Docking Protein 1, 62kDa (Downstream of tyrosine Kinase 1) (DOK1) (AA 331-478) antibody

Details for Product No. ABIN968157
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Antigen
Synonyms 4432404K01Rik, ARTC4, DO, DOK1, AW557123, p62DOK, Dok-1, P62DOK
Epitope
AA 331-478
(40), (35), (14), (13), (12), (4), (4), (3), (2), (2), (2), (2), (2), (1), (1), (1), (1), (1), (1), (1)
Reactivity
Human
(194), (118), (118), (41), (41), (41)
Host
Mouse
(193), (2)
Clonality (Clone)
Monoclonal ()
Conjugate
Un-conjugated
(6), (6), (6), (4), (4), (4), (4), (4), (4), (4), (4), (2), (1), (1), (1), (1), (1), (1)
Application
Western Blotting (WB)
(144), (58), (44), (43), (41), (14), (12), (11), (4), (2), (2)
Pubmed 5 references available
Quantity 50 µg
Options
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Catalog No. ABIN968157
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Immunogen Human p62 [Dok]
Clone DF7
Isotype IgG1
Characteristics 1. Since applications vary, each investigator should titrate the reagent to obtain optimal results.
2. Source of all serum proteins is from USDA inspected abattoirs located in the United States.
3. Caution: Sodium azide yields highly toxic hydrazoic acid under acidic conditions. Dilute azide compounds in running water before discarding to avoid accumulation of potentially explosive deposits in plumbing.
4. Please refer to us for technical protocols.
Purification Purified from tissue culture supernatant or ascites by affinity chromatography.
Alternative Name p62 dok
Background P62 [Dok] (Downstream of tyrosine kinases) was identified as a target of protein tyrosine kinases. Following phosphorylation, p62 [Dok] binds to Ras GTPase activating protein (Ras-GAP), indicating a role for p62 [Dok] in intracellular signaling pathways. p62 [Dok] contains several motifs that signify its important interactions with signaling proteins. These domains include the pleckstrin homology (PH) domain in the amino terminus, numerous tyrosines in the C-terminus, and ten PXXP motifs. p62 [Dok] localizes to the cell membrane by binding to inositol phosphates via its PH domain. When phosphorylated, the tyrosines serve as binding sites for SH2 containing proteins and the polyproline regions serve as binding sites for SH3 containing proteins. p62 [Dok] is constitutively phosphorylated in CML patients, suggesting that it is a target of the translocation induced increase in tyrosine kinase activity of c-Abl. In addition, p62 [Dok] is phosphorylated following c-Kit ligand binding to the c-Kit receptor.
Synonyms: Dok1
Molecular Weight 62 kDa
Comment

Related Products: ABIN967389

Restrictions For Research Use only
Format Liquid
Concentration 250 µg/ml
Buffer Aqueous buffered solution containing BSA, glycerol.
Preservative Sodium azide
Precaution of Use This product contains sodium azide: a POISONOUS AND HAZARDOUS SUBSTANCE which should be handled by trained staff only.
Storage -20 °C
Supplier Images
anti-Docking Protein 1, 62kDa (Downstream of tyrosine Kinase 1) (DOK1) (AA 331-478) antibody Western blot analysis for p62 [Dok]. Hs68 cell lysates (Human skin fibroblasts, ATCC CRL-1635) were probed with the mouse anti-human p62 [Dok] antibody at dilutions of 1:125 (lane 1), 1:250 (lane 2) and 1:500 (lane 3).
anti-Docking Protein 1, 62kDa (Downstream of tyrosine Kinase 1) (DOK1) (AA 331-478) antibody (2) anti-Docking Protein 1, 62kDa (Downstream of tyrosine Kinase 1) (DOK1) (AA 331-478) antibody (Image 2)
Product cited in: Carpino, Wisniewski, Strife et al.: "p62(dok): a constitutively tyrosine-phosphorylated, GAP-associated protein in chronic myelogenous leukemia progenitor cells." in: Cell, Vol. 88, Issue 2, pp. 197-204, 1997 (PubMed).

Yamanashi, Baltimore: "Identification of the Abl- and rasGAP-associated 62 kDa protein as a docking protein, Dok." in: Cell, Vol. 88, Issue 2, pp. 205-11, 1997 (PubMed).

Holland, Gale, Gish et al.: "Juxtamembrane tyrosine residues couple the Eph family receptor EphB2/Nuk to specific SH2 domain proteins in neuronal cells." in: The EMBO journal, Vol. 16, Issue 13, pp. 3877-88, 1997 (PubMed).

Di Cristofano, Carpino, Dunant et al.: "Molecular cloning and characterization of p56dok-2 defines a new family of RasGAP-binding proteins." in: The Journal of biological chemistry, Vol. 273, Issue 9, pp. 4827-30, 1998 (PubMed).

Lindsay, Holaska, Welch et al.: "Ran-binding protein 3 is a cofactor for Crm1-mediated nuclear protein export." in: The Journal of cell biology, Vol. 153, Issue 7, pp. 1391-402, 2001 (PubMed).

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