDSQQLPPYGNYYQNLGGDGNVRRNYELLACFKKDMHKVETYLTVAKCR
      KSLEANCTL.

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

    Growth Hormone Rainbow Trout
  • View Data Sheet

    Name :

    GM-CSF Human, Pichia

    Description:

    Granulocyte Macrophage-Colony Stimulating Factor Human Recombinant, Pichia

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

    Product # :

    CYT-324

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    Description

    Granulocyte Macrophage Colony Stimulating Factor Human Recombinant produced in Yeast is a single, glycosylated, polypeptide chain containing 127 amino acids and having a molecular mass of 26-32 kDa. rhGMCSF differs from the natural human GM-CSF by a substitution of leucine at position 23 (R to L), and the carbohydrate moiety may be different from the native protein. GM-CSF is purified by proprietary chromatographic techniques.

    Source

    Pichia Pastoris.

    Formulation

    The protein was lyophilized from a concentrated (1mg/ml) solution containing 10mM phosphate buffer pH 7.0, 40 mg mannitol and 10 mg sucrose.

    Purity

    Greater than 97.0% as determined by1. Analysis by RP-HPLC.
    2. Analysis by SDS-PAGE.

    Biological Activity

    The ED50 as determined by the dose-dependant stimulation of the proliferation of human TF-1 cells (human erythroleukemic indicator cell line) is < 0.183 ng/ml, corresponding to a Specific Activity of 5,500,000IU/mg.

    More Info

    • Introduction

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

    • Synonyms

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

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Solubility

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

    • Amino Acid Sequence

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

    • Background

      What is the molecular weight/Mw of GM-CSF HUMAN, PICHIA Protein?
      GM-CSF HUMAN, PICHIA Protein has a total Mw of 29kDa.

      What is the source or expression system of GM-CSF HUMAN, PICHIA Protein?
      Pichia Pastoris.
      What is the Purity of GM-CSF HUMAN, PICHIA Protein?
      GM-CSF HUMAN, PICHIA Protein is >97% pure as determined by SDS-PAGE.

      What is the Biological Activity of GM-CSF HUMAN, PICHIA Protein?
      The ED50 as determined by the dose-dependant stimulation of the proliferation of human TF-1 cells (human erythroleukemic indicator cell line) is < 0.183 ng/ml, corresponding to a Specific Activity of 5,500,000IU/mg.

      What is the amino acid sequence of GM-CSF HUMAN, PICHIA Protein?
      The sequence of the first five N-terminal amino acids was determined and was found to be Ala-Pro-Ala-Arg-Ser.

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

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

    Gm Csf Human Pichia
  • View Data Sheet

    Name :

    GH Ovine

    Description:

    Growth Hormone Ovine Recombinant

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

    Product # :

    CYT-237

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    Description

    Growth Hormone Ovine Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 191 amino acids and having a molecular mass of 21833 Dalton. The GH Ovine Recombinant is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

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

    Purity

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

    Biological Activity

    The activity as determined by the dose-dependant stimulation of the proliferation FDCP13B9 cells.

    More Info

    • Introduction

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

    • Synonyms

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

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Amino Acid Sequence

      1 afpamslsgl fanavlraqh lhqlaadtfk efertyipeg qrysiqntqv 51 afcfsetipa ptgkneaqqk sdlellrisl lliqswlgpl qflsrvftns 101 lvfgtsdrvy eklkdleegi lalmreledv tpragqilkq tydkfdtnmr 151 sddallknyg llscfrkdlh ktetylrvmk crrfgeasca f

    • Protein content

      Protein quantitation was carried out by UV spectroscopy at 280 nm using the absorbency value of 0.63 as the extinction coefficient for a 0.1% (1mg/ml) solution. 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.

    Growth Hormone Ovine
  • 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

    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.

    Pon1 Enzyme
  • View Data Sheet

    Name :

    IL 3 Human, His

    Description:

    Interleukin-3 Human Recombinant, His Tag

    MCGF (Mast cell growth factor), Multi-CSF, HCGF, P-cell stimulation factor, IL-3, MGC79398, MGC79399.

