Hyaluronidase-3 Antibodies

Hyaluronidase-3 (HYAL3)

Facilitates sperm penetration into the layer of cumulus cells surrounding the egg by digesting hyaluronic acid. Involved in induction of the acrosome reaction in the sperm.

Involved in follicular atresia, the breakdown of immature ovarian follicles which aren't selected to ovulate. Induces ovarian granulosa cell apoptosis, possibly via apoptotic signaling pathway involving CASP8 and CASP3 activation, and poly(ADP-ribose) polymerase (PARP) cleavage.

Gene Information

Human
Gene Name:	HYAL3
Uniprot:	O43820
Entrez:	8372

Family

Belongs to:
glycosyl hydrolase 56 family

Alternative Names

EC 3.2.1.35; HYAL-3; hyaluronidase-3; hyaluronoglucosaminidase 3; Hyaluronoglucosaminidase-3; LUCA14; LuCa-3; LUCA3LUCA-3; Lung carcinoma protein 3; Minna14

Molecular Weight

Mass (kDA):
46.501 kDA

Genomic Context

Human
Location:	3p21.31
Sequence:	3; NC_000003.12 (50292832..50299405, complement)

Tissue Specificity

Expressed in sperm (PubMed:20586096). Highly expressed in epidermis of the skin, where it is expressed intracellularily in the deep horny layer (at protein level) (PubMed:21699545). Bone marrow, testis and kidney (PubMed:10493834).

Subcellular Localizations

Secreted. Cell membrane. Cytoplasmic vesicle, secretory vesicle, acrosome. Endoplasmic reticulum. Early endosome. Mostly present in low-density vesicles. Low levels in higher density vesicles of late endosomes and lysosomes. Localized in punctate cytoplasmic vesicles and in perinuclear structures, but does not colocalize with LAMP1. Localized on the plasma membrane over the acrosome and on the surface of the midpiece of the sperm tail.

Diseases

• Headache
• Neoplasms
• Mucopolysaccharidoses
• Malignant Neoplasms
• Neoplasm Metastasis
• Carcinoma
• Deficiency Of Hyaluronoglucosaminidase
• Malignant Paraganglionic Neoplasm
• Tumor Progression
• Malignant Neoplasm Of Breast
• Glioma
• Glaucoma, Open-angle

• Hypoxia
• Collagen Arthritis
• Malignant Neoplasm Of Urinary Bladder
• Injury To Kidney
• Ulcer
• Endometriosis, Site Unspecified
• Malignant Catarrhal Fever

Interacting Proteins

• DAB1

Pathways

• Cell Proliferation
• Cell Migration
• Aging
• Glycosylation
• Localization
• Chondrocyte Differentiation
• Methylation
• Cartilage Development
• Regeneration
• Mrna Splicing
• Tissue Regeneration

• Translation
• Keratinocyte Proliferation
• Angiogenesis
• Histone Methylation
• Exocytosis

PTMs

• Glycosylation
• Demethylation

• Acetylation
• Methylation

For details, visit:
bosterbio.com/bosterbio-gene-info-cards/HYAL3

Boster Bio - Best Uses Of The HYAL3 Marker

You've found the right place if you're searching for primary antibodies to detect HYAL3 markers. Boster's high-affinity antibodies have been widely cited and validated for use in immunohistochemistry, Western Blotting, and ELISA. These antibodies are an invaluable resource for a wide range of applications, including cell cultivation, histology, imaging, and many others.

HYAL3 Marker

Using primer extensions, it is possible to amplify the HYAL3 genome. A primer pair of HYAL3L2-R2 and HYAL3L2 was constructed and cloned with human testis cDNA. The resulting fragment contains a full length cDNA sequence (1.8 kb). We were able determine the initiation location of Hyal3 transcript using this sequence.

