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| Cat.No | ACP20573 | Target Name | PTP4A3 |
|---|---|---|---|
| Form | Lyophilized powder | Expression System | Custom Production. Please inquire and provide the desire expression system. |
| Expression Range | 1-170 | Protein Length | Full length protein |
| Purity | >85% (SDS-PAGE) | Storage Buffer | 5%-50% glycerol. Lyophilized powder form: the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, Liquid form: default storage buffer is Tris/PBS-based buffer, pH 8.0. |
| Target Species | Human | Uniprot ID | O75365 |
|---|
Uniprot Id
O75365
Target Species
Human
Target Name
PTP4A3
Target Full Name
Protein tyrosine phosphatase type IVA 3
Target Function
Protein tyrosine phosphatase which stimulates progression from G1 into S phase during mitosis. Enhances cell proliferation, cell motility and invasive activity, and promotes cancer metastasis. May be involved in the progression of cardiac hypertrophy by inhibiting intracellular calcium mobilization in response to angiotensin II.
Target Subcellular Location
Cell membrane. Early endosome.
Target Protein Families
Protein-tyrosine phosphatase family
Target Tissue Specificity
Mainly expressed in cardiomyocytes and skeletal muscle; also found in pancreas. Consistently overexpressed in colon cancer metastasis.
Target Synonyms
Potentially prenylated protein tyrosine phosphatase; PRL 3; PRL R; PRL-3; PRL-R; PRL3; PRLR; Protein tyrosine phosphatase 4a3; Protein tyrosine phosphatase type IVA 3; Protein-tyrosine phosphatase 4a3; Protein-tyrosine phosphatase of regenerating liver 3; PTP 4A3; PTP4A3; TP4A3_HUMAN
Target Background
This gene encodes a member of the protein-tyrosine phosphatase family. Protein tyrosine phosphatases are cell signaling molecules that play regulatory roles in a variety of cellular processes. Studies of this class of protein tyrosine phosphatase in mice demonstrates that they are prenylated in vivo, suggesting their association with cell plasma membrane. The encoded protein may enhance cell proliferation, and overexpression of this gene has been implicated in tumor metastasis. Alternative splicing results in multiple transcript variants.
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