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 |
|
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
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.
- Kjeldsen, L. et al. (1996) FEBS Lett. 380:246.
- Kratzschmar, J. et al. (1996) Eur. J. Biochem. 236:827.
- Udby, L. et al. (2002) J. Immunol. Meth. 263:43.
- Yamazaki, Y. and Morita, T. (2004) Toxicon 44:227.
- Guo, M. et al. (2005) J. Biol. Chem. 280:12405.
- Haendler, B. et al. (1999) J. Cell. Physiol. 178:371.
- Udby, L. et al. (2005) J. Androl. 26:333.
- Haendler, B. et al. (1993) Endocrinology 133:192.
- Haendler, B. et al. (1997) Eur. J. Biochem. 250:440.
- Bjartell, A. et al. (2006) Prostate 66:591.
- Liao, Q. et al. (2003) Histol. Histopathol. 18:425.
- Udby, L. et al. (2005) Biochem. Biophys. Res. Commun. 333:555.
- Udby, L. et al. (2004) Biochemistry 43:12877.
- Pfisterer, P. et al. (1996) Mol. Cell. Biol. 16:6160.
- Udby, L. et al. (2002) J. Leukoc. Biol. 72:462.
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