Recombinant Human Aquaporin-1 (AQP1) Protein, Homo sapiens (Human), in vitro E.coli expression system, N-terminal 6xHis-SUMO-tagged, 41.3kDa, purity >90% as determined by SDS-PAGE.

Recombinant Human Aquaporin-1 (AQP1) Protein

Recombinant Human Aquaporin-1 (AQP1) Protein — Forms a water channel that facilitates the transport of water across cell membranes, playing a crucial role in water homeostasis in various tissues. Purity >90%.

SKU: BCRECP-00318TM Category:
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Product Specifications

Uniprot No.P29972
Gene NamesAQP1
PurityGreater than 90% as determined by SDS-PAGE.
Expression Systemin vitro E.coli expression system
Expression Region2-269aa
SpeciesHomo sapiens (Human)
Tag InfoN-terminal 6xHis-SUMO-tagged
Molecular weight41.3kDa
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.

Function

Forms a water channel that facilitates the transport of water across cell membranes, playing a crucial role in water homeostasis in various tissues. Could also be permeable to small solutes including hydrogen peroxide, glycerol and gases such as amonnia (NH3), nitric oxide (NO) and carbon dioxide (CO2). Recruited to the ankyrin-1 complex, a multiprotein complex of the erythrocyte membrane, it could be part of a CO2 metabolon, linking facilitated diffusion of CO2 across the membrane, anion exchange of Cl(-)/HCO3(-) and interconversion of dissolved CO2 and carbonic acid in the cytosol.

Biological Context

Subcellular Location: Cell membrane (Multi-pass membrane protein)
Tissue Specificity: Detected in erythrocytes (at protein level). Expressed in a number of tissues including erythrocytes, renal tubules, retinal pigment epithelium, heart, lung, skeletal muscle, kidney and pancreas. Weakly expressed in brain, placenta and liver

Product Specifications

Recombinant Human Aquaporin-1 (AQP1) Protein is a recombinant protein from Homo sapiens (Human), expressed in in vitro E.coli expression system, covering amino acids 2-269aa, with N-terminal 6xHis-SUMO-tagged tag, molecular weight 41.3kDa, purity Greater than 90% 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: Not implied unless activity data are explicitly listed on this product page, the datasheet, or the CoA.

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.

Related products

Protein Biology

Function

Forms a water channel that facilitates the transport of water across cell membranes, playing a crucial role in water homeostasis in various tissues (PubMed:1373524, PubMed:23219802). Could also be permeable to small solutes including hydrogen peroxide, glycerol and gases such as amonnia (NH3), nitric oxide (NO) and carbon dioxide (CO2) (PubMed:16682607, PubMed:17012249, PubMed:19273840, PubMed:33028705, PubMed:8584435). Recruited to the ankyrin-1 complex, a multiprotein complex of the erythrocyte membrane, it could be part of a CO2 metabolon, linking facilitated diffusion of CO2 across the membrane, anion exchange of Cl(-)/HCO3(-) and interconversion of dissolved CO2 and carbonic acid in the cytosol (PubMed:17012249, PubMed:35835865). In vitro, it shows non-selective gated cation channel activity and may be permeable to cations like K(+) and Na(+) in vivo (PubMed:36949749, PubMed:8703053)

Subcellular Location

Cell membrane (Multi-pass membrane protein)

Tissue Specificity

Detected in erythrocytes (at protein level). Expressed in a number of tissues including erythrocytes, renal tubules, retinal pigment epithelium, heart, lung, skeletal muscle, kidney and pancreas. Weakly expressed in brain, placenta and liver

Subunit

Homotetramer; each monomer provides an independent water pore (PubMed:11171962, PubMed:35835865). Component of the ankyrin-1 complex in the erythrocyte, composed of ANK1, RHCE, RHAG, SLC4A1, EPB42, GYPA, GYPB and AQP1 (PubMed:35835865). Interacts with EPHB2; involved in endolymph production in the inner ear (By similarity). Identified in a complex with STOM (PubMed:23219802). Interacts (via the N-terminal) with ANK1 (via ANK 1-5 repeats) (PubMed:35835865). Interacts (via the C-terminal) with EPB42 (PubMed:35835865)

Gene: AQP1  |  Organism: Homo sapiens  |  Synonyms: Aquaporin-CHIP; Channel-like integral membrane protein of 28 kDa; Urine water channel
Key Publications

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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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