LRIG1 Protein, Cynomolgus (HEK293, His)

The LRIG1 protein acts as a feedback negative regulator of receptor tyrosine kinase signaling, enhancing receptor ubiquitination and promoting intracellular degradation. It interacts with various receptors, including EGFR/ERBB1, ERBB2, ERBB3, and ERBB4, through its extracellular leucine-rich repeats (LRR) and immunoglobulin-like domains. LRIG1 Protein, Cynomolgus (HEK293, His) is the recombinant cynomolgus-derived LRIG1 protein, expressed by HEK293 , with C-His labeled tag.

LRIG1 protein functions as a feedback negative regulator in receptor tyrosine kinase signaling pathways, employing a mechanism that enhances receptor ubiquitination and expedites intracellular degradation. It interacts with various receptor tyrosine kinases, including EGFR/ERBB1, ERBB2, ERBB3, and ERBB4, through its extracellular leucine-rich repeat (LRR) and immunoglobulin-like domains. However, the physiological relevance of these interactions is subject to controversy, as LRIG1 may exhibit low affinity for EGFR, and the interaction may occur only under conditions of elevated levels of both LRIG1 and the respective receptor tyrosine kinase proteins.

Cynomolgus

HEK293

C-8*His

A0A2K5V8J9 (A34-T792)

/

Extracellular Domain

AAGPRAPCAAACTCAGDSVDCGGRGLAALPGDLPAWTQSLNLSYNKLSEIDPAGFEDLPNLQEVYLNNNELTAIPSLGAASSHVVSLFLQHNKIRSVEGSQLKAYLSLEVLDLSSNNITEVRNTCFPHGPPIKELNLAGNRIGTLELGAFDGLSRSLLTLRLSKNRITQLPVRAFKLPRLTQLDLNRNRIRLIEGLTFQGLNSLEVLKLQRNNISKLTDGAFWGLSKMHVLHLEYNSLVEVNSGSLYGLTALHQLHLSNNSIARIHRKGWSFCQKLHELVLSFNNLTRLDEESLAELSSLSVLRLSHNSISHIAEGAFKGLRSLRVLDLDHNEIAGTIEDTSGAFSGLDSLSKLTLFGNKIKSVAKRAFSGLEGLEHLNLGGNAIRSVQFDAFVKMKNLKELHISSDSFLCDCQLKWLPPWLMGRMLQAFVTATCAHPESLKGQSIFSVPPESFVCDDFLKPQIITQPETTMAMVGKDIRFTCSAASSSSSPMTFAWKKDNEVLTNADMENFVHVHAQDGEVMEYTTILHLRQVTFGHEGRYQCVITNHFGSTYSHKARLTVNVLPSFTKTPHDITIRTTTMARLECAATGHPNPQIAWQKDGGTDFPAARERRMHVMPDDDVFFITDVKIDDAGVYSCTAQNSAGSISANATLTVLETPSLAVPLEDRVVSAGETVALQCKATGNPPPRITWFKGDSPLSLTERHHLTPDNQLLVVQNVVAEDAGRYTCEMSNTLGTERAHSQLSVLPAAGCRKDGTT

Approximately 90-110 kDa,based on SDS-PAGE under reducing conditions,due to the glycosylation.

≥ 95%, as determined by reducing SDS-PAGE.

<1 EU/μg, determined by LAL method.