Recombinant Mouse CRISP-3 Protein, CF Summary
Product Specifications
The ED50 for this effect is 1.3-5.2 μg/mL.
Gln20-Cys241, with a C-terminal 6-His tag
Analysis
Product Datasheets
Carrier Free
CF stands for Carrier Free (CF). We typically add Bovine Serum Albumin (BSA) as a carrier protein to our recombinant proteins. Adding a carrier protein enhances protein stability, increases shelf-life, and allows the recombinant protein to be stored at a more dilute concentration. The carrier free version does not contain BSA.
In general, we advise purchasing the recombinant protein with BSA for use in cell or tissue culture, or as an ELISA standard. In contrast, the carrier free protein is recommended for applications, in which the presence of BSA could interfere.
7056-CR
| Formulation | Lyophilized from a 0.2 μm filtered solution in PBS. |
| Reconstitution | Reconstitute at 250 μg/mL in PBS. |
| Shipping | The product is shipped at ambient temperature. Upon receipt, store it immediately at the temperature recommended below. |
| Stability & Storage: | Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
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Reconstitution Calculator
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). 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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