Mouse Matrilin-4 Biotinylated Antibody

Catalog #: BAF3380 Datasheet / COA / SDS

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BAF3380

All Matrilin-4 Antibodies

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Mouse Matrilin-4 Biotinylated Antibody Summary

Species Reactivity

Mouse

Specificity

Detects mouse Matrilin-4 in Western blots. In Western blots, approximately 15% cross-reactivity with recombinant human Matrilin-4 is observed and less than 2% cross-reactivity with recombinant mouse Matrilin-2 is observed.

Source

Polyclonal Goat IgG

Formulation

Lyophilized from a 0.2 μm filtered solution in PBS with BSA as a carrier protein.

Label

Biotin

Applications

Recommended Concentration

Sample

Western Blot

0.1 µg/mL

Recombinant Mouse Matrilin‑4 (Catalog # 3380-MN)

Please Note: Optimal dilutions should be determined by each laboratory for each application. General Protocols are available in the Technical Information section on our website.

Reconstitution Calculator

Preparation and Storage

Reconstitution

Reconstitute at 0.2 mg/mL in sterile PBS.

Shipping

The product is shipped at ambient temperature. Upon receipt, store it immediately at the temperature recommended below.

Stability & Storage

Store the unopened product at -20 to -70 °C. Use a manual defrost freezer and avoid repeated freeze-thaw cycles. Do not use past expiration date.

Background: Matrilin-4

Matrilin-4 is a 73 kDa secreted glycoprotein that is a member of the matrilin family of the von Willebrand Factor-A (vWA) domain-containing superfamily (1). Matrilins are modular extracellular matrix proteins that serve as adaptors and linkers for other matrix proteins. Matrilin-4, like Matrilin‑2, has a broad distribution in both cartilage and in loose connective tissue such as dermis, lung and kidney, while Matrilins 1 and 3 are limited to cartilage. Matrilin-4 is present in nervous tissue and is abundant in the brain (2, 3). Mature mouse Matrilin-4 shares 98%, 90%, 89% and 66% amino acid (aa) identity with rat, human, canine and chicken Matrilin-4, respectively. The 624 aa mouse Matrilin-4 contains a 22 aa signal sequence, two potential glycosylation sites, and four cysteine-rich EGF-like domains placed between two vWA domains. A short isoform lacks the N-terminal vWA domain (aa 28‑217). A C-terminal alpha -helix/coiled-coil region (aa 590‑623) by which multimers are formed is often proteolytically removed so that Matrilin-4 is found as a mixture of monomers with homo- or hetero- dimers and trimers. Matrilin-4 forms multimers with Matrilins 1 and 2 but not with Matrilin-3 (3, 4). The N-terminal vWA domains of Matrilins associate with collagen IV microfibrils via the proteoglycans biglycan and decorin, linking the fibrils with other matrix constituents aggrecan and collagen II (5, 6). Matrilins also show calcium-dependent binding to the cartilage oligomeric matrix protein (COMP); this interaction is of high affinity for oligomeric Matrilin-4 and somewhat lower affinity for monomeric Matrilin-4 (6). Functions and distributions of Matrilins overlap enough so that knockouts of Matrilins 1, 2 and 3 lack obvious phenotypes (1).

References