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ABL1 recombinant protein :: Tyrosine-protein kinase ABL1 Recombinant Protein

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Catalog # MBS717062
Unit / Price
  0.01 mg  /  $110 +1 FREE 8GB USB
  0.05 mg  /  $190 +1 FREE 8GB USB
  0.1 mg  /  $285 +1 FREE 8GB USB
  0.2 mg  /  $460 +1 FREE 8GB USB
  0.5 mg  /  $750 +1 FREE 8GB USB
  1 mg  /  $1,180 +1 FREE 8GB USB
SDS-PAGE
Product Name

Tyrosine-protein kinase ABL1, Recombinant Protein

Popular Item
Also Known As

Recombinant Human Tyrosine-protein kinase ABL1

Product Synonym Names
Abelson murine leukemia viral oncogene homolog 1; Abelson tyrosine-protein kinase 1; Proto-oncogene c-Ablp150
Product Synonym Gene Name
ABL; JTK7[Similar Products]
Research Use Only
For Research Use Only. Not for use in diagnostic procedures.
MBS717062 COA
Sequence Positions
4-194. Partial.
Sequence Length
194
Sequence
ICLKLVGCKS KKGLSSSSSC YLEEALQRPV ASDFEPQGLS EAARWNSKEN LLAGPSENDP NLFVALYDFV ASGDNTLSIT KGEKLRVLGY NHNGEWCEAQ TKNGQGWVPS NYITPVNSLE KHSWYHGPVS RNAAEYLLSS GINGSFLVRE SESSPGQRSI SLRYEGRVYH YRINTASDGK LYVSSESRFN T
OMIM
189980
3D Structure
ModBase 3D Structure for P00519
Host
E Coli
Purity/Purification
Greater than 90% as determined by SDS-PAGE. (lot specific)
Form/Format
Liquid containing glycerol
Tag Information
This protein contains an N-terminal tag and may also contain a C-terminal tag. Tag types are determined by various factors including tag-protein stability, please inquire for tag information.
Sterility
Sterile filter available upon request.
Endotoxin
Low endotoxin available upon request.
Preparation and Storage
Store at -20 degree C, for extended storage, conserve at -20 degree C or -80 degree C.
ISO Certification
Manufactured in an ISO 9001:2008 Certified Laboratory.
Other Notes
Small volumes of ABL1 recombinant protein vial(s) may occasionally become entrapped in the seal of the product vial during shipment and storage. If necessary, briefly centrifuge the vial on a tabletop centrifuge to dislodge any liquid in the container`s cap. Certain products may require to ship with dry ice and additional dry ice fee may apply.
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

ABL1 recombinant protein SDS-PAGE image
(Note: Representative image, actual molecular weight may vary depending on Tag type and expression host)
NCBI/Uniprot data below describe general gene information for ABL1. It may not necessarily be applicable to this product.
NCBI GI #
NCBI GeneID
NCBI Accession #
NCBI GenBank Nucleotide #
UniProt Primary Accession #
UniProt Secondary Accession #
UniProt Related Accession #
Molecular Weight
48.5kD
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
NCBI Official Synonym Symbols
ABL; JTK7; p150; c-ABL; v-abl; c-ABL1; bcr/abl
  [Similar Products]
NCBI Protein Information
tyrosine-protein kinase ABL1
UniProt Protein Name
Tyrosine-protein kinase ABL1
UniProt Synonym Protein Names
Abelson murine leukemia viral oncogene homolog 1; Abelson tyrosine-protein kinase 1; Proto-oncogene c-Abl; p150
Protein Family
UniProt Gene Name
UniProt Synonym Gene Names
ABL; JTK7  [Similar Products]
UniProt Entry Name
ABL1_HUMAN
NCBI Summary for ABL1
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 Comments for ABL1
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.
Product References and Citations for ABL1 recombinant protein
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)

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While every efforts were made to ensure the accuracy of the information provided in this datasheet, MyBioSource will not be liable for any omissions or errors contained herein. MyBioSource reserves the right to make changes to this datasheet at any time without prior notice.

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