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Recombinant Human TRAF-interacting protein with FHA domain-containing protein A (TIFA)

Recombinant Human TRAF-interacting protein with FHA domain-containing protein A (TIFA)

Code
MSDS	MSDS Datasheet
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Source
Conjugate
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Product Details
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Target Background

Product Details

Abbreviation

TIFA

Purity

>85% (SDS-PAGE)

Target Names

TIFA

Uniprot NO.

Q96CG3

Species

Homo sapiens (Human)

Source

Yeast

Expression Region

1-184

Target Protein Sequence

MTSFEDADTE ETVTCLQMTV YHPGQLQCGI FQSISFNREK LPSSEVVKFG RNSNICHYTF QDKQVSRVQF SLQLFKKFNS SVLSFEIKNM SKKTNLIVDS RELGYLNKMD LPYRCMVRFG EYQFLMEKED GESLEFFETQ FILSPRSLLQ ENNWPPHRPI PEYGTYSLCS SQSSSPTEMD ENES
Note: The complete sequence may include tag sequence, target protein sequence, linker sequence and extra sequence that is translated with the protein sequence for the purpose(s) of secretion, stability, solubility, etc.
If the exact amino acid sequence of this recombinant protein is critical to your application, please explicitly request the full and complete sequence of this protein before ordering.

Protein Length

full length protein

Tag Info

N-terminal His-tagged/Tag-Free
The tag type will be determined during production process. If you have specified tag type, please tell us and we will develop the specified tag preferentially.

Storage

The shelf life is related to many factors, storage state, buffer ingredients, storage temperature and the stability of the protein itself.
Generally, the shelf life of liquid form is 6 months at -20°C/-80°C. The shelf life of lyophilized form is 12 months at -20°C/-80°C.

Shelf Life

Notes

Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.

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Target Background

Function(From Uniprot)

Adapter molecule that plays a key role in the activation of proinflammatory NF-kappa-B signaling following detection of bacterial pathogen-associated molecular pattern metabolites (PAMPs). Promotes activation of an innate immune response by inducing the oligomerization and polyubiquitination of TRAF6, which leads to the activation of TAK1 and IKK through a proteasome-independent mechanism. TIFA-dependent innate immune response is triggered by ADP-D-glycero-beta-D-manno-heptose (ADP-Heptose), a potent PAMP present in all Gram-negative and some Gram-positive bacteria: ADP-Heptose is recognized by ALPK1, which phosphorylates TIFA at Thr-9, leading to TIFA homooligomerization and subsequent activation of proinflammatory NF-kappa-B signaling.

Gene References into Functions

TIFA may serve as a biomarker in the prediction of lung adenocarcinoma. Furthermore, TIFA may modulate lung cancer cell survival and proliferation through regulating the synthesis of apoptosis-associated proteins. PMID:29975933
TIFA is a crucial mediator in the endothelial innate immune response by potentiating and amplifying NLRP3 inflammasome via augmenting signals 1 and 2 PMID:27965388
study revealed that host TIFA and H. pylori-derived heptose-1,7-bisphosphate are critical effectors of innate immune signaling that account for much of the inflammatory response to H. pylori in gastric epithelial cells PMID:28811347
These results define TIFA as a rheostat for intracellular bacterial replication, escalating the immune response to invasive Gram-negative bacteria that exploit the host cytosol for growth. PMID:28514661
we report that Aurora A is essential for phosphorylation of the TRAF-interacting protein TIFA PMID:28069801
This study reports the crystal structures of TIFA (residues 1-150, with the unstructured C-terminal tail truncated) and its complex with the N-terminal phosphothreonine9 peptide (residues 1-15). PMID:26389808
an innate immune signaling axis, mediated by phosphorylation-dependent oligomerization of the TRAF-interacting protein with forkhead-associated domain (TIFA) that is triggered by heptose-1,7-bisphosphate. PMID:26068852
identify a novel threonine phosphorylation site on TIFA and show that this phosphorylated threonine binds with the FHA domain of TIFA, leading to TIFA oligomerization and TIFA-mediated NF-kappaB activation PMID:22566686
TIFA induces the oligomerization and polyubiquitination of TRAF6, which leads to the activation of TAK1 and IKK through a proteasome-independent mechanism PMID:15492226