Recombinant Mouse Kirrel1/Neph1(C-6His)
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| Amount : | 50 µg |
| Content : | Lyophilized from a 0.2 µm filtered solution of PBS,pH7.4. |
| AA sequence : | Recombinant Mouse Kin of IRRE-like protein 1 is produced by our Mammalian expression system and the target gene encoding Leu48-Leu525 is expressed with a 6His tag at the C-terminus. |
| Alternative Name : | Kin of IRRE-like protein 1;Kin of irregular chiasm-like protein 1;Nephrin-like protein 1;Kirrel1;Neph1 |
Source : Human Cells;
Kin of irregular chiasm-like protein 1(Kirrel1), also known as Nephrin-like protein 1(Neph1), belongs to the immunoglobulin superfamily. Kirrel1 plays a significant role in the normal development and function of the glomerular permeability. It is a signaling protein that needs the presence of TEC kinases to fully trans-activate the transcription factor AP-1. The knockout of this gene could result in perinatal lethality accompanied by proteinuria, and effacement of glomerular podocytes. Kirrel1 is abundantly expressed in kidney and specifically expressed in podocytes of kidney glomeruli. ItsÂ’ subunit interacts with TJP1/ZO-1 and with NPHS2/podocin (via the C-terminus) and interacts with NPHS1/nephrin (via the Ig-like domains). This interaction is dependent on KIRREL glycosylation. Kirrel1 also interacts when tyrosine-phosphorylated with GRB2.
Kin of irregular chiasm-like protein 1(Kirrel1), also known as Nephrin-like protein 1(Neph1), belongs to the immunoglobulin superfamily. Kirrel1 plays a significant role in the normal development and function of the glomerular permeability. It is a signaling protein that needs the presence of TEC kinases to fully trans-activate the transcription factor AP-1. The knockout of this gene could result in perinatal lethality accompanied by proteinuria, and effacement of glomerular podocytes. Kirrel1 is abundantly expressed in kidney and specifically expressed in podocytes of kidney glomeruli. ItsÂ’ subunit interacts with TJP1/ZO-1 and with NPHS2/podocin (via the C-terminus) and interacts with NPHS1/nephrin (via the Ig-like domains). This interaction is dependent on KIRREL glycosylation. Kirrel1 also interacts when tyrosine-phosphorylated with GRB2.
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