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Recombinant Rat Albumin protein (His Tag)

Species

Rat

Purity

>90 %, SDS-PAGE

Tag

His Tag

Activity

not tested

Cat no : Eg0935

Validation Data Gallery

  • Purity of Recombinant Rat Albumin was determined by SDS-PAGE. The protein was resolved in an SDS-PAGE in reducing (R) and non-reducing (NR) conditions and stained using Coomassie blue.

    Purity of Recombinant Rat Albumin was determined by SDS-PAGE. The protein was resolved in an SDS-PAGE in reducing (R) and non-reducing (NR) conditions and stained using Coomassie blue.

Product Information

Purity >90 %, SDS-PAGE
Endotoxin <0.1 EU/μg protein, LAL method
Activity 
Not tested
Expression HEK293-derived Rat Albumin protein Glu25-Ala608 (Accession# P02770) with a His tag at the C-terminus.
GeneID 24186
Accession P02770
PredictedSize 67.0 kDa
SDS-PAGE 60-70 kDa, reducing (R) conditions
Formulation Lyophilized from 0.22 μm filtered solution in PBS, pH 7.4. Normally 5% trehalose and 5% mannitol are added as protectants before lyophilization.
Reconstitution Briefly centrifuge the tube before opening. Reconstitute at 0.1-0.5 mg/mL in sterile water.
Storage Conditions
It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
  • Until expiry date, -20℃ to -80℃ as lyophilized proteins.
  • 3 months, -20℃ to -80℃ under sterile conditions after reconstitution.
Shipping The product is shipped at ambient temperature. Upon receipt, store it immediately at the recommended temperature.

Background

Albumin is a multi-functional protein that participates in the regulation of colloid osmotic pressure, transportation of endogenous ligands and drugs, and regulation of microvascular permeability. Albumin is the most abundant protein in blood plasma. Alterations of level of serum albumin are linked to variety of diseases. Albumin is expressed exclusively by well-differentiated hepatocytes, thus anti-albumin has been used to mark hepatocytes. In additon, glycated serum albumin is also a potential diabetes biomarker. Human (HSA) and rat (RSA) serum albumins share similar characteristics of binding biologically active substances.

References:

1. Wang Z, et al. (2012). J Cell Mol Med. 16(1):118-128.
2. Li J, et al. (2013). Nat Immunol.14(8):793-803.
3. Kamali M, et al. (2023). Life Sci. 313:121248.