Procollagen Lysine-2-Oxoglutarate-5-Dioxygenase 2 (PLOD2) Antibody

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292.5€ (80 µl)

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935106861
info@markelab.com
name
Procollagen Lysine-2-Oxoglutarate-5-Dioxygenase 2 (PLOD2) Antibody
category
Primary Antibodies
provider
Abbexa
reference
abx034642
tested applications
ELISA, WB

Description

Forms hydroxylysine residues in Xaa-Lys-Gly-sequences in collagens. These hydroxylysines serve as sites of attachment for carbohydrate units and are essential for the stability of the intermolecular collagen cross-links.

Documents del producto

Instrucciones
Data sheet
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Product specifications

Category
Primary Antibodies
Immunogen Target
Target: Procollagen Lysine-2-Oxoglutarate-5-Dioxygenase 2 (PLOD2)
Immunogen: KLH-conjugated synthetic peptide between 483-512 amino acids from the C-terminal region of human PLOD2.
Host
Rabbit
Reactivity
Human
Recommended Dilution
WB: 1/1000. Optimal dilutions/concentrations should be determined by the end user.
Clonality
Polyclonal
Conjugation
Unconjugated
Isotype
IgG
Observed MW
Calculated MW: 84.7 kDa
Purification
Purified through a protein A column, followed by peptide affinity purification.
Size 1
80 µl
Size 2
400 µl
Form
Liquid
Tested Applications
ELISA, WB
Buffer
PBS containing 0.09% sodium azide.
Availability
Shipped within 5-10 working days.
Storage
Aliquot and store at -20°C. Avoid repeated freeze/thaw cycles.
Dry Ice
No
UniProt ID
O00469
Background
Antibody anti-PLOD2
Status
RUO
Note
THIS PRODUCT IS FOR RESEARCH USE ONLY. NOT FOR USE IN DIAGNOSTIC, THERAPEUTIC OR COSMETIC PROCEDURES. NOT FOR HUMAN OR ANIMAL CONSUMPTION.

Descripción

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Procollagen Lysine-2-Oxoglutarate-5-Dioxygenase 2 (PLOD2) Antibody

PLOD2 Antibody is a Rabbit Polyclonal antibody against PLOD2. The protein encoded by this gene is a membrane-bound homodimeric enzyme that is localized to the cisternae of the rough endoplasmic reticulum. The enzyme (cofactors iron and ascorbate) catalyzes the hydroxylation of lysyl residues in collagen-like peptides. The resultant hydroxylysyl groups are attachment sites for carbohydrates in collagen and thus are critical for the stability of intermolecular crosslinks. Some patients with Ehlers-Danlos syndrome type VIB have deficiencies in lysyl hydroxylase activity. Mutations in the coding region of this gene are associated with Bruck syndrome. Alternative splicing results in multiple transcript variants encoding different isoforms.

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