Paxillin is a signal transduction adaptor protein discovered in 1990 in the laboratory of Keith Burridge. Salgia et al.(1995) mapped the gene to 12q24 using fluorescence in situ hybridization.The C-terminal region of Paxillin contains four LIM domains that target paxillin to focal adhesions, it is presumed through a direct association with the cytoplasmic tail of beta-integrin. The N-terminal region is rich in proteinprotein interaction sites. The proteins that bind to Paxillin are diverse and include protein tyrosine kinases, such as Src and FAK, structural proteins, such as vinculin and actopaxin, and regulators of actin organization, such as COOL/PIX and PKL/GIT. Paxillin is tyrosine-phosphorylated by FAK and Src upon integrin engagement or growth factor stimulation, creating binding sites for the adapter protein Crk. The protein contains 4 LIM domains, a proline-rich domain containing a consensus SH3-binding site, and 3 potential SH2-binding sites.
Formulation
0.5mg/ml if reconstituted with 0.2ml sterile DI water
Host
Rabbit
Immunogen Region
Amino acids 456-472 (HEKDGKAYCRKDYFDMF) were used as the immunogen for this Paxillin antibody (100% homologous in human, mouse and rat).
Isotype
IgG
Predicted Reactivity
Human, Mouse, Rat
Reactivity
Human, Mouse, Rat
Recombinant
No
Uniprot
P49023
Format
Antigen affinity purified
Purification
Antigen affinity
Storage
After reconstitution, the Paxillin antibody can be stored for up to one month at 4°C. For long-term, aliquot and store at -20°C. Avoid repeated freezing and thawing.
Applications
WB, IHC-P, IHC-F, ICC
Dilution
Western blot: 0.5-1ug/ml,Immunohistochemistry (FFPE): 0.5-1ug/ml,Immunohistochemistry (Frozen): 0.5-1ug/ml,Immunocytochemistry: 0.5-1ug/ml