Tyrosine-protein kinase ABL1 Recombinant Protein | ABL1 recombinant protein

Recombinant Human Tyrosine-protein kinase ABL1

Cat. Num. AAA717062

• Gene Names: ABL1; ABL; JTK7; p150; c-ABL; v-abl; c-ABL1; bcr/abl
• Purity: Greater or equal to 85% purity as determined by SDS-PAGE.
• Synonyms: Tyrosine-protein kinase ABL1; Recombinant Human Tyrosine-protein kinase ABL1; Abelson murine leukemia viral oncogene homolog 1; Abelson tyrosine-protein kinase 1; Proto-oncogene c-Ablp150; ABL1 recombinant protein

• Host: E Coli
• Purity/Purification: Greater or equal to 85% purity as determined by SDS-PAGE.
• Form/Format: Liquid containing glycerol
• Sequence Positions: 4-194aa; Partial
• Sequence: ICLKLVGCKSKKGLSSSSSCYLEEALQRPVASDFEPQGLSEAARWNSKENLLAGPSENDPNLFVALYDFVASGDNTLSITKGEKLRVLGYNHNGEWCEAQTKNGQGWVPSNYITPVNSLEKHSWYHGPVSRNAAEYLLSSGINGSFLVRESESSPGQRSISLRYEGRVYHYRINTASDGKLYVSSESRFNT
• Sequence Length: 194

• Production Note: Special Offer: The E Coli host-expressed protein is manufactured from a stock plasmid containing the protein gene. E Colihost-expressed protein is stocked in different unit sizes ranging from as small as 10 ug to as large as 1 mg. Bulk inventory is also available. The E Coli host-expressed protein has been ordered over and over again by researchers and has stood the test of time as both a robust protein and important target for the research community. It is part of our new program to make our most popular protein targets and corresponding hosts available in expanded unit sizes and with a quick processing time. Select E Coli host-expressed protein for the fastest delivery among all hosts. Please contact our technical support team or email to [email protected] for more details.
• Preparation and Storage: Store at -20 degree C, for extended storage, conserve at -20 degree C or -80 degree C.

SDS-PAGE

Related Product Information for ABL1 recombinant protein

Non-receptor tyrosine-protein kinase that plays a role in many key processes linked to cell growth and survival such as cytoskeleton remodeling in response to extracellular stimuli, cell motility and adhesion, receptor endocytosis, autophagy, DNA damage response and apoptosis. Coordinates actin remodeling through tyrosine phosphorylation of proteins controlling cytoskeleton dynamics like WASF3 (involved in branch formation); ANXA1 (involved in membrane anchoring); DBN1, DBNL, CTTN, RAPH1 and ENAH (involved in signaling); or MAPT and PXN (microtubule-binding proteins). Phosphorylation of WASF3 is critical for the stimulation of lamellipodia formation and cell migration. Involved in the regulation of cell adhesion and motility through phosphorylation of key regulators of these processes such as BCAR1, CRK, CRKL, DOK1, EFS or NEDD9. Phosphorylates multiple receptor tyrosine kinases and more particularly promotes endocytosis of EGFR, facilitates the formation of neuromuscular synapses through MUSK, inhibits PDGFRB-mediated chemotaxis and modulates the endocytosis of activated B-cell receptor complexes. Other substrates which are involved in endocytosis regulation are the caveolin (CAV1) and RIN1. Moreover, ABL1 regulates the CBL family of ubiquitin ligases that drive receptor down-regulation and actin remodeling. Phosphorylation of CBL leads to increased EGFR stability. Involved in late-stage autophagy by regulating positively the trafficking and function of lysosomal components. ABL1 targets to mitochondria in response to oxidative stress and thereby mediates mitochondrial dysfunction and cell death. ABL1 is also translocated in the nucleus where it has DNA-binding activity and is involved in DNA-damage response and apoptosis. Many substrates are known mediators of DNA repair: DDB1, DDB2, ERCC3, ERCC6, RAD9A, RAD51, RAD52 or WRN. Activates the proapoptotic pathway when the DNA damage is too severe to be repaired. Phosphorylates TP73, a primary regulator for this type of damage-induced apoptosis. Phosphorylates the caspase CASP9 on 'Tyr-191' and regulates its processing in the apoptotic response to DNA damage. Phosphorylates PSMA7 that leads to an inhibition of proteasomal activity and cell cycle transition blocks

