Recombinant Human CRISP-3 Protein, CF
Recombinant Human CRISP-3 Protein, CF Summary
Asn21-Tyr245 (Ser134Ala), with a C-terminal 6-His tag
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.
|Formulation||Lyophilized from a 0.2 μm filtered solution in PBS.|
|Reconstitution||Reconstitute at 100 μg/mL in sterile 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.
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.
- 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. 18:245.
- 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.
Citations for Recombinant Human CRISP-3 Protein, CF
R&D Systems personnel manually curate a database that contains references using R&D Systems products. The data collected includes not only links to publications in PubMed, but also provides information about sample types, species, and experimental conditions.
Citations: Showing 1 - 2
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Purification and characterization of CRISP-3 from human seminal plasma and its real-time binding kinetics with PSP94
Authors: Smita D Mahale
J. Chromatogr. B Analyt. Technol. Biomed. Life Sci., 2016;1039(0):59-65.
Applications: WB Standard
The novel lipopolysaccharide-binding protein CRISPLD2 is a critical serum protein to regulate endotoxin function.
Authors: 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
J. Immunol., 2009;183(10):6646-56.
Sample Types: Whole Cells
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