The Wiskott-Aldrich syndrome (WAS) family of proteins share similar domain structure, and are involved in transduction of signals from receptors on the cell surface to the actin cytoskeleton.
The presence of a number of different motifs suggests that they are regulated by a number of different stimuli, and interact with multiple proteins.
Recent studies have demonstrated that these proteins, directly or indirectly, associate with the small GTPase, Cdc42, known to regulate formation of actin filaments, and the cytoskeletal organizing complex, Arp2/3, which can nucleate actin polymerization at sites that lead to branched actin structures.
These proteins have 48% identity in human with the highest homology in the functional regions of these proteins.
Serine and tyrosine phosphorylation regulates the activity of both proteins.
WASP is observed as a 63kD protein in hematopoietic cells, while N-WASP is observed as a 65kD in many tissues, especially brain.
Wiskott-Aldrich syndrome is a rare, inherited, X-linked, recessive disease characterized by immune dysregulation and microthrombocytopenia, and is caused by mutations in the WAS gene.
The WAS gene product is a cytoplasmic protein, expressed exclusively in hematopoietic cells, which show signalling and cytoskeletal abnormalities in WAS patients.
These clinical findings as well as the structural properties of WASP (including a cdc42 binding site, SH3 domain binding region and regions for actin cytoskeletal localization) suggest a pivotal role for WASP in regulating the structure and function of platelets and T-lymphocytes.
A transcript variant arising as a result of alternative promoter usage, and containing a different 5' UTR sequence, has been described, however, its full-length nature is not known.
Phosphorylation regulates the activity of both proteins.
Dual phosphorylation of WASP on serine 383 and 384 by casein kinases increase the affinity for the Arp2/3 complex.
Thus, dual serine phosphorylation may be important for formation of actin-based structures in various cell types.
Applications:Suitable for use in ELISA, Western Blot.
Other applications not tested.
Recommended Dilution:Western Blot: 1:1000ELISA: 1:2000Optimal dilutions to be determined by the researcher.
Storage and Stability:May be stored at 4°C for short-term only.
Aliquot to avoid repeated freezing and thawing.
Store at -20°C.
Aliquots are stable for 12 months after receipt.
For maximum recovery of product, centrifuge the original vial after thawing and prior to removing the cap.
仕様
Size：100ul
Host：rabbit
Source Antibody：human
Grade：Affinity Purified
Purity：Purified by immunoaffinity chromatography.
Form：Supplied as a liquid in PBS, 50% glycerol, 1mg/ml BSA, and 0.05% sodium azide.
Specificity：Recognizes a 63kD protein corresponding to the molecular mass of phosphorylated WASP and a 65kD protein corresponding to the molecular mass of phosphorylated N-WASP. Species Crossreactivity: human and rat brains. Species sequence homology: human WASP surrounding serine 383 and 384.
Isotype：IgG
Calc Applications Abbrev：E WB
Calc Crossreactivity：Hu Rt
Immunogen：Synthetic peptide, Phospho-N-WASP (Ser-484/Ser-485) (coupled to carrier protein).The Wiskott-Aldrich syndrome (WAS) family of proteins share similar domain structure, and are involved in transduction of signals from receptors on the cell surface to the actin cytoskeleton. The presence of a number of different motifs suggests that they are regulated by a number of different stimuli, and interact with multiple proteins. Recent studies have demonstrated that these proteins, directly or indirectly, associate with the small GTPase, Cdc42, known to regulate formation of actin filaments, and the cytoskeletal organizing complex, Arp2/3, which can nucleate actin polymerization at sites that lead to branched actin structures. These proteins have 48% identity in human with the highest homology in the functional regions of these proteins. Serine and tyrosine phosphorylation regulates the activity of both proteins. WASP is observed as a 63kD protein in hematopoietic cells, while N-WASP is observed as a 65kD in many tissues, especially brain.Wiskott-Aldrich syndrome is a rare, inherited, X-linked, recessive disease characterized by immune dysregulation and microthrombocytopenia, and is caused by mutations in the WAS gene. The WAS gene product is a cytoplasmic protein, expressed exclusively in hematopoietic cells, which show signalling and cytoskeletal abnormalities in WAS patients. These clinical findings as well as the structural properties of WASP (including a cdc42 binding site, SH3 domain binding region and regions for actin cytoskeletal localization) suggest a pivotal role for WASP in regulating the structure and function of platelets and T-lymphocytes. A transcript variant arising as a result of alternative promoter usage, and containing a different 5' UTR sequence, has been described, however, its full-length nature is not known. Phosphorylation regulates the activity of both proteins. Dual phosphorylation of WASP on serine 383 and 384 by casein kinases increase the affinity for the Arp2/3 complex. Thus, dual serine phosphorylation may be important for formation of actin-based structures in various cell types.Applications: Suitable for use in ELISA and Western Blot. Other applications not tested.Recommended Dilution:Western Blot: 1:1000ELISA: 1:2000Optimal dilutions to be determined by the researcher. Positive Controls: Jurkat cell lysate, rat brain, A431, human endothelial and SKN-SH cells.Storage and Stability:For long-term storage, aliquot and store at -20°C. Aliquots are stable for at least 24 months at -20°C. For maximum recovery of product, centrifuge the original vial after thawing and prior to removing the cap. Further dilutions can be made in assay buffer.
