Synthetic peptide, corresponding to amino acids 88-133 of Human CSRP1.
Conjugation:
Unconjugated
Alternative Names:
Cysteine and glycine-rich protein 1, Cysteine-rich protein 1, CRP, CRP1, Epididymis luminal protein 141, HEL-141, HEL141, CSRP, CYRP
Cysteine-rich proteins (CRPs) participate in the organization of multiprotein complexes, both in the cytoplasm, where they participate in cytoskeletal remodeling, and in the nucleus, where they facilitate smooth muscle differentiation. CRP1 (cysteine and glycine-rich protein 1), also known as CRP, CSRP1 or CYRP, is abundant in the prostate and smooth muscle lineages. It contains two LIM zinc-binding domains and is localized in the nucleus. The LIM domains of CRP1 are critical for binding to the adhesion-plaque protein Zyxin. CRP1 also interacts with a-actinin to mediate muscle differentiation. These associations indicate that the main function of CRP1 may be structural.
The antibody was affinity-purified from rabbit antiserum by affinity-chromatography using epitope-specific immunogen and the purity is > 95% (by SDS-PAGE).
Form:
Rabbit IgG, 1mg/ml in PBS with 0.02% sodium azide, 50% glycerol, pH7.2
