Recombinant Human HABP2 Protein (C-6His)

Name: Recombinant Human HABP2 Protein (C-6His)
Brand: Beta LifeScience
SKU: BL-0924NP
Availability: InStock

BL-0924NP: Greater than 90% as determined by reducing SDS-PAGE. (QC verified)

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

Our products are highly customizable to meet your specific needs. You can choose options such as endotoxin removal, liquid or lyophilized forms, preferred tags, and the desired functional sequence range for proteins. Submitting a written inquiry expedites the quoting process.

Submit an inquiry today to inquire about all available size options and prices! Connect with us via the live chat in the bottom corner to receive immediate assistance.

Product Overview

Description	Recombinant Human Hyaluronan-binding Protein 2 is produced by our Mammalian expression system and the target gene encoding Met1-Gln279 is expressed with a 6His tag at the C-terminus.
Accession	Q14520
Synonym	Hyaluronan-binding protein 2; Factor VII-activating protease; Factor seven-activating protease; Hepatocyte growth factor activator-like protein; Plasma hyaluronan-binding protein
Gene Background	Hyaluronan-binding protein 2（HABP2） is an extracellular serine protease which binds hyaluronic acid. It secreted as an inactive single-chain precursor and is then activated to a heterodimeric form, which consists of a 50 kDa heavy and a 27 kDa light chain linked by a disulfide bond. HABP2 is involved in cell adhesion, it can cleave the alpha-chain at multiple sites and the beta-chain between 'Lys-53' and 'Lys-54' , but not the gamma-chain of fibrinogen. As a result of this, it does not initiate the formation of the fibrin clot and does not cause the fibrinolysis directly. It does not cleave prothrombin and plasminogen but converts the inactive single chain urinary plasminogen activator to the active two chain form, activates coagulation factor VII.
Molecular Mass	32.7 KDa
Apmol Mass	35-40 KDa, reducing conditions
Formulation	Lyophilized from a 0.2 μm filtered solution of PBS, pH 7.4.
Endotoxin	Less than 0.1 ng/µg (1 EU/µg) as determined by LAL test.
Purity	Greater than 90% as determined by reducing SDS-PAGE. (QC verified)
Biological Activity	Not tested
Reconstitution	Always centrifuge tubes before opening. Do not mix by vortex or pipetting. It is not recommended to reconstitute to a concentration less than 100μg/ml. Dissolve the lyophilized protein in distilled water. Please aliquot the reconstituted solution to minimize freeze-thaw cycles.
Storage	Lyophilized protein should be stored at ≤ -20°C, stable for one year after receipt. Reconstituted protein solution can be stored at 2-8°C for 2-7 days. Aliquots of reconstituted samples are stable at ≤ -20°C for 3 months.
Shipping	The product is shipped at ambient temperature. Upon receipt, store it immediately at the temperature listed below.
Usage	For Research Use Only

