B6.129S7-Selp^tm1Bay/J

Stock number: 002289
Product name: P-selectin^-
Research areas: Immunology, Inflammation and Autoimmunity Research

Description

Mice homozygous for Selp^tm1Bay show a deficit in leukocyte rolling and delayed neutrophil extravasation in response to intraperitoneal injections of thioglycollate. The strain can be used as model for human leukocyte adhesion deficiency I syndrome.

Detailed description

Mice homozygous for the Selp^tm1Bay mutation are viable and fertile. Homoyzgous mutant mice show a deficit in leukocyte rolling and delayed neutrophil extravasation in response to intraperitoneal injections of thioglycollate. Neutrophil count is elevated (2-3-fold). Circulating lymphocyte and monocyte counts are normal. 60-70% reduction in neutrophil emigration into the peritoneum during Streptococcus pneumoniae-induced peritonitis is reduced 60-70%. It can be used as model for human leukocyte adhesion deficiency I syndrome (characterized by elevated levels of circulating leukocytes and impaired leukocyte extravasation to sites of inflammation or infection).

Development

A neomycin resistance gene was inserted in the reverse orientation to delete a 4.5kb region containing exons 3 through 5. RT-PCR analysis of lung RNA isolated from homozygous mutant mice showed a transcript 682 base pairs shorter than normal. A clone with the correctly targeted gene was injected into C57BL/6 embryos. The strain has been backcrossed for 10 generations to C57BL/6J.

Allele

Symbol: Selp^tm1Bay
Name: targeted mutation 1, Baylor College of Medicine
MGI accession ID: MGI:1857244
Generation method: Targeted
Attributes: Null/Knockout
Marker symbol: Selp
Marker name: selectin, platelet
Chromosome: 1
Strain of origin: 129S7/SvEvBrd-Hprt^b-m2
Molecular note: A neomycin resistance gene was inserted in the reverse orientation to delete a 4.5kb region containing exons 3 through 5. RT-PCR analysis of lung RNA isolated from homozygous mutant mice showed a transcript 682 base pairs shorter than normal. Immunohistochemical staining showed a lack of encoded protein on both endothelium and platelets.