Recombinant Human PTPRD Fc Chimera Protein, CF Summary
Accession # P23468
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.
|Formulation||Lyophilized from a 0.2 μm filtered solution in PBS with Trehalose.|
|Reconstitution||Reconstitute at 400 μg/mL in PBS.|
|Shipping||The product is shipped at ambient temperature. Upon receipt, store it immediately at the temperature recommended below.|
|Stability & Storage:||
Human protein-tyrosine phosphatase delta (PTPRD) is a type I membrane protein. It contains a 1245 amino acid (aa) long extracellular domain (ECD), a 25 amino acid long transmembrane domain, and a 622 amino acid cytoplasmic domain. A cleavage during post-translational modification separates the extracellular domain from the transmembrane segment through a process called "ectodomain shedding" (1). The extracellular regions are comprised of three Ig-like C2 domains followed immediately by eight fibronectin type-III like domains (1). The human PTPRD extracellular domain shares 98% and 62% aa identity with mouse and rat PTPRD, respectively. Protein-tyrosine phosphatases (PTPs) constitute a structurally diverse family of tightly regulated enzymes with important regulatory roles (1-6). PTPRD is a member of the PTPs and is detected in brain and other tissues including colon and breast (1). It has been demonstrated that phosphorylated STAT3 (p-STAT3) is a direct substrate of PTPRD and that cancer-specific mutations in PTPRD abrogate its ability to dephosphorylate STAT3 (5). PTPRD interacts with NGL-3 (Netrin-G ligand-3) via its first two FNIII repeats to promote synapse formation (3). PTPRD can also bind to IL1RAPL1 and its paralog IL1RAPL2; the IL1RAPL1/PTPRD complex recruits RhoGAP2 at excitatory synapses to induce dendritic spine formation (4). Recent studies have indicated SALM5 forms heterotetramer with PTPRD to induce synaptic differentiation (6).
- Pulido, R. et al. (1995) Proc. Natl. Acad. Sci. USA 92:11686.
- Östman, A. et al. (2006) Nature Reviews Cancer 6:307.
- Kwon, SK. et al. (2010) J. Biol. Chem. 285:13966.
- Valnegri, P. et al. (2011) Hum. Mol. Genet. 20:4797.
- Ortiz, B. et al. (2014) Proc. Natl. Acad. Sci. USA. 111:8149.
- Lin, Z. et al. (2018) Nat, Commun. 9:268.
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