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CTRP5 Polyclonal Antibody, APC-Cy7 Conjugated

Product Specifications

Background

Members of the C1q superfamily have diverse functions that are related to cell adhesion and basement membrane components. CTRP5 (Complement C1q tumor necrosis factor-related protein 5) is a 243 amino acid secreted and membrane-associated protein that contains a collagen-like domain and a C1q domain. CTRP5 is a short-chain collagen that is expressed in retinal pigment epithelium as well as brain, lung, liver and placenta. By forming an extracellular hexagonal lattice, CTRP5 facilitates the adhesion of basal retinal pigment epithelium to Bruch?s membrane, the innermost layer of the choroid. A mutation within the C1q domain of CTRP5 results in abnormal high molecular weight aggregate formation, which alters its structure and interactions. This mutation may result in the presentation of late-onset retinal degeneration (LORD), an autosomal dominant disorder that is characterized by punctate yellow-white deposits in the retinal fundus and night blindness.

Synonyms

C1q and tumor necrosis factor related protein 5; C1QTNF5; Complement C1q tumor necrosis factor related protein 5 precursor; LORD; C1QT5_HUMAN.

Gene ID

114902

Swiss Prot

Q9BXJ0

Cellular Locus

Secreted

Host

Rabbit

Cross Reactivity

Mouse

Immunogen

191-243/243

Target

CTRP5

Clonality

Polyclonal

Isotype

IgG

Conjugation

APC-Cy7

Source

KLH conjugated synthetic peptide derived from human CTRP5

Applications

WB, IF (IHC-P), IF (IHC-F), IF (ICC)

Purification

Purified by Protein A.

Excitation Emission

650nm/780nm

Concentration

1µg/µl

Dilution

WB (1:300-5000), IF (IHC-P) (1:50-200), IF (IHC-F) (1:50-200), IF (ICC) (1:50-200)

Buffer

Aqueous buffered solution containing 0.01M TBS (pH7.4) with 1% BSA, 0.02% Proclin300 and 50% Glycerol.

Modification

Unmodified

Storage Conditions

Store at -20°C. Aliquot into multiple vials to avoid repeated freeze-thaw cycles.

Gene ID URL

114902

Predicted Cross Reactivity

Human, Rat, Dog, Cow, Pig, Rabbit

Curated Selection

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