mature leukemia inhibitory factor (LIF) of mouse origin, lyophilizedavailable as 106 units (10 µg) (sc-4989) or 5x106 units (50 µg) (sc-4989A)potent inhibitor of spontaneous embryonic mouse stem cell differentiation and useful for in vitro maintenance of the pluripotential phenotype of ES cells1000 U per 1 ml of tissue culture media is required to maintain mouse ES cells with a stem cell phenotype; 106 units is sufficient for 1 L of tissue culture media, 107 units is sufficient for 10 L of tissue culture mediaproduced in E. coli as a GST-tagged fusion protein; GST tag is cleaved and LIF is purified by HPLC chromatography>95% pure by SDS-PAGE and 0.22 micron sterile filtered prior to lyophilization; tested negative for mycoplasmasMature, biologically active, recombinant LIF is indistinguishable from native LIF in its biological activities in vitro.Leukemia Inhibitory Factor (LIF) is an important cell culture supplement. LIF suppresses spontaneous differentiation thereby promoting long-term maintenance of embryonic stem cells. Additional LIF functions include stem cell pluripotency control, cholinergic neuron differentiation, metabolism of bone and fat, promotion of megakaryocyte production and mitogenesis of certain factor dependent cell lines in vivo.
mature leukemia inhibitory factor (LIF) of human origin, lyophilizedavailable as 106 units (10 µg) (sc-4988) or 5x106 units (50 µg) (sc-4988A)potent inhibitor of spontaneous embryonic mouse and human stem cell differentiation and useful for in vitro maintenance of the pluripotential phenotype of ES cells; equal activity on both human and mouse cell lines1000 U per 1 ml of tissue culture media is required to maintain ES cells with a stem cell phenotype; 106 units is sufficient for 1 L of tissue culture media, 107 units is sufficient for 10 L of tissue culture mediaproduced in E. coli as a GST-tagged fusion protein; GST tag is cleaved and LIF is purified by HPLC chromatography>95% pure by SDS-PAGE and 0.22 micron sterile filtered prior to lyophilization; tested negative for mycoplasmasMature, biologically active, recombinant LIF is indistinguishable from native LIF in its biological activities in vitro.Leukemia Inhibitory Factor (LIF) is an important cell culture supplement. LIF suppresses spontaneous differentiation thereby promoting long-term maintenance of embryonic stem cells. Additional LIF functions include stem cell pluripotency control, cholinergic neuron differentiation, metabolism of bone and fat, promotion of megakaryocyte production and mitogenesis of certain factor dependent cell lines in vivo.
heterodimer protein corresponding to 463 amino acids of HGFα and 234 amino acids of HGFβ of human origin, 10 µg84 kDa biologically active protein purified from insect lysatesbiologically active as determined by the dose-dependent stimulation of the proliferation of monkey 4MBr-5 cells was found to be in the range of 20.0-40.0 ng/ml
68 amino acid portion of RANTES protein of mouse origin, 50 µg35 kDa biologically active, tagged fusion protein purified from bacterial lysatesbiological activity determined by its ability to chemoattract total human lymphocyte population and total murine T cell population using a concentration range of 1.0-10 mg/ml
108 amino acid protein fragment of PDGF-B of human origin, 50 µg39 kDa, biologically active, tagged fusion protein purified from bacterial lysatesED50 as determined by the dose-dependent stimulation of thymidine uptake by BALB/c 3T3 cells is 1.4 x 106 units/mg
125 amino acid protein fragment of PDGF-A of human origin, 50 µg41 kDa, biologically active, tagged fusion protein purified from bacterial lysatesED50 as determined by the dose-dependent stimulation of thymidine uptake by BALB/c 3T3 cells is 1.4 x 106 units/mg
119 amino acid fragment of NT-3 of human origin, 50 µg40 kDa, biologically active tagged fusion protein dimerpurified from bacterial lysatesbiological activity determined by the dose-dependent induction of choline acetyl transferase activity in rat basal forebrain primary septal cell cultures: ED50 = 20-50 ng/ml
147 amino acid protein representing full length mature Ob of mouse origin, 1000 µg16 kDa, biologically active protein purified from bacterial lysatesbiologically active in two different mouse obesity models
147 amino acid protein representing full length mature Ob of human origin, 1000 µg16 kDa, biologically active protein purified from bacterial lysatesbiologically active in the ob/ob mouse obesity model
125 amino acid protein representing full length mature MCP-1 of mouse origin, 10 µg13.8 kDa, biologically active protein purified from bacterial lysatesbiological activity determined by its ability to chemoattract BALB/c mouse spleen MNCs using a concentration range of 1-20 ng/ml
115 amino acid protein representing full length mature IL-15 of mouse origin, 10 µg13.3 kDa, biologically active protein purified from bacterial lysatesED50 was determined by the stimulation of the proliferation of murine CTLL-2 cells is 2 x 105 units/mg
