Recombinant Human TIM-1/KIM-1/HAVCR Fc Avi-tag Protein, CF

When Human TIM-1/KIM-1/HAVCR Affinity Purified Polyclonal Antibody (AF1750) is immobilized at 0.2 μg/mL, 100 μl/well, Recombinant Human TIM-1/KIM-1/HAVCR Fc Avi-tag Protein (AVI9319) binds with an ED50 of 1.5-9 ng/mL.

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 kDa.

• Reactivity: Hu
• Applications: Binding Activity, Bioactivity
• Format: Carrier-Free

Recombinant Human TIM-1/KIM-1/HAVCR Fc Avi-tag Protein, CF Summary

• Additional Information: Biotinylated
• Details of Functionality: The biotin to protein ratio is greater than 0.7 as determined by the HABA assay. Measured by its binding ability in a functional ELISA. When Human TIM-1/KIM-1/HAVCR Affinity Purified Polyclonal Antibody (Catalog # AF1750) is immobilized at 0.2 μg/mL, 100 μl/well, Recombinant Human TIM-1/KIM-1/HAVCR Fc Chimera Avi-tag Protein (Catalog # AVI9319) binds with an ED₅₀ of 1.5-9 ng/mL. Measured by its ability to inhibit anti-CD3-induced proliferation of stimulated human T cells. The ED₅₀ for this effect is 0.12-1.2 μg/mL.
• Source: Human embryonic kidney cell, HEK293-derived human TIM-1/KIM-1/HAVCR protein
  

  Human TIM-1/KIM-1/HAVCR (Ser21-Thr288) Accession # AAC39862.1	IEGRMD	Human IgG1 (Pro100-Lys330)	Avi-tag
  N-terminus			C-terminus

• Accession #: AAC39862.1
• N-terminal Sequence: Ser21
• Structure / Form: Disulfide-linked homodimer, biotinylated via Avi-tag
• Protein/Peptide Type: Recombinant Proteins
• Purity: >95%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.
• Endotoxin Note: <1.0 EU per 1 μg of the protein by the LAL method.

Applications/Dilutions

• Dilutions:
  • Binding Activity2
  • Bioactivity
  • Bioactivity2
• Theoretical MW: 57 kDa.
  Disclaimer note: The observed molecular weight of the protein may vary from the listed predicted molecular weight due to post translational modifications, post translation cleavages, relative charges, and other experimental factors.
• SDS-PAGE: 115-135 kDa, under reducing conditions

Packaging, Storage & Formulations

• Storage: Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
  • 12 months from date of receipt, -20 to -70 °C as supplied.
  • 1 month, 2 to 8 °C under sterile conditions after reconstitution.
  • 3 months, -20 to -70 °C under sterile conditions after reconstitution.
• Buffer: Lyophilized from a 0.2 μm filtered solution in PBS with Trehalose.
• Purity: >95%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.
• Reconstitution Instructions: Reconstitute at 500 μg/mL in PBS.

Notes

This product is produced by and ships from R&D Systems, Inc., a Bio-Techne brand.

Alternate Names for Recombinant Human TIM-1/KIM-1/HAVCR Fc Avi-tag Protein, CF

• CD365
• HAVCR1
• HAVCR-1
• HAVCRT cell immunoglobin domain and mucin domain protein 1
• hepatitis A virus cellular receptor 1
• Kidney injury molecule 1
• KIM1
• KIM-1
• T-cell immunoglobulin and mucin domain-containing protein 1
• TIM1
• TIM-1
• TIM-1TIM
• TIM1TIMD-1
• TIMD1T-cell membrane protein 1

Background

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.

1. Du, P. et al. (2016) J. Immunol. Res. 2016:8605134.
2. Feigelstock, D. et al. (1998) J. Virol. 72:6621.
3. Ding, Q. et al. (2011) J. Clin. Invest. 121:3645.
4. Ma, J. et al. (2011) Biochem. Biophys. Res. Commun. 406:223.
5. de Souza, A.J. et al. (2005) Proc. Natl. Acad. Sci. USA 102:17113.
6. Kuehn, E.W. et al. (2002) Am. J. Physiol. Renal Physiol. 283:F1326.
7. Umetsu, S.E. et al. (2005) Nat. Immunol. 6:447.
8. Xiao, S. et al. (2011) Eur. J. Immunol. 41:1539.
9. Ichimura, T. et al. (1998) J. Biol. Chem. 273:4135.
10. Bailly, V. et al. (2002) J. Biol. Chem. 277:39739.
11. Kondratowicz, A.S. et al. (2011) Proc. Natl. Acad. Sci. USA 108:8426.
12. Miyanishi, M. et al. (2007) Nature 450:435.
13. Kobayashi, N. et al. (2007) Immunity 27:927.
14. Yamanishi, Y. et al. (2010) J. Exp. Med. 207:1501.
15. Meyers, J.H. et al. (2005) Nat. Immunol. 6:455.
16. Tami, C. et al. (2007) J. Virol. 81:3437.
17. Lee, H.H. et al. (2010) J. Immunol. 185:5225.

Bioinformatics

• Uniprot:
  • AAC39862.1()