Recombinant Human PTPRD Fc Chimera Protein, CF

When Recombinant Human PTPRD Fc Chimera is immobilizedat 1 μg/mL, 100 μL/well, Recombinant Human IL-1 RAPL1/IL-1 R8 FcChimera (Catalog # 9949-ML) binds with an ED50 of 1.5-9 ng/mL.

• Reactivity: Hu
• Applications: Bioactivity
• Format: Carrier-Free

Recombinant Human PTPRD Fc Chimera Protein, CF Summary

• Details of Functionality: Measured by its binding ability in a functional ELISA. When Recombinant Human PTPRD Fc Chimer is immobilized at 1 μg/mL, 100 μL/well, Recombinant Human IL-1 RAPL1/IL-1 R8 Fc Chimera (Catalog # 9949-ML) binds with an ED₅₀ of 1.5-9 ng/mL.
• Source: Human embryonic kidney cell, HEK293-derived human PTPRD protein
  

  Human PTPRD (Glu21-Ser1174) Accession # P23468	IEGRMD	Human IgG1 (Pro100-Lys330)
  N-terminus		C-terminus

• Accession #: P23468
• N-terminal Sequence: Glu21
• Structure / Form: Disulfide-linked homodimer
• Protein/Peptide Type: Recombinant Proteins
• Purity: >80%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.
• Endotoxin Note: <0.10 EU per 1 μg of the protein by the LAL method.

Applications/Dilutions

• Dilutions:
  • Bioactivity
• Theoretical MW: 154 kDa.
  Disclaimer note: The observed molecular weight of the protein may vary from the listed predicted molecular weight due to post translational modifications, post translation cleavages, relative charges, and other experimental factors.
• SDS-PAGE: 137-151 kDa, reducing conditions

Packaging, Storage & Formulations

• Storage:
  • 12 months from date of receipt, ≤ -20 °C as supplied.
  • 1 month, 2 to 8 °C under sterile conditions after reconstitution.
  • 3 months, ≤ -20 °C under sterile conditions after reconstitution.
• Buffer: Lyophilized from a 0.2 μm filtered solution in PBS with Trehalose.
• Purity: >80%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.
• Reconstitution Instructions: Reconstitute at 400 μg/mL in PBS.

Notes

This product is produced by and ships from R&D Systems, Inc., a Bio-Techne brand.

Alternate Names for Recombinant Human PTPRD Fc Chimera Protein, CF

• HPTPDELTA
• HPTPMGC119752
• MGC119750
• MGC119751
• protein tyrosine phosphatase, receptor type, D
• Protein-tyrosine phosphatase delta
• PTP delta
• PTPD
• PTPdelta
• PTP-delta
• PTPDMGC119753
• PTPRD
• receptor type, delta polypeptide
• receptor-type tyrosine-protein phosphatase delta
• R-PTP-Delta
• RPTP-Delta

Background

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).

1. Pulido, R. et al. (1995) Proc. Natl. Acad. Sci. USA 92:11686.
2. Östman, A. et al. (2006) Nature Reviews Cancer 6:307.
3. Kwon, SK. et al. (2010) J. Biol. Chem. 285:13966.
4. Valnegri, P. et al. (2011) Hum. Mol. Genet. 20:4797.
5. Ortiz, B. et al. (2014) Proc. Natl. Acad. Sci. USA. 111:8149.
6. Lin, Z. et al. (2018) Nat, Commun. 9:268.

Bioinformatics

• Uniprot:
  • P23468()