    Product # :

    CYT-482

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    Description

    Interleukin-3 Human Recombinant produced in E.Coli is single, a non-glycosylated, Polypeptide chain containing 154 amino acids fragment (20-152) and having a total molecular mass of 17.3kDa and fused with a 20 aa N-terminal His tag. The IL3 His is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Interleukin-3 His (1mg/ml) is supplied in 20mM Tris-HCl buffer (pH 8.0), 0.2mM PMSF and 10% glycerol.

    Purity

    Greater than 90.0% as determined by analysis by SDS-PAGE.

    Biological Activity

    The ED50 for this effect is <0.53ng/ml. Measured in a cell proliferation assay using TF1 human erythroleukemic cells.

    More Info

    • Introduction

      Interleukin-3 is a pleiotropic cytokine produced primarily by activated T cells. IL-3 is thought to function via specific cell surface receptors to stimulate the proliferation, differentiation and survival of haematopoietic cell lines. IL-3 has also been shown to affect the functional activity of a variety of other cell types including mast cells, eosinophils, megakaryocytes and basophils.

    • Synonyms

      MCGF (Mast cell growth factor), Multi-CSF, HCGF, P-cell stimulation factor, IL-3, MGC79398, MGC79399.

    • Physical Appearance

      Sterile Filtered clear solution.

    • Stability

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

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MAPMTQTTSL KTSWVNCSNM IDEIITHLKQ PPLPLLDFNN LNGEDQDILM ENNLRRPNLE AFNRAVKSLQ NASAIESILK NLLPCLPLAT AAPTRHPIHI KDGDWNEFRR KLTFYLKTLE NAQAQQTTLS LAIF.

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

    Il 3 Human His
  • View Data Sheet

    Name :

    GSTK1 Human

    Description:

    Glutathione S-Transferase Kappa 1 Human Recombinant

    GST13, GST13-13, GSTK1-1, GST class-kappa, EC 2.5.1.18, Glutathione S-transferase kappa 1, Glutathione S-transferase subunit 13, hGSTK1, GSTK1.

    Product # :

    ENZ-476

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    Description

    GSTK1 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 226 amino acids (1-226 a.a.) and having a molecular mass of 25.5 kDa. GSTK1 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    GSTK1 solution containing 20mM Tris pH-8, 1mM DTT and 10% glycerol.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    More Info

    • Introduction

      GSTK1 is involved in cellular detoxification. GSTK1 is localized to the peroxisome and catalyzes the conjugation of the thiol group of glutathione (GSH) to the electrophilic groups of a broad range of hydrophobic substrates, leading to an easier removal of the latter from the cells.

    • Synonyms

      GST13, GST13-13, GSTK1-1, GST class-kappa, EC 2.5.1.18, Glutathione S-transferase kappa 1, Glutathione S-transferase subunit 13, hGSTK1, GSTK1.

    • 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

      MGPLPRTVEL FYDVLSPYSW LGFEILCRYQ NIWNINLQLR PSLITGIMKD SGNKPPGLLP RKGLYMANDL KLLRHHLQIP IHFPKDFLSV MLEKGSLSAM RFLTAVNLEH PEMLEKASRE LWMRVWSRNE DITEPQSILA AAEKAGMSAE QAQGLLEKIA TPKVKNQLKE TTEAACRYGA FGLPITVAHV DGQTHMLFGS DRMELLAHLL GEKWMGPIPP AVNARL.

    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.

    Gstk1 Human
  • View Data Sheet

    Name :

    BDH1 Human

    Description:

    3-Hydroxybutyrate Dehydrogenase, Type 1 Human Recombinant

    D-beta-hydroxybutyrate dehydrogenase, mitochondrial, BDH, 3-hydroxybutyrate dehydrogenase, BDH1, SDR9C1.

    Product # :

    ENZ-215

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    Description

    BDH1 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 318 amino acids (47-343) and having a molecular mass of 35.3kDa.BDH1 is fused to a 21 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    The BDH1 solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH8.0), 30% glycerol, 0.2M NaCl, 2mM DTT and 0.1mM PMSF.

