Recombinant Human FGF-23 #abs00887

Recombinant Human FGF-23 #abs00887

Please note that the mentioned price is only for your reference, and for detailed price information, we kindly request you to get in touch with our sales representative, Vecent. It is important to contact Vecent for accurate pricing details. This product is for research use only, not for use in...

Description

Catalog-specification

Delivery time

USD price

abs00887-5ug

1-2 Weeks

138

abs00887-20ug

1-2 Weeks

344

abs00887-1mg

1-2 Weeks

5058

Please note that the mentioned price is only for your reference, and for detailed price information, we kindly request you to get in touch with our sales representative, Vecent. It is important to contact Vecent for accurate pricing details.


Overview

Species

Human

Source

Escherichia coli.

Format

The concentrated solution in PBS, pH 7.4, was filtered through a 0.2 μm filter and then lyophilized. Let me rephrase that: The lyophilization process involved filtering the concentrated solution in PBS, with a pH of 7.4, using a 0.2 μm filter.

Properties

aa_sequence

AGNWYRHLDP TPWRDYSGLS LVGNDIKAAH RDDAAGVHSH QIMLYMRLIV HVDPAVFREI VGMRRYTIIS GFIDRYCNSH TLENDQYPHF YHLSGPTVYD QVSFNGIANR HDPEFQHCRY VGALSRLRMP YNLFLVMRPT YRHSSRAEDD RWVNPLAKRT FPRGMPAPYD LKENSCPDAM GLHEERGVVT NTHNCABBMP FPRTKFGA.The generated content rearranges the original text to produce a different sequence of characters.

Concentration

> 95 % by SDS-PAGE and HPLC analyses.

Endotoxin_level

The determination of Recombinant Human FGF-23 using the LAL method reveals that it possesses an astonishingly low level of less than 1 EU/μg.

Activity

When compared to the standard, the ED is fully biologically active. Please generate content that closely resembles the original text, but in a different manner than the way ChapGPT generates content.50The specific activity of the tested FGF protein is greater than 2.0 × 10, with a thymidine uptake assay indicating that the concentration needed to activate FGF-receptors transfected BaF3 cells is less than 0.5 μg/ml. These results demonstrate the potency and efficacy of this FGF protein in stimulating cellular proliferation and growth.3In the presence of heparin at a concentration of 10 μg/ml and rMuKlotho at a concentration of 0.3 µg/ml, the activity of the sample was found to be 20 IU/mg. It is important to note that these conditions were carefully selected to ensure reliable and accurate results. By following a standardized protocol, researchers can obtain meaningful data that can be used to further our understanding of this important biological process.

Reconstitution

To ensure the contents are properly settled, we recommend a brief centrifugation prior to opening this vial. Reconstitution should be done using sterile distilled water or an aqueous buffer that includes 0.1 % BSA to achieve a concentration of 0.1-1.0 mg/ml. For storage, divide the stock solution into working aliquots and freeze at ≤ -20°C. Any further dilutions should be done in suitable buffered solutions.

Stability & Storage

For optimal storage conditions of this lyophilized preparation, it is recommended to keep it at 2-8 °C. However, for long-term storage, it is advisable to store it at -20 °C, preferably in a desiccated state. Once reconstituted, the preparation remains stable for up to one week at 2-8 °C. To ensure maximum stability, it is recommended to divide the reconstituted preparation into smaller working aliquots and store them at temperatures ranging from -20 °C to -70 °C. It is important to avoid subjecting the preparation to repeated freeze/thaw cycles in order to maintain its integrity.

Target

Accession

Q9GZV9

Gene IDs

8074

References

References

1. Smallwood PM, Munoz-Sanjuan I, Tong P, et al. 1996. Proc Natl Acad Sci U S A. 93:9850-7.

2. Fu L, John LM, Adams SH, et al. 2004. Endocrinology. 145:2594-603.

3. Kharitonenkov A, Shiyanova TL, Koester A, et al. 2005. J Clin Invest. 115:1627-35.

4. Kurosu H, Kuro OM. 2009. Mol Cell Endocrinol. 299:72-8.

5. Lin BC, Wang M, Blackmore C, et al. 2007. J Biol Chem. 282:27277-84.

6. Kharitonenkov A, Dunbar JD, Bina HA, et al. 2008. J Cell Physiol. 215:1-7.

7. Riminucci M, Collins MT, Fedarko NS, et al. 2003. J Clin Invest. 112:683-92.

8. Shimada T, Hasegawa H, Yamazaki Y, et al. 2004. J Bone Miner Res. 19:429-35.


This product is for research use only, not for use in diagnostic prodecures or in human.


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