Labelling Review row-Online

Calcitonin
Clone CL1948 New!
1 mL, 0.1 mL liquid NCL-L-CALCITONIN P (Enzyme)
Polyclonal
0.5 mL lyophilized NCL-CALp FP
7 mL Bond ready-to-use PA0406 P (Enzyme)
Calcitonin (CT) is a 32 amino acid peptide synthesized by the parafollicular C
cells of the thyroid. It acts through its receptors to inhibit osteoclast
mediated bone resorption, decrease calcium resorption by the kidney and
decrease calcium absorption by the intestines. The action of calcitonin is
therefore to cause a reduction in serum calcium, an effect opposite to that
of parathyroid hormone. The calcitonin gene transcript also encodes the
calcitonin gene-related peptide (CGRP), which is thought to be a potent
vasodilator. The tissue specificity of the transcript produced depends on
alternative splicing of the CT/CGRP gene transcript. In the parafollicular
cells of the thyroid 95 percent of the CT/CGRP is processed and translated to
produce CT, however, in neuronal cells 99 percent of the CT/CGRP RNA is
translated into CGRP. The C cells of the thyroid give rise to an endocrine
tumor, medullary thyroid carcinoma (MTC), which occurs in a sporadic (75
percent of cases) and hereditary form (25 percent of cases). Familial MTC is
associated with C cell hyperplasia (CCH), whereas sporadic MTC is thought
not to be. However, in the general population CCH is present in 20-30
percent of thyroid glands, either with normal histology, thyroiditis or
follicular tumors.
Refer to page 16 for the Bond ready-to-use format.
Human medullary thyroid carcinoma: immunohistochemical staining for calcitonin using
NCL-L- CALCITONIN. Paraffin section.
Calmodulin
Clone 6312
1 mL lyophilized NCL-CALMODULIN P (HIER)
Calmodulin, a ubiquitous eukaryotic calcium binding protein, is a principal
mediator of the calcium signal. It participates in signalling pathways
inducing proliferation, motility and cell cycle progression. Human calmodulin
is encoded by three genes CALM1, CALM2 and CALM3 located on different
chromosomes. The vertebrate CALM family of genes is unique in that its
members specify an identical protein. The protein itself is made up of 148
amino acids and has four calcium binding domains. As calmodulin is
essential for normal cell function, it is likely that levels are tightly controlled
both temporally and spatially. Immunohistochemical staining for calmodulin
has been reported in the epithelia of testis, breast, stomach, prostate, gall
bladder as well as in macrophages, fibroblasts and sebaceous glands within
the dermis of skin. In healing skin wounds, calmodulin is found at its highest
levels in maturing keratinocytes. It is noticeably abundant in epidermis close
to a wound and re-epithelializing margins where calcium levels are highest.
In studies of Alzheimer's brains, calmodulin immunostaining has been
reported to be lost in cortical regions where large amounts of aluminium
have accumulated.
Human in situ ductal carcinoma of breast: immunohistochemical staining for calmodulin using
NCL-CALMODULIN. Note cytoplasmic and membrane staining of malignant cells. Paraffin
section.
Calpain
Clone Calp3d/2C4
2.5 mL lyophilized NCL-CALP-2C4 W
Clone Calp3c/11B3
2.5 mL, 1mL lyophilized NCL-CALP-11B3 W
Clone Calp3c/12A2
2.5 mL, 1 mL lyophilized NCL-CALP-12A2 W
At least seven forms of autosomal recessive muscular dystrophy (MD) have
been included under the banner “limb girdle muscular dystrophy” (LGMD).
These forms may be divided into two groups; those with abnormal
expression of the dystrophin/glycoprotein complex and those in which
labeling of the proteins in this complex is unaffected. Thus the
sarcoglycanopathies (also known as LGMD types 2C, 2D, 2E and 2F) are
caused by defects in the genes for gamma, alpha, beta and deltasarcoglycan
on chromosomes 13q12, 17q21, 4q12 and 5q33, respectively.
Among the dystrophies in which expression of the sarcoglycans is normal,
the gene responsible for LGMD2A has been identified as the chromosome
15q15-encoded muscle-specific calcium-activated neutral protease, calpain
3. Calpain 3 enzyme is only stable in human muscle when homogenized in
treatment buffer immediately after harvest. (Anderson LVB et al. American
Journal of Pathology. 153(4): 1169-1179 (1998)), and in homogenates
containing SDS and is therefore well suited for analysis by Western blot.
Product Specific Information
NCL-CALP-2C4 reacts with the full-size calpain 3 (94 kD) and an additional
fragment (30 kD) in human skeletal muscle. NCL-CALP-12A2 reacts with fullsize
protein plus apparent degradation products at approximately 60 kD.
Specificity of these antibodies has been confirmed by the loss of all these
bands in samples with null gene mutations. NCL-CALP-11B3 reacts with
calpain 3 bands at 94 and 60 kD, pre- and post-autolyzed forms of the
ubiquitous calpains 1 and 2 (� and m-calpain) staining a group of bands
between 76 and 84 kD in human skeletal muscle (Anderson LVB et al.
American Journal of Pathology. 153(4): 1169-1179, (1998)) Cross-reactivities in
different animals and tissues are described (see reference).
F Frozen I Immunofluorescence E Electron microscopy
P Paraffin C Flow cytometry O Other applications
W Western blotting
/65
Primary Antibodies