Polyclonal Anti-ST13

Price

200.00 USD

Size

100ug/vial

Reactivities

Hum

Format

Each vial contains 5mg BSA, 0.9mg NaCl, 0.2mg Na2HPO4, 0.05mg Thimerosal, 0.05mg NaN3.

References

1. Hohfeld, J., Minami, Y., Hartl, F.-U. Hip, a novel cochaperone involved in the eukaryotic Hsc70/Hsp40 reaction cycle. Cell 83: 589-598, 1995.\n2. Prapapanich, V., Chen, S., Nair, S. C., Rimerman, R. A., Smith, D. F. Molecular cloning of human p48, a transient component of progesterone receptor complexes and an Hsp70-binding protein. Molec. Endocr. 10: 420-431, 1996.\n3. Zhang, Y., Cai, X., Schlegelberger, B., Zheng, S. Assignment of human putative tumor suppressor genes ST13 (alias SNC6) and ST14 (alias SNC19) to human chromosome bands 22q13 and 11q24-q25 by in situ hybridization. Cytogenet. Cell Genet. 83: 56-57, 1998.\n

Storage Temp

At -20 degree C for one year. After reconstitution, at 4 degree C for one month. It can also be aliquotted and stored frozen at -20 degree C for a longer time.Avoid repeated freezing and thawing.

Scientific Background

ST13(Suppression of Tumorigenicity 13), also known as P48 or HIP, is a protein that in humans is encoded by the ST13 gene. ST13 is an abundant, highly conserved protein that binds the major cytosolic chaperones heat-shock protein 70-kD (HSP70) and HSP90 during an intermediate stage of steroid receptor assembly, but is absent from the mature receptor complex. Zhang et al. (1998) mapped the ST13 gene to chromosome 22q13 by fluorescence in situ hybridization. They noted that colorectal, breast, and ovarian carcinomas frequently show loss of heterozygosity at this site. Using a yeast 2-hybrid assay, Hohfeld et al. (1995) showed that rat Hip bound Hsc70 (HSPA8). One Hip oligomer bound the ATPase domains of at least 2 Hsc70 molecules, and binding was dependent on activation of the Hsc70 ATPase by Hsp40 (DNAJB1). Hip stabilized the ADP-bound form of Hsc70, which had a high affinity for a test protein substrate. Hohfeld et al. (1995) concluded that HIP contributes to interactions of HSC70 with target proteins through its own chaperone activity.