protein

ILDR2 Protein, Human (HEK293, His)

HY-P70864

10 μg;50 μg

75;215 USD

ILDR2 Protein, Human (HEK293, His)

proteins

HEK293

10 μg;50 μg

75;215 USD

ILDR2 proteins play multiple roles in cellular processes, participating in ER stress pathways, affecting lipid homeostasis, and affecting insulin secretion. It is involved in maintaining epithelial barrier function and recruiting MARVELD2/trifibrin into tight junctions, emphasizing its role in cellular integrity. ILDR2 Protein, Human (HEK293, His) is the recombinant human-derived ILDR2 protein, expressed by HEK293 , with C-6*His labeled tag. The total length of ILDR2 Protein, Human (HEK293, His) is 166 a.a., with molecular weight of 45-55 kDa.

Human

ILDR2 Protein appears to be a multifunctional player with diverse roles in cellular processes. It may be involved in ER stress pathways, exerting effects on lipid homeostasis and insulin secretion, thereby implicating its potential significance in metabolic regulation. Alongside ILDR1 and LSR, ILDR2 is engaged in maintaining the epithelial barrier function by recruiting MARVELD2/tricellulin to tricellular tight junctions, emphasizing its role in cellular integrity. Furthermore, acting as a member of the B7-like protein family expressed on immune cells and inflamed tissue, ILDR2 exhibits T-cell inhibitory activity, suggesting an immunomodulatory function. In the inner ear, it may regulate alternative pre-mRNA splicing through interactions with TRA2A, TRA2B, and SRSF1. The protein's intricate network of interactions, including MARVELD2, OCLN, P4HB, and HSPA5, further underscores its multifaceted nature. Notably, the interaction with HSPA5 stabilizes ILDR2 expression, contributing to its cellular regulation. Understanding the specific mechanisms governing ILDR2's diverse functions could provide valuable insights into its roles in metabolic processes, cellular integrity, immunomodulation, and pre-mRNA splicing regulation.

Angulin-3; C1orf32; Dbsm1; DJ782G3.1; ILDR2; immunoglobulin-like domain containing receptor 2; LISCH-Like

Greater than 95% as determined by reducing SDS-PAGE.

Lyophilized from a 0.2 μm filtered solution of PBS, pH 7.4.

Room temperature in continental US; may vary elsewhere.