E. coli biotin ligase
(BirA) is highly specific in covalently attaching biotin to the 15 amino
acid AviTag peptide. This recombinant protein was biotinylated in vivo
by AviTag-BirA technology, which method is BriA catalyzes amide linkage
between the biotin and the specific lysine of the AviTag.
The tag type will be
determined during production process. If you have specified tag
type, please tell us and we will develop the specified tag
preferentially.
產(chǎn)品提供形式:
Lyophilized powder Note: We will preferentially ship the format that we have in stock, however, if you have any special requirement for the format, please remark your requirement when placing the order, we will prepare according to your demand.
復(fù)溶:
We recommend that this vial be briefly centrifuged prior
to opening to bring the contents to the bottom. Please reconstitute
protein in deionized sterile water to a concentration of 0.1-1.0
mg/mL.We recommend to add 5-50% of glycerol (final concentration) and
aliquot for long-term storage at -20℃/-80℃. Our default final
concentration of glycerol is 50%. Customers could use it as reference.
儲存條件:
Store at -20°C/-80°C upon receipt, aliquoting is necessary for
mutiple use. Avoid repeated freeze-thaw cycles.
保質(zhì)期:
The shelf life is related to many factors, storage state,
buffer ingredients, storage temperature and the stability of the protein
itself.
Generally, the shelf life of liquid form is 6 months at -20°C/-80°C. The
shelf life of lyophilized form is 12 months at -20°C/-80°C.
貨期:
Delivery time may differ from different purchasing way or location, please kindly consult your local distributors for specific delivery time.
Note: All of our
proteins are default shipped with normal blue ice packs, if you
request to ship with dry ice, please communicate with us in advance
and extra fees will be charged.
注意事項:
Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.
Binds heparin and heparan sulfate with high affinity, but lacks heparanase activity. Inhibits HPSE, possibly by competing for its substrates (in vitro).
基因功能參考文獻:
The results of this study the Heparanase 2 appeared overexpressed at different stages of Alzheimer disease. PMID: 28387673
our results suggest that heparanase 2 functions as a tumor suppressor in bladder cancer PMID: 26968815
we provide evidence that Hpa2 overexpression in head and neck cancer cells markedly reduces tumor growth PMID: 27013193
The most common HPA genotypes among Saudis were HPA-1 a + b- (75%), HPA-2 a + b- (62%), HPA-3 a + b- (51.5%), HPA-4 a + b- (99%), HPA-5 a + b- (76.5%), HPA-6 a + b- (100%) and HPA-15 a + b + (50%). The prevalent allele among the HPA systems was (a), except in the HPA-15 system where the (b) allele was found in 52% of the subjects. PMID: 27019315
Our findings identified these 2 genes as a novel breast cancer biomarker gene set, which may facilitate the diagnosis and treatment in breast cancer clinical therapies. PMID: 26084486
HPSE2 mutations were found in one Urofacial syndrome family but not detected in patients with non-neurogenic neurogenic bladder and severe lower urinary tract dysfunction PMID: 25924634
Heparanase 2 is more intensely expressed in the glandular tissue of cancer than in nonneoplastic endometrium; the HPSE2 expression in the stromal tissue is higher in the nonneoplastic controls compared with cancer mainly in the secretory endometrium. PMID: 25423319
autonomic neural protein implicated in bladder emptying PMID: 25145936
High expression of heparanase-2 is associated significantly with gastric tumor growth and differentiation PMID: 24139593
Data indicate that the overexpression of HPSE1 and HPSE2 in the intervertebral degenerated discs suggests a role for these factors in mediating extracellular matrix remodeling in degenerative discs during disease development. PMID: 23370684
HPSE2 c.631T>C (p.Y211H) is a novel benign SNP and c.1628A>T (p.N543I) is the disease-causing mutation in urofacial syndrome. PMID: 21332471
A large region of marker homozygosity was observed at 10q24, consistent with known autosomal recessive inheritance, family consanguinity and previous genetic mapping in other families with Ochoa syndrome. PMID: 21450525
Studies indicate that cathepsin L as the heparanase activating protease. PMID: 21308479
These results indicate a regulatory effect of heparanase on TFPI and TFPI-2 in trophoblasts, suggesting a potential involvement of heparanase in early miscarriages. PMID: 20031192
We now report evidence that Heparanse 2 (HPSE2) is the culprit gene for the syndrome. Mutations with a loss of function in the Heparanase 2 (HPSE2) gene PMID: 20560209
Homozygous exonic deletions, nonsense mutations, and frameshift mutations in five further unrelated families confirmed HPSE2 as the causative gene for UFS PMID: 20560210
Results demonstrated that the effectors from heparanase peptide-immunized mice could effectively lyse various tumor cells that were heparanase positive and HLA-A*0201 matched. PMID: 20182872
Heparanase 2 is involved in neoplastic proliferation, but it was not exclusively associated with the malignant process. PMID: 19955924
Heparanase may facilitate invasion and metastasis of gastric carcinoma cells. PMID: 15475937
Study demonstrating that increased heparanase expression in prostate cancer tissues is due to promoter hypomethylation and up-regulation of transcription factor EGR1. PMID: 15709168
Heparanase expression seems to be involved in the invasiveness and aggressiveness of head and neck squamous cell carcinomas. PMID: 15837740
Heparanase expression is inversely correlated with survival of nasopharyngeal carcinoma (NPC) patients, indicating heparanase is a reliable prognostic factor, and further supports that heparanase is a valid target for the development of anti-cancer drugs. PMID: 16879396
HPSE plays a role in extracellular matrix remodeling and in increasing heparin-binding growth factor release during embryo implantation. PMID: 17989358
Data suggest that loss of modified heparan sulphate in the GBM is mediated by an increased heparanase presence and may play a role in the pathogenesis of diabetes-induced proteinuria. PMID: 18058084
Widely expressed, with the highest expression in brain, mammary gland, prostate, small intestine, testis and uterus. In the central nervous system, expressed in the spinal chord, caudate nucleus, thalamus, substantia nigra, medulla oblongata, putamen and