Code | CSB-YP618635HU |
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Recombinant human Hyaluronidase-2 (HYAL2) production begins with gene cloning. The gene encoding the HYAL2 protein (21-448aa) is inserted into an expression vector along with the N-terminal 6xHis-tag gene and introduced into host cells. The cells are cultured in bioreactors to produce the HYAL2 protein. Once sufficient protein is produced, the cells are lysed, and the HYAL2 protein is purified through affinity chromatography. The final product undergoes an SDS-PAGE test to measure its purity. Its purity is over 90%.
HYAL2 is a lysosomal hyaluronidase enzyme that plays a crucial role in the degradation of hyaluronic acid (HA) within cells. It is a glycosylphosphatidylinositol-linked protein and a member of the hyaluronoglucosaminidase family [1]. HYAL2 is located in lysosomes and is essential for cellular HA catabolism, generating different-sized oligosaccharide fragments for various physiological functions [2]. Research has shown that HYAL2 is a ~53 kDa acid-active hyaluronidase predominantly present in the acrosome and inner acrosomal membrane of sperm, aiding in cleaving high molecular weight HA polysaccharides [3].
Studies have indicated that HYAL2 digests hyaluronan to intermediate-sized fragments of approximately 20 kDa [4]. Additionally, HYAL2 has been identified as a receptor for jaagsiekte sheep retrovirus (JSRV) [5]. In the context of sperm function, HYAL2, along with other hyaluronidases, such as PH20, plays a role in cleaving HA in the cumulus layer to facilitate fertilization [3]. Furthermore, HYAL2 deficiency has been linked to severe cardiopulmonary dysfunction due to extracellular HA accumulation [1].
References:
[1] Y. Li, S. Yang, L. Guo, Y. Xiao, J. Luo, Y. Liet al., Differentiation of intracellular hyaluronidase isoform by degradable nanoassembly coupled with rna-binding fluorescence amplification, Analytical Chemistry, vol. 91, no. 10, p. 6887-6893, 2019. https://doi.org/10.1021/acs.analchem.9b01242
[2] P. Gunasekaran, M. Hemamalini, & V. Rajakannan, Structure prediction and binding site analysis of human sperm hyaluronidases, International Journal of Infertility & Fetal Medicine, vol. 13, no. 3, p. 96-100, 2022. https://doi.org/10.5005/jp-journals-10016-1280
[3] M. Yoshida, S. Sai, K. Marumo, T. Tanaka, N. Itano, K. Kimataet al., Untitled, Arthritis Research, vol. 6, no. 6, p. R514, 2004. https://doi.org/10.1186/ar1223
[4] В. Вигдорович, A. Miller, & R. Strong, Ability of hyaluronidase 2 to degrade extracellular hyaluronan is not required for its function as a receptor for jaagsiekte sheep retrovirus, Journal of Virology, vol. 81, no. 7, p. 3124-3129, 2007. https://doi.org/10.1128/jvi.02177-06
[5] S. Reitinger, J. Müllegger, B. Greiderer, & G. Lepperdinger, Designed human serum hyaluronidase 1 variant, hyal1δl, exhibits activity up to ph 5.9, Journal of Biological Chemistry, vol. 284, no. 29, p. 19173-19177, 2009. https://doi.org/10.1074/jbc.c109.004358
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