Product Categories/Family for ABL1 recombinant protein

Apoptosis

References

Nucleotide sequence of testis-derived c-abl cDNAs implications for testis-specific transcription and abl oncogene activation.Oppi C., Shore S.K., Reddy E.P.Proc. Natl. Acad. Sci. U.S.A. 84:8200-8204(1987) Sequence and analysis of the human ABL gene, the BCR gene, and regions involved in the Philadelphia chromosomal translocation.Chissoe S.L., Bodenteich A., Wang Y.-F., Wang Y.-P., Burian D., Clifton S.W., Crabtree J., Freeman A., Iyer K., Jian L., Ma Y., McLaury H.-J., Pan H.-Q., Sarhan O.H., Toth S., Wang Z., Zhang G., Heisterkamp N., Groffen J., Roe B.A.Genomics 27:67-82(1995) The mouse c-abl locus molecular cloning and characterization.Wang J.Y.J., Ledley F., Goff S., Lee R., Groner Y., Baltimore D.Cell 36:349-356(1984) Four murine c-abl mRNAs arise by usage of two transcriptional promoters and alternative splicing.Bernards A., Paskind M., Baltimore D.Oncogene 2:297-304(1988) Differential phosphorylation of c-Abl in cell cycle determined by cdc2 kinase and phosphatase activity.Kipreos E.T., Wang J.Y.Science 248:217-220(1990) Neonatal lethality and lymphopenia in mice with a homozygous disruption of the c-abl proto-oncogene.Tybulewicz V.L., Crawford C.E., Jackson P.K., Bronson R.T., Mulligan R.C.Cell 65:1153-1163(1991) Mice homozygous for the ablm1 mutation show poor viability and depletion of selected B and T cell populations.Schwartzberg P.L., Stall A.M., Hardin J.D., Bowdish K.S., Humaran T., Boast S., Harbison M.L., Robertson E.J., Goff S.P.Cell 65:1165-1175(1991) Cell cycle-regulated binding of c-Abl tyrosine kinase to DNA.Kipreos E.T., Wang J.Y.Science 256:382-385(1992) c-Abl kinase regulates the protein binding activity of c-Crk.Feller S.M., Knudsen B., Hanafusa H.EMBO J. 13:2341-2351(1994) Evidence that SH2 domains promote processive phosphorylation by protein-tyrosine kinases.Mayer B.J., Hirai H., Sakai R.Curr. Biol. 5:296-305(1995) Functional interaction between DNA-PK and c-Abl in response to DNA damage.Kharbanda S., Pandey P., Jin S., Inoue S., Bharti A., Yuan Z.-M., Weichselbaum R., Weaver D., Kufe D.Nature 386:732-735(1997) Nuclear-cytoplasmic shuttling of C-ABL tyrosine kinase.Taagepera S., McDonald D., Loeb J.E., Whitaker L.L., McElroy A.K., Wang J.Y., Hope T.J.Proc. Natl. Acad. Sci. U.S.A. 95:7457-7462(1998) Cables links Cdk5 and c-Abl and facilitates Cdk5 tyrosine phosphorylation, kinase upregulation, and neurite outgrowth.Zukerberg L.R., Patrick G.N., Nikolic M., Humbert S., Wu C.-L., Lanier L.M., Gertler F.B., Vidal M., Van Etten R.A., Tsai L.-H.Neuron 26:633-646(2000) Cytoskeletal protein PSTPIP1 directs the PEST-type protein tyrosine phosphatase to the c-Abl kinase to mediate Abl dephosphorylation.Cong F., Spencer S., Cote J.F., Wu Y., Tremblay M.L., Lasky L.A., Goff S.P.Mol. Cell 6:1413-1423(2000) Regulation of cell death by the Abl tyrosine kinase.Wang J.Y.Oncogene 19:5643-5650(2000) Inhibition of cell migration by Abl family tyrosine kinases through uncoupling of Crk-CAS complexes.Kain K.H., Klemke R.L.J. Biol. Chem. 276:16185-16192(2001) Targeting of the c-Abl tyrosine kinase to mitochondria in the necrotic cell death response to oxidative stress.Kumar S., Bharti A., Mishra N.C., Raina D., Kharbanda S., Saxena S., Kufe D.J. Biol. Chem. 276:17281-17285(2001) The beta-amyloid precursor protein APP is tyrosine-phosphorylated in cells expressing a