Mouse Hyaluronan Binding Protein 2 (HABP2) Protein

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Description
Mouse Hyaluronan-Binding Protein is a recombinant protein from Mouse produced in Human Cells. 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.
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Product specifications
| Category | Proteins and Peptides |
| Immunogen Target | Hyaluronan-Binding |
| Host | Human |
| Origin | Mouse |
| Observed MW | Molecular Weight: 36.2 kDa Sequence Fragment: Met1-Gln279 Tag: C-terminal 6 His tag |
| Expression | Recombinant |
| Purity | > 90% (SDS-PAGE) |
| Size 1 | 10 µg |
| Size 2 | 50 µg |
| Form | Lyophilized |
| Tested Applications | SDS-PAGE |
| Buffer | PBS, pH 7.4. |
| Availability | Shipped within 5-15 working days. |
| Storage | Store at < -20°C. |
| Dry Ice | No |
| UniProt ID | Q14520 |
| Background | Protein HABP2 |
| Status | RUO |
| Note | This product is for research use only. Not for human consumption, cosmetic, therapeutic or diagnostic use. |
Descripción
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Hyaluronan Binding Protein 2 (HABP2) Antibody
HABP2 Antibody is a Rabbit Polyclonal antibody against HABP2. The protein encoded by this gene is an extracellular serine protease that binds hyaluronic acid and is involved in cell adhesion. The encoded protein is synthesized as a single chain, but then undergoes an autoproteolytic event to form the functional heterodimer. Further autoproteolysis leads to smaller, inactive peptides. This protease is known to cleave urinary plasminogen activator, coagulation factor VII, and the alpha and beta chains of fibrinogen, but not prothrombin, plasminogen, or the gamma chain of fibrinogen. Two transcript variants encoding different isoforms have been found for this gene.
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Hyaluronan Binding Protein 2 (HABP2) Antibody
HABP2 is an extracellular serine protease that binds hyaluronic acid and is involved in cell adhesion. The encoded protein is synthesized as a single chain, but then undergoes an autoproteolytic event to form the functional heterodimer. Further autoproteolysis leads to smaller, inactive peptides. This protease is known to cleave urinary plasminogen activator, coagulation factor VII, and the alpha and beta chains of fibrinogen, but not prothrombin, plasminogen, or the gamma chain of fibrinogen. Two transcript variants encoding different isoforms have been found for this gene.
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