LRIG1 Protein, Human (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, Human (HEK293, His) is the recombinant human-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.

Immobilized Human LRIG1, His Tag at 2μg/ml (100μl/well) on the plate. Dose response curve for Anti-LRIG1 Antibody, hFc Tag with the EC₅₀ of 6.5 ng/ml determined by ELISA.

Human

HEK293

C-8*His

Q96JA1-1 (A35-S779)

26018  [NCBI]

Partial

AGPRAPCAAACTCAGDSLDCGGRGLAALPGDLPSWTRSLNLSYNKLSEIDPAGFEDLPNLQEVYLNNNELTAVPSLGAASSHVVSLFLQHNKIRSVEGSQLKAYLSLEVLDLSLNNITEVRNTCFPHGPPIKELNLAGNRIGTLELGAFDGLSRSLLTLRLSKNRITQLPVRAFKLPRLTQLDLNRNRIRLIEGLTFQGLNSLEVLKLQRNNISKLTDGAFWGLSKMHVLHLEYNSLVEVNSGSLYGLTALHQLHLSNNSIARIHRKGWSFCQKLHELVLSFNNLTRLDEESLAELSSLSVLRLSHNSISHIAEGAFKGLRSLRVLDLDHNEISGTIEDTSGAFSGLDSLSKLTLFGNKIKSVAKRAFSGLEGLEHLNLGGNAIRSVQFDAFVKMKNLKELHISSDSFLCDCQLKWLPPWLIGRMLQAFVTATCAHPESLKGQSIFSVPPESFVCDDFLKPQIITQPETTMAMVGKDIRFTCSAASSSSSPMTFAWKKDNEVLTNADMENFVHVHAQDGEVMEYTTILHLRQVTFGHEGRYQCVITNHFGSTYSHKARLTVNVLPSFTKTPHDITIRTTTMARLECAATGHPNPQIAWQKDGGTDFPAARERRMHVMPDDDVFFITDVKIDDAGVYSCTAQNSAGSISANATLTVLETPSLVVPLEDRVVSVGETVALQCKATGNPPPRITWFKGDRPLSLTERHHLTPDNQLLVVQNVVAEDAGRYTCEMSNTLGTERAHSQLS

Approximately 85-105 kDa,based on SDS-PAGE under reducing conditions,due to the glycosylation.

≥ 95%, as determined by Bis-Tris PAGE.

Lyophilized powder

Lyophilized from a 0.2 μm filtered solution of 50 mM MES, 150 mM NaCl, 1 mM EDTA, pH 5.0, 8% trehalose.

<1 EU/μg, determined by LAL method.

It is not recommended to reconstitute to a concentration less than 100 μg/mL in 50 mM MES, 150 mM NaCl, 1 mM EDTA, pH 5.0.

Stored at -20°C for 2 years from date of receipt. After reconstitution, it is stable at 4°C for 1 week or -20°C for longer (with carrier protein). It is recommended to freeze aliquots at -20°C or -80°C for extended storage.

Room temperature in continental US; may vary elsewhere.