Recombinant Human Hyaluronidase-1 (HYAL1) Protein (His)

Name: Recombinant Human Hyaluronidase-1 (HYAL1) Protein (His)
Brand: Beta LifeScience
SKU: BLC-09594P
Availability: InStock

Greater than 90% as determined by SDS-PAGE.

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Product Overview

Description	Recombinant Human Hyaluronidase-1 (HYAL1) Protein (His) is produced by our Yeast expression system. This is a full length protein.
Purity	Greater than 90% as determined by SDS-PAGE.
Uniprotkb	Q12794
Target Symbol	HYAL1
Synonyms	HYAL 1; Hyal-1; HYAL1; HYAL1_HUMAN; Hyaluronidase 1; Hyaluronidase-1; Hyaluronoglucosaminidase 1; Hyaluronoglucosaminidase-1; Hyaluronoglucosaminidase1; LUCA 1; LUCA-1; LUCA1; Lung carcinoma protein 1; MGC45987; NAT6; Plasma hyaluronidase; Tumor suppressor LUCA 1
Species	Homo sapiens (Human)
Expression System	Yeast
Tag	N-6His
Target Protein Sequence	FRGPLLPNRPFTTVWNANTQWCLERHGVDVDVSVFDVVANPGQTFRGPDMTIFYSSQLGTYPYYTPTGEPVFGGLPQNASLIAHLARTFQDILAAIPAPDFSGLAVIDWEAWRPRWAFNWDTKDIYRQRSRALVQAQHPDWPAPQVEAVAQDQFQGAARAWMAGTLQLGRALRPRGLWGFYGFPDCYNYDFLSPNYTGQCPSGIRAQNDQLGWLWGQSRALYPSIYMPAVLEGTGKSQMYVQHRVAEAFRVAVAAGDPNLPVLPYVQIFYDTTNHFLPLDELEHSLGESAAQGAAGVVLWVSWENTRTKESCQAIKEYMDTTLGPFILNVTSGALLCSQALCSGHGRCVRRTSHPKALLLLNPASFSIQLTPGGGPLSLRGALSLEDQAQMAVEFKCRCYPGWQAPWCERKSMW
Expression Range	22-435aa
Protein Length	Full Length of Mature Protein
Mol. Weight	48.1kDa
Research Area	Cancer
Form	Liquid or Lyophilized powder
Buffer	Liquid form: default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol. Lyophilized powder form: the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, pH 8.0.
Reconstitution	Briefly centrifuged the vial prior to opening to bring the contents to the bottom. Reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL. It is recommended to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20°C/-80°C. The default final concentration of glycerol is 50%.
Storage	1. Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. 2. Avoid repeated freeze-thaw cycles. 3. Store working aliquots at 4°C for up to one week. 4. In general, protein in liquid form is stable for up to 6 months at -20°C/-80°C. Protein in lyophilized powder form is stable for up to 12 months at -20°C/-80°C.
Notes	Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.

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: Hs.75619
Associated Diseases	Mucopolysaccharidosis 9 (MPS9)
Tissue Specificity	Highly expressed in the liver, kidney and heart. Weakly expressed in lung, placenta and skeletal muscle. No expression detected in adult brain. Isoform 1 is expressed only in bladder and prostate cancer cells, G2/G3 bladder tumor tissues and lymph node sp

Gene Functions References

Data revealed a significant inverse correlation between ERalpha and HYAL1 gene expression in human breast tumors. HYAL1 was found repressed by estrogen through ERalpha binding to a consensus response element (ERE) located in the proximal promoter of HYAL1 and flanked by an Sp1 binding site, required to achieve optimal estrogen repression. 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

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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.

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