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Product last modified at: 2025-01-01T09:04:27.496Z
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PDP - Template Name: Monoclonal Antibody
PDP - Template ID: *******c5e4b77
R Recombinant
Recombinant: Superior lot-to-lot consistency, continuous supply, and animal-free manufacturing.

C1R (E3R7T) Rabbit mAb #55653

Filter:
  • WB
Western Blotting Image 1: C1R (E3R7T) Rabbit mAb
Western blot analysis of extracts from human platelets and various human cell lines using C1R (E3R7T) Rabbit mAb (upper) or β-Actin (D6A8) Rabbit mAb #8457 (lower). Negative expression of C1R protein in SU-DHL-4 cells is consistent with the predicted expression pattern.

To Purchase # 55653

Cat. # Size Qty. Price Ships
55653T 20 µl
$156
55653S 100 µl
$371

Supporting Data

REACTIVITY H
SENSITIVITY Endogenous
MW (kDa) 95,55
Source/Isotype Rabbit IgG
Application Key:
  • WB-Western Blotting 
Species Cross-Reactivity Key:
  • H-Human 

Product Information

Product Usage Information

Application Dilution
Western Blotting 1:1000

Storage

Supplied in 10 mM sodium HEPES (pH 7.5), 150 mM NaCl, 100 µg/mL BSA, 50% glycerol, and less than 0.02% sodium azide. Store at –20°C. Do not aliquot the antibody.

Protocol

Specificity / Sensitivity

C1R (E3R7T) Rabbit mAb recognizes endogenous levels of total C1R protein. This antibody reacts with C1R proenzyme and C1R A (heavy) chain proteins.

Species Reactivity:

Human

Source / Purification

Monoclonal antibody is produced by immunizing animals with a synthetic peptide corresponding to residues near the amino terminus of human C1R protein.

Background

Complement C1R subcomponent (C1R) is a secreted serine protease module of the C1 macromolecular complex, which is a central node in complement activation via the classical pathway. Each C1 complex is stabilized by divalent calcium cations and contains, in part, a non-covalent dimer of identical C1R monomers that interact with the C1Q component of the C1 macromolecular complex (1). Each C1R monomer is synthesized as a proenzyme and is auto-activated within the C1 complex upon recognition of antigen-antibody complexes by C1Q (2,3). Activation of C1R leads to its cleavage into a disulfide-linked amino-terminal A (heavy) chain and a carboxyl terminal B (light) chain. The B chain contains serine protease activity that triggers a cascade of downstream enzymatic reactions that govern the classical pathway of complement (4,5).
For Research Use Only. Not For Use In Diagnostic Procedures.
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