Feline Leukaemia Virus p15E antibody | PF6J-2A1
Persistent infection of cats with the oncoretrovirus FeLV can result in the non-neoplastic condition known as FeLV-associated enteritis (FAE). Studies have shown strong expression of the major FeLV proteins p15e and gp70 in intestinal crypt epithelial cells of cats with FAE, compared to FeLV-positive cats without intestinal alterations, thereby suggesting a pathogenic role for these envelope proteins/precursors in FAE.
- Target Species
- Product Form
- Purified IgG - liquid
- Purified IgG prepared by affinity chromatography on Protein A from tissue culture supernatant
- Buffer Solution
- Phosphate buffered saline
- Preservative Stabilisers
0.05% Sodium Azide (NaN3)
- Approx. Protein Concentrations
- IgG concentration 1.0mg/ml
- Store at +4oC or at -20oC if preferred.
Storage in frost-free freezers is not recommended.
This product should be stored undiluted. Avoid repeated freezing and thawing as this may denature the antibody. Should this product contain a precipitate we recommend microcentrifugation before use.
- 18 months from date of despatch.
Applications of Feline Leukaemia Virus p15E antibody
|Application Name||Verified||Min Dilution||Max Dilution|
|Immunohistology - Paraffin|
- Western Blotting
- MCA2550 detects band/s of approximately 15kDa and 20kDa under reducing conditions.
Secondary Antibodies Available
Product Specific References
References for Feline Leukaemia Virus p15E antibody
Kipar, A. et al. (2000) Expression of viral proteins in feline leukemia virus-associated enteritis.
Vet Pathol. 37 (2): 129-36.
Kipar, A. et al. (2001) Comparative examination of cats with feline leukemia virus-associated enteritis and other relevant forms of feline enteritis.
Vet Pathol. 38 (4): 359-71.
Burns, C.C. et al. (1995) Mutations within a putative cysteine loop of the transmembrane protein of an attenuated immunodeficiency-inducing feline leukemia virus variant inhibit envelope protein processing.
J Virol. 69 (4): 2126-32.
Gwynn, S.R. et al. (2000) Feline leukemia virus envelope sequences that affect T-cell tropism and syncytium formation are not part of known receptor-binding domains.
J Virol. 74 (13): 5754-61.
Argaw, T. & Wilson,A. (2015) Mutations altering the gammaretrovirus endoproteolytic motif affect glycosylation of the envelope glycoprotein and early events of the virus life cycle.
Virology. 475: 110-9.