Recombinant Human ITIH5 His-tag Protein, CF Summary
| Details of Functionality |
Measured by its binding ability in a functional ELISA. When Recombinant Human ITIH5 His-tag Protein is coated at 2.00 μg/mL (100 μL/well), it binds to Recombinant Human TSG-6
(Catalog #
2104-TS). The ED 50 for this binding is 1.00-10.0 μg/mL. |
| Source |
Chinese Hamster Ovary cell line, CHO-derived human ITIH5 protein Ser17-Leu942 with a C-terminal 6-His tag |
| Accession # |
|
| N-terminal Sequence |
Ser17 |
| Protein/Peptide Type |
Recombinant Enzymes |
| Purity |
>95%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining. |
| Endotoxin Note |
<0.10 EU per 1 μg of the protein by the LAL method. |
Applications/Dilutions
| Dilutions |
|
| Theoretical MW |
104 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 |
110-122 kDa, under reducing conditions |
Packaging, Storage & Formulations
| Storage |
Use a manual defrost freezer and avoid repeated freeze-thaw cycles. - 6 months from date of receipt, -70 °C as supplied.
- 2 weeks, 2 to 8 °C under sterile conditions after opening.
- 3 months, -20 to -70 °C under sterile conditions after opening.
|
| Buffer |
Supplied as a 0.2 μm filtered solution in Tris and NaCl. |
| Purity |
>95%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining. |
Notes
This product is produced by and ships from R&D Systems, Inc., a Bio-Techne brand.
Alternate Names for Recombinant Human ITIH5 His-tag Protein, CF
Background
Inter-alpha-trypsin inhibitor heavy chain 5 (ITIH5) is a heavy chain (HC) member of the ITIH family with predominant expression in the placenta, mammary gland, and ovary (1). It is composed of an N-terminal signal sequence, vault protein inter‑alpha‑trypsin domain (VIT), von-Willebrand type A domain, C-terminal cleavage site and multicopper oxidase domain conserved within other HCs in the family (1). The cleavage site present in ITIH members is processed during chain assembly (1) to reveal a C-terminal aspartic acid residue that enables crosslinking of the HC directly to chondroitin sulfate (CS) and hence to bikunin (2, 3). ITIHs can alternatively be associated with hyaluronan (HA) to form a Serum-derived hyaluronan associated protein (SHAP)-hyaluronan (HA) complex known to assist in stabilizing HA-rich extracellular matrices in inflammatory processes (3, 4). ITIH5 has been reported to modulate inflammation in skin disease and obesity and was suggested to play an important role more broadly in inflammation through its interaction with HA (5, 6). Tumor necrosis factor-stimulated gene 6 (TSG-6)-mediates interactions with the ITIH5 to enable the transfer of HC to HA matrix by forming a TSG-6:HC complex (7,8) that can facilitate Tumor Growth Factor beta 1 (TGF beta 1)‑dependent myofibroblast differentiation (9). ITIH5 has also been reported as downregulated or epigenetically silenced in several invasive cancers with poor prognosis including lung adenocarcinoma, breast cancer, gastric cancer, bladder cancer, and melanoma highlighting its potential as a therapeutic target (1, 10‑12).
- Himmelfarb, M. et al. (2004) Cancer Lett. 204:69.
- Salier, J.P. et al. (1996) Biochem. J. 315:1.
- Zhuo, L. et al. (2004) J. Biol. Chem. 279:38079.
- Rugg, M.S. et al. (2005) J. Biol. Chem. 280:25674.
- Anveden, A. et al. (2012) Obesity 20:708.
- Huth, S. et al. (2020) Skin Pharmacol. Physiol. 33:198.
- Zhuo, L. et al. (2006) J. Biol. Chem. 281:20303.
- Baranova, N.S. et al. (2013) J. Biol. Chem. 288:29642.
- Martin, J. et al. (2016) J. Biol. Chem. 291:13789.
- Mai, C. et al. (2014) Med. Oncol. 31:53.
- Dotsch, M. et al. (2015) Epigenetics. 10:903.
- Rose, M. et al. (2017) Mol. Cancer 16:44.
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