Recombinant Mouse Collagen XIII alpha 1 Protein, CF

Catalog #: 4627-CL Datasheet / COA / SDS

Catalog #	Availability	Size / Price	Qty
4627-CL-050

R&D Systems Recombinant Proteins and Enzymes

1 Image

All Collagen XIII alpha 1 Proteins and Enzymes

Product Details

Supplemental Products

Reviews

Summary Product Datasheets Carrier Free Data Images Reconstitution Calculator Background Related Research Areas

Recombinant Mouse Collagen XIII alpha 1 Protein, CF Summary

Product Specifications

Purity

>80%, by SDS-PAGE under reducing conditions and visualized by silver stain

Endotoxin Level

<0.01 EU per 1 μg of the protein by the LAL method.

Activity

Measured by the ability of the immobilized protein to support the adhesion of A431 human epithelial carcinoma cells.

When 1 x 10⁵ cells per well are added to rmCOL-13A1 coated plate (2 μg/mL, 100 μL/well), approximately 45%-75% will adhere after 1 hour at 37 °C.

Optimal dilutions should be determined by each laboratory for each application.

Source

Mouse myeloma cell line, NS0-derived mouse Collagen XIII alpha 1 protein
Glu107-Gln565, with an N-terminal 6-His tag

Accession #

AAH34164

N-terminal Sequence
Analysis

His

Predicted Molecular Mass

46.0 kDa

SDS-PAGE

50-60 kDa, reducing conditions

Product Datasheets

4627-CL

Product Datasheet

COA

SDS

Carrier Free

What does CF mean?

CF stands for Carrier Free (CF). We typically add Bovine Serum Albumin (BSA) as a carrier protein to our recombinant proteins. Adding a carrier protein enhances protein stability, increases shelf-life, and allows the recombinant protein to be stored at a more dilute concentration. The carrier free version does not contain BSA.

What formulation is right for me?

In general, we advise purchasing the recombinant protein with BSA for use in cell or tissue culture, or as an ELISA standard. In contrast, the carrier free protein is recommended for applications, in which the presence of BSA could interfere.

4627-CL

Formulation	Lyophilized from a 0.2 μm filtered solution in PBS.
Reconstitution	Reconstitute at 300 μg/mL in PBS.
Shipping	The product is shipped at ambient temperature. Upon receipt, store it immediately at the temperature recommended below.
Stability & Storage:	Use a manual defrost freezer and avoid repeated freeze-thaw cycles. 12 months from date of receipt, -20 to -70 °C as supplied. 1 month, 2 to 8 °C under sterile conditions after reconstitution. 3 months, -20 to -70 °C under sterile conditions after reconstitution.

Reconstitution Calculator

Background: Collagen XIII alpha 1

Collagen XIII alpha 1 is an 85 kDa - 95 kDa protein in the type 2 transmembrane collagen family (1). Mature mouse Collagen XIII alpha 1 consists of a 40 amino acid (aa) cytoplasmic domain, a 19 aa transmembrane segment, and a 692 aa extracellular domain (ECD). The ECD contains three collagenous regions separated by shorter non‑collagenous regions (2, 3). Within comparable regions of the ECD, mouse Collagen XIII alpha 1 shares 85% and 88% aa sequence identity with human and rat Collagen XIII alpha 1, respectively. Mouse Collagen XIII alpha 1 is extensively spliced, with some isoforms showing a tissue specific distribution (2, 4). Collagen XIII alpha 1 is widely expressed during development and in the adult (4, 5). It localizes to intercellular adherens junctions and cell-matrix focal adhesions (6, 7). Collagen XIII alpha 1 assembles into disulfide-linked trimers, a process that is enhanced by proline hydroxylation (2, 8). Trimerization involves triple helix formation within the collagenous domains, although portions of the non‑collagenous regions can also form coiled coils (8 ‑ 10). The ECD of trimeric Collagen XIII alpha 1 is an extended rod-like structure with two flexible hinges that correspond to non‑collagenous regions (11). Collagen XIII alpha 1 clusters in cholesterol-rich domains on the plasma membrane (2, 12), and it can be cleaved from the cell surface or intracellularly by a furin-like protease (12). Collagen XIII alpha 1 binds the extracellular matrix molecules fibronectin, heparin, integrin alpha 1, nidogen‑2, and perlecan (11, 13). The shed ECD retains its ability to bind fibronectin and can interfere with matrix formation (14).

References