Anti-CALR Antibody Prodrug, Protease Activated (8B2-H6-10.7)

CAT#: VS-1025-YC38

The Anti-CALR Antibody Prodrug, Protease Activated (8B2-H6-10.7) is an antibody prodrug comprised of a recombinant mouse antibody targeting human CALR, linked to a masking peptide that conceals the active antigen-binding site via a protease-cleavable linker. The mask peptide is recombinantly attached to the amino terminus of either the light or heavy chain of the antibody, designed to block access to the antigen-binding site and physically prevent the antibody from binding to CALR protein. Once the masking peptide is cleaved by matrix metalloproteinases (MMPs), the prodrug is activated, allowing the unmasked monoclonal antibody component to bind to CALR effectively. CALR (Calreticulin) is an endoplasmic reticulum chaperone whose somatic mutations (primarily exon 9 insertions or deletions) are defining oncogenic drivers of myeloproliferative neoplasms (MPNs), particularly essential thrombocythemia and myelofibrosis. These mutations result in a novel C-terminus that interacts with and activates the TPO receptor (MPL), driving constitutive signaling and the overproduction of blood cells.

Gene Expression
Figure 1 IHC staining of human duodenum Figure 2 IF staining of human cell line U-2 OS Figure 3 Cerebral cortex Figure 4 Thyroid gland Figure 5 RNA cell line category: Low cell line specificity

Specifications

  • Host Animal
  • Mouse
  • Applications
  • In situ zymography (ISZ), Cytotoxicity assay (Cyt), Functional assay
  • Specificity
  • Human CALR
  • Target
  • CALR
  • Species Reactivity
  • Human
  • Isotype
  • IgG2a, kappa
  • Clone
  • 8B2-H6-10.7
  • Epitope
  • RRKMSPARPRTSCREACLQGWTEA
  • Masking Approach
  • Affinity mask
  • Mask
  • A synthetic peptide
  • Protease Cleavable Linker
  • MMP-cleavable linker
  • Protease Substrate
  • MMPs
  • Purification
  • Protein A purified
  • Buffer
  • PBS, pH 7.4
  • Preservative
  • No preservatives
  • Storage
  • Store at 4°C short term. For long term storage, store at -20°C, avoiding freeze/thaw cycles.

Target

  • Introduction
  • Calreticulin is a multifunctional protein that acts as a major Ca(2+)-binding (storage) protein in the lumen of the endoplasmic reticulum. It is also found in the nucleus, suggesting that it may have a role in transcription regulation. Calreticulin binds to the synthetic peptide KLGFFKR, which is almost identical to an amino acid sequence in the DNA-binding domain of the superfamily of nuclear receptors. Calreticulin binds to antibodies in certain sera of systemic lupus and Sjogren patients which contain anti-Ro/SSA antibodies, it is highly conserved among species, and it is located in the endoplasmic and sarcoplasmic reticulum where it may bind calcium. 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 can inhibit the binding of androgen receptor to its hormone-responsive DNA element and can inhibit androgen receptor and retinoic acid receptor transcriptional activities in vivo, as well as retinoic acid-induced neuronal differentiation. Thus, calreticulin can act as an important modulator of the regulation of gene transcription by nuclear hormone receptors. Systemic lupus erythematosus is associated with increased autoantibody titers against calreticulin but calreticulin is not a Ro/SS-A antigen. Earlier papers referred to calreticulin as an Ro/SS-A antigen but this was later disproven. Increased autoantibody titer against human calreticulin is found in infants with complete congenital heart block of both the IgG and IgM classes.
  • Alternative Names
  • Calregulin; ERp60; CRP55; HACBP; Grp60; Epididymis Secretory Sperm Binding Protein Li 99n; Autoantigen Ro; HEL-S-99n; CC1qR; CRTC; SSA; CRT
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