Chemical Name: (Z)-Pregna-4,17(20)-diene-3,16-dione
详细产品信息：
Biological Activity Broad spectrum steroid receptor ligand; mineralocorticoid, progesterone and glucocorticoid receptor antagonist (Ki values are 37, 224 and 252 nM respectively) and weak androgen receptor agonist (Ki = 315 nM). Induces apoptosis in prostate cancer cells and inhibits angiogenesis via suppression of the VEGF-VEGFR2-Akt signaling pathway. Exhibits antilipidemic activity via antagonism of the farnesoid X receptor (FXR) and displays antiseptic, antirheumatic and anti-inflammatory activity in vivo. More active isomer of guggulsterone (Cat. No. 2013).
Technical Data
M.Wt:
312.45
Formula:
C21H28O2
Solubility:
Soluble to 20 mM in DMSO with gentle warming and to 10 mM in ethanol with gentle warming
Purity:
>98%
Storage:
Store at RT
CAS No:
39025-23-5
The technical data provided above is for guidance only. For batch specific data refer to the Certificate of Analysis. All Tocris products are intended for laboratory research use only.
Recombinant Rat FGF basic ，Recombinant Human FGF basic ，Recombinant Human KGF/FGF-7，Recombinant Human/Mouse FGF-8b
详细介绍
DESCRIPTION Source E. coliderived Ala11Ser154 Accession # P13109 Nterminal Sequence Analysis Ala11 Predicted Molecular Mass 16.2 kDa SPECIFICATIONS Activity Measured in a cell proliferation assay using NR6R-3T3 mouse fibroblast cells. Rizzino, A. et al. （1988） Cancer Res. 48:4266; Thomas, K. et al. （1987） Methods Enzymol. 147:120. The ED50 for this effect is typically 0.31.8 ng/mL. Endotoxin Level <1.0 EU per 1 μg of the protein by the LAL method. Purity >95%, by SDSPAGE under reducing conditions and visualized by silver stain. Formulation Lyophilized from a 0.2 μm filtered solution in MOPS, Na2SO4, EDTA and DTT 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 FGF basic （FGF2, HBGF2） is one of at least 22 mitogenic proteins of the FGF family, which show 35 60% amino acid conservation （1 3）. Unlike other FGFs, FGF acidic and basic lack signal peptides and are secreted by an alternate pathway. Storage pools within the cell or on cell surface heparan sulfate proteoglycans （HSPG） are likely. The predicted 18 kDa FGF basic isoform can be located in both the cytoplasm and the nucleus and is presumed to be the form secreted （4）. Transcription from alternate start sites produces 21 23 kDa forms found only in the nucleus. High and low molecular weight human FGF basic targets the expression of different genes when expressed in NIH3T3 cells （5）. The 18 kDa rat sequence has 98% amino acid （aa） identity with mouse, and 96 97% aa identity with human, bovine and sheep FGF basic （6, 7）. Autocrine, intracrine and paracrine actions of FGF basic have been identified. Binding of FGF to heparin or cell surface HSPG is necessary for binding, dimerization and activation of tyrosine kinase FGF receptors. FGF basic binds other proteins, polysaccharides and lipids with lower affinity （3）. Expression of FGF basic is nearly ubiquitous but disruption of the mouse FGF basic gene gives a relatively mild phenotype, suggesting compensation by other FGF family members. FGF basic modulates such normal processes as angiogenesis, wound healing and tissue repair, embryonic development and differentiation, neuronal function and neural degeneration. Transgenic overexpression of FGF basic results in excessive proliferation and angiogenesis reminiscent of a variety of pathological conditions （1 3）. References: 1. Coulier, F. et al. （1997） J. Mol. Evol. 44:43. 2. Fernig, D. et al. （1994） Prog. Growth Factor Res. 5:353. 3. Presta, M. et al. （2005） Cytokine Growth Factor Rev. 16:159. 4. Claus, P. et al. （2003） J. Biol. Chem. 278:479. 5. Quarto, N. et al. （2005） Gene 356:49. 6. Tsuneto, M. et al. （2005） Biochem. Biophys. Res. Commun. 335:1239. 7. Shimasaki, S. et al. （1988） Biochem. Biophys. Res. Commun. 157:256. Recombinant Rat FGF basic Catalog Number: 3339-FB
