CHADL Antibody
- SPECIFICATION
- CITATIONS
- PROTOCOLS
- BACKGROUND
Application ![]()
| WB, IHC, E |
---|---|
Primary Accession | Q6NUI6 |
Other Accession | NP_612490, 150356 |
Reactivity | Human, Mouse, Rat |
Host | Rabbit |
Clonality | Polyclonal |
Isotype | IgG |
Calculated MW | Predicted: 84 kDa Observed: 86 kDa |
Application Notes | CHADL antibody can be used for the detection of CHADL by Western blot at 1 - 2 μg/mL. Antibody can also be used for Immunohistochemistry starting at 5 μg/mL. |
Gene ID | 150356 |
---|---|
Target/Specificity | CHADL antibody was raised against a 19 amino acid peptide from near the carboxy terminus of human CHADL. The immunogen is located within the last 50 amino acids of CHADL. |
Reconstitution & Storage | CHADL antibody can be stored at 4℃ for three months and -20℃, stable for up to one year. |
Precautions | CHADL Antibody is for research use only and not for use in diagnostic or therapeutic procedures. |
Name | CHADL |
---|---|
Synonyms | SLRR4B |
Function | Potential negative modulator of chondrocyte differentiation. Inhibits collagen fibrillogenesis in vitro. May influence chondrocyte's differentiation by acting on its cellular collagenous microenvironment. |
Cellular Location | Secreted. Secreted, extracellular space, extracellular matrix {ECO:0000250|UniProtKB:E9Q7T7} |

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Provided below are standard protocols that you may find useful for product applications.
Background
The Chondroadherin-like (CHADL) protein, also known as SLRR4B, is homologous to the Chondroadherin protein and is expressed cartillaginous tissues (1). Like Chondroadherin, CHADL belongs to the small leucine-rich proteoglycan (SLRP) family and class IV subfamily and plays a significant role in the regulation of chondrocyte growth and proliferation (1,2). CHADL is thought to play a negative regualtory role in collagen fibrillogenesis and chondrocyte differentiation (1).
References
Tillgren V, Ho JC, Onnerfjord P, et al. The novel small leucine-rich protein chondroadherin-like (CHADL) is expressed in cartilage and modulates chondrocyte differentitation. J. Biol. Chem. 2015; 290:918-25.
Neame PJ, Sommarin Y, Boynton RE, et al. The structure of a 38-kDa leucine-rich protein (chondroadherin) isolated from bovine cartilage. J. Biol. Chem. 1994; 269:21547-54.

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