C1QC Antibody
(Synonyms: C1QG, C1QC, Complement C1q subcomponent subunit C)C1QC Antibody is a Rabbit-derived and non-conjugated IgG monoclonal antibody, targeting to C1QC.
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Host:
Rabbit
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Isotype:
IgG
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Application:
WB, IHC-P
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Reactivity :
Human, Rat
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Formulation:
Supplied in PBS with 0.05% sodium azide
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Conjugation:
Non-conjugated
Applications
| Application |
WB
WB: Western Blot
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IHC-P
IHC-P: Immunohistochemistry-Paraffin
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|---|---|---|
| Dilution Ratio | 1:500-3000 | 1:50-100 |
Product Details
C1QC Antibody is a Rabbit-derived and non-conjugated IgG monoclonal antibody, targeting to C1QC.
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Host Rabbit
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Clonality Polyclonal
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Species ReactivityHuman, Rat
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Calculated Molecular Weight Predicted band size: 30kDa;
SwissProt: SwissProt: P02747
Purified recombinant fragment of human C1QC expressed in E. Coli.
Endogenous
affinity purified.
Non-conjugated
Unmodified
IgG
Product Properties
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Appearance
Solution
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Formulation
Supplied in PBS with 0.05% 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
C1QC is a Core component of the complement C1 complex, a multiprotein complex that initiates the classical pathway of the complement system, a cascade of proteins that leads to phagocytosis and breakdown of pathogens and signaling that strengthens the adaptive immune system. The classical complement pathway is initiated by the C1Q subcomplex of the C1 complex, which specifically binds IgG or IgM immunoglobulins complexed with antigens, forming antigen-antibody complexes on the surface of pathogens: C1QA, together with C1QB and C1QC, specifically recognizes and binds the Fc regions of IgG or IgM via its C1q domain. Immunoglobulin-binding activates the proenzyme C1R, which cleaves C1S, initiating the proteolytic cascade of the complement system. The C1Q subcomplex is activated by a hexamer of IgG complexed with antigens, while it is activated by a pentameric IgM. The C1Q subcomplex also recognizes and binds phosphatidylserine exposed on the surface of cells undergoing programmed cell death, possibly promoting activation of the complement system[1][2][3][4][5][6][7][8][9][10].
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Subcellular Localization
Secreted; Cell surface
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Isoforms & Post-Translational Modification
C1QC has an amino acid length of 245, molecular weight is 25774 Da.
O-linked glycans consist of Glc-Gal disaccharides bound to the oxygen atom of post-translationally added hydroxyl groups -
Subunit
Core component of the complement C1 complex, a calcium-dependent complex composed of 1 molecule of the C1Q subcomplex, 2 molecules of C1R and 2 molecules of C1S.
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SwissProt ID
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Synonyms
C1QG, C1QC, Complement C1q subcomponent subunit C
Documentation
[1]. Kishore U, et al. Modular organization of the carboxyl-terminal, globular head region of human C1q A, B, and C chains. J Immunol. 2003 Jul 15;171(2):812-20. [Content Brief]
[2]. Gadjeva MG, et al. Interaction of human C1q with IgG and IgM: revisited. Biochemistry. 2008 Dec 9;47(49):13093-102. [Content Brief]
[3]. Diebolder CA, et al. Complement is activated by IgG hexamers assembled at the cell surface. Science. 2014 Mar 14;343(6176):1260-3. [Content Brief]
[4]. Ugurlar D, et al. Structures of C1-IgG1 provide insights into how danger pattern recognition activates complement. Science. 2018 Feb 16;359(6377):794-797. [Content Brief]
[5]. Duncan AR, et al. The binding site for C1q on IgG. Nature. 1988 Apr 21;332(6166):738-40. [Content Brief]
[6]. Zwarthoff SA, et al. C1q binding to surface-bound IgG is stabilized by C1r(2)s(2) proteases. Proc Natl Acad Sci U S A. 2021 Jun 29;118(26):. [Content Brief]
[7]. Lin TY, et al. Activation of a complex of C1r and C1s subcomponents of human complement C1 by the third subcomponent C1q. J Biol Chem. 1980 Aug 25;255(16):7756-62. [Content Brief]
[8]. Burton DR, et al. The Clq receptor site on immunoglobulin G. Nature. 1980 Nov 27;288(5789):338-44. [Content Brief]
[9]. Czajkowsky DM, et al. The human IgM pentamer is a mushroom-shaped molecule with a flexural bias. Proc Natl Acad Sci U S A. 2009 Sep 1;106(35):14960-5. [Content Brief]
[10]. Païdassi H, et al. C1q binds phosphatidylserine and likely acts as a multiligand-bridging molecule in apoptotic cell recognition. J Immunol. 2008 Feb 15;180(4):2329-38. [Content Brief]