    Purity

    Greater than 85% as determined by SDS-PAGE.

    More Info

    • Introduction

      BDH1 belongs to the short-chain dehydrogenase/reductase gene family. BDH1 forms a homotetrameric lipid-requiring enzyme of the mitochondrial membrane and has a specific necessity for phosphatidylcholine for optimal enzymatic activity. BDH1 catalyzes the interconversion of acetoacetate and (R)-3-hydroxybutyrate, the 2 main ketone bodies formed during fatty acid catabolism.

    • Synonyms

      D-beta-hydroxybutyrate dehydrogenase, mitochondrial, BDH, 3-hydroxybutyrate dehydrogenase, BDH1, SDR9C1.

    • 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 MASAAEPVGS KAVLVTGCDS GFGFSLAKHL HSKGFLVFAG CLMKDKGHDG VKELDSLNSD RLRTVQLNVC SSEEVEKVVE IVRSSLKDPE KGMWGLVNNA GISTFGEVEF TSLETYKQVA EVNLWGTVRM TKSFLPLIRR AKGRVVNISS MLGRMANPAR SPYCITKFGV EAFSDCLRYE MYPLGVKVSV VEPGNFIAAT SLYSPESIQA IAKKMWEELP EVVRKDYGKK YFDEKIAKME TYCSSGSTDT SPVIDAVTHA LTATTPYTRY HPMDYYWWLR MQIMTHLPGA ISDMIYIR.

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    Bdh1 Human
  • View Data Sheet

    Name :

    PGC Human

    Description:

    Progastricsin-C Human Recombinant

    Progastricsin (Pepsinogen C), Pepsinogen C, EC 3.4.23.3, Pepsinogen Group II, Preprogastricsin, EC 3.4.23, Pepsin C, PGII, PEPC.

    Product # :

    ENZ-966

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    Description

    PGC produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 380 amino acids (17-388 a.a.) and having a molecular mass of 41.6kDa (Molecular size on SDS-PAGE will appear at approximately 40-57kDa). PGC is expressed with an 8 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

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

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Progastricsin-C (PGC) is an aspartic proteinase which is synthesized in the gastric mucosa as inactive precursors. PGC is a part of the peptidase family A1 and contains a prosegment which is responsible for stabilizing the inactive form and preventing the entrance of the substrate to the active site. PGC is used as a biomarker for various gastric diseases including Helicobacter pylori related gastritis. PGC is also hydrolyzes various proteins.

    • Synonyms

      Progastricsin (Pepsinogen C), Pepsinogen C, EC 3.4.23.3, Pepsinogen Group II, Preprogastricsin, EC 3.4.23, Pepsin C, PGII, PEPC.

    • 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

      AVVKVPLKKF KSIRETMKEK GLLGEFLRTH KYDPAWKYRF GDLSVTYEPM AYMDAAYFGE ISIGTPPQNF LVLFDTGSSN LWVPSVYCQS QACTSHSRFN PSESSTYSTN GQTFSLQYGS GSLTGFFGYD TLTVQSIQVP NQEFGLSENE PGTNFVYAQF DGIMGLAYPA LSVDEATTAM QGMVQEGALT SPVFSVYLSN QQGSSGGAVV FGGVDSSLYT GQIYWAPVTQ ELYWQIGIEE FLIGGQASGW CSEGCQAIVD TGTSLLTVPQ QYMSALLQAT GAQEDEYGQF LVNCNSIQNL PSLTFIINGV EFPLPPSSYI LSNNGYCTVG VEPTYLSSQN GQPLWILGDV FLRSYYSVYD LGNNRVGFAT AALEHHHHHH.

    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.

    Pgc Human
  • View Data Sheet

    Name :

    HCV Core, HRP

    Description:

    Hepatitis C Virus Core, Horseradish Peroxidase Recombinant

    Product # :

    HCV-243

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    Description

    The E.coli derived recombinant HRP Labeled protein contains the HCV core nucleocapsid immunodominant regions, amino acids 2-119. HCV Core is fused to b-gal (114 kDa) at N-terminus.