constitutively active form of the Abl protoncogene.Zambrano N., Bruni P., Minopoli G., Mosca R., Molino D., Russo C., Schettini G., Sudol M., Russo T.J. Biol. Chem. 276:19787-19792(2001) Aph2, a protein with a zf-DHHC motif, interacts with c-Abl and has pro-apoptotic activity.Li B., Cong F., Tan C.P., Wang S.X., Goff S.P.J. Biol. Chem. 277:28870-28876(2002) Interaction between UV-damaged DNA binding activity proteins and the c-Abl tyrosine kinase.Cong F., Tang J., Hwang B.J., Vuong B.Q., Chu G., Goff S.P.J. Biol. Chem. 277:34870-34878(2002) Regulation of F-actin-dependent processes by the Abl family of tyrosine kinases.Woodring P.J., Hunter T., Wang J.Y.J. Cell Sci. 116:2613-2626(2003) Two distinct phosphorylation pathways have additive effects on Abl family kinase activation.Tanis K.Q., Veach D., Duewel H.S., Bornmann W.G., Koleske A.J.Mol. Cell. Biol. 23:3884-3896(2003) Bidirectional signaling links the Abelson kinases to the platelet-derived growth factor receptor.Plattner R., Koleske A.J., Kazlauskas A., Pendergast A.M.Mol. Cell. Biol. 24:2573-2583(2004) Role of c-Abl in the DNA damage stress response.Shaul Y., Ben-Yehoyada M.Cell Res. 15:33-35(2005) c-Abl and Src-family kinases cross-talk in regulation of myeloid cell migration.Baruzzi A., Iacobucci I., Soverini S., Lowell C.A., Martinelli G., Berton G.FEBS Lett. 584:15-21(2010) ABL tyrosine kinases evolution of function, regulation, and specificity.Colicelli J.Sci. Signal. 3:RE6-RE6(2010) High-resolution crystal structures of tyrosine kinase SH3 domains complexed with proline-rich peptides.Musacchio A., Saraste M., Wilmanns M.Nat. Struct. Biol. 1:546-551(1994) Structural mechanism for STI-571 inhibition of Abelson tyrosine kinase.Schindler T., Bornmann W., Pellicena P., Miller W.T., Clarkson B., Kuriyan J.Science 289:1938-1942(2000) Structural basis for the autoinhibition of c-Abl tyrosine kinase.Nagar B., Hantschel O., Young M.A., Scheffzek K., Veach D., Bornmann W., Clarkson B., Superti-Furga G., Kuriyan J.Cell 112:859-871(2003) Crystal structure of the T315I mutant of AbI kinase.Zhou T., Parillon L., Li F., Wang Y., Keats J., Lamore S., Xu Q., Shakespeare W., Dalgarno D., Zhu X.Chem. Biol. Drug Des. 70:171-181(2007) AP24534, a pan-BCR-ABL inhibitor for chronic myeloid leukemia, potently inhibits the T315I mutant and overcomes mutation-based resistance.O'Hare T., Shakespeare W.C., Zhu X., Eide C.A., Rivera V.M., Wang F., Adrian L.T., Zhou T., Huang W.S., Xu Q., Metcalf C.A. III, Tyner J.W., Loriaux M.M., Corbin A.S., Wardwell S., Ning Y., Keats J.A., Wang Y., Sundaramoorthi R., Thomas M., Zhou D., Snodgrass J., Commodore L., Sawyer T.K., Dalgarno D.C., Deininger M.W., Druker B.J., Clackson T.Cancer Cell 16:401-412(2009) Structural analysis of DFG-in and DFG-out dual Src-Abl inhibitors sharing a common vinyl purine template.Zhou T., Commodore L., Huang W.S., Wang Y., Sawyer T.K., Shakespeare W.C., Clackson T., Zhu X., Dalgarno D.C.Chem. Biol. Drug Des. 75:18-28(2010) Targeting Bcr-Abl by combining allosteric with ATP-binding-site inhibitors.Zhang J., Adrian F.J., Jahnke W., Cowan-Jacob S.W., Li A.G., Iacob R.E., Sim T., Powers J., Dierks C., Sun F., Guo G.R., Ding Q., Okram B., Choi Y., Wojciechowski A., Deng X., Liu G., Fendrich G., Strauss A., Vajpai N., Grzesiek S., Tuntland T., Liu Y., Bursulaya B., Azam M., Manley P.W., Engen J.R., Daley G.Q., Warmuth M., Gray N.S.Nature 463:501-506(2010)

