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Recombinant Mouse CRISP-3 Protein, CF

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Product Details

Summary
Reactivity MuSpecies Glossary
Applications Bioactivity
Format
Carrier-Free

Order Details

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Recombinant Mouse CRISP-3 Protein, CF Summary

Details of Functionality
Measured by its ability to inhibit proliferation/survival of the 3A‑sub E human placenta cell line.

The ED50 for this effect is 1.3-5.2 μg/mL.

Source
Mouse myeloma cell line, NS0-derived mouse CRISP-3 protein
Gln20-Cys241, with a C-terminal 6-His tag
Accession #
N-terminal Sequence
No results obtained: Gln20 predicted (N-sequencing might be blocked)
Protein/Peptide Type
Recombinant Proteins
Gene
Crisp3
Purity
>95%, by SDS-PAGE under reducing conditions and visualized by silver stain
Endotoxin Note
<0.01 EU per 1 μg of the protein by the LAL method.

Applications/Dilutions

Dilutions
  • Bioactivity
Theoretical MW
26 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
30-40 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
>95%, by SDS-PAGE under reducing conditions and visualized by silver stain
Reconstitution Instructions
Reconstitute at 250 μg/mL in PBS.

Notes

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

Alternate Names for Recombinant Mouse 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). Human CRISP-3 is produced by salivary, pancreas, prostate, and lacrimal glands, as well as spermatozoa and mature spermatids (2, 6, 7). In mouse, CRISP-3 has not been detected in the male genital tract, although its salivary gland expression is androgen-dependent (8, 9). CRISP-3 is up‑regulated in human 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 human 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 and is released from human neutrophil and eosinophil granules following cell stimulation (1, 14, 15). Mature mouse CRISP-3 shares 48% and 64% amino acid (aa) sequence identity with human and equine CRISP-3, respectively. It shares 73% and 47% aa sequence identity with mouse 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. 18:425.
  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.

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Bioinformatics

Gene Symbol Crisp3
Uniprot