Cynomolgus Recombinant GPC6 protein, Biotin Conjugated, His & AVI Tag (V2LY-0526-LY1523)

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Basic Information

Expressed Host
HEK293 Cells
Protein Species
Cynomolgus
Tag
His & AVI Tag
Protein Construction
This product is Cynomolgus Recombinant GPC6 protein, Biotin Conjugated, His & AVI Tag consist of Amino Acid: 1-529 and predicts a molecular mass of 60.84 kDa.
Molecule Mass
60.84 kDa
Verified
HPLC
Conjugates
Biotin
Sequence
Amino Acid: 1-529
Species
Cynomolgus

Formulations & Storage [For reference only, actual COA shall prevail!]

Purity
≥90% as determined by SDS-PAGE. ≥90% as determined by SEC-HPLC.
Endotoxin
Please contact us for more information.
Format
Lyophilized
Reconstitution
Allow the vial and reconstitution buffer to equilibrate to room temperature. Briefly centrifuge or tap down the vial to ensure that all lyophilized powder is collected at the bottom of the vial. For the reconstitution of this product, we recommend adding PBS or sterile water to achieve a final antibody concentration of 1 mg/mL. Allow the vial to reconstitute for 10-15 minutes at room temperature with gentle agitation. Avoid vigorous shaking that can cause foaming and antibody denaturation. Aliquot into volumes based on your experiment and store liquid protein at -20°C or -80°C for long time.
Buffer
Lyophilized from sterile Tris, NaCl, Glutathione, EDTA, DTT, PMSF, Glycerol
Preservative
None
Storage
Samples are stable for up to twelve months from date of receipt at -20°C to -80°C. Store it under sterile conditions at -20°C to -80°C. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
More Infomation

Target

Full Name
glypican 6
Function
Cell surface proteoglycan that bears heparan sulfate. Putative cell surface coreceptor for growth factors, extracellular matrix proteins, proteases and anti-proteases (By similarity).

Enhances migration and invasion of cancer cells through WNT5A signaling.
Biological Process
Cell migration Source: UniProtKB
Regulation of neurotransmitter receptor localization to postsynaptic specialization membrane Source: GO_Central
Regulation of presynapse assembly Source: GO_Central
Regulation of protein localization to membrane Source: GO_Central
Regulation of signal transduction Source: InterPro
Synaptic membrane adhesion Source: GO_Central
Cellular Location
Cell membrane
Secreted glypican-6: Extracellular space
Involvement in disease
Omodysplasia 1 (OMOD1):
The disease is caused by variants affecting the gene represented in this entry. Point mutations leading to protein truncation, as well as larger genomic rearrangements resulting in exon deletions, have been found in family segregating omodysplasia type 1. All mutations identified in individuals affected by omodysplasia could lead to the absence of a functional protein, the mutant RNAs being suspected to be nonsense-mediated mRNA decay (NMD) targets. Even if the mRNA escapes NMD and is translated, all mutations are expected to disrupt the three-dimensional protein structure and often to abolish multiple highly conserved cysteine residues.
A rare autosomal recessive skeletal dysplasia characterized by facial dysmorphism and severe congenital micromelia with shortening and distal tapering of the humeri and femora, to give a club-like appearance. Typical facial features include a prominent forehead, frontal bossing, short nose with a depressed broad bridge, short columella, anteverted nostrils, long philtrum, and small chin.

Colin-Pierre, C., Untereiner, V., Sockalingum, G. D., Ramont, L., & Brézillon, S. (2023). Investigation of Glypican-4 and-6 by Infrared Spectral Imaging during the Hair Growth Cycle. International Journal of Molecular Sciences, 24(5), 4291.

Shi, W., & Filmus, J. (2022). Glypican‐6 and Glypican‐4 stimulate embryonic stomach growth by regulating Hedgehog and noncanonical Wnt signaling. Developmental Dynamics, 251(12), 2015-2028.

Lehmkuhl, E. M., Loganathan, S., Alsop, E., Blythe, A. D., Kovalik, T., Mortimore, N. P., ... & Zarnescu, D. C. (2021). TDP-43 proteinopathy alters the ribosome association of multiple mRNAs including the glypican Dally-like protein (Dlp)/GPC6. Acta neuropathologica communications, 9, 1-21.

Ozturk, F., Atici, A., & Barman, H. A. (2021). Can glypican-6 level predict ejection fraction decline after myocardial infarction?. Angiology, 72(6), 582-588.

Tenin, G., Crozier, A., Hentges, K. E., & Keavney, B. (2021). Glypican-6 deficiency causes dose-dependent conotruncal congenital heart malformations through abnormal remodelling of the endocardial cushions. Biorxiv, 2021-06.

Shi, W., Kaneiwa, T., Cydzik, M., Gariepy, J., & Filmus, J. (2020). Glypican-6 stimulates intestinal elongation by simultaneously regulating Hedgehog and non-canonical Wnt signaling. Matrix Biology, 88, 19-32.

Su, Y., Chen, Z., Du, H., Liu, R., Wang, W., Li, H., & Ning, B. (2019). Silencing miR‐21 induces polarization of astrocytes to the A2 phenotype and improves the formation of synapses by targeting Glypican 6 via the signal transducer and activator of transcription‐3 pathway after acute ischemic spinal cord injury. The FASEB Journal, 33(10), 10859-10871.

Li, Y., Li, M., Shats, I., Krahn, J. M., Flake, G. P., Umbach, D. M., ... & Li, L. (2019). Glypican 6 is a putative biomarker for metastatic progression of cutaneous melanoma. PLoS One, 14(6), e0218067.

Fan, C., Tu, C., Qi, P., Guo, C., Xiang, B., Zhou, M., ... & Zeng, Z. (2019). GPC6 promotes cell proliferation, migration, and invasion in nasopharyngeal carcinoma. Journal of Cancer, 10(17), 3926.

Hu, B., Xing, W., Li, F., Huang, Z., Zheng, W., Ji, D., ... & Yang, X. (2019). Association of glypican‐6 polymorphisms with lumbar disk herniation risk in the Han Chinese population. Molecular Genetics & Genomic Medicine, 7(7), e00747.

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For research use only. Not intended for any clinical use.

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