Recombinant Human CD44v5 Fc Chimera Avi-tag Protein, CF
Recombinant Human CD44v5 Fc Chimera Avi-tag Protein, CF Summary
Learn more about Avi-tag Biotinylated ProteinsProduct Specifications
Human CD44v5 | IEGRMD | Human IgG1 (Pro100-Lys330 | Avi-tag |
N-terminus | C-terminus | ||
Analysis
Product Datasheets
Carrier Free
CF stands for Carrier Free (CF). We typically add Bovine Serum Albumin (BSA) as a carrier protein to our recombinant proteins. Adding a carrier protein enhances protein stability, increases shelf-life, and allows the recombinant protein to be stored at a more dilute concentration. The carrier free version does not contain BSA.
In general, we advise purchasing the recombinant protein with BSA for use in cell or tissue culture, or as an ELISA standard. In contrast, the carrier free protein is recommended for applications, in which the presence of BSA could interfere.
AVI10146
Formulation | Lyophilized from a 0.2 μm filtered solution in PBS with Trehalose. |
Reconstitution | Reconstitute at 500 μg/mL in PBS. |
Shipping | The product is shipped at ambient temperature. Upon receipt, store it immediately at the temperature recommended below. |
Stability & Storage: | Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
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Scientific Data
2 μg/lane of Biotinylated Recombinant Human CD44 Fc Chimera Avi-tag Protein (Catalog # AVI10146) was resolved with SDS-PAGE under reducing (R) and non-reducing (NR) conditions and visualized by Coomassie® Blue staining, showing bands at 100-120 kDa and 200‑240 kDa, respectively.
Reconstitution Calculator
Background: CD44
CD44, also known as extracellular matrix receptor III (ECMRIII), is a non-kinase transmembrane glycoprotein that regulates numerous functions including cell proliferation, adhesion, migration, hematopoiesis, and lymphocyte activation. Mature human CD44 consists of an extracellular domain (ECD) with a hyaluronan‑binding, disulfide-stabilized link region and a stem region, a transmembrane domain, and a cytoplasmic domain. The full-length ECD of human CD44 shares 63% amino acid sequence identity with mouse CD44. In humans, CD44 is encoded by 19 exons with 10 constant in all isoforms. The standard form of CD44 (CD44s) is encoded by the 10 constant exons and is the shortest and most abundantly expressed isoform. The remaining 9, variant exons of CD44 can undergo complex alternative splicing and are expressed in a cell-specific manner and in the pathophysiology of many diseases. The N-terminal ECD of CD44 contains a binding site for Hyaluronan (HA), the most common ligand of CD44. CD44 exhibits multiple different functions and is aberrantly up-regulated among diverse tumors. It can bind HA and function as a "platform" for growth factors and metalloproteinases. CD44 can function as a co-receptor that modifies activity of receptors including MET and the ERBB family of tyrosine kinases. Further, CD44 can link the plasma membrane to the actin cytoskeleton via the ERM. CD44 has been found to bind E- and L-selectin on tumor cells and E-selectin on neutrophils. Additionally, distinct variants of CD44 have been found to interact with LSECtin and potentially mediate its function in the immune system. Human CD44v5 contains exon 10 and is associated with tumor progression and metastasis in many cancer types and is considered a functional cancer biomarker. Our Avi-tag Biotinylated CD44 features biotinylation at a single site contained within the Avi-tag, a unique 15 amino acid peptide. Protein orientation will be uniform when bound to streptavidin-coated surface due to the precise control of biotinylation and the rest of the protein is unchanged so there is no interference in the protein's bioactivity.
- Ponta, H. et al. (2003) Nat. Rev. Mol. Cell Biol. 4:33.
- Senbanjo, L.T. and Chellaiah, M.A. (2017) Front Cell Dev Biol. 5:18.
- Chen, C. at al. (2018) J Hematol Oncol 11:64.
- Xu, H. et al. (2020) Hematol Oncol 9:36.
- Nagano, O. and H. Saya (2004) Cancer Sci. 95:930.
- Hanley, W.D. et al. (2005) Cancer Res. 65:5812.
- Katayama, Y. et al. (2005) J. Exp. Med. 18:1183.
- Tang, L. et al. (2010) Eur. J. Immunol. 40:1185.
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