Replaces Prod. #: ALX-804-604
Product Details
| Alternative Name: | ER protein p63, Cytoskeleton-linking membrane protein of 63kDa |
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| Clone: | G1/296 |
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| Host: | Mouse |
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| Isotype: | IgG2aκ |
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| Immunogen: | Human CLIMP-63 (cytoskeleton-linking membrane protein of 63kDa) from Caco-2 cells golgi membrane fraction. |
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| UniProt ID: | Q07065 |
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| Source: | Purified from hybridoma tissue culture supernatant. |
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| Species reactivity: | Human
Monkey
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| Applications: | ELISA, Flow Cytometry, ICC, IHC (FS), IP, WB
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| Purity Detail: | Protein G-affinity purified. |
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| Formulation: | Liquid. In PBS containing 0.1% sodium azide. |
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| Handling: | Avoid freeze/thaw cycles. |
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| Shipping: | Blue Ice |
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| Short Term Storage: | +4°C |
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| Long Term Storage: | -20°C |
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| Scientific Background: | The cytoskeleton-linking membrane protein of 62kDa (CLIMP-63) is a marker for the reticular subdomain of the rough endoplasmatic reticulum (ER) and is excluded from the outer nuclear membrane. Concentration of CLIMP-63 into patches may enhance microtubule binding on the cytosolic side and contribute to ER morphology by the formation of a protein scaffold in the lumen of the ER, linking the rough ER to microtubules. |
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| Regulatory Status: | RUO - Research Use Only |
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Product Literature References
Dynamics of CLIMP-63 S-acylation control ER morphology: P.A. Sandoz, et al.; Nat. Commun.
14, 264 (2023),
Abstract;
Rhomboid protease RHBDL4 promotes retrotranslocation of aggregation-prone proteins for degradation: J. Bock, et al.; Cell Rep.
40, 111175 (2022),
Abstract;
Apogossypol-mediated reorganisation of the endoplasmic reticulum antagonises mitochondrial fission and apoptosis: G. Yedida, et al.; Cell Death Dis.
10, 521 (2019),
Abstract;
Palmitoylation mediates membrane association of hepatitis E virus ORF3 protein and is required for infectious particle secretion: J. Gouttenoire, et al.; PLoS Pathog.
14, e1007471 (2018),
Abstract;
Determinants for Membrane Association of the Hepatitis C Virus NS2 Protease Domain: C.M. Lange, et al.; J. Virol.
88, 6519 (2014),
Abstract;
Protrudin binds atlastins and endoplasmic reticulum-shaping proteins and regulates network formation: J. Chang, et al.; PNAS
110, 14954 (2013),
Application(s): ICC using human cells,
Abstract;
Full Text
Differential NDR/LATS interactions with the human MOB family reveal a negative role for human MOB2 in the regulation of human NDR kinases: R.S. Kohler, et al.; Mol. Cell. Biol.
30, 4507 (2010),
Application(s): WB using human cell lysates,
Abstract;
Full Text
Proteomics of endoplasmic reticulum-golgi intermediate compartment (ERGIC) membranes from brefeldin A-treated HepG2 cells identifies ERGIC-32, a new cycling protein that interacts with human Erv46: L. Breuza, et al.; J. Biol. Chem.
279, 47242 (2004),
Abstract;
Full Text
Subdomain-specific localization of CLIMP-63 (p63) in the endoplasmic reticulum is mediated by its luminal alpha-helical segment: D.R. Klopfenstein, et al.; J. Cell Biol.
153, 1287 (2001),
Abstract;
Full Text
A novel direct interaction of endoplasmic reticulum with microtubules: D.R. Klopfenstein, et al.; EMBO J.
17, 6168 (1998),
Abstract;
Full Text
The plasma cell associated antigen detectable by antibody VS38 is the p63 rough endoplasmic reticulum protein: A.H. Banham, et al.; J. Clin. Pathol.
50, 485 (1997),
Application(s): Flow Cytometry,
Abstract;
Reassessment of the subcellular localization of p63: A. Schweizer, et al.; J. Cell Sci.
108, 2477 (1995),
Abstract;
Full Text
Retention of p63 in an ER-Golgi intermediate compartment depends on the presence of all three of its domains and on its ability to form oligomers: A. Schweizer, et al.; J. Cell Biol.
126, 25 (1994),
Abstract;
Full Text
A reversibly palmitoylated resident protein (p63) of an ER-Golgi intermediate compartment is related to a circulatory shock resuscitation protein: A. Schweizer, et al.; J. Cell Sci.
104, 685 (1993),
Abstract;
Full Text
Characterization of a novel 63 kDa membrane protein. Implications for the organization of the ER-to-Golgi pathway: A. Schweizer, et al.; J. Cell Sci.
104, 671 (1993),
Abstract;
Full Text
