Recombinant Rat Heme oxygenase 1 (Hmox1)

Recombinant Rat Heme oxygenase 1 (Hmox1) — recombinant protein from Rattus norvegicus (Rat), expressed in Yeast. Purity >85%.

SKU: BCRECP-003002 Category:

Product Specifications

Product SkuBCRECP-003002
Product DescriptionRecombinant Rat Heme oxygenase 1 (Hmox1) Protein is expressed from Yeast with N-terminal 6xHis-tagged. It contains 1-289aa. [Accession | P06762].
Uniprot No.P06762
Gene NamesHmox1
PurityGreater than 85% as determined by SDS-PAGE.
Expression SystemYeast
Expression Region1-289aa
SpeciesRattus norvegicus (Rat)
Tag InfoN-terminal 6xHis-tagged
Molecular weight35.0kDa
ActivityPlease contact us to obtain bioactivity data.
BufferIf the delivery form is liquid, the default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol. If the delivery form is lyophilized powder, the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose.
StorageStore at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. Avoid repeated freeze-thaw cycles.
Research AreasCell Biology

Function

Catalyzes the oxidative cleavage of heme at the alpha-methene bridge carbon, released as carbon monoxide (CO), to generate biliverdin IXalpha, while releasing the central heme iron chelate as ferrous iron.

Biological Context

Subcellular Location: Endoplasmic reticulum membrane (Single-pass type IV membrane protein)

Product Specifications

Recombinant Rat Heme oxygenase 1 (Hmox1) is a recombinant protein from Rattus norvegicus (Rat), expressed in Yeast, covering amino acids 1-289aa, with N-terminal 6xHis-tagged tag, molecular weight 35.0kDa, purity Greater than 85% as determined by SDS-PAGE.. Suitable for ELISA and Western Blot applications.

Recommended applications depend on the target, product format, and product-specific validation data. Refer to the product datasheet or Certificate of Analysis (CoA), or contact BioCrest Sci for application guidance.

Biological Activity: Please contact us to obtain bioactivity data.

Storage: Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. Avoid repeated freeze-thaw cycles.

Shipping & Lead Time: Availability, shipping conditions, and estimated lead time are confirmed in the formal quotation or order confirmation based on the product format, destination, and order requirements.

Protein Biology

Function

Catalyzes the oxidative cleavage of heme at the alpha-methene bridge carbon, released as carbon monoxide (CO), to generate biliverdin IXalpha, while releasing the central heme iron chelate as ferrous iron

Subcellular Location

Endoplasmic reticulum membrane (Single-pass type IV membrane protein)

Subunit

Homodimer and higher order homooligomer. Oligomerization is crucial for its stability and function in the endoplasmic reticulum. Interacts with FLVCR2; this interaction is potentiated in the presence of heme

Gene: Hmox1  |  Organism: Rattus norvegicus  |  Synonyms: HSP32
Key Publications

Frequently Asked Questions

How do I order or inquire about this product?

Submit the Online Inquiry form with your required quantity and specifications, or email sales@biocrestsci.com. Available sizes, pricing, stock status, documentation, and estimated lead time are confirmed in the formal quotation.

What is the shipping and delivery time?

Availability, dispatch timing, shipping conditions, and delivery estimates depend on the product format, destination, and order requirements. These details are confirmed in the formal quotation or order confirmation.

How should this product be stored?

Follow the storage and handling instructions in the product-specific datasheet and Certificate of Analysis (CoA). Requirements may vary by product form and formulation; contact BioCrest Sci if product-specific guidance is needed.

What quality controls are performed on your products?

Quality-control data such as identity, purity, endotoxin level, or biological activity are provided only when specified on this product page, the datasheet, or Certificate of Analysis (CoA). Biological activity is not implied unless explicitly stated.

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