    Formulation

    1mg/ml in 20mM Tris-HCl pH-8, and 8M urea.

    Purity

    HCV Core protein is >95% pure as determined by 10% PAGE (coomassie staining).

    More Info

    • Introduction

      HCV is a small 50nm, enveloped, single-stranded, positive sense RNAvirus 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 Core HRP although stable at 4°C for 1 week, should be stored below -18°C.Please prevent freeze thaw cycles.

    • Applications

      HCV Core antigen is suitbale for ELISA and Western blots, excellent antigen for detection of HCV with minimal specificity problems.

    • Specificity

      Immunoreactive with sera of HCV-infected individuals.

    • Purification Method

      HCV Core protein was purified by proprietary 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.

    Hcv Core Hrp
  • View Data Sheet

    Name :

    Leptin-A Tilapia

    Description:

    Leptin-A Tilapia Recombinant

    Product # :

    CYT-1109

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    Description

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

    Source

    Escherichia Coli.

    Formulation

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

    Purity

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

    Biological Activity

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

    More Info

    • Introduction

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

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Solubility

      It is recommended to reconstitute the lyophilized Leptin-A Tilapia in sterile water or 0.4% NaHCO3 adjusted to pH 8-9, not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      The first six N-terminal amino acids of recombinant Tilapia leptin A are Ala-Pro-Leu-Pro-Val-Glu.

    • Protein content

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

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

    Leptin A
  • View Data Sheet

    Name :

    Leptin-B Tilapia

    Description:

    Leptin-B Tilapia Recombinant

    Product # :

    CYT-1110

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    Description

    Leptin-B Tilapia Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 152 amino acids and having a molecular mass of 15,243 Dalton. The Leptin-B Tilapia is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

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

    Purity

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

    Biological Activity

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

    More Info

    • Introduction

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

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Solubility

      It is recommended to reconstitute the lyophilized Leptin-B Tilapia in sterile water or 0.4% NaHCO3 adjusted to pH 8-9, not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      The first six N-terminal amino acids of recombinant Tilapia leptin B are Ala-Leu-Leu-Thr-Lys-Gly.

    • Protein content

      Protein quantitation was carried out by UV spectroscopy at 280 nm using the absorbency value of 0.19 for 1 mg/ml Leptin-B Tilapia as the extinction coefficient for a 0.1% (1mg/ml) solution at pH 8.0. This value is calculated by the DNAman computer analysis program of protein sequences.

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

    Leptin B
  • View Data Sheet

    Name :

    GM-CSF Monkey

    Description:

    Granulocyte Macrophage-Colony Stimulating Factor Rhesus Macaque Recombinant

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

    Product # :

    CYT-720

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    Description

    Granulocyte Macrophage Colony Stimulating Factor Monkey Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 127 amino acids and having a molecular mass of 14.4 kDa.GM-CSF is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    GM-CSF was lyophilized from a concentrated (1mg/ml) solution containing 1x PBS pH 7.4.

    Purity

    Greater than 98.0% as determined by SDS-PAGE and RP-HPLC.

    Biological Activity

    The ED50 as determined by a cell proliferation assay using human TF-1 cells is less than 0.1ng/ml, corresponding to a specific activity of > 10,000,000 IU/mg.

    More Info

    • Introduction

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

    • Synonyms

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

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Solubility

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

    • Amino Acid Sequence

      APARSPSPGT QPWEHVNAIQ EARRLLNLSR DTAAEMNKTV EVVSEMFDLQ EPSCLQTRLE LYKQGLQGSL TKLKGPLTMM ASHYKQHCPP TPETSCATQI ITFQSFKENL KDFLLVIPFD CWEPVQE.

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    Gm Csf Monkey
  • View Data Sheet

    Name :

    TGFB2 Mouse

    Description:

    Transforming Growth Factor-Beta 2 Mouse Recombinant

    Transforming growth factor beta-2, TGF-beta-2, G-TSF, Tgfb-2, TGFbeta2.

