Technical Data
Integrin, beta1 (CD29, Very Late Antigen, VLAb1, Platelet gplla)
CD29 or the integrin B1 belongs to the family of cell adhesion receptors. It was initially characterized independently as protein gpIIa appearing on platelets, as the common b-subunit of the very late activation antigen (VLA) and as a component of various protein complexes binding to extracellular matrix proteins. CD29 is expressed at the cell surface exclusively as part of a heterodimer, in association with one of at least nine different integrin alpha subunits (alpha1-8; alpha V). With the exception of red blood cells and possible weak expression on granulocytes, CD29 is expressed in nearly all cell and tissue types.

Suitable for use in Immunohistochemistry. Other applications have not been tested.

Recommended Dilution:
Immunohistochemistry (Formalin/paraffin): 1:15-1:30 for 60 minutes at RT. Staining of formalin-fixed tissues requires boiling tissue sections in 1mM EDTA, pH 8.0, for 10-20 minutes followed by cooling at RT for 20 minutes. Use of a high-sensitivity detection system may be required.
Optimal dilutions to be determined by the researcher.

Positive Control:

Storage and Stability:
May be stored at 4C for short-term only. Aliquot to avoid repeated freezing and thawing. Store at -20C. Aliquots are stable for at least 12 months. For maximum recovery of product, centrifuge the original vial after thawing and prior to removing the cap.
500ul-20CBlue IceHumanMouse
Not Determined
Recombinant protein encoding the N-terminal region of human CD29. Cellular Localization: Cell membrane. MW of Antigen: 110kD (non-reducing) and 130kD (reducing).
Tissue culture supernatant .
Supplied as a liquid, 0.09% sodium azide.
Recognizes human CD29.
Intended for research use only. Not for use in human, therapeutic, or diagnostic applications.
1. Friedlander, D.R., Zagzag, D., Shiff, B., Cohen, H., Allen, J.C., Kelly, P.J., Grumet, M., Migration of brain tumor cells on extracellular matrix proteins in vitro correlates with tumor type and grade and involves alphaV and beta1 integrins. Cancer Research 56(8): 1939-47 (1996). 2. Hieken, T.J., Ronan, S.G., Farolan, M., Shilkaitis, A.L., Das Gupta, T.K., Beta 1 integrin expression: a marker of lymphatic metastases in cutaneous malignant melanoma. Anticancer Res. 16(4B): 2321-4 (1996). 3. Lanzafame, S., Emmanuele, C., Torrisi, A., Correlation of alpha 2 beta 1 integrin expression with histological type and hormonal receptor status in breast carcinomas. Pathology, Research and Practice 192(10): 1031-8 (1996). 4. Price, E.A., Coombe, D.R., Murray, J.C., beta-1 Integrins mediate tumour cell adhesion to quiescent endothelial cells in vitro. British Journal of Cancer 74(11): 1762-6 (1996). 5. Shiokawa, S., Yoshimura, Y., Nagamatsu, S., Sawa, H., Hanashi, H., Oda, T., Katsumata, Y., Koyama, N., Nakamura, Y., Expression of beta 1 integrins in human endometrial stromal and decidual cells. Journal of Clinical Endocrinology and Metabolism 81(4): 1533-40 (1996). 6. Marshall, J.F., Rutherford, D.C., McCartney, A.C., Mitjans, F., Goodman, S.L., Hart, I.R., Alpha v beta 1 is a receptor for vitronectin and fibrinogen, and acts with alpha 5 beta 1 to mediate spreading on fibronectin. Journal of Cell Science 108: 1227-38 (1995). 7. el Gabalawy, H., Wilkins, J., Beta 1 (CD29) integrin expression in rheumatoid synovial membranes: an immunohistologic study of distribution patterns. Journal of Rheumatology 20(2): 231-7 (1993). 8. Marshall, J.F., Nesbitt, S.A., Helfrich, M.H., Horton, M.A., Polakova, K., Hart, I.R., Integrin expression in human melanoma cell lines: heterogeneity of vitronectin receptor composition and function. International Journal of Cancer 49(6): 924-31 (1991).