Select country set
Menu Shopping cart 0,00 Search
Manufactured by BioVendor

Hyaluronidase-1 (HYAL1) Human HEK293 Recombinant

  • Regulatory status:RUO
  • Type:Recombinant protein
  • Source:HEK293 cells
  • Other names: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
  • Species:Human
Please select your region to see available products and prices.
Cat. No. Size Price

New RP1791155010 10 μg
New RP17911551MG 1 mg
Product Details
Technical Data


Recombinant protein


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.

Amino Acid Sequence



HEK293 cells


Greater than 90.0%


The HYAL1 solution (0.25mg/ml) contains 10% Glycerol and Phosphate-Buffered Saline (pH 7.4).


Cell culture and/or animal studies, In vitro


On frozen gel ice packs. Upon receipt, store the product at the temperature recommended below.


Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA). Avoid multiple freeze-thaw cycles.


This BioVendor product is furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.



Human hyaluronidase-1 (Hyal-1) is a 435 amino acid residue protein exhibiting a narrow acidic pH activity (3−4.5), consistent with the low pH in the lysosome. The protein contains 10 cysteines, three predicted N-glycosylation sites, and an N-terminal endoplasmic reticulum signal sequence. It cleaves hyaluronic acid (HA) substrates of all sizes into short chains, down to tetrasaccharides.

Human Hyal-1 is a lysosomal enzyme responsible for the hydrolysis of intracellular HA and is also detected in the plasma and in urine. Increased expression of HYAL1 mRNA and higher levels of hHyal-1 are documented in many diseases, and in bladder and prostate cancers. The enzyme is responsible for the production of angiogenic HA fragments. Because of its presence in urine and change in expression level in bladder and prostate cancers, the use of hHyal-1 as a marker of these diseases has been considered. The role of hHyal-1 in tumor progression depends on its cellular concentration; it functions as a tumor suppressor at low or very high concentration and as a tumor promoter at moderate concentration.

Inactivating mutations of hHyal-1 are linked to the human genetic disorder mucopolysaccharidosis IX (also known as hyaluronidase deficiency), characterized by diminished stature, periarticular soft tissue masses, and absence of neurological and visceral involvement. The plasma HA concentration of patients with this disorder is 40−90-fold higher than in normal serum.

Summary References (5)

References to

  • Ahmed MH, Aldesouki HM, Badria FA. Effect of phenolic compounds from the leaves of Psidium guajava on the activity of three metabolism-related enzymes. Biotechnol Appl Biochem. 2020 May 20. doi: 10.1002/bab.1956. Epub ahead of print. PMID: 32432341. See more on PubMed
  • Duan H, Donovan M, Hernandez F, Di Primo C, Garanger E, Schultze X, Lecommandoux S. Hyaluronic-Acid-Presenting Self-Assembled Nanoparticles Transform a Hyaluronidase HYAL1 Substrate into an Efficient and Selective Inhibitor. Angew Chem Int Ed Engl. 2020 Aug 3;59(32):13591-13596. doi: 10.1002/anie.202005212. Epub 2020 Jun 3. PMID: 32363767. See more on PubMed
  • Chao KL, Muthukumar L, Herzberg O. Structure of human hyaluronidase-1, a hyaluronan hydrolyzing enzyme involved in tumor growth and angiogenesis. Biochemistry. 2007 Jun 12;46(23):6911-20. doi: 10.1021/bi700382g. Epub 2007 May 16. PMID: 17503783. See more on PubMed
  • Krupkova O, Greutert H, Boos N, Lemcke J, Liebscher T, Wuertz-Kozak K. Expression and activity of hyaluronidases HYAL-1, HYAL-2 and HYAL-3 in the human intervertebral disc. Eur Spine J. 2020 Mar;29(3):605-615. doi: 10.1007/s00586-019-06227-3. Epub 2019 Nov 22. PMID: 31758257. See more on PubMed
  • Tiwari S, Bahadur P. Modified hyaluronic acid based materials for biomedical applications. Int J Biol Macromol. 2019 Jan;121:556-571. doi: 10.1016/j.ijbiomac.2018.10.049. Epub 2018 Oct 12. PMID: 30321638. See more on PubMed