|
|
GENTAUR
 +32 1658 9045
or
0032 (0)16 41 44 07
 +32 1650 9045
[email protected]
Av. de l' Armée 68
B-1040 Brussels
BELGIUM
France
tel 01 43 25 01 50
fax01 43 25 01 60
9, rue Lagrange
75005 Paris
Italia
tel 02 36 00 65 93
fax 02 36 00 65 94
20135 Milano
Deutschland
tel +32 1658 9045
fax +32 1650 9045
Polska
Tel 058 710 33 44
Fax 00 32 16 50 90 45
ul. Grunwaldzka 88A/2
81-771 Sopot
日本
tel +81 78 386 0860
fax +81 78 306 0296
Minaatojimaminami-manchi
Chuo-ku, Kobe
065-0047
Österreich
+43720880899
Canada Montreal
+15149077481
Česká republika Praha
+420246019719
Danmark
+4569918806
Finland Helsset
+358942419041
Ελλάς Αθήνα
+302111768494
Magyarország Budapest
+3619980547
Ireland Dublin
+35316526556
Luxembourg
+35220880274
Nederland
+31208080893
Norge Oslo
+4721031366
Polska Warszawa
+48223988221
Sverige Stockholm
+46852503438
Schweiz Züri
+41435006251
US New York
+17185132983
Other Countries
0032 (0)16 41 44 07
|
|
| |
|
Recombinant Mouse Fibroblast Growth Factor-acidic (FGF-acidic)
(Cat. No.: C043)
Background:
FGF acidic, also known as FGF-1, ECGF, and HBGF-1, is a 17 kDa nonglycosylated member of the FGF family of mitogenic peptides. FGF acidic, which is produced by multiple cell types, stimulates the proliferation of all cells of mesodermal origin and many cells of neuroectodermal, ectodermal, and endodermal origin. It plays a number of roles in development, regeneration, and angiogenesis. FGF-acidic is a non-glycosylated heparin binding growth factor that is expressed in the brain, kidney, retina, smooth muscle cells, bone matrix, osteoblasts, astrocytes and endothelial cells. FGF-acidic has the ability to signal through all the FGF receptors.
Description:
Recombinant Mouse FGF-acidic produced in E. coli is a non-glycosylated polypeptide chain containing 140 amino acids and having a molecular mass of 15796 Dalton.
Quality Control:
Biological activity: The ED50 as determined by the dose-dependant stimulation of thymidine uptake by 3T3 cells in the presence of heparin was found to be less than 0.5 ng/ml, corresponding to a Specific Activity of 2.0 x 106 IU/mg.
Purity:Greater than 95% as determined by
(a) Analysis by HPLC.
(b) Analysis by reducing and non-reducing SDS-PAGE Silver Stained gel..
Amino-Acid Sequence: The sequence of the first five N-terminal amino acids was determined and was found to be Phe-Asn-Leu-Pro-Leu.
Endotoxin: Less than 0.1ng/µg (1 IEU/µg) of FGF-acidic.
Formulation:
Mouse FGF-acidic was lyophilized after extensive dialysis against PBS.
Storage:
Lyophilized rmFGF-acidic although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution rmFGF-acidic 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 avoid freeze-thaw cycles.
Reconstitution:
It is recommended to reconstitute the lyophilized rmFGF-acidic in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Latest Publications:
1: Development 2008 Jan;Vol 135(2)
FGF signals guide migration of mesenchymal cells, control skeletal morphogenesis [corrected] and regulate gastrulation during sea urchin development.
[Abstract] The sea urchin embryo is emerging as an attractive model to study morphogenetic processes such as directed migration of mesenchyme cells and cell sheet invagination, but surprisingly, few of the genes regulating these processes have yet been characterized. We present evidence that FGFA, the first FGF family member characterized in the sea urchin, regulates directed migration of mesenchyme cells, morphogenesis of the skeleton and gastrulation during early development. We found that at blastula stages, FGFA and a novel putative FGF receptor are expressed in a pattern that prefigures morphogenesis of the skeletogenic mesoderm and that suggests that FGFA is one of the elusive signals that guide migration of primary mesenchyme cells (PMCs). We first show that fgfA
expression is correlated with abnormal migration and patterning of the PMCs following treatments that perturb specification of the ectoderm along the oral-aboral and animal-vegetal axes. Specification of the ectoderm initiated by Nodal is required to restrict fgfA to the lateral ectoderm, and in the absence of Nodal, fgfA is expressed ectopically throughout most of the ectoderm. Inhibition of either FGFA, FGFR1 or FGFR2 function severely affects morphogenesis of the skeleton. Furthermore, inhibition of FGFA and FGFR1 signaling dramatically delays invagination of the archenteron, prevents regionalization of the gut and abrogates formation of the stomodeum. We identified several genes acting downstream of fgfA in these processes, including the transcription factors pea3 and pax2/5/8 and the
signaling molecule sprouty in the lateral ectoderm and SM30 and SM50 in the primary mesenchyme cells. This study identifies the FGF signaling pathway as an essential regulator of gastrulation and directed cell migration in the sea urchin embryo and as a key player in the gene regulatory network directing morphogenesis of the skeleton.
2: Acta Cir Bras ;Vol 22
Effects of the basic fibroblast growth factor and its anti-factor in the healing and collagen maturation of infected skin wound.
