Complement C3 Protein, Mouse (HEK293, His)

Complement C3 protein activates the complement system, playing a central role in both classical and alternative pathways. C3b binds covalently to cell surface carbohydrates or immune aggregates, while C3a acts as an inflammatory mediator, inducing neutrophil chemoattraction and promoting smooth muscle contraction, increased vascular permeability, and histamine release. The shorter isoform of C3a stimulates B-cells. Complement C3 Protein, Mouse (HEK293, His) is the recombinant mouse-derived Complement C3 protein, expressed by HEK293 , with C-His labeled tag.

Complement C3/C3a protein plays a pivotal role in the activation of the complement system, being the central reaction in both classical and alternative pathways. Following activation, C3b can bind covalently to cell surface carbohydrates or immune aggregates through its reactive thioester. C3a, derived from the proteolytic degradation of complement C3, acts as a local inflammatory mediator, inducing neutrophil chemoattraction and promoting smooth muscle contraction, increased vascular permeability, and histamine release from mast cells and basophilic leukocytes. Additionally, the shorter isoform of C3a exhibits B-cell stimulatory activity.

Mouse

HEK293

C-His

P01027-1 (I25-N1663)

12266  [NCBI]

65-68 kDa & 110-115 kDa & 165-180 kDa

Greater than 95% as determined by Tris-Bis PAGE.

Lyophilized powder

Lyophilized from a 0.22 μm filtered solution of PBS, pH 7.4. Normally 8% trehalose is added as protectant before lyophilization.

<1 EU/μg, determined by LAL method.

It is not recommended to reconstitute to a concentration less than 100 μg/mL in ddH₂O. For long term storage it is recommended to add a carrier protein (0.1% BSA, 5% HSA, 10% FBS or 5% Trehalose).

Stored at -20°C for 2 years. After reconstitution, it is stable at 4°C for 1 week or -20°C for longer (with carrier protein). It is recommended to freeze aliquots at -20°C or -80°C for extended storage.

Room temperature in continental US; may vary elsewhere.