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CLIMP-63 monoclonal antibody (G1/296)

ENZ-ABS669-0100 100 µg 476.00 USD
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Replaces Prod. #: ALX-804-604

Product Details

Alternative Name:ER protein p63, Cytoskeleton-linking membrane protein of 63kDa
Immunogen:Human CLIMP-63 (cytoskeleton-linking membrane protein of 63kDa) from Caco-2 cells golgi membrane fraction.
UniProt ID:Q07065
Source:Purified from hybridoma tissue culture supernatant.
Species reactivity:Human
Applications:ELISA, Flow Cytometry, ICC, IHC (FS), IP, WB
Purity Detail:Protein G-affinity purified.
Formulation:Liquid. In PBS containing 0.1% sodium azide.
Handling:Avoid freeze/thaw cycles.
Shipping:Blue Ice
Short Term Storage:+4°C
Long Term Storage:-20°C
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.
Regulatory Status:RUO - Research Use Only

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

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