NCBI and Uniprot Product Information

• NCBI GI #: 62362414
• NCBI GeneID: 25
• NCBI Accession #: NP_005148.2
• NCBI GenBank Nucleotide #: NM_005157.5
• UniProt Accession #: P00519; Q13869; Q13870; Q16133; Q17R61; Q45F09; A3KFJ3
• Molecular Weight: 48.1 kDa
• NCBI Official Full Name: tyrosine-protein kinase ABL1 isoform a
• NCBI Official Synonym Full Names: ABL proto-oncogene 1, non-receptor tyrosine kinase
• NCBI Official Symbol: ABL1
• NCBI Official Synonym Symbols: ABL; JTK7; p150; c-ABL; v-abl; c-ABL1; bcr/abl
• NCBI Protein Information: tyrosine-protein kinase ABL1
• UniProt Protein Name: Tyrosine-protein kinase ABL1
• Protein Family: Tyrosine-protein kinase
• UniProt Gene Name: ABL1
• UniProt Synonym Gene Names: ABL; JTK7
• UniProt Entry Name: ABL1_HUMAN

NCBI Description

This gene is a protooncogene that encodes a protein tyrosine kinase involved in a variety of cellular processes, including cell division, adhesion, differentiation, and response to stress. The activity of the protein is negatively regulated by its SH3 domain, whereby deletion of the region encoding this domain results in an oncogene. The ubiquitously expressed protein has DNA-binding activity that is regulated by CDC2-mediated phosphorylation, suggesting a cell cycle function. This gene has been found fused to a variety of translocation partner genes in various leukemias, most notably the t(9;22) translocation that results in a fusion with the 5' end of the breakpoint cluster region gene (BCR; MIM:151410). Alternative splicing of this gene results in two transcript variants, which contain alternative first exons that are spliced to the remaining common exons. [provided by RefSeq, Aug 2014]

Uniprot Description

Non-receptor tyrosine-protein kinase that plays a role in many key processes linked to cell growth and survival such as cytoskeleton remodeling in response to extracellular stimuli, cell motility and adhesion, receptor endocytosis, autophagy, DNA damage response and apoptosis. Coordinates actin remodeling through tyrosine phosphorylation of proteins controlling cytoskeleton dynamics like WASF3 (involved in branch formation); ANXA1 (involved in membrane anchoring); DBN1, DBNL, CTTN, RAPH1 and ENAH (involved in signaling); or MAPT and PXN (microtubule-binding proteins). Phosphorylation of WASF3 is critical for the stimulation of lamellipodia formation and cell migration. Involved in the regulation of cell adhesion and motility through phosphorylation of key regulators of these processes such as BCAR1, CRK, CRKL, DOK1, EFS or NEDD9. Phosphorylates multiple receptor tyrosine kinases and more particularly promotes endocytosis of EGFR, facilitates the formation of neuromuscular synapses through MUSK, inhibits PDGFRB-mediated chemotaxis and modulates the endocytosis of activated B-cell receptor complexes. Other substrates which are involved in endocytosis regulation are the caveolin (CAV1) and RIN1. Moreover, ABL1 regulates the CBL family of ubiquitin ligases that drive receptor down-regulation and actin remodeling. Phosphorylation of CBL leads to increased EGFR stability. Involved in late-stage autophagy by regulating positively the trafficking and function of lysosomal components. ABL1 targets to mitochondria in response to oxidative stress and thereby mediates mitochondrial dysfunction and cell death. ABL1 is also translocated in the nucleus where it has DNA-binding activity and is involved in DNA-damage response and apoptosis. Many substrates are known mediators of DNA repair: DDB1, DDB2, ERCC3, ERCC6, RAD9A, RAD51, RAD52 or WRN. Activates the proapoptotic pathway when the DNA damage is too severe to be repaired. Phosphorylates TP73, a primary regulator for this type of damage-induced apoptosis. Phosphorylates the caspase CASP9 on 'Tyr-153' and regulates its processing in the apoptotic response to DNA damage. Phosphorylates PSMA7 that leads to an inhibition of proteasomal activity and cell cycle transition blocks. ABL1 acts also as a regulator of multiple pathological signaling cascades during infection. Several known tyrosine-phosphorylated microbial proteins have been identified as ABL1 substrates. This is the case of A36R of Vaccinia virus, Tir (translocated intimin receptor) of pathogenic E.coli and possibly Citrobacter, CagA (cytotoxin-associated gene A) of H.pylori, or AnkA (ankyrin repeat-containing protein A) of A.phagocytophilum. Pathogens can highjack ABL1 kinase signaling to reorganize the host actin cytoskeleton for multiple purposes, like facilitating intracellular movement and host cell exit. Finally, functions as its own regulator through autocatalytic activity as well as through phosphorylation of its inhibitor, ABI1.