Anti-Hsp47 Picoband Antibody
- SPECIFICATION
- CITATIONS
- PROTOCOLS
- BACKGROUND
Application
| WB, IHC-P |
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Primary Accession | P50454 |
Host | Rabbit |
Reactivity | Human, Rat |
Clonality | Polyclonal |
Format | Lyophilized |
Description | Rabbit IgG polyclonal antibody for Serpin H1(SERPINH1) detection. Tested with WB, IHC-P in Human;Rat. |
Reconstitution | Add 0.2ml of distilled water will yield a concentration of 500ug/ml. |
Gene ID | 871 |
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Other Names | Serpin H1, 47 kDa heat shock protein, Arsenic-transactivated protein 3, AsTP3, Cell proliferation-inducing gene 14 protein, Collagen-binding protein, Colligin, Rheumatoid arthritis-related antigen RA-A47, SERPINH1, CBP1, CBP2, HSP47, SERPINH2 |
Calculated MW | 46441 MW KDa |
Application Details | Immunohistochemistry(Paraffin-embedded Section), 0.5-1 µg/ml, Human, Rat, By Heat Western blot, 0.1-0.5 µg/ml, Human |
Subcellular Localization | Endoplasmic reticulum lumen. |
Protein Name | Serpin H1 |
Contents | Each vial contains 5mg BSA, 0.9mg NaCl, 0.2mg Na2HPO4, 0.05mg NaN3. |
Immunogen | E.coli-derived human Hsp47 recombinant protein (Position: D247-L418). Human Hsp47 shares 97% amino acid (aa) sequence identity with both mouse and rat Hsp47. |
Purification | Immunogen affinity purified. |
Cross Reactivity | No cross reactivity with other proteins |
Storage | At -20˚C for one year. After r˚Constitution, at 4˚C for one month. It˚Can also be aliquotted and stored frozen at -20˚C for a longer time.Avoid repeated freezing and thawing. |
Sequence Similarities | Belongs to the serpin family. |
Name | SERPINH1 |
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Synonyms | CBP1, CBP2, HSP47, SERPINH2 |
Function | Binds specifically to collagen. Could be involved as a chaperone in the biosynthetic pathway of collagen. |
Cellular Location | Endoplasmic reticulum lumen. |
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Provided below are standard protocols that you may find useful for product applications.
Background
Heat shock protein 47, also known as SERPINH1 or HSP47, is a serpin which serves as a human chaperone protein for collagen. This protein is a member of the serpin superfamily of serine proteinase inhibitors. Its expression is induced by heat shock. The protein localizes to the endoplasmic reticulum lumen and binds collagen; thus it is thought to be a molecular chaperone involved in the maturation of collagen molecules. Autoantibodies to this protein have been found in patients with rheumatoid arthritis. It has been found that HSP47 monitors the integrity of the triple helix of type I procollagen at the ER/cis-Golgi boundary and, when absent, the rate of transit from the ER to the Golgi is increased and the helical structure is compromised.
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