C1q Antibody (Polyclonal)

A goat antiserum raised against human C1q protein


Product Specifications

Citations14
Clonality

Polyclonal

Immnogen

Highly purified human human C1q protein

Applications

See citations and technical data sheet for application info.

Concentration> 40 mg/mL
ConjugateUnconjugated
Cross Reactivity

Human, Baboon, Horse, Dog, Cat, Rabbit, Hamster, Mouse, Rat, Guinea Pig

Ordering Information

For Research Use Only in the United States. Not for use in diagnostic procedures.
Catalog NumberA301
Catalog Number (CE)N/A
Size2.0 mL
Price (USD)$235.00
Price (EURO)205,00 €

Contact us

US Phone+1 (858) 552 1100
EU Phone+353 (91) 412 474
US Emailcontact-us@quidelortho.com
EU Emailcontact-emea@quidelortho.com

Specifications

Description

A goat antiserum raised against human C1q protein

Size

2.0 mL

Concentration> 40 mg/mL
ApplicationsSee citations and technical data sheet for application info.
FormLiquid. Whole Antiserum. ≤ 0.1% Sodium Azide
ClonalityPolyclonal
Immunogen

Highly purified human human C1q protein

ConjugateUnconjugated
Cross ReactivityHuman, Baboon, Horse, Dog, Cat, Rabbit, Hamster, Mouse, Rat, Guinea Pig
Isotype

Goat IgG

Purity

N/A

SourceGoat
Specificity

The Anti-human C1q was tested against normal human plasma by double immunodiffusion, one-dimensional immunoelectrophoresis, two-dimensional immunoelectrophoresis, and quantitative rocket immunoelectrophoresis. The antiserum was determined to be monospecific for C1q at varying concentrations.

Storage

Short term (30 days) 4˚C. Long term at or below –20˚C.

Background

The C1q molecule is a large protein with a molecular weight of 410 kD. This hexamer is composed of three unique protein subunits (A, B, and C) with molecular weights of 29, 26, and 22 kD respectively, and is present in normal human serum at an approximate concentration of 70 µg/mL. The assembled C1q molecule contains a central core or stalk, six collagen-like domains and six globular protein heads, resulting in a the appearance of a “bouquet of tulips.” The globular or terminal regions are responsible for binding the Fc portion of immunoglobulin (IgM, and IgG). C1q is one of three subcomponents that together make the first component of the classical complement pathway, C1. C1q complexes with two C1s and two C1r components, and together, they form the C1 complex. Initiation of the classical complement pathway occurs when C1q binds with IgM or IgG containing antigen-antibody complexes.

Citations

TitleYearApplicationsSample SpeciesSampleSample Details

The Alternative Pathway Is Necessary and Sufficient for Complement Activation by Anti-THSD7A Autoantibodies, Which Are Predominantly IgG4 in Membranous Nephropathy.

2022ELISAHuman

Serum

N/A

Differential and Altered Spatial Distribution of Complement Expression in Age-Related Macular Degeneration.

2021ELISAHuman

Eye Tissue

Age-Related Macular Degeneration

The Surface-Exposed Protein SntA Contributes to Complement Evasion in Zoonotic Streptococcus suis

2018ELISAHuman

Purified protein

N/A

Serologic features of cohorts with variable genetic risk for systemic lupus erythematosus

2018ELISAHuman

Serum

Systemic Lupus Erythematosus

Neurotoxic reactive astrocytes are induced by activated microglia

2017NeutralizationRat

Protein Injection

N/A

Broad Susceptibility of Nucleolar Proteins and Autoantigens to Complement C1 Protease Degradation.

2017WBHuman

HeLa Cells

N/A

Intravenous Immunoglobulin With Enhanced Polyspecificity Improves Survival in Experimental Sepsis and Aseptic Systemic Inflammatory Response Syndromes.

2016ELISAN/A

IVIg

Exposed to ferrous ions

Proteolytic inactivation of nuclear alarmin high-mobility group box 1 by complement protease C1s during apoptosis

2016WBCell Culture

Jurkat Cells

N/A

Complement protein C1q modulates neurite outgrowth in vitro and spinal cord axon regeneration in vivo

2015IPMouse

Brain Tissue

Cerebellum myelin substrate

Inhibition of aberrant complement activation by a dimer of acetylsalicylic acid.

2015WBHuman

Serum

Acetyl salicylic acid dimer 5,5'-methylenebis(2-acetoxybenzoic acid) (DAS)

DC-SIGN, C1q, and gC1qR form a trimolecular receptor complex on the surface of monocyte-derived immature dendritic cells

2012ELISA, IF, WBHuman

Dendritic Cell

N/A

Mutations within a human IgG2 antibody form distinct and homogeneous disulfide isomers but do not affect Fc gamma receptor or C1q binding

2010ELISAN/A

CD44 (coating)

N/A

Early Involvement of Immune/Inflammatory Response Genes in Retinal Degeneration in DBA/2J Mice

2010IFMouse

Microglial Cells

N/A

Binding of vitronectin by the Moraxella catarrhalis UspA2 protein interferes with late stages of the complement cascade

2006WBHuman

Serum

Moraxella catarrhalis