    Product # :

    CYT-1266

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    Description

    Transforming Growth Factor-Beta 2 Mouse Recombinant produced in CHO is a homodimer, polypeptide chain containing 2 x 112 amino acids and having a total molecular mass of 25.4kDa.
    TGFB2 Mouse Recombinant is purified by proprietary chromatographic techniques.

    Source

    CHO Cells.

    Formulation

    The protein was lyophilized with 0.1% (v/v) TFA and 35% (v/v) Acetonitrile.

    Purity

    Greater than 97.0% as determined by SDS-PAGE and SEC-HPLC analyses.

    Biological Activity

    The biological activity was determined by TGFB2 ability to inhibit the mouse IL-4-dependent proliferation of mouse HT-2 cells. The expected ED50 for this effect is <0.05ng/ml, corresponding to a specific activity of ≥ 2.0 × 107 units/mg.

    More Info

    • 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 TGFB2 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Transforming Growth Factor-Beta 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 Transforming Growth Factor-Beta 2 in sterile 4mM HCl not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      ALDAAYCFRN VQDNCCLRPL YIDFKRDLGW KWIHEPKGYN ANFCAGACPY LWSSDTQHTK VLSLYNTINP EASASPCCVS QDLEPLTILY YIGNTPKIEQ LSNMIVKSCK CS.

    • Background

      TGFB2 differ from TGFB1 in the tissue distribution, receptor interactions, and several biological roles.
      TGFB2 requires TGFBR3 for its binding to TGFBR2 while TGFB1 binds directly to the receptor TGFBR2.
      TGFB2 is crucial for embryonic development ocular biology, neural development, and tissue morphogenesis while TGFB1 is crucial for immune regulation and fibrosis.
      TGFB2 exhibits more tissue-specific developmental expression Vs TGFB1.


      What is the source or expression system of Mouse TGFB2 Protein?
      CHO Cells

      What is the Purity of Mouse TGFB2 Protein?
      Mouse TGFB2 Protein is >97% pure as determined by SDS-PAGE.

      What is the molecular weight / Mw of Mouse TGFB2 Protein?
      Mouse TGFB2 Protein having a total Mw of 25.6kDa.

      What is the Biological Activity of Mouse TGFB2 Protein?
      The biological functionality of Mouse TGFB2 Protein is determined by mouse HT-2 cells.

      What is the endotoxin level for Mouse TGFB2 Protein?
      The endotoxin level is minimal, Mouse TGFB2 Protein was purified using conventional chromatography techniques.

      What is the amino acid sequence of Mouse TGFB2 Protein?
      ALDAAYCFRN VQDNCCLRPL YIDFKRDLGW KWIHEPKGYN ANFCAGACPY LWSSDTQHTK VLSLYNTINP EASASPCCVS QDLEPLTILY YIGNTPKIEQ LSNMIVKSCK CS.

      Is TGFB2 a homodimer / homodimeric protein?
      Yes, TGFB2 is homo dimer consisting of 2 identical chains.

    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.

    tgfb2 mouse
  • View Data Sheet

    Name :

    CTF2P Mouse

    Description:

    Neuropoietin Mouse Recombinant

    Cardiotrophin-2, CT-2, Neuropoietin, Np, Ctf2, Gm494.

    Product # :

    CYT-1128

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    Description

    Neuropoietin Mouse Recombinant produced in E.Coli is a non-glycosylated polypeptide chain containing 182 amino acids and having a molecular mass of approximately 19.7kDa.CTF2P is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Lyophilized from a 0.2μm filtered concentrated solution in 20mM Tris-HCl, pH 8.0, 0.5mM DTT and 500mM NaCl.

    Purity

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

    Biological Activity

    The ED50 as determined by a cell proliferation assay using human TF-1 cells is < 200 ng/ml, corresponding to a specific activity of > 5000 IU/mg.

    More Info

    • Introduction

      CTF2P, aka Neuropoietinis a part of the IL-6 family of cytokines. CTF2P is the outcome of a gene duplication event involving cardiotrophin-1 (CT-1) and it helps to define a subfamily within the IL-6 family that includes CT-1, CLC and CTNF. CTF2P Increases the platelet count associated with splenomegaly and takes part in neuronal precursor development and maturation.

