Recombinant Human HYAL1 Protein (C-6His)

Name: Recombinant Human HYAL1 Protein (C-6His)
Brand: Beta LifeScience
SKU: BL-1420NP
Availability: InStock

BL-1420NP: Greater than 95% as determined by reducing SDS-PAGE. (QC verified)

Collections: All products, High-quality recombinant proteins, Other recombinant proteins

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Product Overview

Description	Recombinant Human Hyaluronidase-1 is produced by our Mammalian expression system and the target gene encoding Phe22-Trp435 is expressed with a 6His tag at the C-terminus.
Accession	Q12794
Synonym	Hyaluronidase-1; Hyal-1; Hyaluronoglucosaminidase-1; Lung Carcinoma Protein 1; LuCa-1; HYAL1; LUCA1
Gene Background	Hyaluronidase-1 (HYAL1) is a secreted lysosomal hyaluronidase that belongs to the glycosyl hydrolase 56 family. HYAL1 contains one EGF-like domain and is highly expressed in the liver, kidney, and heart, but it is weakly expressed in the lung, placenta, and skeletal muscle. HYAL1 is thought to be involved in cell proliferation, migration, and differentiation. It may play a role in promoting tumor progression and blocking the TGFB1-enhanced cell growth. Mutations in HYAL1 are associated with mucopolysaccharidosis type IX, or hyaluronidase deficiency.
Molecular Mass	47.18 KDa
Apmol Mass	50-65 KDa, reducing conditions
Formulation	Supplied as a 0.2 μm filtered solution of 20mM Tris-HCl, 150mM NaCl, 10% Glycerol, pH 7.5.
Endotoxin	Less than 0.1 ng/µg (1 EU/µg) as determined by LAL test.
Purity	Greater than 95% as determined by reducing SDS-PAGE. (QC verified)
Biological Activity	Not tested
Reconstitution
Storage	Store at ≤-70°C, stable for 6 months after receipt. Store at ≤-70°C, stable for 3 months under sterile conditions after opening. Please minimize freeze-thaw cycles.
Shipping	The product is shipped on dry ice/polar packs. Upon receipt, store it immediately at the temperature listed below.
Usage	For Research Use Only

