Human CRISP-3 Antibody Summary
Asn21-Tyr245 (Ser134Ala)
Accession # CAA63984
Applications
Please Note: Optimal dilutions should be determined by each laboratory for each application. General Protocols are available in the Technical Information section on our website.
Reconstitution Calculator
Preparation and Storage
- 12 months from date of receipt, -20 to -70 °C as supplied.
- 1 month, 2 to 8 °C under sterile conditions after reconstitution.
- 6 months, -20 to -70 °C under sterile conditions after reconstitution.
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). 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.
Product Datasheets
Citations for Human CRISP-3 Antibody
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.
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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., 2016-10-26;1039(0):59-65.
Species: Human
Sample Types: Protein
Applications: Western Blot -
Growth inhibition mediated by PSP94 or CRISP-3 is prostate cancer cell line specific
Authors: Bhakti R. Pathak, Ananya A. Breed, Vaishali H. Nakhawa, Dhanashree D. Jagtap, Smita D. Mahale
Asian Journal of Andrology
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