CCDC22 Antibody (YA8238)
(Synonyms: CXorf37; JM1; RTSC2)CCDC22 Antibody (YA8238) is a Mouse-derived and non-conjugated IgG1 monoclonal antibody, targeting to CCDC22.
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Host:
Mouse
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Isotype:
IgG
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Application:
IHC-P
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Reactivity :
Human, Mouse, Rat
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Formulation:
Spplied in PBS (pH 7.3) containing 1% BSA, 50% glycerol and 0.02% sodium azide.
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Conjugation:
Non-conjugated
Applications
| Application |
IHC-P
IHC-P: Immunohistochemistry-Paraffin
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|---|---|
| Dilution Ratio | 1:500-800 |
Product Details
CCDC22 Antibody (YA8238) is a Mouse-derived and non-conjugated IgG1 monoclonal antibody, targeting to CCDC22.
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Host Mouse
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Clonality Monoclonal
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Species ReactivityHuman, Mouse, Rat
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Calculated Molecular Weight Predicted band size: 70.6 kDa
Full length human recombiant protein of human CCDC22 produced in E.coli.
Endogenous
Affinity purified
Non-conjugated
Unmodified
IgG
Product Properties
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Appearance
Solution
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Formulation
Spplied in PBS (pH 7.3) containing 1% BSA, 50% glycerol and 0.02% sodium azide.
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Storage & Stability
Stored at -20°C for 1 year. Avoid repeated freeze / thaw cycles.
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Shipping
Shipping with blue ice.
Background
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Function
CCDC22 component of the commander complex that is essential for endosomal recycling of transmembrane cargos; the Commander complex is composed of composed of the CCC subcomplex and the retriever subcomplex. Component of the CCC complex, which is involved in the regulation of endosomal recycling of surface proteins, including integrins, signaling receptor and channels. Involved in regulation of NF-kappa-B signaling. Promotes ubiquitination of I-kappa-B-kinase subunit IKBKB and its subsequent proteasomal degradation leading to NF-kappa-B activation; the function may involve association with COMMD8 and a CUL1-dependent E3 ubiquitin ligase complex. May down-regulate NF-kappa-B activity via association with COMMD1 and involving a CUL2-dependent E3 ubiquitin ligase complex. Regulates the cellular localization of COMM domain-containing proteins, such as COMMD1 and COMMD10. Component of the CCC complex, which is involved in the regulation of endosomal recycling of surface proteins, including integrins, signaling receptor and channels. The CCC complex associates with SNX17, retriever and WASH complexes to prevent lysosomal degradation and promote cell surface recycling of numerous cargos such as integrins ITGA5:ITGB1. Plays a role in copper ion homeostasis. Involved in copper-dependent ATP7A trafficking between the trans-Golgi network and vesicles in the cell periphery; the function is proposed to depend on its association within the CCC complex and cooperation with the WASH complex on early endosomes |(Microbial infection) The CCC complex, in collaboration with the heterotrimeric retriever complex, mediates the exit of human papillomavirus to the cell surface[1][2][3][4][5].
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Subcellular Localization
Endosome,Cytoplasm, cytoskeleton, microtubule organizing center, centrosome
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Expression
Tissue_Specificity: Widely expressed in adult tissues and in fetal liver and brain, with highest levels in prostate and lowest in skeletal muscle -
Isoforms & Post-Translational Modification
O60826: 627 amino acids, molecular weight 70756 Da.
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Subunit
Component of the commander complex consisting of the CCC subcomplex and the retriever subcomplex (PubMed:37172566, PubMed:38459129, PubMed:25355947, PubMed:28892079)
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SwissProt ID
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Synonyms
CXorf37; JM1; RTSC2
Documentation
[1]. Healy MD, et al. Structure of the endosomal Commander complex linked to Ritscher-Schinzel syndrome. Cell. 2023 May 11;186(10):2219-2237.e29. [Content Brief]
[2]. Laulumaa S, et al. Structure and interactions of the endogenous human Commander complex. Nat Struct Mol Biol. 2024 Jun;31(6):925-938. [Content Brief]
[3]. Starokadomskyy P, et al. CCDC22 deficiency in humans blunts activation of proinflammatory NF-κB signaling. J Clin Invest. 2013 May;123(5):2244-56. [Content Brief]
[4]. Phillips-Krawczak CA, et al. COMMD1 is linked to the WASH complex and regulates endosomal trafficking of the copper transporter ATP7A. Mol Biol Cell. 2015 Jan 1;26(1):91-103. [Content Brief]
[5]. McNally KE, et al. Retriever is a multiprotein complex for retromer-independent endosomal cargo recycling. Nat Cell Biol. 2017 Oct;19(10):1214-1225. [Content Brief]