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    M-CSF的重組小鼠細胞因子Recombinant Mouse M-CSF

    • 更新時間:  2023-07-24
    • 產品型號:  RD 416-ml-010
    • 簡單描述
    • M-CSF的重組小鼠細胞因子Recombinant Mouse M-CSF也被稱為CSF1細胞因子,巨噬細胞的存活,增殖和分化(1)主要監管機構纖細說明書在產品詳細介紹中
    詳細介紹

    M-CSF的重組小鼠細胞因子Recombinant Mouse M-CSF

    DESCRIPTION
    Source E. coliderived
    Lys33Glu262,
    with an Nterminal
    Met
    Accession # Q3U4F9
    Nterminal
    Sequence
    Analysis
    Met
    Structure / Form Disulfidelinked
    homodimer
    Predicted Molecular
    Mass
    26 kDa (monomer)
    SPECIFICATIONS
    SDSPAGE
    29 kDa, reducing conditions
    Activity Measured in a cell proliferation assay using M-NFS-60 mouse myelogenous leukemia lymphoblast cells. Halenbeck, R. et al. (1989)
    Biotechnology 7:710.
    The ED50 for this effect is typically 0.5-3 ng/mL.
    Endotoxin Level <1.0 EU per 1 μg of the protein by the LAL method.
    Purity >97%, by SDSPAGE
    under reducing conditions and visualized by silver stain.
    Formulation Lyophilized from a 0.2 μm filtered solution in PBS with BSA as a carrier protein. See Certificate of Analysis for details.
    PREPARATION AND STORAGE
    Reconstitution Reconstitute at 100 μg/mL in sterile PBS containing at least 0.1% human or bovine serum albumin.
    Shipping The product is shipped at ambient temperature. Upon receipt, store it immediay at the temperature recommended below.
    Stability & Storage Use a manual defrost freezer and avoid repeated freezethaw
    cycles.
    l 12 months from date of receipt, 20
    to 70
    °C as supplied.
    l 1 month, 2 to 8 °C under sterile conditions after reconstitution.
    l 3 months, 20
    to 70
    °C under sterile conditions after reconstitution.
    BACKGROUND
    MCSF,
    also known as CSF1,
    is a fourαhelicalbundle
    cytokine that is the primary regulator of macrophage survival, proliferation and differentiation (1 3).
    MCSF
    is also essential for the survival and proliferation of osteoclast progenitors (1, 4). MCSF
    also primes and enhances macrophage killing of tumor cells and
    microorganisms, regulates the release of cytokines and other inflammatory modulators from macrophages, and stimulates pinocytosis (2, 3). MCSF
    increases during
    pregnancy to support implantation and growth of the decidua and placenta (5). Sources of MCSF
    include fibroblasts, activated macrophages, endometrial secretory
    epithelium, bone marrow stromal cells and activated endothelial cells (1 5).
    The MCSF
    receptor (cfms)
    transduces its pleotropic effects and mediates its
    endocytosis. MCSF
    mRNAs of various sizes occur (3 9).
    Full length mouse MCSF
    transcripts encode a 520 amino acid (aa) type I transmembrane (TM) protein with
    a 462 aa extracellular region, a 21 aa TM domain, and a 37 aa cytoplasmic tail that forms a 140 kDa covalent dimer. Differential processing produces two
    proteolytically cleaved, secreted dimers. One is an Nand
    Oglycosylated
    86 kDa dimer, while the other is modified by both glycosylation and chondroitinsulfate
    proteoglycan (PG) to generate a 200 kDa subunit. Although PGmodified
    MCSF
    can circulate, it may be immobilized by attachment to type V collagen (8). Shorter
    transcripts encode M CSF
    that lacks cleavage and PG sites and produces an Nglycosylated
    68 kDa TM dimer and a slowly produced 44 kDa secreted dimer (7).
    Although forms may vary in activity and halflife,
    all contain the Nterminal
    150 aa portion that is necessary and sufficient for interaction with the M CSF
    receptor
    (10, 11). The first 229 aa of mature mouse MCSF
    shares 87%, 83%, 82% and 81% aa identity with corresponding regions of rat, dog, cow and human MCSF,
    respectively (12, 13). Human MCSF
    is active in the mouse, but mouse MCSF
    is reported to be speciesspecific.
    M-CSF的重組小鼠細胞因子Recombinant Mouse M-CSF

    References:
    1. Pixley, F.J. and E.R. Stanley (2004) Trends Cell Biol. 14:628.
    2. Chitu, V. and E.R. Stanley (2006) Curr. Opin. Immunol. 18:39.
    3. Fixe, P. and V. Praloran (1997) Eur. Cytokine Netw. 8:125.
    4. Ryan, G.R. et al. (2001) Blood 98:74.
    5. Makrigiannakis, A. et al. (2006) Trends Endocrinol. Metab. 17:178.
    6. Nandi, S. et al. (2006) Blood 107:786.
    7. Rettenmier, C.W. and M.F. Roussel (1988) Mol. Cell Biol. 8:5026.
    8. Suzu, S. et al. (1992) J. Biol. Chem. 267:16812.
    9. Manos, M.M. (1988) Mol. Cell. Biol. 8:5035.
    10. Koths, K. (1997) Mol. Reprod. Dev. 46:31.
    11. Jang, MH.
    et al. (2006) J. Immunol. 177:4055.
    12. DeLamarter, J.F. et al. (1987) Nucleic Acids Res. 15:2389.
    13. Ladner, M.B. et al. (1988) Proc. Natl. Acad. Sci. USA 85:6706.

     

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