• Purity

  >90%, by SDS-PAGE under reducing conditions and visualized by silver stain

• Endotoxin Level

  <0.10 EU per 1 μg of the protein by the LAL method.  

• Activity

  Measured by its ability to bind immobilized Recombinant Human PSP94/MSMB (Catalog # ) in a functional ELISA. Udby, L.     et al. (2005) BBRC     333:555.

• Source

  Mouse myeloma cell line, NS0-derived Asn21-Tyr245 (Ser134Ala), with a C-terminal 6-His tag

• Accession #

• N-terminal Sequence    
  Analysis

  Asn21

• Predicted Molecular Mass

  26.3 kDa

• SDS-PAGE

  27 kDa, 31 kDa and 67 kDa, reducing conditions

Background: CRISP-3

CRISP-3 is one of three CRISPs (cysteine-rich secretory proteins) found in mammalian exocrine secretions and granulocytes that may play a role in innate immunity (1-3). CRISPs and several snake, insect, and lizard venom proteins are characterized by 16 invariant cysteine residues (4). Structurally, they consist of an N-terminal SCP domain, a hinge region, and a cysteine-rich domain (5). CRISP-3 is produced by salivary, pancreas, prostate, and lacrimal glands, as well as spermatozoa and mature spermatids (2, 6, 7). In mouse, however, CRISP-3 has not been detected in the male genital tract (8, 9). CRISP-3 is up-regulated in epithelial prostate cancer and chronic pancreatitis (10, 11). It is present as 30 kDa and 28 kDa species, corresponding to glycosylated and nonglycosylated forms (1, 3, 7, 10, 12). In serum and seminal fluid, CRISP-3 forms high affinity noncovalent complexes with the more abundant alpha 1B-glycoprotein and beta -microseminoprotein/PSP94, respectively (12, 13). Binding is mediated by the SCP domain of CRISP-3 and is independent of glycosylation (12). CRISP-3 is also expressed in pre-B cells but not in T cells or monocytes (14, 15). CRISP-3 is released from neutrophil and eosinophil granules following cell stimulation (1, 15). Mature human CRISP-3 shares 48% and 65% amino acid (aa) sequence identity with mouse and equine CRISP-3, respectively. It shares 44% and 72% aa sequence identity with human CRISP-1 and -2, respectively.

• References:

1. Kjeldsen, L. et al. (1996) FEBS Lett. 380:246.

2. Kratzschmar, J. et al. (1996) Eur. J. Biochem. 236:827.

3. Udby, L. et al. (2002) J. Immunol. Meth. 263:43.

4. Yamazaki, Y. and Morita, T. (2004) Toxicon 44:227.

5. Guo, M. et al. (2005) J. Biol. Chem. 280:12405.

6. Haendler, B. et al. (1999) J. Cell. Physiol. 178:371.

7. Udby, L. et al. (2005) J. Androl. 26:333.

8. Haendler, B. et al. (1993) Endocrinology 133:192.

9. Haendler, B. et al. (1997) Eur. J. Biochem. 250:440.

10. Bjartell, A. et al. (2006) Prostate 66:591.

11. Liao, Q. et al. (2003) Histol. Histopathol. 18:245.

12. Udby, L. et al. (2005) Biochem. Biophys. Res. Commun. 333:555.

13. Udby, L. et al. (2004) Biochemistry 43:12877.

14. Pfisterer, P. et al. (1996) Mol. Cell. Biol. 16:6160.

15. Udby, L. et al. (2002) J. Leukoc. Biol. 72:462.

• Long Name:

  Cysteine-rich Secretory Protein 3

• Entrez Gene IDs:

  10321 (Human); 11572 (Mouse)

• Alternate Names:

  Aeg2; CRISP3; CRISP-3; CRISP-3MGC126588; CRS3; cysteine-rich secretory protein 3; cysteine-rich secretory protein-3; dJ442L6.3; SGP28; SGP28Aeg2; specific granule protein (28 kDa); Specific granule protein of 28 kDa