Loading...
Custom Services order now ship next day

TNFAIP6

The protein encoded by this gene is a secretory protein that contains a hyaluronan-binding domain, and thus is a member of the hyaluronan-binding protein family. The hyaluronan-binding domain is known to be involved in extracellular matrix stability and cell migration. This protein has been shown to form a stable complex with inter-alpha-inhibitor (I alpha I), and thus enhance the serine protease inhibitory activity of I alpha I, which is important in the protease network associated with inflammation. This gene can be induced by proinflammatory cytokines such as tumor necrosis factor alpha and interleukin-1. Enhanced levels of this protein are found in the synovial fluid of patients with osteoarthritis and rheumatoid arthritis.[provided by RefSeq, Dec 2010]
Protein class

Plasma proteins

Predicted location

Secreted

Single cell type specificity

Cell type enhanced (Early spermatids, Fibroblasts, Langerhans cells, Melanocytes)

Immune cell specificity

Immune cell enriched (neutrophil)

Cell line specificity

Cell line enhanced (BJ hTERT+, HHSteC, hTEC/SVTERT24-B, SH-SY5Y, U-2197)

Interaction

Interacts (via Link domain) with inter-alpha-inhibitor (I-alpha-I) component bikunin (PubMed:15917224). Interacts with ITIH2/HC2; this interaction is required for transesterification of the HC to hyaluronan (PubMed:20463016). Interacts (via Link and CUB domains) with ITIH1 (PubMed:26468290). Chondroitin sulfate may be required for the stability of the complex (PubMed:7516184). Interacts (via Link domain) with various C-X-C and C-C chemokines including PF4, CXCL8, CXCL11, CXCL12, CCL2, CCL7, CCL19, CCL21, and CCL27; this interaction interferes with chemokine binding to glycosaminoglycans (PubMed:24501198, PubMed:27044744). Interacts (primarily via Link domain) with BMP2; this interaction is inhibited by hyaluronan (PubMed:16771708). Interacts (via both Link and CUB domains) with TNFSF11 (PubMed:18586671). Interacts (via CUB domain) with FN1 (via type III repeats 9-14); this interaction enhances fibronectin fibril assembly. TNFAIP6 may act as a bridging molecule between FN1 and THBS1 (PubMed:18042364).

More Types Infomation

Our customer service representatives are available 24 hours a day, from Monday to Sunday. Contact Us

Can't find the products you're looking for? Try to filter in the left sidebar.Filter By Tag

For Research Use Only. Not For Clinical Use.

© 2024 Creative Biolabs.
  • 0
  • 0
Cart

    Go to compare