Recombinant Human PLUNC BPIFA1 His-tag Protein, CF

Measured by its ability to bind fluorescein conjugated E. coli bio-particles. The ED50 for this effect is 0.500-5.00 μg/mL.

2 μg/lane of Recombinant Human PLUNC BPIFA1 His-tag Protein (Catalog # 11221-BF) was resolved with SDS-PAGE under reducing (R) and non-reducing (NR) conditions and visualized by Coomassie® Blue staining, showing bands at 21-28 kDa.

• Reactivity: Hu
• Applications: Bioactivity
• Format: Carrier-Free

Recombinant Human PLUNC BPIFA1 His-tag Protein, CF Summary

• Details of Functionality: Measured by its ability to bind fluorescein conjugated E. coli bio-particles. The ED₅₀ for this effect is 0.500-5.00 μg/mL.
• Source: Human embryonic kidney cell, HEK293-derived human PLUNC protein
  Gln20-Val256, with a C-terminal 6-His tag
• Accession #: Q9NP55.1
• N-terminal Sequence: Gln20; deblocked shows Phe21
• Protein/Peptide Type: Recombinant Proteins
• Purity: >95%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.
• Endotoxin Note: <0.10 EU per 1 μg of the protein by the LAL method.

Applications/Dilutions

• Dilutions:
  • Bioactivity
• Theoretical MW: 25 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: 21-28 kDa, under 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 with Trehalose.
• Purity: >95%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.
• 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 Human PLUNC BPIFA1 His-tag Protein, CF

• bA49G10.5
• BPIFA1
• ligand-binding protein RYA3
• LPLUNC3
• Lung-specific protein X
• LUNX
• LUNXNASG
• Nasopharyngeal carcinoma-related protein
• Palate lung and nasal epithelium clone protein
• palate, lung and nasal epithelium associated
• palate, lung and nasal epithelium carcinoma associated
• PLUNC
• protein Plunc
• Secretory protein in upper respiratory tracts
• SPLUNC1
• SPLUNC1SPURT
• tracheal epithelium enriched protein
• Tracheal epithelium-enriched protein
• Von Ebner protein Hl

Background

BPIFA1 (BPI fold-containing family A member 1), also named SPLUNC1, is a member of the BPI-fold (BPIF) containing/Plunc (palate, lung, and nasal epithelium clone) superfamily of putative innate defense molecules which are predominantly expressed in regions of the oral cavity, nasopharynx, and upper respiratory tract (1, 2). BPIF proteins exist as two subgroups, BPIFA (formally SPLUNCs) and BPIFB (formally LPLUNCs) (1, 3). BPIFA proteins have structural homology to the N‑terminal domain of BPI whereas BPIFB proteins have structural homology to both domains of BPI (2). The mature human BPIFA1 shares 68% amino acid (aa) identity with mouse and rat BIPFA1. BPIF proteins appear to exhibit distinct tissue and cell specific expression patterns with various family members, being localized to several glandular structures within the upper respiratory tract, nasopharyngeal regions and oral cavity where they are secreted from these tissues and are found in high levels in saliva and nasal and respiratory lining fluids (2). BPI proteins play a role in diverse functions, including neutralization of endotoxin (LPS) in septic shock patients, inhibition of endothelial cell growth, dendritic cell maturation, and function as an anti-angiogenic, chemoattractant or opsonization agent (2). BPIFA1 and BPIFB1 expression was increased in late-stage chronic obstructive pulmonary disease (COPD) patients, and elevated levels correlate with disease severity (4). BPIFs are also upregulated in cystic fibrosis (CF) lung disease and may play a role in the pathogenesis of the disease (5).

1. Bingle, C.D. and C. J. Craven (2002) Hum. Mol. Genet. 11:937.
2. Alves, D.B. et al. (2017) Braz. Oral Res. 31:e6.
3. Bingle, L. et al. (2012) Histochem. Cell Biol. 138:749.
4. De Smet, E.G. et al. (2017) Int. J. Chron. Obstruct. Pulmon. Dis. 13:11.
5. Saferali, A. et al. (2015) Am. J. Respir. Cell. Mol. Biol. 53:607.

Bioinformatics

• Uniprot:
  • Q9NP55.1()