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ELK Biotechnology
SKU:ES7480
VASP (phospho Ser238) rabbit pAb
VASP (phospho Ser238) rabbit pAb
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Applications: WB;IHC;IF;ELISA
Reactivity: Human;Mouse;Rat
Source: Rabbit
Dilution: Western Blot: 1/500 - 1/2000. Immunohistochemistry: 1/100 - 1/300. ELISA: 1/20000. Not yet tested in other applications.
Immunogen: The antiserum was produced against synthesized peptide derived from human VASP around the phosphorylation site of Ser238. AA range:206-255
Storage_stability: -20°C/1 year
Clonality: Polyclonal
Isotype: IgG
Concentration: 1 mg/ml
Observed_band(KD): 46+50kD
Human_gene_id: 7408
Human_swiss_prot_no: P50552
Subcellular_location: Cytoplasm. Cytoplasm, cytoskeleton. Cell junction, focal adhesion. Cell junction, tight junction . Cell projection, lamellipodium membrane. Cell projection, filopodium membrane. Targeted to stress fibers and focal adhesions through interaction with a number of proteins including MRL family members. Localizes to the plasma membrane in protruding lamellipodia and filopodial tips. Stimulation by thrombin or PMA, also translocates VASP to focal adhesions. Localized along the sides of actin filaments throughout the peripheral cytoplasm under basal conditions. In pre-apoptotic cells, colocalizes with MEFV in large specks (pyroptosomes).
Other_name: VASP; Vasodilator-stimulated phosphoprotein; VASP
Background: Vasodilator-stimulated phosphoprotein (VASP) is a member of the Ena-VASP protein family. Ena-VASP family members contain an EHV1 N-terminal domain that binds proteins containing E/DFPPPPXD/E motifs and targets Ena-VASP proteins to focal adhesions. In the mid-region of the protein, family members have a proline-rich domain that binds SH3 and WW domain-containing proteins. Their C-terminal EVH2 domain mediates tetramerization and binds both G and F actin. VASP is associated with filamentous actin formation and likely plays a widespread role in cell adhesion and motility. VASP may also be involved in the intracellular signaling pathways that regulate integrin-extracellular matrix interactions. VASP is regulated by the cyclic nucleotide-dependent kinases PKA and PKG. [provided by RefSeq, Jul 2008],
Reactivity: Human;Mouse;Rat
Source: Rabbit
Dilution: Western Blot: 1/500 - 1/2000. Immunohistochemistry: 1/100 - 1/300. ELISA: 1/20000. Not yet tested in other applications.
Immunogen: The antiserum was produced against synthesized peptide derived from human VASP around the phosphorylation site of Ser238. AA range:206-255
Storage_stability: -20°C/1 year
Clonality: Polyclonal
Isotype: IgG
Concentration: 1 mg/ml
Observed_band(KD): 46+50kD
Human_gene_id: 7408
Human_swiss_prot_no: P50552
Subcellular_location: Cytoplasm. Cytoplasm, cytoskeleton. Cell junction, focal adhesion. Cell junction, tight junction . Cell projection, lamellipodium membrane. Cell projection, filopodium membrane. Targeted to stress fibers and focal adhesions through interaction with a number of proteins including MRL family members. Localizes to the plasma membrane in protruding lamellipodia and filopodial tips. Stimulation by thrombin or PMA, also translocates VASP to focal adhesions. Localized along the sides of actin filaments throughout the peripheral cytoplasm under basal conditions. In pre-apoptotic cells, colocalizes with MEFV in large specks (pyroptosomes).
Other_name: VASP; Vasodilator-stimulated phosphoprotein; VASP
Background: Vasodilator-stimulated phosphoprotein (VASP) is a member of the Ena-VASP protein family. Ena-VASP family members contain an EHV1 N-terminal domain that binds proteins containing E/DFPPPPXD/E motifs and targets Ena-VASP proteins to focal adhesions. In the mid-region of the protein, family members have a proline-rich domain that binds SH3 and WW domain-containing proteins. Their C-terminal EVH2 domain mediates tetramerization and binds both G and F actin. VASP is associated with filamentous actin formation and likely plays a widespread role in cell adhesion and motility. VASP may also be involved in the intracellular signaling pathways that regulate integrin-extracellular matrix interactions. VASP is regulated by the cyclic nucleotide-dependent kinases PKA and PKG. [provided by RefSeq, Jul 2008],
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