Technical Data

145249
Clone Type
Polyclonal
Host
Rabbit
Source
Human
Isotype
IgG
Grade
Affinity Purified
Applications
WB
Crossreactivity
Hu Mo Rt
Gene ID
TAZ
Shipping Temp
Blue Ice
Storage Temp
-20°C
Rabbit Anti-TAZ (G4.5, BTHS, XAP-2, CMD3A, EFE, EFE2, Tafazzin, Barth syndrome, Protein G4.5, Endocardial fibroelastosis 2, Cardiomyopathy, dilated 3A (X-linked))

Tafazzin, also known as G4.5 is a protein that in humans is encoded by the TAZ gene. Cardiolipin is a complex glycerophospholipid with 4 acyl groups that localizes to the mitochondrial inner membrane and has a role in mitochondrial structure and function. By positional cloning, TAZ was identified within the critical Barth syndrome region on Xq28. Tafazzin is involved in the metabolism of cardiolipin. It is a component of the hippo signaling pathway thatcontrols tissue growth in animals. And it can function as aphospholipid lysophospholipid transacylase.

UniProt Number
Q16635
Gene ID
TAZ
Applications
Suitable for use in Western Blot. Other applications not tested.
Recommended Dilution
Optimal dilutions to be determined by the researcher.
Storage and Stability
Lyophilized and reconstituted products are stable for 12 months after receipt at -20°C. Reconstitute with sterile ddH2O. Aliquot to avoid repeated freezing and thawing. Store 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.
Immunogen
A synthetic peptide corresponding to a sequence in the middle region of human TAZ, identical to the related mouse and rat sequences.
Form
Supplied as a lyophilized powder from PBS, 5% BSA, 0.05% Thimerosal, 0.05% sodium azide. Reconstitutie with 200ul sterile ddH2O.
Purity
Purified by immunoaffinity chromatography.
Specificity
Recognizes human,mouse and rat TAZ. No crossreactivity with other proteins.

Intended for research use only. Not for use in human, therapeutic, or diagnostic applications.

References
1. Acehan, D., Vaz, F., Houtkooper, R. H., James, J., Moore, V., Tokunaga, C., Kulik, W., Wansapura, J., Toth, M. J., Strauss, A., Khuchua, Z. Cardiac and skeletal muscle defects in a mouse model of human Barth syndrome. J. Biol. Chem. 286: 899-908, 2011.|2. Barth, P. G., Valianpour, F., Bowen, V. M., Lam, J., Duran, M., Vaz, F. M., Wanders, R. J. A. X-linked cardioskeletal myopathy and neutropenia (Barth syndrome): an update. Am. J. Med. Genet. 126A: 349-354, 2004.|3. Claypool, S. M., McCaffery, J. M., Koehler, C. M. Mitochondrial mislocalization and altered assembly of a cluster of Barth syndrome mutant tafazzins. J. Cell Biol. 174: 379-390, 2006.|4. Hastings, R., Steward, C., Tsai-Goodman, B., Newbury-Ecob, R. Dysmorphology of Barth syndrome. Clin. Dysmorph. 18: 185-187, 2009.|
USBio References
No references available
United States Biological | 4 Technology Way | Salem, MA 01970
Phone 800-520-3011 | Fax 978-594-8052 | Website www.usbio.net