Target Details

Target Function	May have a role in promoting tumor progression. May block the TGFB1-enhanced cell growth.
Subcellular Location	Secreted. Lysosome.
Protein Families	Glycosyl hydrolase 56 family
Database References	HGNC: 5320 OMIM: 601492 KEGG: hsa:3373 STRING: 9606.ENSP00000266031 UniGene: PMID: 27764788 Ureaplasma urealyticum infection may affect the activity of hyaluronidase on spermatozoa PMID: 28012250 our results suggest that the enzyme HYAL1 plays a role in tumor dissemination and brain-specific colonization, rather than in subsequent metastatic out-growth. PMID: 28168629 HAS2 and HAS3 were the only hyaluronan synthases detected, the expression of which was almost similar in NPs and NM. PMID: 26661071 Molecular docking simulation explains the less favorable binding energy of substrate towards mutant E268K, thereby providing a structural basis for its reduced catalytic activity. PMID: 27424109 The receiver-operating characteristic curve analyses demonstrated that each one had good sensitivity and specificity for distinguishing BC patients from non-BC ones (HYAL1, miR-210, miR-96, lncRNA-UCA1, 91.5 and ). PMID: 26138586 Study showed that reduced HYAL1 expression was associated with endometrial carcinoma aggressiveness, which further supported the role of hyaluronan degradation in cancer progression. PMID: 25584766 Results demonstrated that HYAL1 was C-mannosylated and suggest the possible role of C-mannosylation for secretion and enzymatic activity of HYAL1. PMID: 24820161 In contrast to the previously described MPS IX patient, our three patients display a phenotype limited to the joints, suggesting that this is the primary manifestation of HYAL1 deficiency. PMID: 21559944 Upregulation of HYAL1 expression in breast cancer promoted tumor cell proliferation, migration, invasion and angiogenesis. PMID: 21829529 This is the first report showing high HYAL-1 levels in epithelial ovarian cancer. PMID: 21695196 HYAL-1 and HAS1 expression predicted BCa metastasis, and HYAL-1 expression also predicted disease-specific survival. PMID: 20960509 HYAL1 overexpression is correlated with the malignant behavior of breast cancer. PMID: 20473947 Hyaluronan synthases (HAS1-3) and hyaluronidases (HYAL1-2) in the accumulation of hyaluronan in endometrioid endometrial carcinoma PMID: 20875124 Overexpression of HYAL1 is associated with colorectal cancer. PMID: 20849597 The protein products HABP2 and HYAL1 were associated with plasma PAI-1 concentration and play key roles in hyaluronan metabolism, providing genetic evidence to link these pathways. PMID: 20558613 rhHyal-1 is endocytosed by the liver. PMID: 20572808 HYAL-1 is a potential prognostic marker for predicting progression to muscle invasion and recurrence in bladder cancer. PMID: 19345473 Data show that a significant in expression levels of HA synthases (HASs) and hyaluronidases (Hyals) was observed in vitro on stimulation of epithelial ovarian carcinoma cells by gonadotropins. PMID: 20072653 Characterization of the murine hyaluronidase gene region reveals complex organization and cotranscription of Hyal1 with downstream genes, Fus2 and Hyal3. PMID: 11929860 Alternative mRNA splicing controls cellular expression of enzymatically active hyaluronidase. PMID: 12084718 Down-regulation of HYAL1 is associated with small cell lung cancer and glioma PMID: 12684632 Increased expression of hyaluronidase is associated with head and neck tumors PMID: 12845686 Hyaluronidase and CD44 hyaluronan receptor are expressed in squamous cell laryngeal carcinoma PMID: 16713680 Gene silencing of HYAL1 inhibited cell proliferation and induced cell cycle arrest in human breast cancer cells. PMID: 16831275 HYAL1-v1 transfectants grew 3- to 4-fold slower due to cell cycle arrest in the G(2)-M phase and increased apoptosis. PMID: 17145867 Purified recombinant Hyal-1 from Drosophila cells was used for the investigation of the inhibitory activity of new ascorbic acid derivatives PMID: 17227790 further support to altered glycosaminoglycan metabolism (hyaluronan and hyaluronidase blood levels)in type 1 diabetes as a potential mechanism involved in accelerated atherogenesis. PMID: 17415544 hyaluronan processing by elevated HYAL1 expression in invasive prostate cancer is a requirement for progression. PMID: 17502371 crystal structure reveals a molecule composed of two closely associated domains: a catalytic domain that adopts a distorted (beta/alpha)8 barrel resembling that of bee venom hyaluronidase, and a novel, EGF-like domain PMID: 17503783 Hyaluronidase activity is modulated by complexing with various polyelectrolytes including hyaluronan PMID: 18083358 The expression of HYAL1 in ductal hyperplastic tissues is a strong predictor of subsequent development of invasive breast cancer PMID: 18281563 Bovine serum albumin competes with human hyalurinodase and thus increases hyaluronidase release resulting in a large increase in the hydrolysis rate. PMID: 18677769 HYAL-1 expression is epigenetically regulated by the binding of different transcription factors to the methylated and unmethylated HYAL-1 promoter PMID: 18718911 Down-regulation of RBSP3/CTDSPL, NPRL2/G21, RASSF1A, ITGA9, HYAL1 and HYAL2 genes in non-small cell lung cancer PMID: 19140316 define key components of Hyal1 active site catalysis, and structural factors critical for stability PMID: 19201751 HYAL1, but not HYAL2, expression is reduced and correlates with the accumulation of hyaluronan in ovarian carcinomas. PMID: 19435493 Data showed that the HYAL1 variant exhibited hyaluronan degradation at elevated pH. PMID: 19478093 Invasive features of ER(-) breast cancer cells can be characterized in vitro by higher secretion of hyaluronidase, higher expression of proteinases MMP-9, cath-D, and the angiogenesis promoting factor VEGF. PMID: 19567141

FAQs

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Proteins are sensitive to heat, and freeze-drying can preserve the activity of the majority of proteins. It improves protein stability, extends storage time, and reduces shipping costs. However, freeze-drying can also lead to the loss of the active portion of the protein and cause aggregation and denaturation issues. Nonetheless, these adverse effects can be minimized by incorporating protective agents such as stabilizers, additives, and excipients, and by carefully controlling various lyophilization conditions.

Commonly used protectant include saccharides, polyols, polymers, surfactants, some proteins and amino acids etc. We usually add 8% (mass ratio by volume) of trehalose and mannitol as lyoprotectant. Trehalose can significantly prevent the alter of the protein secondary structure, the extension and aggregation of proteins during freeze-drying process; mannitol is also a universal applied protectant and fillers, which can reduce the aggregation of certain proteins after lyophilization.

Our protein products do not contain carrier protein or other additives (such as bovine serum albumin (BSA), human serum albumin (HSA) and sucrose, etc., and when lyophilized with the solution with the lowest salt content, they often cannot form A white grid structure, but a small amount of protein is deposited in the tube during the freeze-drying process, forming a thin or invisible transparent protein layer.

Reminder: Before opening the tube cap, we recommend that you quickly centrifuge for 20-30 seconds in a small centrifuge, so that the protein attached to the tube cap or the tube wall can be aggregated at the bottom of the tube. Our quality control procedures ensure that each tube contains the correct amount of protein, and although sometimes you can't see the protein powder, the amount of protein in the tube is still very precise.

To learn more about how to properly dissolve the lyophilized recombinant protein, please visit Lyophilization FAQs.

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Recombinant Human HYAL1 Protein (C-6His)

Recombinant Human HYAL1 Protein (C-6His)

Product Overview

Target Details

FAQs