CALR/Calreticulin His Tag Protein, Human,specification,price,image-Bio-Equip in China

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Product Specification

Species	Human
Synonyms	CRT, HEL-S-99n, RO, SSA
Accession	P27797
Amino Acid Sequence	Glu18-Ala413, with C-terminal His
Expression System	HEK293
Molecular Weight	50-60kDa (Reducing)
Purity	＞95% by SDS-PAGE
Endotoxin	<0.1EU/μg
Conjugation	Unconjugated
Tag	His Tag
Physical Appearance	Lyophilized Powder
Storage Buffer	PBS, pH7.4.
Reconstitution	Reconstitute at 0.1-1 mg/ml according to the size in ultrapure water after rapid centrifugation.
Stability & Storage	· 12 months from date of receipt, lyophilized powder stored at -20 to -80℃. · 3 months, -20 to -80℃ under sterile conditions after reconstitution. · 1 week, 2 to 8℃ under sterile conditions after reconstitution. · Please avoid repeated freeze-thaw cycles.
Reference	1.Michalak M, et al. (2002) Calreticulin in cardiac development and pathology. Biochim Biophys Acta. 1600(1-2):32-7. 2.Chao MP, et al. (2010) Calreticulin is the dominant pro-phagocytic signal on multiple human cancers and is counterbalanced by CD47. Sci Transl Med. 2(63):63ra94. 3.Andrin, C, et al. (1998) Interaction between a Ca2+-binding protein calreticulin and perforin, a component of the cytotoxic T-cell granules. Biochemistry. 37(29):10386-94.

Background

Calreticulin is a multifunctional protein. It acts as a main Ca(2+)-binding (storage) protein in the lumen of the endoplasmic reticulum. Calreticulin binds Ca2+ ions (a second messenger in signal transduction), rendering it inactive. The Ca2+ is bound with low affinity, but high capacity, and can be released on a signal. Located in storage compartments associated with the endoplasmic reticulum, calreticulin also binds to misfolded proteins and prevents them from being exported from the endoplasmic reticulum to the golgi apparatus. The amino terminus of calreticulin interacts with the DNA-binding domain of the glucocorticoid receptor and prevents the receptor from binding to its specific glucocorticoid response element. Calreticulin reduces the binding of androgen receptor to its hormone-responsive DNA element and inhibits androgen receptor and retinoic acid receptor transcriptional activities in vivo, as well as retinoic acid-induced neuronal differentiation. Therefore, calreticulin acts as a significant modulator of the regulation of gene transcription by nuclear hormone receptors.