HEK293 Cells.
Hyaluronidase-1, Hyal-1,Hyaluronoglucosaminidase-1, Lung carcinoma protein 1, LuCa-1, HYAL1, Hyaluronidase 1, Hyaluronoglucosaminidase 1, Hyaluronoglucosaminidase1, LUCA 1,MPS9, NAT6, Plasma hyaluronidase, Tumor suppressor LUCA 1.
Greater than 90.0% as determined by SDS-PAGE.
HYAL1 Human Recombinant produced in HEK cells is a single, glycosylated, polypeptide chain (22-435 a.a) containing a total of 420 amino acids, having a molecular mass of 46.9 kDa.
HYAL1 is fused to a 6 amino acid His-tag at C-terminus,and is purified by proprietary chromatographic techniques.
Hyaluronidase-1, also known as HYAL1, is a protein that belongs to the endolytic glycoside hydrolase family. In humans, there are five endo-β-N-acetylhexosaminidase enzymes, including HYAL1, HYAL2, and HYAL3. HYAL1 plays a crucial role in the breakdown of hyaluronic acid within the extracellular matrix of body tissues. It functions optimally in acidic environments and is the most prevalent hyaluronidase found in plasma. Genetic mutations affecting the HYAL1 gene can lead to mucopolysaccharidosis type IX and hyaluronidase deficiency.
Recombinant human HYAL1, expressed in HEK cells, is a single-chain polypeptide with glycosylation. It consists of 420 amino acids (22-435 a.a) and has a molecular weight of 46.9 kDa. The HYAL1 protein includes a 6-amino acid His-tag at the C-terminus and is purified using proprietary chromatographic methods.
The HYAL1 solution is supplied at a concentration of 0.25 mg/ml and contains 10% glycerol in phosphate-buffered saline (pH 7.4).
The purity of HYAL1 is determined by SDS-PAGE analysis and is greater than 90.0%.
Hyaluronidase-1, Hyal-1,Hyaluronoglucosaminidase-1, Lung carcinoma protein 1, LuCa-1, HYAL1, Hyaluronidase 1, Hyaluronoglucosaminidase 1, Hyaluronoglucosaminidase1, LUCA 1,MPS9, NAT6, Plasma hyaluronidase, Tumor suppressor LUCA 1.
HEK293 Cells.
FRGPLLPNRP FTTVWNANTQ WCLERHGVDV DVSVFDVVAN PGQTFRGPDM TIFYSSQLGT YPYYTPTGEP VFGGLPQNAS LIAHLARTFQ DILAAIPAPD FSGLAVIDWE AWRPRWAFNW DTKDIYRQRS RALVQAQHPD WPAPQVEAVA QDQFQGAARA WMAGTLQLGR ALRPRGLWGF YGFPDCYNYD FLSPNYTGQC PSGIRAQNDQ LGWLWGQSRA LYPSIYMPAV LEGTGKSQMY VQHRVAEAFR VAVAAGDPNL PVLPYVQIFY DTTNHFLPLD ELEHSLGESA AQGAAGVVLW VSWENTRTKE SCQAIKEYMD TTLGPFILNV TSGALLCSQA LCSGHGRCVR RTSHPKALLL LNPASFSIQL TPGGGPLSLR GALSLEDQAQ MAVEFKCRCY PGWQAPWCER KSMWHHHHHH
The action of hyaluronidase was first described in 1936 and named in 1939 . Early research identified it as a “spreading factor” due to its ability to increase the permeability of connective tissue . This property has made hyaluronidase a valuable tool in medical and surgical settings for over 60 years, particularly for improving the diffusion of local anesthetics .
Hyaluronidase is an enzyme that catalyzes the degradation of hyaluronic acid, a major component of the extracellular matrix . By hydrolyzing hyaluronic acid, hyaluronidase lowers its viscosity, thereby increasing tissue permeability . This action facilitates the absorption and dispersion of parenterally administered fluids, drugs, and contrast agents .
Hyaluronidase is used in various medical applications, including: