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Calreticulin Mouse, Unlabeled, Clone: 16, BD

Mouse Monoclonal Antibody

$286.00 - $532.00

Specifications

Antigen Calreticulin
Clone 16
Concentration 250μg/mL
Applications Western Blot
Classification Monoclonal
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Products 2
Catalog Number Mfr. No. Quantity Price Quantity & Availability  
Catalog Number Mfr. No. Quantity Price Quantity & Availability  
BDB612136
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BD Biosciences
612136
50 μg
Each for $286.00
Only null left
Add to Cart
 
BDB612137
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BD Biosciences
612137
150 μg
Each for $532.00
Only null left
Add to Cart
 
Description

Description

Proteins undergo numerous modifications, including folding, translocation, and degradation. During such modifications, polypeptides are rarely in a native, stable state. Molecular chaperones are a diverse group of proteins that modulate polypeptide stability through ATP-dependent folding. Many chaperone proteins are found in the endoplasmic reticulum (ER). Calreticulin is a luminal ER protein that is 39% homologous to the ER chaperone protein, calnexin. Calreticulin contains a C-terminal KDEL ER retention signal, and can bind Ca2+;, Zn2+, ATP, and the proteins, ERp57 and protein disulfide isomerase. The molecular chaperone activities of calreticulin may include folding of both Asn-linked glycoproteins and non-glycosylated proteins. In addition, calreticulin is a component of MHC I/transporter associated with Ag presentation (TAP) complex where it may function in peptide assembly onto nascent class I molecules. Calreticulin may also function in integrin signaling, since it binds a3-integrin subunits and regulates integrin-mediated metalloprotease secretion. Thus, calreticulin may be involved in Ca2+; storage, cell adhesion, and protein folding.

Immunofluorescence, Western Blotting

Specifications

Specifications

Calreticulin
250μg/mL
Monoclonal
Mouse
Cell Biology
Aqueous buffered solution containing BSA, glycerol, and ≤0.09% sodium azide.
IgG1
Affinity Purified
16
Western Blot
Unconjugated
RUO
Human, Mouse, Rat
Mouse Calreticulin aa. 270-390
Primary
Store undiluted at -20°C.
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