Target Details

Target Function	Cleaves the alpha-chain at multiple sites and the beta-chain between 'Lys-53' and 'Lys-54' but not the gamma-chain of fibrinogen and therefore does not initiate the formation of the fibrin clot and does not cause the fibrinolysis directly. It does not cleave (activate) prothrombin and plasminogen but converts the inactive single chain urinary plasminogen activator (pro-urokinase) to the active two chain form. Activates coagulation factor VII. May function as a tumor suppressor negatively regulating cell proliferation and cell migration.
Subcellular Location	Secreted. Note=Secreted as an inactive single-chain precursor and is then activated to a heterodimeric form.
Protein Families	Peptidase S1 family
Database References	HGNC: 4798 OMIM: 603924 KEGG: hsa:3026 STRING: 9606.ENSP00000277903 UniGene: PMID: 29895015 The MI-SNP and MII-SNP FSAP gene polymorphisms were not predictive or prognostic biomarkers for coronary artery diseaseor its main risk factors. PMID: 29927903 NETs bind to FSAP, but do not activate pro-FSAP unless histones are released from NETs by DNAse. This activation of FSAP is likely to be important in diminishing the cytotoxic effect of histones, thus limiting the damaging effect of NETosis. PMID: 29178989 Regulation of gene expression by FSAP in vascular smooth muscle/endothelial cells accounts for its vasculo-regulatory properties. PMID: 28881271 The extent of CAC in women is positively associated with total FSAP, but negatively associated with the specific activity of FSAP suggesting that FSAP may play a role in the evolution of CVD in women. PMID: 28548975 Report peptide substrates used in determining substrate specificity of Factor VII activating protease. PMID: 28726978 Two of 20 probands from families with history of PTC and breast carcinoma (BC) were evaluated by whole exome sequencing (WES) revealing HABP2 p.G534E. PMID: 28402931 No significant association was found between rs11196288 and early-onset ischemic stroke, large artery atherosclerotic stroke, or small vessel disease stroke. rs11196288 presented significant effect on late-onset SVD stroke susceptibility in the older population. PMID: 28501930 study on a wide series of familial non-medullary thyroid cancers indicates that the HABP2(G534E) variant is frequent, but does not segregate with the disease PMID: 28222214 Letter: G534E variant in HABP2 is not associated with non-medullary thyroid cancer in the Spanish population. PMID: 27245704 mutations were not found in familial non-medullary thyroid cancer, and the G534E variant is not the underlying genetic defect in a large sample of sporadic non-medullary thyroid cancer from the Middle East. PMID: 26906432 Study showed that lower FSAP antigen plasma levels were associated with a higher chance of arterial recanalization after tissue plasminogen activator treatment, suggesting an involvement of FSAP in tissue plasminogen activator-induced clot lysis. FSAP antigen determination might be useful in predicting tissue plasminogen activator response in stroke patients. PMID: 27073188 HABP2 polymorphisms are not associated with thyroid cancer. PMID: 27873212 the promoter activity, which could phenocopy changes in Habp2 mRNA in response to TGF-beta, was found to be located in the 177-bp region upstream of the transcription start site, and this region did not contain any SMAD binding sites. PMID: 27462075 Results show that G534E germline variant in HABP2 does not account for the familial nature of nonmedullary thyroid cancer in Australian kindreds but and is common in the general population. PMID: 27530615 omology modeling suggested that the Glu-221 side chain could sterically hinder insertion of the N terminus into the HABP2 protease domain, helping to explain the detrimental effects of Glu-221 substitution on HABP2 activity. PMID: 28246168 The data do not support the pathogenicity of the HABP2 c.1601G > A variant but highlight the existence of a new one that should be more extensively searched for in familial papillary thyroid carcinoma patients and its pathogenicity more carefully evaluated. PMID: 28089742 No evidence supporting a role for the HABP2 G534E variant (SNP rs7080536) in papillary thyroid carcinoma. PMID: 26745718 HABP2 G534E appears to be a susceptibility gene in a subgroup of Familial Non-Medullary Thyroid Cancer (FNMTC), providing important diagnostic implications for this hereditary thyroid cancer. PMID: 26832773 HABP2, which encodes an extracellular serine protease involved in coagulation, fibrinolysis, and inflammatory pathways, may be a genetic susceptibility locus for early-onset stroke. [Meta-Analysis] PMID: 26732560 Patients with Gram-negative sepsis caused by B. pseudomallei have abundant FSAP activation, which significantly correlates with stage of disease. PMID: 25370187 results suggest that the HABP2 G534E variant is a susceptibility gene for familial nonmedullary thyroid cancer PMID: 26222560 