    • Synonyms

      Cardiotrophin-2, CT-2, Neuropoietin, Np, Ctf2, Gm494.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized CTF2P although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Neuropoietin 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 Neuropoietin in sterile PBS not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      APISPSEPIG QAYSLALYMQ KNTSALLQTY LQHQGSPFSD PGFSAPELQL STLPSAAVSF KTWHAMEDAE RLSRAQGAFL ALTQHLQLVG DDQSYLNPGS PILLAQLGAA RLRAQGLLGN MAAIMTALGL PIPPEEDTLG FVPFGASAFE RKCRGYIVTR EYGHWTDRAV RDLALLKAKY SA.

    • Background

      What is the molecular weight/Mw of CTF2P Protein?
      CTF2P Protein has a total Mw of 19.7kDa.

      What is the source or expression system of CTF2P Protein?
      Escherichia Coli.

      What is the Purity of CTF2P Protein?
      CTF2P Protein is >98% pure as determined by SDS-PAGE.

      What is the Biological Activity of CTF2P Protein?
      The ED50 as determined by a cell proliferation assay using human TF-1 cells is < 200 ng/ml, corresponding to a specific activity of > 5000 IU/mg.

      What is the amino acid sequence of CTF2P Protein?
      APISPSEPIG QAYSLALYMQ KNTSALLQTY LQHQGSPFSD PGFSAPELQL STLPSAAVSF KTWHAMEDAE RLSRAQGAFL ALTQHLQLVG DDQSYLNPGS PILLAQLGAA RLRAQGLLGN MAAIMTALGL PIPPEEDTLG FVPFGASAFE RKCRGYIVTR EYGHWTDRAV RDLALLKAKY SA.

      What applications can CTF2P Protein be used in?
      CTF2P Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for CTF2P Protein?
      The endotoxin level is minimal, CTF2P 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.

    Neuropoietin Mouse
  • View Data Sheet

    Name :

    HSA Fatty Acid free

    Description:

    Human Serum Albumin Recombinant, Fatty Acid Free

    Serum albumin, ALB, PRO0883, PRO0903, PRO1341, DKFZp779N1935, GIG20, GIG42,   PRO1708, PRO2044, PRO2619, PRO2675, UNQ696, SA, HSA.

    Product # :

    PRO-1917

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    Description

    HSA Human Recombinant Fatty Acid reduced produced in Plant contains 585 amino acids having a molecular mass of 67 kDa. The recombinant Albumin is purified by proprietary chromatographic techniques.

    Source

    Rice Grain.

    Formulation

    solution containing no additives.

    Purity

    Greater than 97% as determined by SDS-PAGE.

    More Info

    • Introduction

      Albumin is synthesized in the liver as preproalbumin which has an N-terminal peptide that is removed before the nascent protein is released from the rough endoplasmic reticulum. The product, proalbumin, is in turn cleaved in the Golgi vesicles to produce the secreted albumin. Albumin is a soluble, monomeric protein which comprises about one-half of the blood serum protein. Albumin functions primarily as a carrier protein for steroids, fatty acids, and thyroid hormones and plays a role in stabilizing extracellular fluid volume. Mutations in this gene on chromosome 4 result in various anomalous proteins. Albumin is a globular unglycosylated serum protein of molecular weight 65,000. The human albumin gene is 16,961 nucleotides long from the putative 'cap' site to the first poly (A) addition site. It is split into 15 exons which are symmetrically placed within the 3 domains that are thought to have arisen by triplication of a single primordial domain.
      HSA is widely used to stabilize

    • Synonyms

      Serum albumin, ALB, PRO0883, PRO0903, PRO1341, DKFZp779N1935, GIG20, GIG42, PRO1708, PRO2044, PRO2619, PRO2675, UNQ696, SA, HSA.

    • Physical Appearance

      Sterile Filtered clear yellowish solution.

    • Stability

      Recombinant Albumin stable at room temperature for 2 weeks should be stored at 4°C.

    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.

