Recombinant Human TIM-1/KIM-1/HAVCR Fc Avi-tag Protein, CF Summary
Accession # AAC39862.1
CF stands for Carrier Free (CF). We typically add Bovine Serum Albumin (BSA) as a carrier protein to our recombinant proteins. Adding a carrier protein enhances protein stability, increases shelf-life, and allows the recombinant protein to be stored at a more dilute concentration. The carrier free version does not contain BSA.
In general, we advise purchasing the recombinant protein with BSA for use in cell or tissue culture, or as an ELISA standard. In contrast, the carrier free protein is recommended for applications, in which the presence of BSA could interfere.
|Formulation||Lyophilized from a 0.2 μm filtered solution in PBS with Trehalose.|
|Reconstitution||Reconstitute at 500 μg/mL in PBS.|
|Shipping||The product is shipped at ambient temperature. Upon receipt, store it immediately at the temperature recommended below.|
|Stability & Storage:||Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
2 μg/lane of Biotinylated Recombinant Human TIM-1/KIM-1/HAVCR Fc Chimera Avi-tag (Catalog # AVI9319) was resolved with SDS-PAGE under reducing (R) and non-reducing (NR) conditions and visualized by Coomassie® Blue staining, showing bands at 115-135 kDa and 230-270 kDa, respectively.
T cell immunoglobulin and mucin domain 1 (TIM-1), also known as KIM-1 and HAVcr1, is a member of the TIM family which is involved in the regulation of innate and adaptive immune responses (1). TIM-1 is a type I transmembrane protein that contains an N-terminal immunoglobulin-like domain, a mucin domain with O- and N-linked carbohydrates, a transmembrane segment, and a cytoplasmic signaling domain (2). Multiple TIM-1 variants can be produced due to polymorphisms or alternative splicing resulting in deletions in the mucin domain. Within the extracellular domain, human TIM-1 shares 41% amino acid sequence identity with mouse and rat TIM-1. TIM-1 is expressed on splenic B cells, IL-10+ regulatory B cells, CD4+ T cells, mast cells, invariant NKT (iNKT) cells, dendritic cells, kidney epithelium and a broad range of mucosal epithelium (1, 3-5). It is upregulated on activated Th2 cells, after dendritic cell maturation, and on kidney tubular epithelial cells after injury (6-9). Metalloproteinase-mediated cleavage of TIM-1 at the membrane-proximal region results in the release of a soluble form of TIM-1 which is detectable in the urine and in circulation (10). TIM-1 serves as a receptor for phosphatidylserine, LMIR5/CD300b, TIM-1 (homophilic), TIM-4, IgA, and the glycoproteins of a number of enveloped viruses (2, 11-16). Its interaction with phosphatidylserine enables TIM-1 to mediate the phagocytosis of apoptotic cells (12, 13) and iNKT cell activation (17). TIM-1 binding induces the activation of LMIR5-expressing myeloid cells, contributing to tissue homeostasis as well as damage following kidney injury (14). TIM-1 ligation co-stimulates T cell activation and enhances Th2 cytokine production (7, 15). In humans, TIM-1 serves as a cellular entry receptor for various viruses, including hepatitis A virus, Ebolavirus and Marburgvirus (2, 11). Our Avi-tag Biotinylated human TIM-1 Fc Chimera features biotinylation at a single site contained within the Avi-tag, a unique 15 amino acid peptide. Protein orientation will be uniform when bound to streptavidin-coated surface due to the precise control of biotinylation and the rest of the protein is unchanged so there is no interference in the protein's bioactivity.
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