antibody

Parvin, alpha

P3113-60

100 ul

polyclonal

domestic rabbit

nonconjugated

Parvin, alpha

rabbit

Pab

Antibodies

100 ul

IgG

The extracellular matrix (ECM) is a complex structure of secreted macromolecules surrounding mammalian organs and tissues. Controlled interactions between cells and the ECM are important in proliferation, migration, survival, polarity and differentiation. Cells contact the ECM primarily through heterodimeric integral membrane proteins called integrins. Integrins connect the ECM to the cytoskeleton, and therefore the cell signaling machinery, through protein complexes called focal adhesions (1). The ILK/PINCH/Parvin (IPP) complex is composed of three highly conserved proteins recruited to sites of ECM contact as pre-assembled structures. The IPP acts at the interface of the integrin/actin connection to regulate formation of focal adhesions and integrin signaling. All three proteins contain multiple protein binding domains allowing them to function as adaptor proteins in the formation of focal adhesions. ILK (integrin-linked kinase) also has a catalytic (protein Ser/Thr kinase) domain, but may or may not function as a kinase in vivo. Roles for IPP proteins outside of the IPP complex have been proposed, including regulation of gene expression (2,3). The parvin family consists of 3 members, alpha-parvin/actopaxin, beta-parvin/affixin and gamma-parvin. alpha-parvin and beta-parvin are expressed ubiquitously, while expression of gamma-parvin is restricted to haematopoietic cells (4). alpha-parvin binds to F-actin both directly and via interaction with the focal adhesion protein paxillin (5). alpha-parvin regulates cell spreading and motility through interactions with the cofilin kinase TESK1 (6), and with the GTPase activating protein CdGAP (7). Phosphorylation of alpha-parvin during mitosis may have a role in the regulation of actin dynamics during the cell cycle (8). Applications: Suitable for use in Immunofluorescence and Western Blot. Other applications not tested. Recommended Dilution: Western Blot: 1:1000, incubate membrane with diluted antibody in 5% BSA, 1X TBS, 0.1% Tween-20 at 4°C with gentle shaking, overnight. Immunofluorescence (IF-IC): 1:400 Optimal 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. For maximum recovery of product, centrifuge the original vial after thawing and prior to removing the cap.

Ca Hm Hu Mk Mo Rt

Synthetic peptide corresponding to residues near the N-terminus of human alpha-parvin. Uniprot Accession: Q9NVD7

Recognizes endogenous levels of total human alpha-parvin protein. Species Crossreactivity: mouse, rat, hamster, monkey and canine

Purified by peptide affinity chromatography.

Supplied as a liquid in 10mM sodium HEPES, pH 7.5, 150mM sodium chloride, 0.1mg/ml BSA, 50% glycerol.

Not determined

Product Type: Pab Isotype: IgG Host: rabbit Source: human Concentration: Not determined Form: Supplied as a liquid in 10mM sodium HEPES, pH 7.5, 150mM sodium chloride, 0.1mg/ml BSA, 50% glycerol. Purity: Purified by peptide affinity chromatography. Immunogen: Synthetic peptide corresponding to residues near the N-terminus of human alpha-parvin. Uniprot Accession: Q9NVD7 Specificity: Recognizes endogenous levels of total human alpha-parvin protein. Species Crossreactivity: mouse, rat, hamster, monkey and canine Important Note: This product as supplied is intended for research use only, not for use in human, therapeutic or diagnostic applications without the expressed written authorization of United States Biological.

IF WB

-20°C

(1) Burridge, K. et al. (1988) Annu Rev Cell Biol 4, 487–525. (2) Legate, K.R. et al. (2006) Nat Rev Mol Cell Biol 7, 20–31. (3) Wu, C. (2004) Biochim Biophys Acta 1692, 55–62. (4) Korenbaum, E. et al. (2001) Gene 279, 69–79. (5) Nikolopoulos, S.N. and Turner, C.E. (2000) J Cell Biol 151, 1435–48. (6) LaLonde, D.P. et al. (2005) J Biol Chem 280, 21680–8. (7) LaLonde, D.P. et al. (2006) Curr Biol 16, 1375–85. (8) Curtis, M. et al. (2002) Biochem J 363, 233–42.

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