Human and mouse genomic DNA are highly conserved for the HYAL3 locus. The HYAL3 locus shares many similarities with the HYAL1 & –SEMA3B gene. The human genome sequence was derived primarily using two GenBank sequences. In contrast, the mouse genomic sequence was derived mainly from the high-throughput Phase I draft of RP23–93E19 clone. The sequence of a mouse gene was aligned. The gap between Hyal2 (and -SEMA3B) was 275 bp. Two full-length EST clones later were assembled.

The chromosomes for both human and mouse cells contain the HYAL3 gene. The brain also contains Hyal3, where it is expressed in its entirety. It is believed that HYAL3 may regulate IFRD2's function. HYAL3 has not been expressed in any other gene in your brain, so its role is unknown in brain development.

The Y chromosomes of HYAL3 are very similar to the Y-chromosomes in human and mouse. Hyal2 is closely related to HYAL3, which is why they look so similar. Furthermore, these genes are also closely related to the same tissues. This suggests that these genes may work in concert. There is a potential role for HYAL3 in the degradation of HA.

The protein HYAL1 degrades the hyaluronic. Hyaluronidase may be found in many toxins. The progression of bladder cancer in patients with HYAL1 hyaluronidase is correlated with their levels. It is also found in kidney tissues and prostate cancer cells. There are many splice variations of HYAL3 genes. They are expressed in a wide variety cancer cells.

CHA

The HYAL3 gene is a small, non-coding RNA found in many different tissues. Its splicing mutations can occur at various locations, including exons 2 and 1. One HYAL3 splice variant, referred to as HYAL1wt, is generated by an internal splicing event that involves nucleotides 109 and 596 as donor/acceptor sites. The HYAL1v3 splice variation is produced by two separate splicing event. The first involves nucleotides 1239 (exon 1) and the second involves nucleotides 1477 (exon 2).

The HYAL3 sequence contains a 30-aa sequence, which is crucial for HAase activities. The sequence is encoded using a 90-bp exon independent of the gene. The resulting protein has a predicted amino acid sequence of 253 amino acids. Although the HYAL3 genome is highly conserved among mammals, it wasn't known if it had a function in the immune systems.

A 30-aa sequence is conserved in several HAases, and it is necessary for the enzyme activity of at least two human HAases. The human LUCA13 cosmid clone is composed of three exons plus two introns. However HYAL3v3 lacks a 90-bp sequence.

HYAL1v1 & HYAL3 are similar in their amino acid sequences. The HYAL1v1 Glu sequence contains a Glu at aa 129 compared to aa 131. The 30-aa sequence, although not required for catalysis is required to produce a functional CYP protein. Its function can be used to diagnose disease, although there are no definitive answers.

cDNA cloning, sequencing and analysis of bladder tumors revealed that the YYC genes are expressed in both hematopoid cells and malignant cells. The expression of HYAL3 in bladder cancer tissues may be heterogeneous. This is one of the reasons why researchers have been very interested in HYAL3 mRNA.

HYAL3 is involved in cancer, despite being a unique function. In addition to its prognostic function, HYAL1 also plays an important role in promoting and suppressing malignant growth in a specific cell type. This marker is important for cancer research. This enzyme is a component many toxins, and was recently discovered in bladder cancer cells.

CHA-luciferase

Boster Bio has created several primary antibodies to detect the HYAL3 hormone, a lipid soluble hormone. These antibodies are well cited and trusted by the research community. They have also been validated on immunohistochemistry, Western Blotting, and ELISA. Boster Bio antibodies are highly specific, making it ideal for different types of research. They can distinguish between normal cells and cancer cells.

CHA-bioluminescence

Bostern Bio has CHA-bioluminescence. You may be wondering how to optimize your experiments. There are many options when it comes to setting up a flow process. Whether you're using a Boster Bio automated or manual system, these guides can help you optimize your experiment. For any questions, please contact us. We'll be happy to answer your questions and guide you through the process of implementing this technology in your own experiments.