Apolipoprotein H / APOH Recombinant Protein | APOH recombinant protein

Recombinant Human Apolipoprotein H / APOH Protein (His tag)

Cat. Num. AAA2545857

• Gene Names: APOH; BG; B2G1; B2GP1
• Purity: > 96 % as determined by SDS-PAGE
• Synonyms: Apolipoprotein H / APOH; Recombinant Human Apolipoprotein H / APOH Protein (His tag); B2G1; BG; APOH; APOH recombinant protein

• Host: Human Cells
• Purity/Purification: > 96 % as determined by SDS-PAGE
• Form/Format: Lyophilized from sterile PBS, pH 7.4
• Sequence Length: 345

• Application Notes: The recombinant human APOH consists of 337 amino acids and predictes a molecular mass of 37.7 kDa. In SDS-PAGE under reducing conditions, the apparent molecular mass of rhAPOH is approximately 53 kDa due to different glycosylation.
• Predicted N Terminal: Gly 20
• Endotoxin: < 1.0 EU per mug of the protein as determined by the LAL method
• Preparation and Storage: Samples are stable for up to twelve months from date of receipt at -70 degree C

SDS-PAGE

Related Product Information for APOH recombinant protein

Background: Apolipoprotein H (APOH), also known as Beta-2-glycoprotein 1, Activated protein C-binding protein, B2GPI, and B2G1, is a glycoprotein synthesized by liver cells and it is present in the blood associated with plasma lipoproteins. It is an essential cofactor for the binding of certain antiphospholipid antibodies (APA) to anionic phospholipid. APOH binds to various kinds of negatively charged substances such as heparin, phospholipids, and dextran sulfate. APOH may prevent activation of the intrinsic blood coagulation cascade by binding to phospholipids on the surface of damaged cells. APOH appears to completely inhibit serotonin release by the platelets and prevents subsequent waves of the ADP-induced aggregation. The activity of APOH appears to involve the binding of agglutenating, negatively charged compounds, and inhibits agglutenation by the contact activation of the intrinsic blood coagulation pathway. APOH causes a reduction of the prothrombinase binding sites on platelets and reduces the activation caused by collagen when thrombin is present at physiological serum concentrations of APOH suggesting a regulatory role of APOH in coagulation. APOH plasma concentrations are strongly associated to metabolic syndrome alterations and vascular disease in type 2 diabetic and could be considered as a clinical marker of cardiovascular risk. APOH is found on several classes of lipoproteins, and is involved in the activation of lipoprotein lipase in lipid metabolism. This single-chain glycoprotein also has been implicated in several physiologic pathways including coagulation and the production of hypertension, which are related to the pathogenesis of primary cerebral hemorrhage (PICH).

Description: A DNA sequence encoding the human APOH (NP_000033.2) (Met 1-Cys 345) was expressed, with a polyhistidine tag at the C-terminus.

NCBI and Uniprot Product Information

• NCBI GI #: 153266841
• NCBI GeneID: 350
• NCBI Accession #: NP_000033.2
• NCBI GenBank Nucleotide #: NM_000042.2
• UniProt Accession #: P02749; Q9UCN7; B2R9M3
• Molecular Weight: 38,298 Da
• NCBI Official Full Name: beta-2-glycoprotein 1
• NCBI Official Synonym Full Names: apolipoprotein H
• NCBI Official Symbol: APOH
• NCBI Official Synonym Symbols: BG; B2G1; B2GP1
• NCBI Protein Information: beta-2-glycoprotein 1
• UniProt Protein Name: Beta-2-glycoprotein 1
• Protein Family: Beta-2-glycoprotein
• UniProt Gene Name: APOH
• UniProt Synonym Gene Names: B2G1; Apo-H; B2GPI; Beta(2)GPI

NCBI Description

Apolipoprotein H has been implicated in a variety of physiologic pathways including lipoprotein metabolism, coagulation, and the production of antiphospholipid autoantibodies. APOH may be a required cofactor for anionic phospholipid binding by the antiphospholipid autoantibodies found in sera of many patients with lupus and primary antiphospholipid syndrome, but it does not seem to be required for the reactivity of antiphospholipid autoantibodies associated with infections. [provided by RefSeq, Jul 2008]

Uniprot Description

Binds to various kinds of negatively charged substances such as heparin, phospholipids, and dextran sulfate. May prevent activation of the intrinsic blood coagulation cascade by binding to phospholipids on the surface of damaged cells.