calreticulin

Calreticulin Protein, Cricetulus griseus, Recombinant (His) is expressed in yeast with C-6xHis tag. The predicted molecular weight is 48.1 kDa and the accession number is Q8K3H7.

Calreticulin Protein, Mouse, Recombinant (GST) is expressed in E. coli expression system with N-GST tag. The predicted molecular weight is 73.3 kDa and the accession number is P14211.

Calreticulin Protein, Human, Recombinant (hFc) is expressed in HEK293 mammalian cells with hFc tag. The predicted molecular weight is 73 kDa and the accession number is P27797.

Calreticulin Protein, Human, Recombinant (His) is expressed in HEK293 mammalian cells with His tag. The predicted molecular weight is 47.4 kDa and the accession number is P27797.

Calreticulin Protein, Mouse, Recombinant (His) is expressed in yeast with N-6xHis tag. The predicted molecular weight is 48.3 kDa and the accession number is P14211.

Calreticulin Protein, Pig, Recombinant (His) is expressed in yeast with N-6xHis tag. The predicted molecular weight is 48.6 kDa and the accession number is P28491.

Calreticulin Protein, Human, Recombinant is expressed in HEK293 mammalian cells. The predicted molecular weight is 45.99 kDa and the accession number is P27797.

Calreticulin-3 belongs to the calreticulin family, members of which are calcium binding chaperones localized mainly in the endoplasmic reticulum. It can be divided into a N-terminal globular domain, a proline-rich P-domain forming an elongated arm-like structure and a C-terminal acidic domain. During spermatogenesis process, Calreticulin-3 may act as a lectin-independent chaperone for specific client proteins such as ADAM3. Defects in CALR3 are the cause of familial hypertrophic cardiomyopathy type 19 (CMH19), it is a hereditary heart disorder characterized by ventricular hypertrophy, which is usually asymmetric and often involves the interventricular septum. The symptoms include dyspnea, syncope, collapse, palpitations, and chest pain.

Calnexin CANX is a single-pass type I membrane protein which belongs to the calreticulin family. It consists of a large N-terminal calcium-binding lumenal domain, a single transmembrane helix and a short (90 residues), acidic cytoplasmic tail. The function of calnexin is to retain unfolded or unassembled N-linked glycoproteins in the endoplasmic reticulum. Calnexin is a calcium-binding protein that interacts briefly with newly synthesized glycoproteins in the endoplasmic reticulum. Calnexin may act in assisting protein assembly and or in the retention within the ER of unassembled protein subunits. Calnexin seems to play a major role in the quality control apparatus of the ER by the retention of incorrectly folded proteins. Calnexin dwindles with aging and might contribute to a cytoprotection in an array of human age-related diseases.

Calmegin (CLGN) is a member of the calreticulin family. Calmegin is a testis-specific endoplasmic reticulum chaperone protein. The functions during spermatogenesis as a chaperone for a range of client proteins that is important for sperm adhesion onto the egg zona pellucida and for subsequent penetration of the zona pellucida. It is required for normal male fertility, normal sperm migration from the uterus into the oviduct. Calmegin binds calcium ions and interacts with PDILT. Calmegin may play a role in spermatogeneisis and infertility.

Surfactant Pulmonary-Associated Protein D (SP-D) is a 43 kDa member of the collectin family of innate immune modulators. Its principal components consist of a collagen-like region and a C-terminal carbohydrate recognition domain (CRD), a structure that places it in a subset of pattern recognition proteins termed defense collagens. SP-D is constitutively secreted by alveolar lining cells and epithelium associated with tubular structures and induced in cardiac smooth muscle and endothelial cells. It binds both secreted and transmembrane proteins that transduce its function. It binds human neutrophil defensins, modulating influenza anti-viral defense. It binds MD-2 LY96, a secreted protein that cooperates with Toll-like receptors (TLRs) in the response of macrophages to bacterial lipopolysaccharides (LPS) or cell wall components. It also binds macrophage CD14 and TLRs directly, blocking binding of LPS and down-regulating TNF-α secretion. SP-D binding of both SIRPα and the calreticulin CD91 complex on macrophages allows for a graded response to environmental challenge.

PDIA3 protein is also known as Protein disulfide-isomerase A3. It is a protein that in humans is encoded by the PDIA3 gene.PDIA3 is an enzyme that belongs to the endoplasmic reticulum and interacts with lectin chaperones calreticulin and calnexin to modulate folding of newly synthesized glycoproteins. PDIA3 interacts with thiazide-sensitive sodium-chloride cotransporter in the kidney and is induced by glucose deprivation. PDIA3 is part of the major histocompatibility complex (MHC) class I peptide-loading complex (TAP1), which is important for formation of the final antigen conformation and export from the endoplasmic reticulum to the cell surface.