CD44 expression in squamous cell carcinoma of the penis cannot predict the need of performing inguinal lymphadenectomy. PMID: 25847894 FSAP functions in initiation and progression of hepatic fibrosis PMID: 24497464 The possible effects of omega-3 FA on clinical AF potential could be linked with modulation of circulating FSAP levels. PMID: 23575879 FSAP activates the NF-kappaB pathway and the associated downstream pro-inflammatory factors in monocytic cells PMID: 24075769 The study demonstrated that a single nucleotide polymorphism (Marburg I) in the FSAP gene (HABP-2)results in a weak proteolytic activity against all substrates including FVII. PMID: 22906531 Lower FSAP expression is associated with enhanced liver fibrosis and inflammation in patients with chronic hepatic disorders and murine experimental liver injury. PMID: 22989567 Data indicate that FSAP mediates proteolytic cleavage and activation of bone morphogenetic protein-2 (BMP-2). PMID: 23341458 High levels of FSAP activity were predictive of adverse events during follow-up, suggesting its potential role in risk stratification and clinical management of CAD patients. PMID: 22850287 We conclude that FSAP Marburg-I genotyping may be used to determine the risk for thromboembolic disorders in patients with suspected thrombophilia and known DVT or PE. PMID: 22421107 Report tissue factor pathway inhibitor as an efficient inhibitor of factor VII-activating protease. PMID: 22449009 Increased plasma FSAP antigen levels and activity were associated with ischemic stroke and all main etiologic subtypes. PMID: 22409238 These results indicate that polymorphisms in the regulatory region of HABP2 gene could influence gene expression levels in the receptive endometrium and be one reason for infertility complications in women with unexplained infertility. PMID: 21098215 Data suggest that plasma FSAP activity levels were higher in women with recurrent pregnancy loss than in fertile women. PMID: 22383781 A high correlation between FSAP activity and C5a was found in multiple trauma patients PMID: 22308306 Factor VII-activating protease promotes the proteolysis and inhibition of tissue factor pathway inhibitor. PMID: 22116096 SNP analyses indicate an important role for FSAP in the regulation of the haemostasis system as well as fibroproliferative inflammatory processes. [review] PMID: 21655671 these results suggest pathophysiological relevance of histone-dependent pro-PHBP activation in hyperinflammatory process. PMID: 21600885 Marburg I polymorphism of FSAP might not be associated with cerebral infarction. PMID: 20045910 identified laccaic acid as a potent inhibitor of the protease in terms of both autoactivation of the PHBP proenzyme (IC(50) = 0.35-0.55 microg/ml) and the catalytic activity of the active enzyme (IC(50) = 1.1 microg/ml). PMID: 21071862 FSAP inhibited platelet-derived growth factor-stimulated proliferation, migration, p42/p44 MAPK phosphorylation and collagen III synthesis of the human pulmonary fibroblasts. PMID: 20818495 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 Report that polyamine induces the formation of pro-PHBP autoactivation complex, in which an intermolecular interaction between N-terminal region and the third EGF-like domain (E3) plays a role. PMID: 19817990 Hyaluronic acid binding protein 2 (HABP2) negatively regulates vascular integrity via activation of protease-activated receptor/RhoA/Rho kinase signaling. It represents a potential therapeutic target for syndromes of increased vascular permeability. PMID: 20042707 The frequency of factor VII-activating protease Marburg I is significantly increased in patients with a history of venous thromboembolism (VTE) or idiopathic VTE compared to healthy controls. PMID: 15486068 An interactive effect upon risk was found between the 511E allele and elevated levels of cholesterol and triglyceride or fibrinogen. The findings support the proposal that the FSAP 511E allele exacerbates atherosclerosis or its clinical sequelae PMID: 15543324 extracellular RNA, present at sites of cell damage or vascular injury, can serve an important as yet unrecognized cofactor function in haemostasis by inducing (auto-)activation of FSAP through a novel surface-dependent mechanism PMID: 15654766 Marburg I polymorphism of factor VII-activating protease does not have a role in venous thrombosis [letter] PMID: 15933067 exhibits a significant growth factor-like activity on quiescent human lung and dermal fibroblasts PMID: 16153533

FAQs

Please fill out the Online Inquiry form located on the product page. Key product information has been pre-populated. You may also email your questions and inquiry requests to sales1@betalifesci.com. We will do our best to get back to you within 4 business hours.

Feel free to use the Chat function to initiate a live chat. Our customer representative can provide you with a quote immediately.

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.