PTPRD Antibody
- SPECIFICATION
- CITATIONS
- PROTOCOLS
- BACKGROUND
Application
| WB, E |
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Primary Accession | P23468 |
Other Accession | NP_569075, 289547551 |
Reactivity | Human |
Host | Rabbit |
Clonality | Polyclonal |
Isotype | IgG |
Calculated MW | Predicted: 165, 210 kDa (130 kDa for cleavage product) Observed: 130 kDa |
Application Notes | PTPRD antibody can be used for detection of PTPRD by Western blot at 1 - 2 µg/mL. |
Gene ID | 5789 |
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Target/Specificity | PTPRD; PTPRD antibody is human specific. At least three alternatively spliced transcript variants encoding distinct isoforms have been observed. PTPRD cleavage products are often observed in vivo |
Reconstitution & Storage | PTPRD antibody can be stored at 4℃ for three months and -20℃, stable for up to one year. As with all antibodies care should be taken to avoid repeated freeze thaw cycles. Antibodies should not be exposed to prolonged high temperatures. |
Precautions | PTPRD Antibody is for research use only and not for use in diagnostic or therapeutic procedures. |
Name | PTPRD |
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Function | Can bidirectionally induce pre- and post-synaptic differentiation of neurons by mediating interaction with IL1RAP and IL1RAPL1 trans-synaptically. Involved in pre-synaptic differentiation through interaction with SLITRK2. |
Cellular Location | Membrane; Single-pass type I membrane protein. |
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Provided below are standard protocols that you may find useful for product applications.
Background
PTPRD Antibody: PTPRD (Protein tyrosine phosphatase receptor type D) is a member of the protein tyrosine phosphatase (PTP) family that plays diverse roles during development including cell growth, differentiation, mitotic cycle and oncogenic transformation. PTPRD contains an extracellular region, a single transmembrane segment and two tandem intracytoplasmic catalytic domains. The extracellular region of PTPRD is composed of three Ig-like and eight fibronectin type III-like domains (1,3). PTPRD interacts with PPFIA1-3 and is a tumor suppressor on chromosome 9p that is involved in the development of glioblastoma multiforme (GBMs) and multiple human cancers.
References
Krueger NX, Streuli M, and Saito H. Structural diversity and evolution of human receptor-like protein tyrosine phosphatases. EMBO J. 1990; 9:3241-52.
Fischer EH, Charbonneau H and Tonks NK. Protein tyrosine phosphatases: a diverse family of intracellular and transmembrane enzymes. Science 1991; 253:401-6.
Pan MG, Rim C, Lu KP et al. Cloning and expression of two structurally distinct receptor-linked protein-tyrosine phosphatases generated by RNA processing from a single gene. J. Biol. Chem. 1993; 268:19284-91.
Veeriah S, Brennan C, Meng S, et al. The tyrosine phosphatase PTPRD is a tumor suppressor that is frequently inactivated and mutated in glioblastoma and other human cancers. Proc. Natl. Acad. Sci. USA 2009; 106: 9435-40.
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