homodimeric protein containing two 159 amino acid polypeptide subunits of M-CSF of human origin, 10 µg36.8 kDa, biologically active, tagged fusion protein purified from bacterial lysatesbiological activity determined by a cell proliferation assay using M-CSF-dependent murine monocytic cell line, M-NSF-60: ED50 = 0.5 - 1.5 ng/ml
156 amino acid protein representing full length mature TNFα of mouse origin, 50 µg42 kDa, biologically active protein purified from bacterial lysatesED50 as determined by the cytolysis of murine L929 cells in the presence of Actinomycin D is 1 x 107 units/mg
104 amino acid protein fragment of SAA of human origin, 50 µg11.7 kDa, biologically active protein purified from bacterial lysatesFor most in vitro applications, SAA exerts its biological activity in the concentration range of 10-50 µg/ml
dimer formed by two identical 92 amino acid subunits of resistin of human origin, 25 µg19.5 kDa, biologically active protein dimer purified from bacterial lysates
dimer formed by two identical 134 amino acid subunits of GDNF of human origin, 10 µg30.4 kDa, biologically active protein dimerpurified from bacterial lysatesbiological activity determined by the dose-dependent dopamine uptake by rat mesencephalic cultures
145 amino acid protein fragment of Acrp30 of murine origin, 25 µg16 kDa, biologically active protein purified from bacterial lysatesbiological activity determined by its ability to inhibit the proliferation of murine myeloid cell lines M1; ED50 < 3 µg/ml
155 amino acid protein fragment corresponding to an extracellular domain of Flt 3-L of human origin, 10 µg17.6 kDa, biologically active protein purified from bacterial lysatesbiological activity determined by the dose-dependent stimulation of the proliferation of human AML5 cells: ED50 < 1.0 ng/ml
156 amino acid protein fragment corresponding to an extracellular domain of FAS of human origin, 50 µg44 kDa, biologically active, tagged fusion protein purified from bacterial lysatesbiological activity determined by its ability to inhibit the cytotoxicity of Jurkat cells: ED50 is between 10-15 µg/ml in the presence of 2 ng/ml of human FAS-L.
175 amino acid protein fragment corresponding to an extracellular domain of FAS-L of human origin, 50 µg47 kDa, biologically active, tagged fusion protein purified from bacterial lysatesbiological activity determined by its ability to induce cytotoxicity in Jurkat cells in the absence of any cross-linkingED50 for this effect is 1 x 105 units/mg
53 amino acid protein representing full length EGF of mouse origin, 500 µg33 kDa, biologically active protein purified from bacterial lysatesED50 as determined by the dose-dependent stimulation of thymidine uptake by BALB/c 3T3 cells is 1.4 x 106 units/mg
45 amino acid protein fragment of β-defensin 3 of human origin, 50 µg32 kDa, biologically active, tagged fusion protein purified from bacterial lysatesbiological activity determined by anti-microbial activity against gram-positive bacteria S. aureus and gram-negative P. aeruginosa and E. coli
41 amino acid protein fragment of β-defensin 2 of human origin, 20 µg4.3 kDa, biologically active protein purified from bacterial lysatesbiological activity determined by its ability to chemoattract immature dendritic cells
full length Bad of human origin corresponding to amino acids 1-168, 50 µg45 kDa tagged fusion proteinRecognition Motif: S/T-X-X-E and K/R-X-X-S/TWestern blotting control for sc-942, sc-6541, sc-6542, sc-7869 and sc-8044
72 amino acid human SDF-1β protein, 10 µg8.5 kDa, biologically active protein purified from bacterial lysatesbiological activity determined by its ability to chemoattract human peripheral T cells activated with PHA and IL-2 using a concentration range of 20-80 ng/ml
68 amino acid human SDF-1α protein, 50 µg35 kDa, biologically active, tagged fusion protein purified from bacterial lysatesbiological activity determined by its ability to chemoattract human peripheral T cells activated with PHA and IL-2 using a concentration range of 20-80 ng/ml
68 amino acid human RANTES protein, 50 µg35 kDa, biologically active, tagged fusion protein purified from bacterial lysatesbiological activity determined by its ability to chemoattract human blood monocytes using a concentration range of 1.0–10.0 ng/ml
165 amino acid human IFN-α2a protein, 100 µg19.2 kDa, biologically active protein purified from bacterial lysatesbiological activity determined by viral resistance assay: specific activity = 2.7 x 108 IU/mg
124 amino acid mouse GM-CSF protein, 50 µg41 kDa, biologically active, tagged fusion protein purified from bacterial lysatesbiological activity determined by the dose-dependent stimulation of the proliferation of murine FDC-P1 cells: ED50 < 0.2 ng/ml
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