抗FGF basic抗体(Anti-FGF Basic, Bovine, Rabbit-Poly antibody)

• 価格
• Product Details
• Applications and Data
• Related Product & Information
• Citations

価格

目次に戻る

Product Details

Species Reactivity	Bovine
Label	Unconjugated
Immunogen	Bovine brain-derived FGF acidic
Source	Polyclonal Rabbit IgG
Purification	Protein A or G purified
Specificity	Detects bovine FGF basic in direct ELISAs and Western blots. In direct ELISAs, approximately 5% cross-reactivity with FGF acidic and recombinant human (rh)  beta -ECGF is observed and less than 1% cross-reactivity with rhFGF-4, rhFGF-5, rhFGF-6, rhFGF-7, recombinant mouse (rm) FGF-8b, rmFGF-8c, rhFGF-9, rhFGF-10, rmFGF-15, rhFGF-17, and rhFGF-18 is observed. Neutralizes the biological activity of bovine FGF basic and will also neutralize the biological activity of recombinant human FGF basic.

目次に戻る

Applications and Data

	Recommended Concentration	Sample
Western Blot	1 µg/mL	Bovine FGF basic (Catalog # 133-FB)
Neutralization	Measured by its ability to neutralize FGF basic-induced proliferation in the NR6R‑3T3 mouse fibroblast cell line. Rizzino, A. et al. (1988) Cancer Res. 48:4266. The Neutralization Dose (ND50) is typically 1.5-4.5 µg/mL in the presence of 0.5 ng/mL Bovine FGF basic.

Neutralization

Cell Proliferation Induced by FGF basic and Neutralization by Bovine FGF basic Antibody. Bovine FGF basic (Catalog # 133-FB) stimulates proliferation in the NR6R‑3T3 mouse fibroblast cell line in a dose-dependent manner (orange line). Proliferation elicited by Bovine FGF basic (0.5 ng/mL) is neutralized (green line) by increasing concentrations of Rabbit Anti-Bovine FGF basic Polyclonal Antibody (Catalog # AB-33-NA). The ND50 is typically 1.5-4.5 µg/mL.

目次に戻る

Related Product & Information

Long Name	Fibroblast Growth Factor basic
Entrez Gene IDs	2247 (Human); 14173 (Mouse); 281161 (Bovine); 403857 (Canine); 100033955 (Equine)
Background	FGF basic
background_content	Background: FGF basic FGF basic is a member of the FGF family, currently comprised of seven related mitogenic proteins which show 35‑55% amino acid conservation. FGF acidic and basic, unlike the other members of the family, lack signal peptides and are apparently secreted by mechanisms other than the classical protein secretion pathway. FGF basic has been isolated from a number of sources, including neural tissue, pituitary, adrenal cortex, corpus luteum and placenta. This factor contains four cysteine residues but reduced FGF basic retains full biological activity, indicating that disulfide bonds are not required for this activity. Several reports indicate that a variety of forms of FGF basic are produced as a result of N-terminal extensions. These extensions apparently affect localization of FGF basic in cellular compartments but do not affect biological activity. Studies indicate that binding of FGF to heparin or cell surface heparan sulfate proteoglycans is necessary for binding of FGF to high affinity FGF receptors. FGF acidic and basic appear to bind to the same high affinity receptors and show a similar range of biological activities. FGF basic stimulates the proliferation of all cells of mesodermal origin, and many cells of neuroectodermal, ectodermal and endodermal origin. The cells include fibroblasts, endothelial cells, astrocytes, oligodendrocytes, neuroblasts, keratinocytes, osteoblasts, smooth muscle cells, and melanocytes. FGF basic is chemotactic and mitogenic for endothelial cells in vitro. FGF basic induces neuron differentiation, survival and regeneration. FGF basic has also been shown to be crucial in modulating embryonic development and differentiation. These observed in vitro functions of FGF basic suggest FGF basic may play a role in vivo in the modulation of such normal processes as angiogenesis, wound healing and tissue repair, embryonic development and differentiation, and neuronal function and neural degeneration. Additionally, FGF basic may participate in the production of a variety of pathological conditions resulting from excessive cell proliferation and excessive angiogenesis.

目次に戻る

Citations

1. Maternal obesity and overnutrition alter fetal growth rate and cotyledonary vascularity and angiogenic factor expression in the ewe.
   Authors: Ma Y, Zhu MJ, Zhang L, Hein SM, Nathanielsz PW, Ford SP
   Am. J. Physiol. Regul. Integr. Comp. Physiol., 2010;299(1):R249-58.
   Species: Ovine
   Sample Type: Whole Tissue
   Application: IHC Paraffin-embedded


2. Mediation of electronegative low-density lipoprotein signaling by LOX-1: a possible mechanism of endothelial apoptosis.
   Authors: Lu J, Yang JH, Burns AR, Chen HH, Tang D, Walterscheid JP, Suzuki S, Yang CY, Sawamura T, Chen CH
   Circ. Res., 2009;104(5):619-27.
   Species: Bovine
   Sample Type: Cell Lysates
   Application: WB


3. Dedicated epithelial recipient cells determine pigmentation patterns.
   Authors: Weiner L, Han R, Scicchitano BM, Li J, Hasegawa K, Grossi M, Lee D, Brissette JL
   Cell, 2007;130(5):932-42.
   Species: Mouse
   Sample Type: In Vivo
   Application: In vivo


4. Wnt regulation of progenitor maturation in the cortex depends on Shh or fibroblast growth factor 2.
   Authors: Viti J, Gulacsi A, Lillien L
   J. Neurosci., 2003;23(13):5919-27.
   Species: Mouse
   Sample Type: Whole Tissue
   Application: Neut

目次に戻る