DESCRIPTION Source E. coliderived Asn974Arg1026, with an Nterminal Met Accession # P07522 Nterminal Sequence Analysis Met Predicted Molecular Mass 6.3 kDa SPECIFICATIONS Activity Measured in a cell proliferation assay using Balb/3T3 mouse embryonic fibroblast cells. Rubin, J.S. et al. （1991） Proc. Natl. Acad. Sci. USA 88:415. The ED50 for this effect is typically 1060 pg/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 Acetonitrile and TFA with BSA as a carrier protein. See Certificate of Analysis for details. PREPARATION AND STORAGE Reconstitution Reconstitute at 100 μg/mL in sterile 10 mM Acetic Acid 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 Epidermal growth factor （EGF） is the founding member of the EGF family that also includes TGFα, amphiregulin （AR）, betacellulin （BTC）, epiregulin （EPR）, heparinbinding EGFlike growth factor（HBEGF）, epigen, and the neuregulins （NRG）1 through 6 （1）. Members of the EGF family share a structural motif, the EGFlike domain, which is characterized by three intramolecular disulfide bonds that are formed by six similarly spaced conserved cysteine residues （2）. All EGF family members are synthesized as type I transmembrane precursor proteins that may contain several EGF domains in the extracellular region. The mature proteins are released from the cell surface by regulated proteolysis （1）. The 1133 amino acid （aa） rat EGF precursor contains nine EGF domains and nine LDLR class B repeats. The mature protein consists of 53 aa and is generated by proteolytic excision of the EGF domain proximal to the transmembrane region （3）. Mature rat EGF shares 70% and 77% aa sequence identity with mature human and mouse EGF, respectively. EGF is present in various body fluids, including blood, milk, urine, saliva, seminal fluid, pancreatic juice, cerebrospinal fluid, and amniotic fluid （4）. Four ErbB （HER） family receptor tyrosine kinases including EGFR/ErbB1, ErbB2, ErbB3 and ErbB4, mediate responses to EGF family members （5）. These receptors undergo a complex pattern of ligand induced homoor heterodimerization to transduce EGF family signals （6, 7）. EGF binds ErbB1 and depending on the context, induces the formation of homodimers or heterodimers containing ErbB2. Dimerization results in autophosphorylation of the receptor at specific tyrosine residues to create docking sites for a variety of signaling molecules （5, 8）. Biological activities ascribed to EGF include epithelial development, angiogenesis, inhibition of gastric acid secretion, fibroblast proliferation, and colony formation of epidermal cells in culture. References: 1. Harris, R.C. et al. （2003） Exp. Cell Res. 284:2. 2. Carpenter, G. and Cohen, S. （1990） J. Biol. Chem. 265:7709. 3. Saggi, S.J. et al. （1992） DNA Cell Biol. 11:481. 4. Carpenter, G. and Zendegui, J.G. （1986） Exp. Cell Res. 164:1. 5. Jorissen, R.N. et al. （2003） Exp. Cell Res. 284:31. 6. Gamett, D.C. et al. （1997） J. Biol. Chem. 272:12052. 7. Qian, X. et al. （1994） Proc. Natl. Acad. Sci. 91:1500. 8. Qian, X. et al. （1999） J. Biol. Chem. 274:574. Recombinant Rat EGF Catalog Number: 3214-EG www.
RD Recombinant human IL-17A人白介17因子Source E. coliderived此产品还有小鼠IL-17A
详细介绍
RD Recombinant human IL-17A人白介17因子
DESCRIPTION Source E. coliderived Thr22Ala158 Accession # Q62386.1 Nterminal Sequence Analysis Thr22 Structure / Form Disulfidelinked homodimer Predicted Molecular Mass 15.5 kDa （monomer） SPECIFICATIONS Activity Measured by its ability to induce IL6 secretion by NIH-3T3 mouse embryonic fibroblast cells. Yao, Z. et al. （1995） Immunity 3:811. The ED50 for this effect is typically 0.251.25 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 Acetonitrile and TFA with BSA as a carrier protein. See Certificate of Analysis for details. PREPARATION AND STORAGE Reconstitution Reconstitute at 25 μg/mL in sterile 4 mM HCl 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 Interleukin 17 （also known as CTLA8） is a T cellexpressed pleiotropic cytokine that exhibits a high degree of homology to a protein encoded by the ORF13 gene of herpesvirus Saimiri. cDNA clones encoding IL17 have been isolated from activated rat, mouse and human T cells. Mouse IL17 cDNA encodes a 158 amino acid （aa） residue precursor protein with a 21 amino acid residue signal peptide that is cleaved to yield the 137 aa residue mature IL17. Both recombinant and natural IL17 have been shown to exist as disulfide linked homodimers. At the amino acid level, mIL17 shows 57% and 87% sequence identity with herpesvirus and rat IL17, respectively. An IL17 specific mouse cell surface receptor （IL17 R） has been cloned. While the expression of IL17 mRNA is restricted to activated alpha beta TCR+CD4CD8T cells, the expression of mIL17 R mRNA has been detected in virtually all cells and tissues tested. IL17 exhibits multiple biological activities on a variety of cells including: the induction of IL6 and IL8 production in fibroblasts? the enhancement of surface expression of ICAM1 in fibroblasts? activation of NFκB and costimulation of T cell proliferation. References: 1. Kennedy, J. et al., （1996） J. Interferon Cytokine Res. 16:611. 2. Yao, Z. et al., （1995） J. Immunol. 155:5483. 3. Yao, Z. et al., （1995） Immunity 3:811. 4. Rouvier, E. et al., （1993） J. Immunol. 150:5445.
