Human Recombinant GPC1 protein, Biotin Conjugated, His & AVI Tag (V2LY-0526-LY4341)

Name: Human Recombinant GPC1 protein, Biotin Conjugated, His & AVI Tag
SKU: V2LY-0526-LY4341
Rating: 5 (1 reviews)

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Datasheet

SDS

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Datasheet Target References Q & As Review & reward Protocols Associated Products

Basic Information

Expressed Host

HEK293 Cells

Protein Species

Human

Tag

His & AVI Tag

Protein Construction

This product is Human Recombinant GPC1 protein, Biotin Conjugated, His & AVI Tag consist of Amino Acid: 24-529 and predicts a molecular mass of 60.73 kDa.

Molecule Mass

60.73 kDa

Verified

HPLC

Conjugates

Biotin

Sequence

Amino Acid: 24-529

Species

Human

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

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 1

Function

Cell surface proteoglycan that bears heparan sulfate. Binds, via the heparan sulfate side chains, alpha-4 (V) collagen and participates in Schwann cell myelination (By similarity).

May act as a catalyst in increasing the rate of conversion of prion protein PRPN(C) to PRNP(Sc) via associating (via the heparan sulfate side chains) with both forms of PRPN, targeting them to lipid rafts and facilitating their interaction. Required for proper skeletal muscle differentiation by sequestering FGF2 in lipid rafts preventing its binding to receptors (FGFRs) and inhibiting the FGF-mediated signaling.

Biological Process

Cell migration Source: GO_Central
Heparan sulfate proteoglycan catabolic process Source: UniProtKB
Myelin assembly Source: UniProtKB
Negative regulation of fibroblast growth factor receptor signaling pathway Source: UniProtKB
Positive regulation of skeletal muscle cell differentiation Source: UniProtKB
Regulation of protein localization to membrane Source: GO_Central
Schwann cell differentiation Source: UniProtKB

Cellular Location

Cell membrane; Endosome. S-nitrosylated form recycled in endosomes. Localizes to CAV1-containing vesicles close to the cell surface. Cleavage of heparan sulfate side chains takes place mainly in late endosomes. Associates with both forms of PRNP in lipid rafts. Colocalizes with APP in perinuclear compartments and with CP in intracellular compartments. Associates with fibrillar APP amyloid-beta peptides in lipid rafts in Alzheimer disease brains.
Secreted glypican-1: Extracellular space

Involvement in disease

Associates (via the heparan sulfate side chains) with fibrillar APP amyloid-beta peptides in primitive and classic amyloid plaques and may be involved in the deposition of these senile plaques in the Alzheimer disease (AD) brain (PubMed:15084524).
Misprocessing of GPC1 is found in fibroblasts of patients with Niemann-Pick Type C1 disease. This is due to the defective deaminative degradation of heparan sulfate chains (PubMed:16645004).

PTM

S-nitrosylated in a Cu2+-dependent manner. Nitric acid (NO) is released from the nitrosylated cysteines by ascorbate or by some other reducing agent, in a Cu2+ or Zn2+ dependent manner. This free nitric oxide is then capable of cleaving the heparan sulfate side chains.
N- and O-glycosylated. N-glycosylation is mainly of the complex type containing sialic acid. O-glycosylated with heparan sulfate. The heparan sulfate chains can be cleaved either by the action of heparanase or, degraded by a deaminative process that uses nitric oxide (NO) released from the S-nitrosylated cysteines. This process is triggered by ascorbate, or by some other reducing agent, in a Cu2+- or Zn2+ dependent manner. Cu2+ ions are provided by ceruloproteins such as APP, PRNP or CP which associate with GCP1 in intracellular compartments or lipid rafts.
This cell-associated glypican is further processed to give rise to a medium-released species.

Pan, J., & Ho, M. (2021). Role of glypican-1 in regulating multiple cellular signaling pathways. American Journal of Physiology-Cell Physiology, 321(5), C846-C858.

Munekage, E., Serada, S., Tsujii, S., Yokota, K., Kiuchi, K., Tominaga, K., ... & Naka, T. (2021). A glypican-1-targeted antibody-drug conjugate exhibits potent tumor growth inhibition in glypican-1-positive pancreatic cancer and esophageal squamous cell carcinoma. Neoplasia, 23(9), 939-950.

Lund, M. E., Campbell, D. H., & Walsh, B. J. (2020). The role of glypican-1 in the tumour microenvironment. Tumor Microenvironment: Extracellular Matrix Components–Part A, 163-176.

Nishigaki, T., Takahashi, T., Serada, S., Fujimoto, M., Ohkawara, T., Hara, H., ... & Naka, T. (2020). Anti-glypican-1 antibody–drug conjugate is a potential therapy against pancreatic cancer. British journal of cancer, 122(9), 1333-1341.

Wang, S., Qiu, Y., & Bai, B. (2019). The expression, regulation, and biomarker potential of glypican-1 in cancer. Frontiers in oncology, 9, 614.

Zhou, C. Y., Dong, Y. P., Sun, X., Sui, X., Zhu, H., Zhao, Y. Q., ... & Han, S. X. (2018). High levels of serum glypican‐1 indicate poor prognosis in pancreatic ductal adenocarcinoma. Cancer Medicine, 7(11), 5525-5533.

Frampton, A. E., Prado, M. M., López-Jiménez, E., Fajardo-Puerta, A. B., Jawad, Z. A., Lawton, P., ... & Jiao, L. R. (2018). Glypican-1 is enriched in circulating-exosomes in pancreatic cancer and correlates with tumor burden. Oncotarget, 9(27), 19006.

Matsuzaki, S., Serada, S., Hiramatsu, K., Nojima, S., Matsuzaki, S., Ueda, Y., ... & Naka, T. (2018). Anti‐glypican‐1 antibody‐drug conjugate exhibits potent preclinical antitumor activity against glypican‐1 positive uterine cervical cancer. International journal of cancer, 142(5), 1056-1066.

Campbell, D. H., Lund, M. E., Nocon, A. L., Cozzi, P. J., Frydenberg, M., De Souza, P., ... & Walsh, B. J. (2018). Detection of glypican-1 (GPC-1) expression in urine cell sediments in prostate cancer. PLoS One, 13(4), e0196017.

Huang, X., Fan, C., Zhu, H., Le, W., Cui, S., Chen, X., ... & Chen, B. (2018). Glypican-1-antibody-conjugated Gd–Au nanoclusters for FI/MRI dual-modal targeted detection of pancreatic cancer. International Journal of Nanomedicine, 13, 2585.

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Please try the standard protocols which include: protocols, troubleshooting and guide.

Enzyme-linked Immunosorbent Assay (ELISA)
Flow Cytometry
Immunofluorescence (IF)
Immunohistochemistry (IHC)
Immunoprecipitation (IP)
Western Blot (WB)
Enzyme Linked Immunospot (ELISpot)
Proteogenomic
Other Protocols

Alternative Versions

Rat Gpc1 ELISA Kit (CAT#: V2LY-0626-LY2262)

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

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