Recombinant Human CRISP-3 Protein, CF

• Reactivity: Hu
• Applications: Binding Activity
• Format: Carrier-Free

Recombinant Human CRISP-3 Protein, CF Summary

• Details of Functionality: Measured by its ability to bind immobilized Recombinant Human PSP94/MSMB (Catalog # 3780-PS) in a functional ELISA. Udby, L. et al. (2005) BBRC 333:555.
• Source: Mouse myeloma cell line, NS0-derived human CRISP-3 protein
  Asn21-Tyr245 (Ser134Ala), with a C-terminal 6-His tag
• Accession #: CAA63984
• N-terminal Sequence: Asn21
• Protein/Peptide Type: Recombinant Proteins
• Gene: CRISP3
• Purity: >90%, by SDS-PAGE under reducing conditions and visualized by silver stain
• Endotoxin Note: <0.10 EU per 1 μg of the protein by the LAL method.

Applications/Dilutions

• Dilutions:
  • Binding Activity
• Theoretical MW: 26.3 kDa.
  Disclaimer note: The observed molecular weight of the protein may vary from the listed predicted molecular weight due to post translational modifications, post translation cleavages, relative charges, and other experimental factors.
• SDS-PAGE: 27 kDa, 31 kDa and 67 kDa, reducing conditions

Packaging, Storage & Formulations

• Storage: Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
  • 12 months from date of receipt, -20 to -70 °C as supplied.
  • 1 month, 2 to 8 °C under sterile conditions after reconstitution.
  • 3 months, -20 to -70 °C under sterile conditions after reconstitution.
• Buffer: Lyophilized from a 0.2 μm filtered solution in PBS.
• Purity: >90%, by SDS-PAGE under reducing conditions and visualized by silver stain
• Reconstitution Instructions: Reconstitute at 100 μg/mL in sterile PBS.

Notes

This product is produced by and ships from R&D Systems, Inc., a Bio-Techne brand.

Alternate Names for Recombinant Human CRISP-3 Protein, CF

• 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

Background

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.

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.

Publications for CRISP-3 (2397-CR)(3)

Publications using 2397-CR

• J Sheng, NK Olrichs, WJ Geerts, X Li, AU Rehman, BM Gadella, DV Kaloyanova, B Helms Zinc binding regulates amyloid-like aggregation of GAPR-1 Biosci. Rep., 2019-02-12;0(0):. 2019-02-12 [PMID: 30700571] (ThT Fluorescence, Human)
• Smita D Mahale Purification and characterization of CRISP-3 from human seminal plasma and its real-time binding kinetics with PSP94 J. Chromatogr. B Analyt. Technol. Biomed. Life Sci., 2016-10-26;1039(0):59-65. 2016-10-26 [PMID: 27825912] (Western Blot)
• Wang ZQ, Xing WM, Fan HH, Wang KS, Zhang HK, Wang QW, Qi J, Yang HM, Yang J, Ren YN, Cui SJ, Zhang X, Liu F, Lin DH, Wang WH, Hoffmann MK, Han ZG The novel lipopolysaccharide-binding protein CRISPLD2 is a critical serum protein to regulate endotoxin function. J. Immunol., 2009-10-28;183(10):6646-56. 2009-10-28 [PMID: 19864597] (Bioassay, In Vivo, Human, Mouse)

Bioinformatics

• Gene Symbol: CRISP3
• Uniprot:
  • CAA63984()