CALR Human

Calreticulin Human Recombinant
Cat. No.
BT3342
Source
Escherichia Coli.
Synonyms
cC1qR, CRT, FLJ26680, RO, SSA, CRP55, Calreticulin, ERp60, CRTC, CALR.
Appearance
Sterile filtered colorless solution.
Purity
Greater than 85% as determined by SDS-PAGE.
Usage
THE BioTek's products are furnished for LABORATORY RESEARCH USE ONLY. They may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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In Stock

Description

CALR Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 421 amino acids (18-417 a.a.) and having a molecular mass of 48.7 kDa. CALR protein is fused to a 21 amino acid His-Tag at N-terminus and purified by standard chromatography.

Product Specs

Introduction
Calreticulin (CALR) is a multifunctional protein primarily located within the endoplasmic reticulum where it serves as a major calcium-binding protein. It plays a crucial role in calcium homeostasis within this organelle. Beyond its function in the endoplasmic reticulum, CALR is also found in the nucleus, where it participates in the regulation of gene transcription. Notably, CALR interacts with a specific amino acid sequence (KLGFFKR) that closely resembles a region within the DNA-binding domain of nuclear receptors, a superfamily of transcription factors. This interaction suggests a mechanism by which CALR may influence gene expression. CALR has been identified as an autoantigen, meaning it is targeted by antibodies in the sera of certain individuals with autoimmune disorders such as systemic lupus and Sjogren's syndrome, particularly those with anti-Ro/SSA antibodies. The protein exhibits a high degree of conservation across different species, highlighting its fundamental biological importance. CALR's ability to modulate the activity of nuclear hormone receptors is noteworthy. For instance, it can hinder the glucocorticoid receptor from binding to its specific DNA response element, thereby influencing glucocorticoid signaling. Similarly, CALR can interfere with the androgen receptor's interaction with its hormone-responsive DNA element, ultimately suppressing both androgen receptor and retinoic acid receptor transcriptional activities. Moreover, CALR has been shown to inhibit retinoic acid-induced neuronal differentiation. These findings collectively suggest that CALR functions as a crucial regulator of gene transcription, particularly in pathways governed by nuclear hormone receptors.
Description
Recombinant human CALR protein, expressed in E. coli, is a single polypeptide chain that lacks glycosylation. This protein consists of 421 amino acids (residues 18-417) and possesses a molecular weight of 48.7 kDa. A 21 amino acid His-Tag is fused to the N-terminus to facilitate purification, which is achieved using standard chromatography techniques.
Physical Appearance
A clear, colorless solution that has been sterilized by filtration.
Formulation
The CALR Human solution is formulated in a buffer containing 20mM Tris-HCl (pH 8.0), 1mM DTT, 0.1M NaCl, and 10% glycerol.
Stability
For short-term storage (up to 4 weeks), the product should be stored at 4°C. Long-term storage requires freezing at -20°C. The addition of a carrier protein (0.1% HSA or BSA) is recommended for extended storage durations. Repeated freezing and thawing should be avoided to maintain product integrity.
Purity
The purity of the CALR Human Recombinant protein is determined by SDS-PAGE analysis and is greater than 85%.
Synonyms
cC1qR, CRT, FLJ26680, RO, SSA, CRP55, Calreticulin, ERp60, CRTC, CALR.
Source
Escherichia Coli.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MEPAVYFKEQ FLDGDGWTSR WIESKHKSDF GKFVLSSGKF YGDEEKDKGL QTSQDARFYA LSASFEPFSN KGQTLVVQFT VKHEQNIDCG GGYVKLFPNS LDQTDMHGDS EYNIMFGPDI CGPGTKKVHV IFNYKGKNVL INKDIRCKDD EFTHLYTLIV RPDNTYEVKI DNSQVESGSL EDDWDFLPPK KIKDPDASKP EDWDERAKID DPTDSKPEDW DKPEHIPDPD AKKPEDWDEE MDGEWEPPVI QNPEYKGEWK PRQIDNPDYK GTWIHPEIDN PEYSPDPSIY AYDNFGVLGL DLWQVKSGTI FDNFLITNDE AYAEEFGNET WGVTKAAEKQ MKDKQDEEQR LKEEEEDKKR KEEEEAEDKE DDEDKDEDEE DEEDKEEDEE EDVPGQAKDE L.

Product Science Overview

Structure and Function

Calreticulin is a calcium-binding chaperone protein that ensures proper folding of newly synthesized glycoproteins. It works in conjunction with other ER chaperones like calnexin and ERp57 to maintain protein quality control . The protein has a highly conserved structure, which includes a N-terminal signal sequence, a central proline-rich P-domain, and a C-terminal acidic domain that binds calcium ions .

Biological Roles
  1. Protein Folding: Calreticulin assists in the proper folding of glycoproteins by binding to misfolded proteins and preventing their aggregation .
  2. Calcium Homeostasis: It acts as a major calcium storage protein in the ER, regulating intracellular calcium levels and signaling pathways .
  3. Immune Response: Calreticulin is involved in the presentation of antigens to the immune system, particularly in the processing of MHC class I molecules .
Recombinant Production

Recombinant human calreticulin is produced using various expression systems, including yeast species like Saccharomyces cerevisiae and Pichia pastoris. These systems allow for high-level secretion of mature recombinant protein into the culture medium . The recombinant protein is structurally and functionally identical to native calreticulin, ensuring its biological activity is preserved .

Therapeutic Applications

Calreticulin has shown potential in therapeutic applications, particularly in wound healing. Topical application of recombinant calreticulin has demonstrated pro-healing effects, such as enhanced keratinocyte and fibroblast migration, induction of extracellular matrix proteins, and increased granulation tissue formation . These properties make it a promising candidate for treating chronic wounds and other conditions requiring tissue regeneration.

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