Recombinant Mouse Haptoglobin (HP) Protein (His)

Name: Recombinant Mouse Haptoglobin (HP) Protein (His)
Brand: Beta LifeScience
SKU: BLC-00918P
Availability: InStock

Greater than 85% as determined by SDS-PAGE.

Collections: High-quality recombinant proteins, Other recombinant proteins

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Product Overview

Description	Recombinant Mouse Haptoglobin (HP) Protein (His) is produced by our E.coli expression system. This is a full length protein.
Purity	Greater than 85% as determined by SDS-PAGE.
Uniprotkb	Q61646
Target Symbol	HP
Species	Mus musculus (Mouse)
Expression System	E.coli
Tag	N-6His
Target Protein Sequence	VELGNDAMDFEDDSCPKPPEIANGYVEHLVRYRCRQFYRLRAEGDGVYTLNDEKQWVNTVAGEKLPECEAVCGKPKHPVDQVQRIIGGSMDAKGSFPWQAKMISRHGLTTGATLISDQWLLTTAKNLFLNHSETASAKDITPTLTLYVGKNQLVEIEKVVLHPNHSVVDIGLIKLKQRVLVTERVMPICLPSKDYIAPGRVGYVSGWGRNANFRFTDRLKYVMLPVADQDKCVVHYENSTVPEKKNLTSPVGVQPILNEHTFCAGLTKYQEDTCYGDAGSAFAIHDMEEDTWYAAGILSFDKSCAVAEYGVYVRATDLKDWVQETMAKN
Expression Range	19-347aa
Protein Length	Full Length of Mature Protein
Mol. Weight	40.9 kDa
Research Area	Cardiovascular
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	As a result of hemolysis, hemoglobin is found to accumulate in the kidney and is secreted in the urine. Haptoglobin captures, and combines with free plasma hemoglobin to allow hepatic recycling of heme iron and to prevent kidney damage. Haptoglobin also acts as an antioxidant, has antibacterial activity and plays a role in modulating many aspects of the acute phase response. Hemoglobin/haptoglobin complexes are rapidly cleared by the macrophage CD163 scavenger receptor expressed on the surface of liver Kupfer cells through an endocytic lysosomal degradation pathway.
Subcellular Location	Secreted.
Protein Families	Peptidase S1 family
Database References	KEGG: mmu:15439 STRING: 10090.ENSMUSP00000074436 UniGene: PMID: 28440464 Data show that zonulin-dependent small intestinal barrier impairment is an early step leading to the break of tolerance with subsequent development of chronic inflammatory diseases (CIDs). PMID: 28423466 the interaction between haptoglobin genotype and vitamin E affects atherosclerotic plaque progression and stability PMID: 25618031 Suggest haptoglobin is an enhancer of inflammation after cardiac transplantation, contributing to graft rejection. PMID: 25801896 Zonulin facilitates development of acute lung injury (ALI) both by enhancing albumin leak and complement activation as well as increased buildup of neutrophils and cytokines during development of ALI. PMID: 23564505 Haptoglobin deficiency is associated with leakage-prone vessels via isolated VEGFA induction and/or suppressed Ang-1 expression, resulting in unbalanced VEGFalpha/Ang-1 transcription. PMID: 23274064 Hp generated by the B-cell compartment, rather than by the liver, is functionally contributing to a normal immune response. PMID: 23548836 the Hp2-2 protein is involved in aneurysm formation and that the Hp genotype may be a useful biomarker in predicting aneurysm progression PMID: 23096414 Experimental models of colitis showed that haptoglobin has a protective role in inflammatory colitis PMID: 21708824 these studies provide direct evidence that the increased oxidative stress in Hp 2-2 atherosclerotic plaques is due to hemoglobin derived iron. PMID: 19775690 Synthetic PPAR gamma ligands selectively activate PPAR gamma bound to the haptoglobin gene promoter to arrest haptoglobin gene transcription. PMID: 19952271 Hp may be regarded as a regulator of the Th1/Th2 balance in both human and murine immune systems. PMID: 11865978 Hp plays a pivotal role in reducing renal oxidative damage during haemolysis. PMID: 11865980 Haptoglobin gene expression regulation PMID: 11865981 haptoglobin and hemopexin together are essential for protection from splenomegaly and liver fibrosis resulting from intravascular hemolysis PMID: 12393471 the haptoglobin gene expression in adipocytes is stimulated by inflammatory cytokines, glucocorticoids, and the sympathetic system PMID: 14697247 haptoglobin-mediated heme-iron recovery may contribute significantly to iron loading in hemochromatosis PMID: 15613548 a direct linkage between diabetic vascular disease and the Hp genotype. PMID: 15852445 Increased prevalence of diabetic retinopathy in individuals with the haptoglobin 2 genotype. PMID: 16742000 Increased iron, lipid peroxidation and macrophage accumulation in ApoE-/- Hp 2-2 plaques suggests that the haptoglobin genotype plays a critical role in the oxidative and inflammatory response to intraplaque hemorrhage. PMID: 17068284 The reduction in reverse cholesterol transport associated with diabetes mellitus was significantly greater in Hp2-2 mice as compared with Hp1-1 mice PMID: 17082477 results suggest that correct processing of haptoglobin may be sensitive to ER stress & that, in absence of GRP78-mediated assistance, Hp is degraded; data show that iron regulates haptoglobin synthesis & suggest possible link with iron-induced ER stress PMID: 17644369 Suggest that haptoglobin, by controlling plasma levels of hemoglobin, participates in the regulation of ferroportin expression, thus contributing to the regulation of iron transfer from duodenal mucosa to plasma. PMID: 17919498 the Hp 2-2 genotype is critical for the development of severe vasospasm, which typically occurs 24 hours after SAH in mice PMID: 17962599 The phenotype of Hp-deficient mice suggests a major regulatory activity for Hp in supporting proliferation and functional differentiation of B and T cells as part of homeostasis and in response to antigen stimulation. PMID: 18436583 Pharmacogenomic effect of vitamin E on kidney structure and function in transgenic mice with the haptoglobin 2-2 genotype and diabetes mellitus. PMID: 19176700 HDL can become proinflammatory via the hemoglobin x Hp pathway in mice and humans PMID: 19433579 In diabetic mice the Hp 2-2 genotype is associated with increased mortality and more severe cardiac remodeling 30 days after myocardial infarct. PMID: 19490627 Results suggest that HP plays a modulatory and protective role on autoimmune inflammation of the CNS. PMID: 19795414

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.