C5 Antibody (Polyclonal)

A goat antiserum raised against human C5 protein.


Product Specifications

Citations 13
Clonality

Polyclonal

Immunogen Highly purified human C5 protein
Applications See citations and technical data sheet for application info.
Concentration > 40 mg/mL
Conjugate Unconjugated
Cross Reactivity

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

Ordering Information

For Research Use Only in the United States. Not for use in diagnostic procedures.
Catalog Number A306
Catalog Number (CE) N/A
Size 2.0 mL
Price (USD) $330.00
Price (EURO) 170,00 €

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 C5 protein.

Size 2.0 mL
Concentration

> 40 mg/mL

Applications See citations and technical data sheet for application info.
Form Liquid. Whole Antiserum. ≤ 0.1% Sodium Azide
Clonality Polyclonal
Immunogen Highly purified human C5 protein
Conjugate Unconjugated
Cross Reactivity Human, Baboon, Dog, Horse, Rabbit, Guinea Pig, Rat, Mouse, Cat, Hamster, Pig, Rhesus macaque
Isotype Goat IgG
Purity N/A
Source

Goat

Specificity The anti-human C5 polyclonal antisera was tested against normal human plasma by double immunodiffusion, one-dimensional immunoelectrophoresis, quantitative radial immunodiffusion, and quantitative rocket immunoelectrophoresis. The antiserum was determined to be monospecific for C5 at varying concentrations.
Storage

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

Background

C5, is a plasma glycoprotein which is present in normal human serum/plasma at approximately 70 µg/mL, and is key to all complement pathways. C5 is synthesized by a wide variety of cells, including liver hepatocytes, epithelial cells of the genitourinary and intestinal tract, and phagocytic mononuclear cells. The precursor protein to C5 (pro-C5) is a single chain polypeptide which undergoes proteolytic cleavage to yield the circulating form of C5. This circulating form contains 2 disulfide-bonded subunits: α – 115 kD, β – 75 kD, which gives the intact C5 protein an approximate total molecular weight of 190 kD. Activation of the classical or alternative complement pathway results in the assembly of C5 convertase enzymes (C4b,2a,3b and C3b,Bb,C3b) on the target cell surface. Both convertase enzymes cleave C5 into C5a and C5b. C5a is a complement-derived anaphylatoxin. It also expresses potent chemotactic activities for neutrophils and monocytes. C5 can be further cleaved and activated by a variety of non-complement proteolytic enzymes to express C5a-like biological activities without the release of a polypeptide fragment. C5a can also function as an immunoregulator, enhancing both antigen-specific and non-specific antibody response in vitro. C5b remains bound to the C5 convertase on the cell surface. Upon interaction with C6 and C7, a C5b,C6,C7 complex is formed that partially inserts into the cell surface. It subsequently binds C8 and several C9 molecules to form the C5b-9 complex, also known as the Membrane Attack Complex (MAC) which causes irreversible target cell damage. C5 convertase enzymes can be assembled in solution (with cobra venom factor or on particles which do not have a membranous surface and lack a C5b-9 binding site). In these cases, the C5b-9 complex disassociates from the C5 convertase and combines with S-proteins to form a soluble SC5b-9 complex. This complex has no known membranolytic function.

Citations

Title Year Applications Sample Species Sample Sample Details

Borrelia valaisiana resist complement-mediated killing independently of the recruitment of immune regulators and inactivation of complement components

2013

WB

Bacteria

Borrelia valaisiana

Involvement of C3a and C5a in Interleukin-8 Secretion by Human Polymorphonuclear Cells in Response to Capsular Material of Cryptococcus neoformans.

1998

Complement Activation Assay

Human

Polymorphonuclear Cells

Cryptococcus neoformans

FACIN, a Double-Edged Sword of the Emerging Periodontal Pathogen Filifactor Alocis: A Metabolic Enzyme Moonlighting as a Complement Inhibitor.

2016

ELISA

Human

Serum

Novel Assays to Distinguish Between Properdin-Dependent and Properdin-Independent C3 Nephritic Factors Provide Insight Into Properdin-Inhibiting Therapy.

2019

ELISA

Human

Plasma

Novel Assays to Distinguish Between Properdin-Dependent and Properdin-Independent C3 Nephritic Factors Provide Insight Into Properdin-Inhibiting Therapy.

2019

ELISA

Human

Serum

Weak Expression of Terminal Complement in Active Antibody-Mediated Rejection of the Kidney.

2022

IHC

Human

Kidney Tissue

Antibody Mediated Rejection

C3(H2O) prevents rescue of complement-mediated C3 glomerulopathy in Cfh-/- Cfd-/- mice

2020

WB

Mouse

Plasma

Loss of properdin exacerbates C3 glomerulopathy resulting from factor H deficiency

2013

WB

Mouse

Plasma

C3 dysregulation due to factor H deficiency is mannan-binding lectin-associated serine proteases (MASP)-1 and MASP-3 independent in vivo

2014

WB

Mouse

Plasma

Regulation of C3 Activation by the Alternative Complement Pathway in the Mouse Retina

2016

WB

Mouse

Plasma

Efficacy of GalNAc C3 siRNAs in factor H-deficient mice with C3 glomerulopathy

2024

WB

Mouse

Plasma

C3G

Neutrophils from Patients with Advanced Human Immunodeficiency Virus Infection Have Impaired Complement Receptor Function and Preserved Fcγ Receptor Function

1999

ELISA

Purified Protein

Purified Protein

HIV

Activation of early components of complement targets myelin and oligodendrocytes in the aged rhesus monkey brain.

2005

IHC

Rhesus Monkey

Brain Tissue