Recombinant Human CRISP-3 Protein, CF

Catalog # Availability Size / Price Qty
2397-CR-050
R&D Systems Recombinant Proteins and Enzymes
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Citations (3)
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Recombinant Human CRISP-3 Protein, CF Summary

Product Specifications

Purity
>90%, by SDS-PAGE under reducing conditions and visualized by silver stain
Endotoxin Level
<0.10 EU per 1 μg of the protein by the LAL method.
Activity
Measured by its ability to bind immobilized Recombinant Human PSP94/MSMB (Catalog # 3780-PS) in a functional ELISA. Udby, L. et al. (2005) BBRC 333:555.
Source
Mouse myeloma cell line, NS0-derived human CRISP-3 protein
Asn21-Tyr245 (Ser134Ala), with a C-terminal 6-His tag
Accession #
N-terminal Sequence
Analysis
Asn21
Predicted Molecular Mass
26.3 kDa
SDS-PAGE
27 kDa, 31 kDa and 67 kDa, reducing conditions

Product Datasheets

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2397-CR

Carrier Free

What does CF mean?

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.

What formulation is right for me?

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.

2397-CR

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.
  • 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.
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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.

References
  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. 18:245.
  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.
Long Name
Cysteine-rich Secretory Protein 3
Entrez Gene IDs
10321 (Human); 11572 (Mouse)
Alternate Names
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

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.

3 Citations: Showing 1 - 3
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  1. Zinc binding regulates amyloid-like aggregation of GAPR-1
    Authors: J Sheng, NK Olrichs, WJ Geerts, X Li, AU Rehman, BM Gadella, DV Kaloyanova, B Helms
    Biosci. Rep., 2019-02-12;0(0):.
    Species: Human
    Sample Types: Recombinant Protein
    Applications: ThT Fluorescence
  2. 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.
    Applications: Western Blot
  3. 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., 2009-10-28;183(10):6646-56.
    Species: Human, Mouse
    Sample Types: In Vivo, Whole Cells
    Applications: Bioassay, In Vivo

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