    Hsa Lipid Free
  • View Data Sheet

    Name :

    FCGRT Human

    Description:

    Fc Fragment Of IgG Receptor And Transporter Human Recombinant

    IgG receptor FcRn large subunit p51, FcRn, IgG Fc fragment receptor transporter alpha chain, Neonatal Fc receptor, Fcgrt, Fcrn.

    Product # :

    PRO-2806

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    Description

    FCGRT Human Recombinant is a glycosylated, polypeptide chain conteining 2 fragments: FCGRT (24-297aa) having a total 280 a.a and a a molecular weigh of 31.1kDa & B2M (21-119 aa) having a total 99 a.a and a a molecular weigh of 11.7kDa. FCGRT is fused to a 6 a.a his-Tag at C-terminus and is purified by proprietary chromatographic techniques.

    Source

    HEK293 Cells.

    Formulation

    The FCGRT solution (0.25mg/ml) contains 10% Glycerol and Phosphate-Buffered Saline (pH 7.4).

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Biological Activity

    Measured by its binding ability in a functional ELISA with Human IgG1 Fc.

    More Info

    • Synonyms

      IgG receptor FcRn large subunit p51, FcRn, IgG Fc fragment receptor transporter alpha chain, Neonatal Fc receptor, Fcgrt, Fcrn.

    • 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

      FCGRT

      AESHLSLLYH LTAVSSPAPG TPAFWVSGWL GPQQYLSYNS LRGEAEPCGA WVWENQVSWY WEKETTDLRI KEKLFLEAFK ALGGKGPYTL QGLLGCELGP DNTSVPTAKF ALNGEEFMNF DLKQGTWGGD WPEALAISQR WQQQDKAANK ELTFLLFSCP HRLREHLERG RGNLEWKEPP SMRLKARPSS PGFSVLTCSA FSFYPPELQL RFLRNGLAAG TGQGDFGPNS DGSFHASSSL TVKSGDEHHY CCIVQHAGLA QPLRVELESP AKSSHHHHHH.

      B2M

      IQRTPKIQVY SRHPAENGKS NFLNCYVSGF HPSDIEVDLL KNGERIEKVE HSDLSFSKDW SFYLLYYTEF TPTEKDEYAC RVNHVTLSQP KIVKWDRDM.

    • Background

      Applications in Drug Delivery and Therapy:

      The unique ability of FCGRT to transport immunoglobulins has spurred investigations into its potential applications in drug delivery. FCGRT Human Recombinant is being explored as a tool to improve the pharmacokinetics of therapeutic antibodies, enhancing their stability and extending their half-life in circulation. This holds significant implications for the development of antibody-based therapies for a range of diseases, including autoimmune disorders and cancer.

      Modulation of Immune Responses:

      Beyond its role in immunoglobulin transport, FCGRT is implicated in the modulation of immune responses. FCGRT Human Recombinant studies have unveiled its interactions with immune cells and its potential influence on the activation and regulation of the immune system. This dual role positions FCGRT as a key player not only in passive immunity but also in the dynamic orchestration of immune responses.

      Challenges and Future Directions:

      While the potential of FCGRT Human Recombinant in drug delivery is promising, challenges persist. Fine-tuning its applications, understanding its interactions with diverse antibodies, and optimizing strategies for therapeutic use are critical considerations for translational success. Additionally, deciphering the intricate balance between immunoglobulin transport and immune modulation is an active area of investigation.

      FCGRT Human Recombinant emerges as a sentinel in the realm of immunoglobulin transport and drug delivery, offering a controlled platform for scientific exploration. Its structural insights, immunoglobulin transport functions, and therapeutic applications position it as a key player in the evolving landscape of biopharmaceuticals. As researchers continue to delve into the molecular intricacies of FCGRT, they not only enhance our understanding of immunoglobulin transport but also pave the way for transformative advancements in drug delivery and antibody-based therapies, shaping the future of precision medicine and targeted therapeutics.

    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.

