Hyaluronan Binding Protein 2 (HABP2) Antibody

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Description
Hyaluronan Binding Protein 2 (HABP2) Antibody is a Rabbit Polyclonal antibody against Hyaluronan Binding Protein 2 (HABP2).
Documents del producto
Product specifications
Category | Primary Antibodies |
Immunogen Target | Hyaluronan Binding Protein 2 (HABP2) |
Host | Rabbit |
Reactivity | Human, Mouse, Rat |
Recommended Dilution | Optimal dilutions/concentrations should be determined by the end user. |
Clonality | Polyclonal |
Conjugation | Unconjugated |
Purification | Purified by affinity chromatography using epitope-specific immunogen. |
Size 1 | 100 µg |
Form | Liquid |
Tested Applications | ELISA, WB |
Buffer | PBS, 50% glycerol, 0.5% BSA and 0.02% sodium azide. |
Availability | Shipped within 5-12 working days. |
Storage | Aliquot and store at -20°C. Avoid repeated freeze/thaw cycles. |
Dry Ice | No |
UniProt ID | Q14520 |
Gene ID | 3026 |
Background | Antibody anti-HABP2 |
Status | RUO |
Note | Concentration: 1 mg/ml - |
Descripción
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Recombinant Human HABP2
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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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