Recombinant Human TIR domain-containing adapter molecule 1 (TICAM1) | CSB-CF811598HUe1

Recombinant Human TIR domain-containing adapter molecule 1 (TICAM1) | CSB-CF811598HUe1 | Cusabio

Alternative Name(s): Proline-rich, vinculin and TIR domain-containing protein B Putative NF-kappa-B-activating protein 502H Toll-interleukin-1 receptor domain-containing adapter protein inducing interferon beta

Gene Names: TICAM1

Research Areas: Immunology

Organism: Homo sapiens (Human)

AA Sequence: MACTGPSLPSAFDILGAAGQDKLLYLKHKLKTPRPGCQGQDLLHAMVLLKLGQETEARISLEALKADAVARLVARQWAGVDSTEDPEEPPDVSWAVARLYHLLAEEKLCPASLRDVAYQEAVRTLSSRDDHRLGELQDEARNRCGWDIAGDPGSIRTLQSNLGCLPPSSALPSGTRSLPRPIDGVSDWSQGCSLRSTGSPASLASNLEISQSPTMPFLSLHRSPHGPSKLCDDPQASLVPEPVPGGCQEPEEMSWPPSGEIASPPELPSSPPPGLPEVAPDATSTGLPDTPAAPETSTNYPVECTEGSAGPQSLPLPILEPVKNPCSVKDQTPLQLSVEDTTSPNTKPCPPTPTTPETSPPPPPPPPSSTPCSAHLTPSSLFPSSLESSSEQKFYNFVILHARADEHIALRVREKLEALGVPDGATFCEDFQVPGRGELSCLQDAIDHSAFIILLLTSNFDCRLSLHQVNQAMMSNLTRQGSPDCVIPFLPLESSPAQLSSDTASLLSGLVRLDEHSQIFARKVANTFKPHRLQARKAMWRKEQDTRALREQSQHLDGERMQAAALNAAYSAYLQSYLSYQAQMEQLQVAFGSHMSFGTGAPYGARMPFGGQVPLGAPPPFPTWPGCPQPPPLHAWQAGTPPPPSPQPAAFPQSLPFPQSPAFPTASPAPPQSPGLQPLIIHHAQMVQLGLNNHMWNQRGSQAPEDKTQEAE

Source: in vitro E.coli expression system

Tag Info: Tag-Free

Expression Region: 1-712aa

Sequence Info: Full Length

MW: 76.4 kDa

Purity: Greater than 90% as determined by SDS-PAGE.

Relevance: Involved in innate immunity against invading pathogens. Adapter used by TLR3 and TLR4 (through TICAM2) to mediate NF-kappa-B and interferon-regulatory factor (IRF) activation, and to induce apoptosis. Ligand binding to these receptors results in TRIF recruitment through its TIR domain. Distinct protein-interaction motifs allow recruitment of the effector proteins TBK1, TRAF6 and RIPK1, which in turn, lead to the activation of transcription factors IRF3 and IRF7, NF-kappa-B and FADD respectively.

Reference: "TICAM-1, an adapter molecule that participates in Toll-like receptor 3 mediated interferon-beta induction."Oshiumi H., Matsumoto M.,Funami K., Akazawa T., Seya T.Nat. Immunol. 4:161-167(2003)

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?/-80?. The shelf life of lyophilized form is 12 months at -20?/-80?.

Notes: Repeated freezing and thawing is not recommended. Store working aliquots at 4? for up to one week.

Function: Involved in innate immunity against invading pathogens. Adapter used by TLR3 and TLR4 (through TICAM2) to mediate NF-kappa-B and interferon-regulatory factor (IRF) activation, and to induce apoptosis. Ligand binding to these receptors results in TRIF recruitment through its TIR domain. Distinct protein-interaction motifs allow recruitment of the effector proteins TBK1, TRAF6 and RIPK1, which in turn, lead to the activation of transcription factors IRF3 and IRF7, NF-kappa-B and FADD respectively.

Involvement in disease: Herpes simplex encephalitis 4 (HSE4)

Subcellular Location: Cytoplasmic vesicle, autophagosome

Protein Families:

Tissue Specificity: Ubiquitously expressed but with higher levels in liver.

Paythway: NF-kappaBsignalingpathway

Form: Liquid or Lyophilized powder

Buffer: If the delivery form is liquid, the default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol. If the delivery form is lyophilized powder, the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, pH 8.0.

Reconstitution: We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Please reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL.We recommend to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20?/-80?. Our default final concentration of glycerol is 50%. Customers could use it as reference.

Uniprot ID: Q8IUC6

HGNC Database Link: HGNC

UniGene Database Link: UniGene

KEGG Database Link: KEGG

STRING Database Link: STRING

OMIM Database Link: OMIM