[Abstract] PURPOSE: The infection is one of the main factors that affect the physiological evolution of the surgical wounds. The aim of this work is to evaluate the effects of fibroblast growth factor (FGFa) and anti-FGFa in the healing, synthesis and maturation of collagen when topically used on infected skin wounds of rats. METHODS: An experimental study was performed in 60 male Wistar rats. All animals were divided in two groups (A and B). Each group was divided in three subgroups A1, B1; A2, B2 and A3, B3. After anesthesia with pentobarbital, two open squared wounds (1cm(2)), 4 cm distant to each other, were done in the dorsal skin of all the rats. In group A (n=30) the wounds were contaminated with multibacterial standard solution, and in group B(n=30) the wounds
were maintained sterile. These wounds were named F1 (for inflammation analysis) and F2 (for collagen study). The open wounds of A1 and B1 rats were topically treated with saline solution, A2 and B2 were treated with FGFa and subgroups A3 and B3 were treated with FGFa and anti-FGFa. The rats were observed until complete epitelization of F2 wounds for determination of healing time and the expression of types I and III collagen, using Picro Sirius Red staining. Inflammatory reaction in F1 wounds was studied using hematoxilineosin staining. The three variable was measured by the Image Pro-Plus Média Cybernetics software. The statistical analysis was performed by ANOVA and Tukey test, considering p<0.05 as significant. RESULTS: It was observed that infection retarded significantly (p<0.05) the
time of wound scarring and the topical application of FCFb reverted the inhibition of healing caused by bacteria. The inflammatory reaction was greater in the subgroup B2 than in B1 and A3, and the difference was significant (p<0.05). It was observed greater expression of type I collagen in all the subgroups treated with FCFb, when compared with the untreated subgroups. Type III collagen was significantly decreased in wounds of B3 rats, comparing to the other subgroups. CONCLUSIONS: The FCFb accelerated the healing of open infected wounds and contributed with maturation of collagen, enhancing the type I collagen density. The anti-FCFb antibody was able to attenuate the production of both type I and III collagen.
3: J Cell Physiol 2007 Jun;Vol 211(3)
Reduced chondrogenic potential of adipose tissue derived stromal cells correlates with an altered TGFbeta receptor and BMP profile and is overcome by BMP-6.
[Abstract] Recent interest has focused on mesenchymal stem cells (MSC) for tissue engineering and regenerative therapy of cartilage defects. MSC originating from adipose tissue (ATSC) are attractive as they are easily available and abundant. They have similar properties like bone marrow derived MSC (BMSC), except for a reduced chondrogenic potential under standard culture conditions driven by TGFbeta. Aim of this study was to search for possible differences explaining the reduced differentiation capacity of ATSC and to eliminate it by adaptation of induction protocols. Expanded MSC were analyzed for their growth factor and related receptor repertoire and ATSC spheroid cultures were supplemented with BMP-2,-4,-6,-7, TGFbeta, FGFa, FGFb, IGF-1, and PTHrP alone or in
combination with TGFbeta. In contrast to BMSC, ATSC showed reduced expression of BMP-2, -4, and -6 mRNA and did not express TGFbeta-receptor-I protein. Consistent with this, increased concentrations of TGFbeta did not improve chondrogenesis of ATSC. BMP6 treatment induced TGFbeta-receptor-I expression and combined application of TGFbeta and BMP-6 eliminated the reduced chondrogenic potential of ATSC inducing a gene expression profile similar to differentiated BMSC. Like in BMSC, chondrogenesis of ATSC was associated with hypertrophy according to premature collagen Type X expression, upregulation of alkaline-phosphatase activity and in vivo calcification of spheroids after ectopic transplantation in SCID mice. In conclusion, a distinct BMP and TGFbeta-receptor repertoire may explain the
reduced chondrogenic capacity of ATSC in vitro, which could be compensated by exogenous application of lacking factors. Further studies should now be directed to induce chondrogenesis in the absence of hypertrophy.
4: J Biomed Mater Res A 2007
May;Vol 81(2)
Quantification of various growth factors in different demineralized bone matrix preparations.
[Abstract] Besides autografts, allografts, and synthetic materials, demineralized bone matrix (DBM) is used for bone defect filling and treatment of non-unions. Different DBM formulations are introduced in clinic since years. However, little is known about the presents and quantities of growth factors in DBM. Aim of the present study was the quantification of eight growth factors important for bone healing in three different "off the shelf" DBM formulations, which are already in human use: DBX putty, Grafton DBM putty, and AlloMatrix putty. All three DBM formulations are produced from human donor tissue but they differ in the substitutes added. From each of the three products 10 different lots were analyzed. Protein was extracted from the samples with Guanidine HCL/EDTA
method and human ELISA kits were used for growth factor quantification. Differences between the three different products were seen in total protein contend and the absolute growth factor values but also a large variability between the different lots was found. The order of the growth factors, however, is almost comparable between the materials. In the three investigated materials FGF basic and BMP-4 were not detectable in any analyzed sample. BMP-2 revealed the highest concentration extractable from the samples with approximately 3.6 microg/g tissue without a significant difference between the three DBM formulations. In DBX putty significantly more TGF-beta1 and FGFa were measurable compared to the two other DBMs. IGF-I revealed the significantly highest value in the AlloMatrix and PDGF in
Grafton. No differences were accessed for VEGF. Due to the differences in the growth factor concentration between the individual samples, independently from the product formulation, further analyzes are required to optimize the clinical outcome of the used demineralized bone matrix.
The related infomation not found or no info
|
 *NOTE: ALL PRODUCTS ARE FOR RESEARCH USE ONLY |
|
