Phospho-SSH3 (Ser37) Antibody
Purified Rabbit Polyclonal Antibody (Pab)
- SPECIFICATION
- CITATIONS
- PROTOCOLS
- BACKGROUND
Application
| WB, E |
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Primary Accession | Q8TE77 |
Reactivity | Human |
Host | Rabbit |
Clonality | polyclonal |
Isotype | Rabbit IgG |
Calculated MW | 72996 Da |
Gene ID | 54961 |
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Other Names | Protein phosphatase Slingshot homolog 3, 3.1.3.16, 3.1.3.48, SSH-like protein 3, SSH-3L, hSSH-3L, SSH3, SSH3L |
Target/Specificity | This Phospho-SSH3 (Ser37) antibody is generated from a rabbit immunized with a KLH conjugated synthetic peptide between 10-43 amino acids from human SSH3. |
Dilution | WB~~1:500 |
Format | Purified polyclonal antibody supplied in PBS with 0.09% (W/V) sodium azide. This antibody is purified through a protein A column, followed by peptide affinity purification. |
Storage | Maintain refrigerated at 2-8°C for up to 2 weeks. For long term storage store at -20°C in small aliquots to prevent freeze-thaw cycles. |
Precautions | Phospho-SSH3 (Ser37) Antibody is for research use only and not for use in diagnostic or therapeutic procedures. |
Name | SSH3 |
---|---|
Synonyms | SSH3L |
Function | Protein phosphatase which may play a role in the regulation of actin filament dynamics. Can dephosphorylate and activate the actin binding/depolymerizing factor cofilin, which subsequently binds to actin filaments and stimulates their disassembly (By similarity). |
Cellular Location | Cytoplasm, cytoskeleton. Nucleus |
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Provided below are standard protocols that you may find useful for product applications.
Background
Protein phosphatase which may play a role in the regulation of actin filament dynamics. Can dephosphorylate and activate the actin binding/depolymerizing factor cofilin, which subsequently binds to actin filaments and stimulates their disassembly (By similarity).
References
Niwa R.,et al.Cell 108:233-246(2002).
Ohta Y.,et al.Genes Cells 8:811-824(2003).
Ota T.,et al.Nat. Genet. 36:40-45(2004).
Matsuoka S.,et al.Science 316:1160-1166(2007).
Daub H.,et al.Mol. Cell 31:438-448(2008).
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