    Fcgrt Human
  • View Data Sheet

    Name :

    HIV-2 gp32, HRP

    Description:

    HIV-2 gp32 Recombinant, HRP Labeled

    Product # :

    HIV-137

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    Description

    HIV-2 gp32 HRP Labeled recombinant- contains the full-length sequence of HIV-2 envelope immunodominant regions gp32 having a Mw of 32kDa and fused to a beta-galactosidase at N-terminus.

    Source

    Escherichia Coli.

    Formulation

    0.01M Na2CO3, 10mM EDTA, 14mM beta-ME and 0.02% Sarcosyl.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      HIV-1 and HIV-2 appear to package their RNA differently. HIV-1 binds to any appropriate RNA whereas HIV-2 preferentially binds to mRNA which creates the Gag protein itself. This means that HIV-1 is better able to mutate. HIV-2 is transmitted in the same ways as HIV-1: Through exposure to bodily fluids such as blood, semen, tears and vaginal fluids.
      Immunodeficiency develops more slowly with HIV-2.
      HIV-2 is less infectious in the early stages of the virus than with HIV-1.
      The infectiousness of HIV-2 increases as the virus progresses.
      Major differences include reduced pathogenicity of HIV-2 relative to HIV-1, enhanced immune control of HIV-2 infection and often some degree of CD4-independence. Despite considerable sequence and phenotypic differences between HIV-1 and 2 envelopes, structurally they are quite similar. Both membrane-anchored proteins eventually form the 6-helix bundles from the N-terminal and C-terminal regions of the ectodomain, which is common to many viral and cellular fusion proteins and which seems to drive fusion.
      HIV-1 gp41 helical regions can form more stable 6-helix bundles than
      HIV-2 gp41 helical regions however HIV-2 fusion occurs at a lower threshold temperature (25°C), does not require Ca2+ in the medium, is insensitive to treatment of target cells with cytochalasin B, and is not affected by target membrane glycosphingolipid composition.

    • Physical Appearance

      Sterile filtered colorless clear solution.

    • Stability

      HIV-2 gp-32 although stable at room temperature for 3 weeks, should be stored at 4°C.

    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.

    Hiv 2 Gp 32 Hrp
  • View Data Sheet

    Name :

    MPG Human

    Description:

    N-Methylpurine-DNA Glycosylase Human Recombinant

    DNA-3-methyladenine glycosylase, 3-alkyladenine DNA glycosylase, 3-methyladenine DNA glycosidase, ADPG, N-methylpurine-DNA glycosylase, MPG, AAG, ANPG, MID1, MDG, PIG11, PIG16, CRA36.1.

    Product # :

    ENZ-151

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    Description

    MPG Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 306 amino acids (1-298 a.a.) and having a molecular mass of 33.9kDa (Molecular weight on SDS-PAGE will appear higher).MPG is fused to an 8 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    MPG protein solution (0.25mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 1mM DTT, 30% glycerol, 200mM NaCl and 1mM EDTA.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      DNA-3-methyladenine glycosylase (MPG) is a member of the DNA glycosylase MPG family. MPG initiates base excision repair in DNA by removing a wide variety of alkylated, deaminated, and lipid peroxidation-induced purine adducts.

    • Synonyms

      DNA-3-methyladenine glycosylase, 3-alkyladenine DNA glycosylase, 3-methyladenine DNA glycosidase, ADPG, N-methylpurine-DNA glycosylase, MPG, AAG, ANPG, MID1, MDG, PIG11, PIG16, CRA36.1.

    • 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

      MVTPALQMKK PKQFCRRMGQ KKQRPARAGQ PHSSSDAAQA PAEQPHSSSD AAQAPCPRER CLGPPTTPGP YRSIYFSSPK GHLTRLGLEF FDQPAVPLAR AFLGQVLVRR LPNGTELRGR IVETEAYLGP EDEAAHSRGG RQTPRNRGMF MKPGTLYVYI IYGMYFCMNI SSQGDGACVL LRALEPLEGL ETMRQLRSTL RKGTASRVLK DRELCSGPSK LCQALAINKS FDQRDLAQDE AVWLERGPLE PSEPAVVAAA RVGVGHAGEW ARKPLRFYVR GSPWVSVVDR VAEQDTQALE 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.

    Mpg Human
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