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Mouse Anti-GP5 Recombinant Antibody (CBYJL-029) (CBMAB-L0058-YJ)

Provided herein is a Mouse monoclonal antibody, which binds to Glycoprotein V Platelet (GP5). The antibody can be used for immunoassay techniques, such as ELISA, WB.
See all GP5 antibodies

Summary

Host Animal
Mouse
Specificity
Human
Clone
CBYJL-029
Antibody Isotype
IgG2b
Application
ELISA, WB

Basic Information

Immunogen
NS0-derived, recombinant human Glycoprotein V (aa17-253, Accession # P40197). Species Sequence Homology: mouse (70%).
Specificity
Human
Antibody Isotype
IgG2b
Clonality
Monoclonal
Application Notes
The COA includes recommended starting dilutions, optimal dilutions should be determined by the end user.

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

Buffer
0.01 M PBS, pH 7.4, 0.5 M NaCl
Preservative
15 mM Sodium Azide
Storage
Store at 4°C short term (1-2 weeks). Aliquot and store at -20°C long term. Avoid repeated freeze/thaw cycles.
Epitope
aa 17-253

Target

Full Name
Glycoprotein V Platelet
Introduction
GP5 (Human platelet glycoprotein V) is a part of the Ib-V-IX system of surface glycoproteins that form the receptor for von Willebrand factor (VWF; MIM 613160) and mediate the adhesion of platelets to injured vascular surfaces in the arterial circulation, a crucial initiating event in hemostasis. The main parts of the receptor is a heterodimer composed of 2 polypeptide chains, an alpha chain (GP1BA; MIM 606672) and a beta chain (GP1BB; MIM 138720), that are linked by disulfide bonds.
Entrez Gene ID
2814
UniProt ID
P40197
Alternative Names
Glycoprotein V Platelet; Platelet Glycoprotein V; Glycoprotein 5; GPV; Glycoprotein V (Platelet); CD42d Antigen; CD42d
Function
The GPIb-V-IX complex functions as the vWF receptor and mediates vWF-dependent platelet adhesion to blood vessels. The adhesion of platelets to injured vascular surfaces in the arterial circulation is a critical initiating event in hemostasis.
Biological Process
Blood coagulation Source: UniProtKB-KW
Cell adhesion Source: ProtInc
Cellular Location
Membrane
Topology
Extracellular: 17-523
Helical: 524-544
Cytoplasmic: 545-560
PTM
The N-terminus is blocked.

Luo, Q., Zheng, Y., Zhang, H., Yang, Z., Sha, H., Kong, W., ... & Wang, N. (2023). Research Progress on Glycoprotein 5 of Porcine Reproductive and Respiratory Syndrome Virus. Animals, 13(5), 813.

Zhang, X., Chen, Y., Li, S., Wang, J., He, Z., Yan, J., ... & Guo, C. (2023). MARCO Inhibits Porcine Reproductive and Respiratory Syndrome Virus Infection through Intensifying Viral GP5-Induced Apoptosis. Microbiology Spectrum, e04753-22.

Choi, H. Y., Kim, M. S., Kang, Y. L., Choi, J. C., Choi, I. Y., Jung, S. W., ... & Lee, J. B. (2022). Development of a Chimeric Porcine Reproductive and Respiratory Syndrome Virus (PRRSV)-2 Vaccine Candidate Expressing Hypo-Glycosylated Glycoprotein-5 Ectodomain of Korean Lineage-1 Strain. Veterinary Sciences, 9(4), 165.

Akter, F., Roychoudhury, P., Dutta, T. K., Subudhi, P. K., Kumar, S., Gali, J. M., ... & Singh, Y. D. (2021). Isolation and molecular characterization of GP5 glycoprotein gene of Betaarterivirus suid 2 from Mizoram, India. VirusDisease, 32, 748-756.

Liu, X., Liu, X., Bai, J., Gao, Y., Song, Z., Nauwynck, H., ... & Jiang, P. (2021). Glyceraldehyde-3-Phosphate Dehydrogenase Restricted in Cytoplasmic Location by Viral Gp5 Facilitates Porcine Reproductive and Respiratory Syndrome Virus Replication Via Its Glycolytic Activity. Journal of Virology, 95(18), e00210-21.

Wang, M., Du, S., Xu, W., Song, L., Hao, P., Jin, N., ... & Li, C. (2020). Construction and optimization of Lactobacillus plantarum expression system expressing glycoprotein 5 of porcine reproductive and respiratory syndrome virus. International journal of biological macromolecules, 143, 112-117.

Hou, J., Li, R., Qiao, S., Chen, X. X., Xing, G., & Zhang, G. (2020). Glycoprotein 5 is cleaved by cathepsin E during porcine reproductive and respiratory syndrome virus membrane fusion. Journal of Virology, 94(10), e00097-20.

Li, L., Zhang, L., Hu, Q., Zhao, L., Nan, Y., Hou, G., ... & Zhou, E. M. (2019). MYH9 key amino acid residues identified by the anti-idiotypic antibody to porcine reproductive and respiratory syndrome virus glycoprotein 5 involve in the virus internalization by porcine alveolar macrophages. Viruses, 12(1), 40.

Zhang, M., & Zakhartchouk, A. (2018). Characterization of the interactome of the porcine reproductive and respiratory syndrome virus glycoprotein-5. Archives of virology, 163, 1595-1605.

Li, L., Xue, B., Sun, W., Gu, G., Hou, G., Zhang, L., ... & Zhou, E. M. (2018). Recombinant MYH9 protein C-terminal domain blocks porcine reproductive and respiratory syndrome virus internalization by direct interaction with viral glycoprotein 5. Antiviral Research, 156, 10-20.

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

Custom Antibody Labeling

We also offer labeled antibodies developed using our catalog antibody products and nonfluorescent conjugates (HRP, AP, Biotin, etc.) or fluorescent conjugates (Alexa Fluor, FITC, TRITC, Rhodamine, Texas Red, R-PE, APC, Qdot Probes, Pacific Dyes, etc.).

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