Mouse COL1A1 Protein, His Tag, low endotoxin (MALS verified)

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Cat. No. / Size
Price
Availability
Qty
CO1-M5243-100ug
$360.00
In Stock - Delivery in 2-3 business days
CO1-M5243-1mg
$2380.00
In Stock - Delivery in 2-3 business days

Product Details

  • Synonyms

    COL1A1

  • Source

    Mouse COL1A1 Protein, His Tag (CO1-M5243) is expressed from human 293 cells (HEK293). It contains AA Leu 1218 - Val 1453 (Accession # P11087).

    Predicted N-terminus: His

    Request for sequence
  • Molecular Characterization

    COL1A1 Structure

    Other Tags and Version Biotin & Other Labeled Version

    This protein carries a polyhistidine tag at the N-terminus.

    The protein has a calculated MW of 28.8 kDa. The protein migrates as 33-37 kDa when calibrated against Star Ribbon Pre-stained Protein Marker under reducing (R) condition (SDS-PAGE) due to glycosylation.

    The protein is designed as a trimer.

  • Endotoxin

    Less than 0.01 EU per μg by the LAL method / rFC method.

  • Purity

    >90% as determined by SDS-PAGE.

  • Formulation

    Lyophilized from 0.22 μm filtered solution in 50 mM Tris, 150 mM NaCl, pH7.5 with trehalose as protectant.

    Contact us for customized product form or formulation.

  • Reconstitution

    Please see Certificate of Analysis for specific instructions.

    For best performance, we strongly recommend you to follow the reconstitution protocol provided in the CoA.

  • Shipping and Storage

    This product is shipped at ambient temperature.

    For long term storage, the product should be stored at lyophilized state at -20°C or lower.

    Please avoid repeated freeze-thaw cycles.

    This product is stable after storage at:

    1. -20°C to -70°C for 12 months in lyophilized state;
    2. -70°C for 3 months under sterile conditions after reconstitution.
  • ACRO Quality Management System

    1. QMS(ISO, GMP)
    2. Quality Advantages
    3. Quality Control Process

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Performance Data

  • SDS-PAGE

    COL1A1 SDS-PAGE

    Mouse COL1A1 Protein, His Tag on SDS-PAGE under reducing (R) condition. The gel was stained with Coomassie Blue. The purity of the protein is greater than 90% (With Star Ribbon Pre-stained Protein Marker).

  • SEC-MALS

    COL1A1 SEC-MALS

    The purity of Mouse COL1A1 Protein, His Tag (Cat. No. CO1-M5243) is more than 85% and the molecular weight of this protein is around 87-102 kDa verified by SEC-MALS.

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FAQ

  • product

    Can lyophilized proteins remain stable during room-temperature shipping or temporary room-temperature exposure?

    In general, lyophilized proteins remain stable during room-temperature shipping or temporary exposure to room-temperature conditions.


    Many ACROBiosystems recombinant proteins are supplied in lyophilized (freeze-dried) form. The lyophilization process effectively removes moisture from the product, helping reduce degradation-related reactions and improve protein stability during transportation and storage.


    To evaluate the stability of lyophilized proteins under normal temperature conditions, ACROBiosystems conducted a stability study on 11 representative lyophilized protein products at 37°C. The study demonstrated that these proteins maintained good quality stability after storage at 37°C for approximately 20 days. Based on these validation results, temporary room-temperature exposure during shipping or handling is generally not expected to have a significant impact on product quality or downstream application performance.


    To ensure optimal long-term stability, products should be stored according to the storage conditions specified in the product Certificate of Analysis (COA) upon receipt.


    Supporting Document


Background

Type I collagen is the most abundant structural protein of connective tissues such as skin, bone and tendon. It is synthesized as a procollagen molecule which is characterized by a 300 nm triple helical domain flanked by globular N- and C-terminal propeptides. The triple helical domain contains Gly-Xaa-Yaa triplets where Xaa and Yaa are frequently proline and hydroxyproline, respectively. The non-helical propeptides are removed by procollagen N- and C-proteinase activities so that the mature triple helices can self-assemble into collagen fibrils that provide tensile strength to tissues. Type I collagen is a heterotrimer that consists of two alpha 1(I) chains and one alpha 2(I) chain, although homotrimers consisting of three identical alpha 1(I) chains have also been described .

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