Tyrosine-protein kinase BTK (BTK), human, recombinant

Organism: Homo sapiens (Human). Source: Yeast. Expression Region: 2-659aa. Protein Length: Full Length of Mature Protein. Tag Info: N-terminal 6xHis-tagged. Target Protein Sequence: AAVILESIFL KRSQQKKKTS PLNFKKRLFL LTVHKLSYYE YDFERGRRGS KKGSIDVEKI TCVETVVPEK NPPPERQIPR RGEESSEMEQ ISIIERFPYP FQVVYDEGPL YVFSPTEELR KRWIHQLKNV IRYNSDLVQK YHPCFWIDGQ YLCCSQTAKN AMGCQILENR NGSLKPGSSH RKTKKPLPPT PEEDQILKKP LPPEPAAAPV STSELKKVVA LYDYMPMNAN DLQLRKGDEY FILEESNLPW WRARDKNGQE GYIPSNYVTE AEDSIEMYEW YSKHMTRSQA EQLLKQEGKE GGFIVRDSSK AGKYTVSVFA KSTGDPQGVI RHYVVCSTPQ SQYYLAEKHL FSTIPELINY HQHNSAGLIS RLKYPVSQQN KNAPSTAGLG YGSWEIDPKD LTFLKELGTG QFGVVKYGKW RGQYDVAIKM IKEGSMSEDE FIEEAKVMMN LSHEKLVQLY GVCTKQRPIF IITEYMANGC LLNYLREMRH RFQTQQLLEM CKDVCEAMEY LESKQFLHRD LAARNCLVND QGVVKVSDFG LSRYVLDDEY TSSVGSKFPV RWSPPEVLMY SKFSSKSDIW AFGVLMWEIY SLGKMPYERF TNSETAEHIA QGLRLYRPHL ASEKVYTIMY SCWHEKADER PTFKILLSNI LDVMDEES. Purity: Greater than 90% as determined by SDS-PAGE. Endotoxin: Not test. Biological Activity: n/a. 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 °C/-80 °C. Our default final concentration of glycerol is 50%. Customers could use it as reference. 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. Notes: Repeated freezing and thawing is not recommended. Store working aliquots at 4 °C for up to one week. Relevance: Non-receptor tyrosine kinase indispensable for B lymphocyte development, differentiation and signaling. Binding of antigen to the B-cell antigen receptor (BCR) triggers signaling that ultimately leads to B-cell activation. After BCR engagent and activation at the plasma mbrane, phosphorylates PLCG2 at several sites, igniting the downstream signaling pathway through calcium mobilization, followed by activation of the protein kinase C (PKC) family mbers. PLCG2 phosphorylation is performed in close cooperation with the adapter protein B-cell linker protein BLNK. BTK acts as a platform to bring together a diverse array of signaling proteins and is implicated in cytokine receptor signaling pathways. Plays an important role in the function of immune cells of innate as well as adaptive immunity, as a component of the Toll-like receptors (TLR) pathway. The TLR pathway acts as a primary surveillance syst for the detection of pathogens and are crucial to the activation of host defense. Especially, is a critical molecule in regulating TLR9 activation in splenic B-cells. Within the TLR pathway, induces tyrosine phosphorylation of TIRAP which leads to TIRAP degradation. BTK plays also a critical role in transcription regulation. Induces the activity of NF-kappa-B, which is involved in regulating the expression of hundreds of genes. BTK is involved on the signaling pathway linking TLR8 and TLR9 to NF-kappa-B. Transiently phosphorylates transcription factor GTF2I on tyrosine residues in response to BCR. GTF2I then translocates to the nucleus to bind regulatory enhancer elents to modulate gene expression. ARID3A and NFAT are other transcriptional target of BTK. BTK is required for the formation of functional ARID3A DNA-binding complexes. There is however no evidence that BTK itself binds directly to DNA. BTK has a dual role in the regulation of apoptosis. Reference: Identification of nine novel mutations in the Bruton's tyrosine kinase gene in X-linked agammaglobulinaemia patients.Orlandi P., Ritis K., Moschese V., Angelini F., Arvanitidis K., Speletas M., Sideras P., Plebani A., Rossi P.3.0.CO,2-H>Hum. Mutat. 15:117-117(2000). Function: Non-receptor tyrosine kinase indispensable for B lymphocyte development, differentiation and signaling. Binding of antigen to the B-cell antigen receptor (BCR) triggers signaling that ultimately leads to B-cell activation. After BCR engagement and activation at the plasma membrane, phosphorylates PLCG2 at several sites, igniting the downstream signaling pathway through calcium mobilization, followed by activation of the protein kinase C (PKC) family members. PLCG2 phosphorylation is performed in close cooperation with the adapter protein B-cell linker protein BLNK. BTK acts as a platform to bring together a diverse array of signaling proteins and is implicated in cytokine receptor signaling pathways. Plays an important role in the function of immune cells of innate as well as adaptive immunity, as a component of the Toll-like receptors (TLR) pathway. The TLR pathway acts as a primary surveillance system for the detection of pathogens and are crucial to the activation of host defense. Especially, is a critical molecule in regulating TLR9 activation in splenic B-cells. Within the TLR pathway, induces tyrosine phosphorylation of TIRAP which leads to TIRAP degradation. BTK plays also a critical role in transcription regulation. Induces the activity of NF-kappa-B, which is involved in regulating the expression of hundreds of genes. BTK is involved on the signaling pathway linking TLR8 and TLR9 to NF-kappa-B. Transiently phosphorylates transcription factor GTF2I on tyrosine residues in response to BCR. GTF2I then translocates to the nucleus to bind regulatory enhancer elements to modulate gene expression. ARID3A and NFAT are other transcriptional target of BTK. BTK is required for the formation of functional ARID3A DNA-binding complexes. There is however no evidence that BTK itself binds directly to DNA. BTK has a dual role in the regulation of apoptosis.